6-Phosphogluconate Dehydrogenase, domain 3
6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING
6-phosphogluconate dehydrogenase C-terminal domain-like
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Belongs to the 6-phosphogluconate dehydrogenase family.
Developmentally regulated neuraminidase implicated in parasite invasion of cells. May contribute to the pathology during T.cruzi infection by cleaving sialic acid from cells of the immune system.
The parasite mammalian stage surface antigen exhibits extensive antigenic diversity.
Belongs to the glycosyl hydrolase 33 family.
Cloning and characterization of two virulent-related actin genes in Naegleria fowleri.
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
The regulation of actin gene expression during Naegleria differentiation.
Molecular characterization of Trypanosoma brucei alkyl-dihydroxyacetonephosphate synthase.
Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2
ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL
FAD-binding/transporter-associated domain-like
Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids.
Belongs to the FAD-binding oxidoreductase/transferase type 4 family.
Microtubule-associated protein that may be involved in cross-linking microtubules.
Ribonuclease H-like superfamily/Ribonuclease H
EUKARYOTIC TRANSLATION INITIATION FACTOR 2C
Involved in RNA-mediated gene silencing (RNAi) of mobile elements and repeats including retroposons SLACS (Spliced Leader Associated Conserved Sequence), TATE (Telomere-Associated Transposable Element) and TAS-like sequences (Telomere Associated Sequence), and a family of 74-nucleotide long tandem repeats, CIR74 (PubMed:21060810, PubMed:23217017). Predominantly binds to siRNAs derived from SLACS and TATE transposable elements and to a lesser extent to siRNAs from TAS-like and CIR74 elements (PubMed:23217017).
RNAi-mediated knockdown reduces RNAi activity (PubMed:21060810, PubMed:23217017). Levels of mobile elements TATE, SLACS, TAS-like and repeat element CIR74 siRNAs are reduced (PubMed:23217017).
ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1
Could have an RNA-binding activity in addition of its catalytic role.
Belongs to the aldehyde dehydrogenase family.
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-371
Fructose-bisphosphate aldolase, glycosomal
Belongs to the class I fructose-bisphosphate aldolase family.
Schiff-base intermediate with dihydroxyacetone-P
Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
S-adenosyl-L-methionine-dependent methyltransferases
Arginine methyltransferase that specifically catalyzes the formation of omega-N monomethylarginine (MMA). Has activity toward multiple substrates in vitro. Able to mediate the arginine methylation of histones and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.
Present in large multiprotein complexes.
Expressed during both bloodstream (BF) and procyclic insect (PF) life cycle stages.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.
Compared to PRMT7 orthologs in other metazoans, it is shorter and lacks the C-terminal part.
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH IRON IONS
Catalyzes cyanide-resistant oxygen consumption. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures.
Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane.
Belongs to the alternative oxidase family.
N-terminal acetyltransferase complex ARD1 subunit homolog
Belongs to the acetyltransferase family. ARD1 subfamily.
EXPORTED CALCIUM-BINDING GLYCOPROTEIN-RELATED
May function as a calcium-binding protein.
P-loop containing nucleotide triphosphate hydrolases
ARSENICAL PUMP-DRIVING ATPASE ARSENITE-TRANSLOCATING ATPASE
P-loop containing nucleoside triphosphate hydrolases
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released.
Belongs to the acetyltransferase ATAT1 family.
Calcium-transporting ATPase, cytoplasmic domain N
Calcium-transporting ATPase, cytoplasmic transduction domain A
Calcium-transporting ATPase, transmembrane domain
CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC/ENDOPLASMIC RETICULUM TYPE
Metal cation-transporting ATPase, ATP-binding domain N
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium.
May be located in the flagellar pocket of the membrane.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-188
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 19-188
the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily
Mitochondrial membrane ATP synthase (F(1)F(o) ATP synthase) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:19436713, PubMed:29247468). F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(o) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:19436713, PubMed:29247468, PubMed:29440423). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1) (PubMed:19436713, PubMed:29440423). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (Probable). Contrary to the procyclic, insect form that requires F(1)F(o) ATP synthase for ATP synthesis, the bloodstream form relies on ATP hydrolysis by F(1)F(o) ATP synthase to maintain its mitochondrial membrane potential (PubMed:29247468).
F-type ATPases have 2 components, F(1) - the catalytic core - and F(o) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1), plus the additional subunit P18 (Tb427.05.1710) that is not present in F(1)F(o) ATP synthase from metazoa (PubMed:19436713, PubMed:29247468, PubMed:29440423). Subunit P18 (Tb927.5.1710) interacts with the alpha subunit with a 1:1 stoichiometry; the interaction is direct (PubMed:29440423). Subunit gamma is part of the central stalk (PubMed:29440423). F(o) has three main subunits: a, b and c (PubMed:19436713). The trypanosomal ATPase complex contains additional subunits that are not present in the F(1)F(o) ATP synthase from metazoa (PubMed:19436713, PubMed:29247468, PubMed:29440423).
RNAi-mediated knockdown of the protein impairs assembly of the F(1) component and slows the proliferation rate of procyclic cells that are cultivated in vitro in the presence of glucose. RNAi-mediated knockdown of the protein also slows the proliferation rate of the bloodstream form of the parasite, despite the fact that the organism can profit from blood glucose as source of energy. Mitochondrial membrane potential is dramatically reduced in the bloodstream form that relies on ATP hydrolysis to maintain mitochondrial membrane potential.
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 10-75
ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial
Epsilon subunit of mitochondrial F1F0-ATP synthase
ATP synthase subunit epsilon, mitochondrial
Belongs to the eukaryotic ATPase epsilon family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-119
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
ATP synthase alpha/beta chain, C-terminal domain
ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
C-terminal domain of alpha and beta subunits of F1 ATP synthase
N-terminal domain of alpha and beta subunits of F1 ATP synthase
ATP synthase subunit alpha, chloroplastic
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a, b, b' and c.
Belongs to the ATPase alpha/beta chains family.
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 25-584 IN COMPLEX WITH ADP
Mitochondrial membrane ATP synthase (F(1)F(o) ATP synthase) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:19436713, PubMed:29247468). F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(o) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:19436713, PubMed:29247468, PubMed:29440423). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1) (PubMed:19436713, PubMed:29440423). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (Probable). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (PubMed:29440423). Contrary to the procyclic, insect form that requires F(1)F(o) ATP synthase for ATP synthesis, the bloodstream form relies on ATP hydrolysis by F(1)F(o) ATP synthase to maintain its mitochondrial membrane potential (PubMed:29247468).
RNAi-mediated knockdown of the protein in procyclic, insect stage cells impairs assembly of the F(1) component and slows the proliferation rate of procyclic cells that are cultivated in vitro, both in the presence and in the absence of glucose in the growth medium. ATP synthesis by oxidative phosphorylation is dramatically reduced in procyclic cells.
ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
ATP synthase subunit beta, chloroplastic
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(9-12).
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 22-519 IN COMPLEX WITH ATP
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 18-182
F0F1 ATP synthase delta/epsilon subunit, N-terminal
ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL
Epsilon subunit of F1F0-ATP synthase N-terminal domain
Belongs to the ATPase epsilon chain family.
ATP SYNTHASE EPSILON CHAIN, CHLOROPLASTIC
Produces ATP from ADP in the presence of a proton gradient across the membrane.
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains.
In plastids the F-type ATPase is also known as CF(1)CF(0).
ATP synthase, gamma subunit, helix hairpin domain
ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL
Belongs to the ATPase gamma chain family.
Confers resistance to killing by ethidium bromide and isometamidium. Decreases mitochondrial membrane potential, and increases time required to reach lethal levels of parasitemia in vivo. Loss of the kinetoplast, a specialized mitochondrial structure that harbors the mitochondrial genome.
PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA]
ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Reversibly protonated during proton transport
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
Type I PLP-dependent aspartate aminotransferase-like (Major domain)
L-tyrosine:2-oxoglutarate aminotransferase
Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate (By similarity).
Mainly cytoplasmic. Present to a small extent in the mitochondrial fraction.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Was originally thought to have three internal disulfide bonds.
the p-type atpase (p-atpase) superfamily
More abundant in promastigotes than amastigotes.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily.
More abundant in amastigotes than promastigotes.
YVTN repeat-like/Quinoprotein amine dehydrogenase
RIBOSOME BIOGENESIS PROTEIN BOP1 BLOCK OF PROLIFERATION 1 PROTEIN
Ribosome biogenesis protein BOP1 homolog
Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit.
Belongs to the WD repeat BOP1/ERB1 family.
Belongs to the protein disulfide isomerase family.
Lowers pKa of C-terminal Cys of second active site
Fumarate reductase/succinate dehydrogenase, transmembrane subunit
SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT
SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT, MITOCHONDRIAL
Fumarate reductase respiratory complex transmembrane subunits
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
The heme is bound between the two transmembrane subunits.
Forms part of complex II containing four subunits: a 70 kDa flavoprotein (FP), a 27 kDa iron-sulfur protein (IP), a cytochrome B and a membrane-anchoring protein.
ligand shared with second transmembrane subunit
Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Two calmodulins are synthesized during differentiation of Naegleria gruberi from amoebae to flagellates; one remains in the cell body and the other becomes localized in the flagella. Flagellar calmodulin first appears during early stages of differentiation, is maximally expressed at the time that flagella first appear and then levels rapidly decline.
This protein has four functional calcium-binding sites.
Evidence for conservation of a calcium homeostat component: purification characterization and cloning of calreticulin from Euglena gracilis.
Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity).
The interaction with glycans occurs through a binding site in the globular lectin domain.
The zinc binding sites are localized to the N-domain.
PROTEIN PHOSPATASE 3 REGULATORY SUBUNIT B ALPHA ISOFORM TYPE 1
Protein phosphatase 2B regulatory subunit
Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity (By similarity).
Composed of a catalytic subunit (A) and a regulatory subunit (B).
Belongs to the calcineurin regulatory subunit family.
Plays a fundamental role in microtubule-organizing center structure and function.
Centrosome of interphase and mitotic cells.
Binds two moles of calcium per mole of protein.
CHLOROPHYLL A-B BINDING PROTEIN 1, CHLOROPLASTIC-RELATED
Chlorophyll a-b binding protein of LHCII type 1
Chlorophyll a-b binding protein of LHCII type I
The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
The LHC complex consists of chlorophyll a-b binding proteins.
The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Photoregulated by reversible phosphorylation of its threonine residues.
Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.
Cytochrome b6/f complex 12.6 kDa peptide
May be a component of the cytochrome b6/f complex which is part of the photosynthetic respiratory chain.
Transferase(Phosphotransferase) domain 1
Cell division control protein 2 homolog 1
Probably involved in the control of the cell cycle.
Phosphorylation at Ser-15 or Tyr-16 inactivates the enzyme, while phosphorylation at Thr-160 activates it.
Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CELL DIVISION CONTROL PROTEIN 2 HOMOLOG 2
Phosphorylation at Ser-56 or Tyr-57 inactivates the enzyme.
Cell division control protein 2 homolog 3
Phosphorylation at Thr-33 or Tyr-34 inactivates the enzyme.
Cytochrome c biogenesis ATP-binding export protein CcmA
Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system (By similarity).
The complex is composed of two ATP-binding proteins (CcmA) and two transmembrane proteins (ccmB).
Belongs to the ABC transporter superfamily. CcmA exporter (TC 3.A.1.107) family.
Essential for the control of the cell cycle at the G2/M (mitosis) transition.
Belongs to the cyclin family. Cyclin AB subfamily.
CELL DIVISION CONTROL PROTEIN 2 HOMOLOG 4
Serine/threonine-protein kinase (By similarity). Involved in the control of the cell cycle. Required for entry into S-phase and mitosis (By similarity). Probable component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II (By similarity).
Phosphorylation at Thr-17 or Tyr-18 inactivates the enzyme, while phosphorylation at Ser-230 activates it.
May form a complex composed of at least the catalytic subunit CRK2 and a cyclin.
CILIA- AND FLAGELLA-ASSOCIATED PROTEIN 43
Flagellar protein involved in flagellum axoneme organization and function.
Closely associated to the axoneme along the paraflagellar rod.
CILIA- AND FLAGELLA-ASSOCIATED PROTEIN 44
CILIA- AND FLAGELLA-ASSOCIATED PROTEIN 91
Axoneme-associated protein involved in flagellum motility and central pair positioning.
Knockdown of CFAP91 does not affect the cell morphology and the flagella appears normal in number and length. However, flagella exhibit an abnormal axoneme with a rotated central pair complex (CPC) and an impaired flagellar motility.
TCP-1-like chaperonin intermediate domain
60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL
Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.
Belongs to the chaperonin (HSP60) family.
Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (By similarity).
More abundant in the procyclic forms than in the bloodstream forms.
By heat shock. There are multiple isoforms that, with increasing temperature, shift in relative abundance from the more basic to the more acidic.
Exists in at least five isoforms that are not related by a simple post-translational modification and may represent the products of different genes.
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HUMAN CTSL
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH P.FALCIPARUM FP2A
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH HUMAN CTSB
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH C.PAPAYA PAPAIN
Cysteine protease inhibitor (PubMed:17561110, PubMed:11719560, PubMed:17502099, PubMed:18515357, PubMed:19143838). Inhibits cysteine protease cruzipain (PubMed:11719560, PubMed:17561110).
Flagellar pocket and cytoplasmic vesicles of trypomastigotes and to the cell surface of amastigotes.
Highly expressed in trypomastigotes and to a lesser extent in epimastigotes and amastigotes (at protein level).
The BC, DE and FG loops form a tripartite wedge that blocks the substrate-binding site of target cysteine proteases (PubMed:17561110, PubMed:17502099, PubMed:18515357, PubMed:19143838). The BC loop interacts with the catalytically active cysteine and histidine residues of the of the protease catalytic center (PubMed:17561110, PubMed:17502099, PubMed:18515357, PubMed:19143838).
Belongs to the protease inhibitor I42 family.
Magnesium chelatase subunit I, C-Terminal domain
MAGNESIUM-CHELATASE SUBUNIT CHLI-2, CHLOROPLASTIC
Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
Belongs to the Mg-chelatase subunits D/I family.
Probable citrate synthase, mitochondrial
Citrate synthase is found in nearly all cells capable of oxidative metabolism.
MUTAGENESIS OF ASP-133 AND 299-ARG--VAL-332
Serine/threonine protein kinase (PubMed:19450734, PubMed:27002830). May phosphorylate ZC3H11 during unstressed conditions, leading to proteasome-dependent degradation of ZC3H11 (PubMed:27002830).
Optimum temperature is about 27 degrees Celsius. Loses activity at 41 degrees Celsius.
RNAi-mediated knockdown in the bloodstream form inhibits cell population growth and leads to gross morphological changes and multinucleation (PubMed:19450734). RNAi-mediated knockdown in the procyclic form inhibits cell population growth and decreases ZC3H11 phosphorylation (PubMed:27002830).
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Abolishes protein kinase activity; when associated with 299-R--V-332 DEL.
Catalytic active. Abolishes protein kinase activity; when associated with A-133.
Cyclin-dependent kinase, regulatory subunit
CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT-RELATED
CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT/60S RIBOSOME SUBUNIT BIOGENESIS PROTEIN NIP7
Cyclin-dependent kinases regulatory subunit
Binds to the catalytic subunit of the cyclin dependent kinases (Cdc2) and is essential for their biological function.
Forms a homohexamer that can probably bind six kinase subunits.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.
The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it.
UBIQUINONE BIOSYNTHESIS PROTEIN COQ4 HOMOLOG, MITOCHONDRIAL
Ubiquinone biosynthesis protein COQ4 homolog 1, mitochondrial
Coenzyme Q biosynthesis protein 4 homolog 1
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Component of a multi-subunit COQ enzyme complex.
This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
Ubiquinone biosynthesis protein COQ4 homolog 2, mitochondrial
Coenzyme Q biosynthesis protein 4 homolog 2
Coenzyme Q biosynthesis protein 4 homolog
2-METHOXY-6-POLYPRENYL-1,4-BENZOQUINOL METHYLASE, MITOCHONDRIAL
Ubiquinone biosynthesis methyltransferase COQ5
Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.
Cytochrome c oxidase-like, subunit I domain
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Binds 2 heme A groups non-covalently per subunit.
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII).
Belongs to the heme-copper respiratory oxidase family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-402
Binds a dinuclear copper A center per subunit.
Some positions are modified by RNA editing via nucleotide insertion.
Belongs to the cytochrome c oxidase subunit 2 family.
Same abundance in amastigote, epimastigote, and trypomastigote.
Cytochrome c oxidase, subunit III, four-helix bundle
Belongs to the cytochrome c oxidase subunit 3 family.
CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX11, MITOCHONDRIAL-RELATED
CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX11-RELATED
Cytochrome c oxidase assembly protein ctaG
Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES 1 AND 2)
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE 1)
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES 1 AND 2)
24-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE
Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol (By similarity). Favors C4 dimethylated substrates, the substrate preference order is 24-methylenedihydrolanosterol > 24,25-dihydrolanosterol > lanosterol > obtusifoliol > norlanosterol.
Expressed in both the insect and mammalian life-cycle stages.
Increases activity on norlanosterol and obtusifoliol.
the selenoprotein p receptor (selp-receptor) family
CYSTEINE-RICH, ACIDIC INTEGRAL MEMBRANE PROTEIN
CYSTEINE-RICH, ACIDIC INTEGRAL MEMBRANE PROTEIN-RELATED
Supposed to function as cell surface receptor. Possibly involved in receptor-mediated endocytosis.
66 X 12 AA tandem repeats of D-D-C-[ND]-I-T-G-D-G-N-E-T
Cell division protein kinase 2 homolog CRK1
May be involved in some stage-specific role in the promastigote cell cycle.
Phosphorylation at Thr-15 or Tyr-16 inactivates the enzyme, while phosphorylation at Thr-160 activates it.
Expressed in all life cycle stages, promastigote, metacyclic and amastigote forms but is found in the active form only in the promastigote stage.
Essential protein involved in pre-mRNA cis- and trans-splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate.
Associates with the NTC complex (or PRP19-associated complex) (By similarity). The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex reminiscent of a late-stage spliceosome (By similarity). Associates specifically with U5-containing snRNPs.
Cytochrome c1, transmembrane anchor, C-terminal
CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL
Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor
Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c.
Binds 1 heme group covalently per subunit.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 3 respiratory subunits cytochrome b, cytochrome c1 and Rieske protein, 2 core protein subunits, and additional low-molecular weight protein subunits. The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with cytochrome c oxidase (complex IV, CIV).
This cytochrome c1 is unusual, its alpha-band exists at 561 nm instead at 553 nm.
ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC
ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED
Receptor-type adenylate cyclase GRESAG 4.1
Could act as a receptor for an unknown ligand.
Belongs to the adenylyl cyclase class-3 family.
Receptor-type adenylate cyclase GRESAG 4.2
Receptor-type adenylate cyclase GRESAG 4.3
Expressed in the insect stage (promastigote) but not in the mammalian host stage of the parasite life cycle.
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Binds 2 heme b groups non-covalently with two histidine residues as axial ligands.
Binds one heme group covalently by a single cysteine link with no axial amino acid ligand. This heme was named heme ci.
The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer.
Heme 1 (or BH or b566) is high-potential and absorbs at about 566 nm, and heme 2 (or BL or b562) is low-potential and absorbs at about 562 nm.
Belongs to the cytochrome b family. PetB subfamily.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-371
a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
The main subunits of complex b-c1 are: cytochrome b, cytochrome c1 and the Rieske protein.
Some positions are modified by RNA editing via nucleotide insertion or deletion. The initiator methionine is created by RNA editing.
Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm.
The protein contains an even number of transmembrane helices, fewer than predicted by bioinformatics tools.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (KINETOPLAST)
Some positions are modified by RNA editing via nucleotide insertion or deletion.
Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
Binds 1 heme c group covalently per subunit.
Belongs to the cytochrome c family. PetJ subfamily.
Protein Spotlight; Life shuttle - Issue 76 of November 2006
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Loosely associated with the inner membrane.
Cytochrome f subunit of the cytochrome b6f complex, transmembrane anchor
Translocates protons across the thylakoid membrane and transfers electrons from photosystem II to photosystem I. It receives electrons from the Rieske iron-sulfur protein and passes them to plastocyanin.
Interacts with plastocyanin and Rieske iron-sulfur protein.
This polypeptide is nuclear encoded in Euglena gracilis, but is chloroplast encoded in other plant species.
The cysteine proteinases have a potential role in host-parasite interaction and virulence.
Primarily expressed by the amastigote stage. Expressed 4 times more in amastigotes than in promastigotes.
Associated with megasome, a unique lysosomal organelle found in intracellular amastigotes of the L.mexicana complex.
Primarily expressed by the amastigote stage. Expressed 15 times more in amastigotes than in promastigotes.
Predominantly expressed by stumpy forms, which are preadapted for differentiation into procyclic trypanosomes in the tse-tse midgut.
The 108-residue extension appears likely to be processed in part to produce the mature enzyme, and may be involved in targeting the protein within the cell.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONES 1800-2 AND 1800-4)
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-306
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 123-337
4-Nitrophenyl (3S)-3-({N-[(benzyloxy)carbonyl]-L-phenylalanyl}amino)-5-phenyl-1-pentanesulfonate
[1-(1-Benzyl-3-Hydroxy-2-Oxo-Propylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester
[1-(1-Methyl-4,5-Dioxo-Pent-2-Enylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester
[1-(3-hydroxy-2-oxo-1-phenethyl-propylcarbamoyl)2-phenyl-ethyl]-carbamic acid pyridin-4-ylmethyl ester
Benzyl N-[(2S)-5-(diaminomethylamino)-1-[[(2S)-4-fluoro-3-oxobutan-2-yl]amino]-1-oxopentan-2-yl]carbamate
Hydrolyzes chromogenic peptides at the carboxyl Arg or Lys; requires at least one more amino acid, preferably Arg, Phe, Val or Leu, between the terminal Arg or Lys and the amino-blocking group.
The cysteine protease may play an important role in the development and differentiation of the parasites at several stages of their life cycle.
Strongly inhibited by E-64 (L-trans-epoxysuccinylleucylamido(4-guanidino)butane), Leupeptin, and N-alpha-p-tosyl-L-lysine chloromethyl ketone.
Purified cruzipain is able to degrade itself, yielding a complex mixture of small peptides, and a major 25 kDa fragment.
Cytochrome b5-like heme/steroid binding domain
Fatty acid desaturase that introduces a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta(7) double bond, resulting in the production of delta-4 desaturated fatty acid docosahexanoic acid (DHA). Also acts on the 16-carbon polyunsaturated fatty acids.
The cytochrome b5 heme-binding domain acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.
Belongs to the fatty acid desaturase type 1 family.
CILIA- AND FLAGELLA-ASSOCIATED PROTEIN 410-RELATED
Leucine-rich repeat-containing protein 6
Involved in the regulation of the cell cycle; is required for the basal body replication and new flagellum biogenesis.
Trypomastigote decay-accelerating factor
Interferes with the efficient assembly of the host C3 convertase. Could protect parasites from complement-mediated lysis by sera from a number of different species.
Belongs to the receptors of complement activation (RCA) family.
Molecular cloning and functional expression of the S-adenosylmethionine decarboxylase gene of Leishmania donovani and Trypanosoma brucei.
S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME
S-adenosylmethionine decarboxylase alpha chain
S-adenosylmethionine decarboxylase beta chain
In association with the catalytically inactive AdoMetDC prozyme, catalyzes the decarboxylation of S-adenosyl-L-methionine which is essential for the biosynthesis of the polyamine spermidine. Required for growth and survival during the bloodstream life cycle stage (PubMed:18949025).
Binds 1 pyruvoyl group covalently per subunit.
Allosterically activated by AdoMetDC prozyme. Activated by putrescine and to a lesser extent by spermidine, norspermidine and spermine. Inhibited by 5'-([(Z)-4-amino-2-butenyl]methylamino)-5'-deoxyadenosine (MDL 73811).
0.38 mM for S-adenosyl-L-methionine (at 37 degrees Celsius)
0.24 mM for S-adenosyl-L-methionine (in presence of putrescine and at 37 degrees Celsius)
0.11 mM for S-adenosyl-L-methionine (in presence of AdoMetDC prozyme and at 37 degrees Celsius)
0.17 mM for S-adenosyl-L-methionine (in presence of AdoMetDC prozyme and putrescine and at 37 degrees Celsius)
Forms a heterodimer with catalytically inactive AdoMetDC prozyme; heterodimerization is required to activate AdoMetDC.
Is synthesized initially as an inactive proenzyme (PubMed:17485680). Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification (By similarity). Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme (By similarity). The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain (By similarity).
RNAi-mediated knockdown causes cell growth arrest followed by death. Putrescine levels are increased and the production of spermidine, glutathionyl-spermidine and trypanothione is severely reduced. In addition, expression levels of AdoMetDC prozyme and ornithine carboxylase (ODC) are increased.
Belongs to the eukaryotic AdoMetDC family.
Schiff-base intermediate with substrate; via pyruvic acid
Proton acceptor; for processing activity
Probably in association with catalytically inactive AdoMetDC prozyme, catalyzes the decarboxylation of S-adenosyl-L-methionine which is essential for the biosynthesis of the polyamine spermidine (PubMed:9677309, PubMed:10413038). Required for growth and survival during the bloodstream life cycle stage (By similarity).
Allosterically activated by AdoMetDC prozyme (By similarity). Activated by putrescine (PubMed:9677309, PubMed:10413038). Inhibited by spermine and methylglyoxal-bis(guanylhydrazone) (MGBG) and slightly by spermidine (PubMed:9677309). Inhibited by 5'-([(Z)-4-amino-2-butenyl]methylamino)-5'-deoxyadenosine (MDL 73811) (PubMed:10413038).
0.21 mM for S-adenosyl-L-methionine (at pH 7.5)
0.051 mM for S-adenosyl-L-methionine (in presence of putrescine)
Is synthesized initially as an inactive proenzyme (PubMed:9677309, PubMed:10413038). Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification (By similarity). Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme (By similarity). The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to the alpha chain (By similarity).
DECARBOXYLASE PROENZYME-LIKE, PUTATIVE-RELATED
Inactive S-adenosylmethionine decarboxylase prozyme
Probably has no catalytic activity due to the loss of several residues required for processing and catalysis (PubMed:17485680). Forms a complex with S-adenosylmethionine decarboxylase AdoMetDC which is essential to activate AdoMetDC (PubMed:17485680, PubMed:18949025). Required for the biosynthesis of the polyamine spermidine (PubMed:18949025). Required for growth and survival during the bloodstream life cycle stage (PubMed:18949025).
Forms a heterodimer with S-adenosylmethionine decarboxylase AdoMetDC; heterodimerization is required to activate AdoMetDC.
RNAi-mediated knockdown at the bloodstream life cycle stage causes cell growth arrest followed by death. Putrescine levels are increased and the production of spermidine, glutathione, glutathionyl-spermidine and trypanothione is severely reduced. In addition, protein expression levels of ornithine carboxylase (ODC) are increased.
Heterotetramer of two alpha and two beta chains.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain (By similarity).
Leishmania infantum S-adenosylmethionine decarboxylase.
ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Inhibited by antizyme (AZ) in response to polyamine levels. AZ inhibits the assembly of the functional homodimer by binding to ODC monomers and targeting them for ubiquitin-independent proteolytic destruction by the 26S proteasome (By similarity). Inhibited by 1-amino-oxy-3-aminopropane (APA, an isosteric analog of putrescine) (PubMed:17407445). Irreversibly inhibited by alpha-difluoromethylornithine (DFMO, a curative agent of West African sleeping sickness) (PubMed:3098971, PubMed:17407445).
kcat is 8.1 sec(-1) with L-ornithine as substrate.
Homodimer. Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers.
Belongs to the Orn/Lys/Arg decarboxylase class-II family.
Proton donor; shared with dimeric partner
Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH COFACTOR AND PUTRESCINE
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH COFACTOR AND SUBSTRATE ANALOG
Inhibited by antizyme (AZ) in response to polyamine levels. AZ inhibits the assembly of the functional homodimer by binding to ODC monomers and targeting them for ubiquitin-independent proteolytic destruction by the 26S proteasome.
kcat is 15 sec(-1) with L-ornithine as substrate.
Converts the enzyme into a decarboxylation-dependent transaminase, producing gamma-aminobutyaldehyde (gamma-ABA) and pyridoxamine 5-phosphate (PMP) instead of putrescine.
Aspartic protease (PubMed:22933181, PubMed:21266539).
Inhibited by pepstatin, diazoacetyl-DL-norleucine methyl ester (DAN) and nelfinavir (PubMed:22933181). Inhibited by the proteinase inhibitors lopinavir and ritonavir (PubMed:21266539).
0.57 uM for RE-(EDANS)-SQNYPIVQK-(DABCYL)-R (at 37 degrees Celsius and pH 4-6.5)
7.6 uM for Bz-RGFFL-4MbetaNA (at 37 degrees Celsius and pH 4)
1.18 uM for Bz-RGFFP-4MbetaNA (at 37 degrees Celsius and pH 8)
Optimum pH is 5 with RE-(EDANS)-SQNYPIVQK-(DABCYL)-R as substrate.
When expressed in a DDI1-deficient yeast mutant with high levels of protein secretion, fails to restore normal low protein secretion levels probably due to loss of catalytic activity.
DEAD/H RNA HELICASE HEL64, PUTATIVE-RELATED
Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.
Succinate dehydrogenase membrane anchor subunit
Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur protein, plus two membrane-anchoring proteins.
In association with the non-catalytic regulatory subunit DHSp, catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF5A precursor protein to form the intermediate deoxyhypusine residue. Regulates protein levels of its regulatory subunit DHSp. Required for cell growth and survival.
The binding sites for NAD(+) are contained in the regulatory subunit DHSp.
Allosterically activated by DHSp. Inhibited by spermididine analog N1-guanyl-1,7-diamineoheptane (GC7).
82 uM for NAD(+) (at 37 degrees Celsius when bound to regulatory subunit DHSp)
0.7 uM for IF5A (at 37 degrees Celsius when bound to regulatory subunit DHSp)
43 uM for spermidine (at 37 degrees Celsius when bound to regulatory subunit DHSp)
Heterotetramer formed by a homodimer of the non-catalytic regulatory subunit DHSp and a homodimer of the catalytic subunit DHSc where DHSc appears to bind spermidine and DHSp appears to bind NAD(+).
RNAi-mediated knockdown causes cell growth arrest followed by death, loss of DHSp expression and a failure to sustain infection in mice.
Belongs to the deoxyhypusine synthase family.
Deoxyhypusine synthase-like protein from chromosome 20
Although similar to deoxyhypusine synthase, lacks the active site Lys at position 344 and does not show deoxyhypusine synthase activity. Converting Leu-344 to a lysine does not restore activity.
Deoxyhypusine synthase regulatory subunit
Required for the activation and stability of deoxyhypusine synthase DHSc. Required for cell growth and survival.
Lacks the conserved active site Lys, and therefore lacks catalytic activity.
Deoxyhypusine synthase from chromosome 34
Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
N1-guanyl-1,7-diaminoheptane has a small inhibitory effect on activity.
569 pmol/h/mg enzyme for the forward reaction
DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL
FAD/NAD-linked reductases, dimerisation (C-terminal) domain
The active site is a redox-active disulfide bond.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]
Comparative study of protein profiles on pathogenic and nonpathogenic Naegleria species by 2D-PAGE.
By stress conditions e.g. heat shock (By similarity).
On the 2D-gel the determined pI of this protein is: 5.7, its MW is: 46 kDa.
Belongs to the heat shock protein 70 family.
Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate produced by deoxyhypusine synthase/DHPS on a critical lysine of the eukaryotic translation initiation factor 5A/eIF-5A. This is the second step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function.
Inhibited by metal chelators ciclopirox olamine and mimosine, both of which also significantly inhibit growth. Kojic acid has no effect on activity.
Belongs to the deoxyhypusine hydroxylase family.
DNA polymerase family B, C-terminal domain
Polymerase alpha in a complex with DNA primase is a replicative polymerase.
In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.
Belongs to the DNA polymerase type-B family.
Cytoskeletal linker that plays a central role in the flagellum cell motility. Required for directional cell motility. Plays a role as part of a dynein regulatory system that regulates flagellar beat in response to signals from the central pair apparatus and radial spokes in procyclic cells. Also plays an essential role in the bloodstream form of the trypanosomes as its silencing is lethal for the circulating form.
Associated with the cytoskeleton. Localized to the site of attachment of the flagellum to the subpellicular cytoskeleton. Also localized in the flagellum of the bloodstream form trypanosomes.
Procyclic parasite mutants lacking trypanin exhibit a motility defect indicative of abnormal dynein regulation, but have an actively beating flagellum and are able to spin and tumble in place. However, bloodstream form mutants lacking trypanin exhibit a severe growth defect and are not viable. They revealed a failure of cytokinesis.
Fe-S cluster assembly protein DRE2 homolog 1
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters.
The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Fe-S cluster assembly protein DRE2 homolog 2
Fe-S cluster assembly protein DRE2 homolog
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase (PubMed:25040552). Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit (By similarity).
Thymidylate synthase/dCMP hydroxymethylase domain
Thymidylate synthase/dCMP hydroxymethylase
Bifunctional dihydrofolate reductase-thymidylate synthase
Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP (By similarity).
In the N-terminal section; belongs to the dihydrofolate reductase family.
In the C-terminal section; belongs to the thymidylate synthase family.
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEXES WITH NADP; METHOTREXATE AND TRIMETREXATE
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEXES WITH NADP; UMP; METHOTREXATE AND TRIMETREXATE
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH NADP; UMP AND THE SYNTHETIC INHIBITORS C-448; CYC AND Q-8
Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
IDENTIFICATION IN THE MITOCHONDRIAL DEGRADOSOME COMPLEX
3'-5'exoribonuclease which is involved in the post-transcriptional processing, editing and degradation of mitochondrial RNAs, including mRNAs, rRNAs and guided RNAs (gRNA) (PubMed:15470249, PubMed:26833087). As part of the mitochondrial 3' processome (MPsome), involved in the maturation of guided RNA (gRNA) precursors by catalyzing the processive 3'-5' degradation of uridylated gRNA precursors (PubMed:26833087). Plays a role in the degradation of 12S rRNA processing intermediates and maturation by-products (PubMed:18032430).
Component of the mitochondrial 3' processome (MPsome) complex composed at least of terminal uridylyltransferase KRET1/TUT1, 3'-5' exonuclease DSS1, MPSS1, MPSS2 and MPSS3 (PubMed:26833087). Within the complex, interacts with KRET1 and MPSS2 (PubMed:26833087). Component of the mitochondrial degradosome complex composed at least of 3'-5' exonuclease DSS1 and helicase SUV3 (PubMed:19540236). Within the complex, interacts with helicase SUV3 (PubMed:19540236).
Expressed at the procyclic stage (at protein level).
RNAi-mediated knockdown at the procyclic stage causes moderate growth defect and reduces the levels of several mitochondrial RNAs, including never edited, unedited, and edited mRNAs as well as guided RNAs (gRNA) (PubMed:15470249, PubMed:26833087). Also results in the accumulation of fragments of the flanking region upstream of the mature 5'end of 12S rRNA, the 5' flanking sequence and the truncated 12S rRNA sequence, and the 5' full-length 12S rRNAs (PubMed:18032430).
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs (By similarity). Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) (PubMed:27224426). Deacylates mischarged D.melanogaster and E.coli glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS (PubMed:28362257). Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality (By similarity).
A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Gly-cisPro motif, important for rejection of L-amino acids
Structural analysis of a probable eukaryotic D-amino acid tRNA deacylase.
Putative D-tyrosyl-tRNA(Tyr) deacylase 2
May hydrolyze D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). Could be a defense mechanism against a harmful effect of D-tyrosine (By similarity).
Belongs to the DTD family. Highly divergent.
Belongs to the protease inhibitor I11 (ecotin) family.
EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Phosphatidylethanolamine (PE) is a direct precursor of the ethanolamine-phosphoglycerol (EPG) moiety.
The Kennedy pathway is the major route for phosphatidylethanolamine (PE) synthesis, as shown by reduced levels after using RNAi against the first two enzymes of the Kennedy pathway.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
5-glutamyl glycerylphosphorylethanolamine
EF-HAND AND COILED-COIL DOMAIN-CONTAINING FAMILY MEMBER
ELONGATION FACTOR 1-BETA, PUTATIVE-RELATED
EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.
EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
Belongs to the EF-1-beta/EF-1-delta family.
Translation elongation factor EF1B, gamma chain, conserved domain
Probably plays a role in anchoring the complex to other cellular components.
EF-1 is composed of four subunits: alpha, beta, delta, and gamma.
Calmodulin-ubiquitin-associated protein CUB2.65
This protein has four EF-hand domains, two of which may be functional calcium-binding sites.
Calmodulin-ubiquitin-associated protein CUB2.8
A homologue of the T. brucel EFH5 gene in leishmania tarentolae.
This protein has four EF-hand homolog domains, two of which may be functional calcium-binding sites.
Present at similar levels in the mammalian bloodstream form and the insect procyclic form.
DNA helicase RuvA subunit, C-terminal domain
Elongation factor Ts, dimerisation domain
Elongation factor Ts (EF-Ts), dimerisation domain
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
Heat shock protein 90, C-terminal domain
Histidine kinase-like ATPase, C-terminal domain
ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Lipophosphoglycan biosynthetic protein 3
Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). Required for the synthesis of lipophosphoglycan (LPG), a cell surface glycoconjugate (PubMed:12198148). Necessary for the attachment of the galactosyl residue to the mannose within the phosphoglycan repeats of the nascent LPG chain (PubMed:12198148). Also required for addition of phosphoglycan to acid phosphatase (PubMed:12198148). Not required for normal growth (PubMed:12198148). Has ATPase activity (By similarity). Binds heparin with micromolar affinity which may facilitate infection of host cells (By similarity).
Expressed throughout the life cycle with lower expression in stationary phase promastigotes and higher levels in amastigotes.
Not induced by stress conditions such as heat, glucose deprivation or treatment with the glycosylation inhibitor tunicamycin.
Defective lipophosphoglycan synthesis and reduced levels of the surface glycoproteins gp46 and gp63.
Belongs to the heat shock protein 90 family.
In OB1; defective lipophosphoglycan (LPG) synthesis with production of a truncated LPG form lacking phosphoglycan repeats; defective addition of phosphoglycan to acid phosphatase.
Molecular cloning of the LPG3 gene from Leishmania infantum.
Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). Required for the synthesis of lipophosphoglycan (LPG), a cell surface glycoconjugate (By similarity). Necessary for the attachment of the galactosyl residue to the mannose within the phosphoglycan repeats of the nascent LPG chain (By similarity). Also required for addition of phosphoglycan to acid phosphatase (By similarity). Not required for normal growth (By similarity). Has ATPase activity (PubMed:29568220). Binds heparin with micromolar affinity which may facilitate infection of host cells (PubMed:29568220).
Prominent antigen during human and canine visceral leishmaniasis.
Eukaryotic release factor 1 from Trypanosoma brucei.
EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 1
N-terminal domain of eukaryotic peptide chain release factor subunit 1, ERF1
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
Heterodimer of two subunits, one of which binds GTP.
Belongs to the eukaryotic release factor 1 family.
Zinc/RING finger domain, C3HC4 (zinc finger)
LEUCINE-RICH REPEAT-CONTAINING PROTEIN 57
Putative adenylate cyclase regulatory protein
May interact with adenylate cyclase to regulate its activity.
May be involved in the postranscriptional regulation of genes in VSG expression sites.
Expressed only in the bloodstream form of the parasite.
Construction and Characterization of Three Bacterial Artificial Chromosome Libraries for Trypanosoma brucei.
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH ESAG7 AND HUMAN TF
Variant Surface Glycoprotein, subunit A domain 1
Variant surface glycoprotein (N-terminal domain)
Transferrin receptor subunit involved in receptor-mediated acquisition of iron from the environment by binding host TF/transferrin.
Heterodimer composed of ESAG6 and ESAG7.
Upon host TF/transferrin binding, the complex formed by ESAG6-ESAG7-TF is endocytosed and delivered to the lysosome where iron is released and host TF is degraded. ESAG6-ESAG7 are then recycled back to the flagellar pocket membrane (PubMed:7957316, PubMed:8522581). May also be secreted (PubMed:7957316).
Expressed in the bloodstream form (at protein level).
N-glycosylated (PubMed:7957316, PubMed:8522581, PubMed:18680745). Glycosylation is dispensable for heterodimer formation and host transferrin binding (PubMed:18680745).
There are about 20 variants for ESAG6. ESAG6 is one of the expression site-associated genes (ESAGs) which, together with the variable surface glycoprotein (VSG) gene, are part of polycistronic transcriptional units known as the bloodstream-form expression sites (BESs) (PubMed:12106867). The number of BES is strain-dependent and only a single BES is expressed at any given time (PubMed:12106867). This monoallelic expression is responsible for the parasite's evasion of the host immune response by antigenic variation (PubMed:12106867). This entry is encoded by the BES17 locus and can bind transferrin from human, cow, goat, horse, rat, mouse, pig and rabbit (PubMed:12106867, PubMed:31636418).
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH ESAG6 AND HUMAN TF
There are about 20 variants for ESAG7. ESAG7 is one of the expression site-associated genes (ESAGs) which, together with the variable surface glycoprotein (VSG) gene, are part of polycistronic transcriptional units known as the bloodstream-form expression sites (BESs) (PubMed:12106867). The number of BES is strain-dependent and only a single BES is expressed at any given time (PubMed:12106867). This monoallelic expression is responsible for the parasite's evasion of the host immune response by antigenic variation (PubMed:12106867). This entry is encoded by the BES17 locus and can bind transferrin from human, cow, goat, horse, rat, mouse, pig and rabbit (PubMed:12106867, PubMed:31636418).
VSG expression site-associated protein F14.9
VSG expression site-associated protein 117A
Not known but may be related to activation of the variant surface glycoprotein genes.
VSG expression site-associated protein 221A
CILIA AND FLAGELLA-ASSOCIATED PROTEIN 58-RELATED
A component of FAZ filament that is required for correct FAZ assembly and attachment. Not essential for new flagellum growth.
The flagellum attachment zone (FAZ) is a complex structure comprising a FAZ filament structure, a specialised microtubule quartet (MtQ) and the plasma membrane attachment, a specialised area of flagellum.
Assembly of a compromised FAZ and defects in flagellum attachment and cytokinesis in procyclic trypanosomes resulting in generation of 0N1K cells (zoids) and multinucleated cells, demonstrates the role of an attached flagellum in cellular morphogenesis.
37 X 14 AA tandem repeats of E-E-L-E-L-K-[VA]-A-E-N-E-K-L-A
A component of FAZ filament that is required for correct FAZ assembly and attachment. Not essential for new flagellum growth (By similarity).
41 X 14 AA tandem repeats of E-E-L-E-L-K-[VA]-A-E-N-E-K-L-A
S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).
Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. It is associated with the U3, U8 and U13 small nuclear RNAs.
By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA).
Belongs to the methyltransferase superfamily. Fibrillarin family.
Putative flagellar calcium-binding protein
May contribute to the rapid motility of the trypanosomes, playing a role either in flagellar structure or in calcium metabolism. Could alternate between a GDP-bound inactive form to a calcium/GTP-bound active form.
This protein has four EF-hand domains, three of which may be functional calcium-binding sites.
Flagellar calcium-binding protein TB-44A
This protein has 8 EF-hand domains, 6 of which may be functional calcium-binding sites.
Flagellar calcium-binding protein TB-1.7G
5' to 3' exonuclease, C-terminal subdomain
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Interacts with PCNA. Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.
Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Belongs to the 2Fe2S plant-type ferredoxin family.
Biochemical characterization of LdFr and LdIsd11 proteins and their interaction.
FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): Supporting development and validation of Infectious Disease Dx tests.
Iron-binding protein which binds 2 iron atoms per monomer (PubMed:26032732). Probably, acts as an iron carrier for the biosynthesis of Fe-S clusters (PubMed:26032732). Stimulates the cysteine desulphurase activity of IscS in the presence of IscU (PubMed:26032732).
Interacts with IscU; the interaction is direct.
Expressed in promastigotes (at protein level).
Frataxin protein levels are up-regulated in ampicillin-resistant strains.
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 10-549 IN COMPLEX WITH IRON-SULFUR AND 2-THIOMALATE INHIBITOR
Fe-S hydro-lyase, tartrate dehydratase beta-type, catalytic domain
Catalyzes the reversible hydration of fumarate to (S)-malate (PubMed:22569531, PubMed:30645090). Catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energy in the form of NADH (Probable).
Specifically and competitively inhibited by 2-thiomalate, which coordinates with the catalytic [4Fe-4S] cluster.
kcat is 28.3 sec(-1) for fumarate (in anaerobic conditions) (PubMed:22569531). kcat is 1.9 sec(-1) for fumarate (in aerobic conditions) (PubMed:22569531). kcat is 12.9 sec(-1) for (S)-malate (in anaerobic conditions) (PubMed:22569531). kcat is 0.55 sec(-1) for (S)-malate (in aerobic conditions) (PubMed:22569531).
1.3 mM for fumarate (in anaerobic conditions)
2.5 mM for fumarate (in aerobic conditions)
2.3 mM for (S)-malate (in anaerobic conditions)
1.2 mM for (S)-malate (in aerobic conditions)
26.4 umol/min/mg enzyme with fumarate as substrate (in anaerobic conditions)
1.8 umol/min/mg enzyme with fumarate as substrate (in aerobic conditions)
11.8 umol/min/mg enzyme with (S)-malate as substrate (in anaerobic conditions)
0.5 umol/min/mg enzyme with (S)-malate as substrate (in aerobic conditions)
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR; MALATE AND MALONATE
X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 28-568 IN COMPLEX WITH 2-THIOMALATE INHIBITOR
Cytosolic fumarate hydratase that catalyzes the reversible hydration of fumarate to (S)-malate.
Specifically and competitively inhibited by 2-thiomalate, which coordinates with the catalytic [4Fe-4S] cluster (PubMed:30645090). Weakly inhibited by malonate (PubMed:27528683).
kcat is 204.2 sec(-1) for fumarate (in anaerobic conditions) (PubMed:22569531). kcat is 48.6 sec(-1) for fumarate (in aerobic conditions) (PubMed:22569531). kcat is 151.4 sec(-1) for (S)-malate (in anaerobic conditions) (PubMed:22569531). kcat is 24.9 sec(-1) for (S)-malate (in aerobic conditions) (PubMed:22569531).
5.7 mM for fumarate (in anaerobic conditions)
1.9 mM for fumarate (in aerobic conditions)
12.6 mM for (S)-malate (in anaerobic conditions)
5.7 mM for (S)-malate (in aerobic conditions)
186.2 umol/min/mg enzyme with fumarate as substrate (in anaerobic conditions)
44.3 umol/min/mg enzyme with fumarate as substrate (in aerobic conditions)
138.1 umol/min/mg enzyme with (S)-malate as substrate (in anaerobic conditions)
22.7 umol/min/mg enzyme with (S)-malate as substrate (in aerobic conditions)
GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED
Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-347
Glyceraldehyde-3-phosphate dehydrogenase, glycosomal
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD AND INORGANIC PHOSPHATE
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH ADENOSINE ANALOGS
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ADENOSINE ANALOGS
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH NAD
There are two identical genes that code for glycosomal GAPDH.
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH CHALEPIN
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG
Glyceraldehyde-3-phosphate dehydrogenase
On the 2D-gel the determined pI of this protein is: 7.0, its MW is: 37.5 kDa.
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate (PubMed:29777624). May be important for growth and survival (PubMed:29777624).
Inhibited by L-proline as part of a negative feedback loop. Also inhibited by L-proline analogs 3,4-dehydro-L-proline, L-azetidine-2-carboxylic acid and L-4-thiazolidine carboxylic acid.
Homotetramer; oligomerization is not affected by L-proline feedback inhibition.
Belongs to the glutamate 5-kinase family.
Glucose-6-phosphate isomerase, glycosomal
GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED
GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A, B and C subunits.
Belongs to the GatB/GatE family. GatB subfamily.
RECEPTOR FOR ACTIVATED PROTEIN KINASE C RACK1
RECEPTOR OF ACTIVATED PROTEIN C KINASE 1
Guanine nucleotide-binding protein subunit beta-like protein
Expressed in both stages of the parasite life cycle.
Belongs to the WD repeat G protein beta family. Ribosomal protein RACK1 subfamily.
Molecular cloning and expression in E.coli of activated protein kinase C receptor of Trypanosoma brucei.
Activated protein kinase C receptor homolog
Tetrahydrobiopterin biosynthesis enzymes-like
GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity.
Toroid-shaped homodecamer, composed of two pentamers of five dimers.
Belongs to the GTP cyclohydrolase I family.
Catalyzes the phosphorylation of glycerol using ATP (PubMed:10759857, PubMed:11154065). Under anoxic conditions, when glycerol 3-phosphate accumulates in the glycosome, it catalyzes the reverse reaction, maintaining the ATP balance (PubMed:10759857, PubMed:11154065). Key enzyme for the survival of bloodstream forms under anoxic conditions (PubMed:11154065).
Optimum pH is 8.0 (PubMed:10759857). Optimum pH is 8.5 for glycerol phosphorylation and 7.0 for ATP formation (PubMed:11154065).
Increased affinity for glycerol and glycerol 3-phosphate.
CALPAIN CATALYTIC DOMAIN-CONTAINING PROTEIN
Located on fibers which connect the microtubules of the membrane skeleton with the flagellum.
INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED
Inosine monophosphate dehydrogenase (IMPDH)
Guanosine 5'-monophosphate oxidoreductase
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP (PubMed:7159467). It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides (By similarity).
Activated by GTP and inhibited by XMP and the IMP analogs allopurinol nucleotide and thiopurinol nucleotide.
Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
ligand shared between two neighboring subunits
Characterization of a novel Leishmania guanosine 5'-monophosphate reductase.
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
Activated by GTP and inhibited by ATP and IMP. Mycophenolic acid (MPA) is a competitive inhibitor of the enzyme with respect to NADPH.
kcat is 0.059 min(-1) with GMP as substrate and 0.043 min(-1) with NADPH as substrate.
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 5-147
GLUCOSAMINE 6-PHOSPHATE N-ACETYLTRANSFERASE
Involved in the biosynthesis of UDP-N-acetyl-alpha-D-glucosamine. Catalyzes the formation of N-acetyl-D-glucosamine 6-phosphate from acetyl-coenzyme A (acetyl-CoA) and D-glucosamine 6-phosphate.
144 uM for glucosamine 6-phosphate (at pH 7.2 and room temperature)
234 uM for acetyl-CoA (at pH 7.2 and room temperature)
Predominantly located in glycosome microbodies in the bloodstream form of T.brucei.
Conditional knockout mutant of the infectious bloodstream form (BSF) of T.brucei has rapid discontinuance of growth and death by cell lysis after 48 to 72 hours under nonpermissive (without tetracycline) conditions, but grow similarly to wild-type under permissive (with tetracycline) conditions. However, commonly in trypanosomatids, conditional knockout mutants become tetracycline-independent after 10 days resuming growth, indicating the essentiality of this gene and demonstrating that there are no other routes to UDP-N-acetyl-glucosamine (UDP-GlcNAc) than via formation of N-acetyl-glucosamine 6-phosphate (GlcNAc-6P). Dramatically reduced UDP-GlcNAc levels, slightly increased UDP-glucose and UDP-galactose levels, and significantly reduced poly-N-acetyllactosamine structures under nonpermissive conditions. The glycosylation profile of the principal surface coat component, the variant surface glycoprotein (VSG), is modified under nonpermissive conditions. VSG lacks the higher-molecular-mass glycoforms and the oligomannose structures from the C-terminal N-glycosylation site.
Potential novel drug target for African sleeping sickness as this protein is essential for the infectious bloodstream form of T.brucei. Therapeutic application depends on development of parasite-specific inhibitors, because this enzyme is also generally essential for eukaryotes.
Belongs to the acetyltransferase family. GNA1 subfamily.
CALMODULIN-BINDING RECEPTOR-LIKE CYTOPLASMIC KINASE 2
Metalloproteases ('zincins'), catalytic domain
Plays an integral role during the infection of macrophages in the mammalian host.
Has an integral role during the infection of macrophages in the mammalian host.
MUTAGENESIS OF TYR-254; HIS-264; GLU-265; HIS-268; ASN-300; ASN-407; ASN-534 AND ASN-577
GLYCOSYLATION AT ASN-300; ASN-407 AND ASN-534
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH ZINC
The phosphatidylinositol moiety of the GPI-anchor contains a fully saturated, unbranched 1-O-alkyl chain (mainly C24:0) and a mixture of fully saturated unbranched 2-O-acyl chains (C12:0, C14:0, C16:0, and C18:0).
No significant effect on protein expression levels or catalytic activity.
No detectable overexpression of mutant protein and hence little catalytic activity.
No significant effect on protein expression levels but almost abolishes catalytic activity.
Increases electrophoretic mobility of the protein.
Causes extracellular release of the protein.
Expressed in both the promastigote and the amastigote forms.
Genetic diversity in the Leishmania donovani complex.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES MSPCLTA1 AND MSPCLTA2)
Implicated in attachment and penetration of host cells, possibly via a neuraminidase activity.
Characterisation and expression of a G-alpha protein gene from Leishmania donovani.
Transducin (alpha subunit), insertion domain
Putative guanine nucleotide-binding protein subunit alpha
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.
In the N-terminal section; belongs to the G-alpha family.
In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family.
According to Ref.2, this sequence seems to be a hybrid that consists of parts of a G protein alpha subunit and a lysyl-tRNA synthetase.
GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC
Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD ANALOG
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NAD
Glycosylphosphatidylinositol-anchor biosynthesis protein 10
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
The protozoan parasite evades the immune response of mammalian hosts and digestion in the gut of the insect vector by means of its coat proteins tethered to the cell surface via GPI-anchors. GPI10 is essential for growth of mammalian stage bloodstream form, while procyclic form (insect stage parasites) are viable but grow slower, suggesting that inhibition of GPI synthesis may be an effective chemotherapy against African trypanosomiasis (By similarity).
Belongs to the glycosyltransferase 22 family. PIGB subfamily.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly.
The protozoan parasite evades the immune response of mammalian hosts and digestion in the gut of the insect vector by means of its coat proteins tethered to the cell surface via GPI-anchors. GPI10 is essential for growth of mammalian stage bloodstream form, while procyclic form (insect stage parasites) are viable but grow slower, suggesting that inhibition of GPI synthesis may be an effective chemotherapy against African trypanosomiasis.
UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE
N-acetylglucosamine-1-phosphate transferase
Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol.
In Leishmania sp., tunicamycin-resistant variants are associated with increased levels of NAGT gene transcription due to gene amplification.
Belongs to the glycosyltransferase 4 family.
Inhibited by cyclin kinase 2 (CDK2) inhibitors, including GW8510.
Was identified as a drug target for the treatment of African sleeping sickness. RNA interference leads to growth arrest and altered parasite morphology, demonstrating requirement for cell survival.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
endopeptidase domain like (from Nostoc punctiforme)
BIFUNCTIONAL GLUTATHIONYLSPERMIDINE SYNTHETASE/AMIDASE-RELATED
Glutathione synthetase ATP-binding domain-like
Conjugates glutathione (gamma-Glu-Cys-Gly) and spermidine to form glutathionylspermidine in the biosynthesis trypanothione (N(1),N(8)-bis(glutathionyl)spermidine), which is involved in maintaining intracellular thiol redox and in defense against oxidants.
In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.
MFS general substrate transporter like domains
Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.
FACILITATED GLUCOSE TRANSPORTER PROTEIN 1
Elongation Factor G (Translational Gtpase), domain 3
Translation factor GUF1 homolog 1, mitochondrial
Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
Translation factor GUF1 homolog 2, mitochondrial
Translation factor GUF1 homolog, mitochondrial
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
The expression of this protein depends on the parasite life cycle. It accumulates to a higher level in the extracellular promastigotes than in the intracellular amastigotes.
INTERACTION WITH THE GRBC COMPLEX; RECC COMPLEX; REMC COMPLEX AND REH2
INTERACTION WITH THE GRBC COMPLEX; RECC COMPLEX AND REMC COMPLEX
Plays an important role in mitochondrial mRNA editing by promoting the assembly of the mRNA editosome (PubMed:26769962, PubMed:31034523). Facilitates the recruitment of mRNA to the REH2C complex and promotes the interaction between various editing complexes including REH2C, GRBC, REMC and RECC complexes (PubMed:26769962, PubMed:31034523).
Component of the REH2-associated complex (REH2C) composed of helicase REH2, associated factors H2F1 and H2F2, and mRNAs at various editing stages; the formation of the complex is RNA-independent (PubMed:26769962, PubMed:31034523). Within the complex, interacts with REH2; the interaction is direct (PubMed:26769962). Interacts with various editing complexes including the RNA editing core (RECC) complex, the gRNA-binding (GRBC) complex (also known as the MRB1 complex) and the RNA editing mediator (REMC) complex (PubMed:26769962, PubMed:31034523).
RNAi-mediated knockdown at the procyclic stage causes a reduction in mitochondrial mRNA editing (PubMed:26769962). Formation of the REH2C complex is not affected but REH2C complex association with the GRBC, REMC, RECC complexes and with and pre-mRNA is impaired (PubMed:26769962). Integrity of the GRBC complex is not affected but GRBC complex association with the RECC complex and pre-mRNA is reduced (PubMed:26769962). Causes a slight decrease in REH2 protein levels (PubMed:26769962, PubMed:31034523). Does not affect the RNA unwinding activity of the REH2C complex (PubMed:26769962).
INTERACTION WITH THE GRBC COMPLEX; RECC COMPLEX; REMC COMPLEX
Fumarylacetoacetase-like, C-terminal domain
May play a role in mitochondrial mRNA editing by facilitating the association of the gRNA-binding (GRBC) complex with the RNA editing core (RECC) complex (PubMed:26769962). However, appears to be dispensable for mRNA editing per se (PubMed:26769962).
Component of the REH2-associated complex (REH2C) composed of helicase REH2, associated factors H2F1 and H2F2, and mRNAs at various editing stages; the formation of the complex is RNA-independent (PubMed:26769962). Interacts with various editing complexes including the RNA editing core (RECC) complex, the gRNA-binding (GRBC) complex (also known as the MRB1 complex) and the RNA editing mediator (REMC) complex (PubMed:26769962).
RNAi-mediated knockdown at the procyclic stage does not cause defects in RHE2 interaction with H2F1 or their association with components of the RECC and GRBC editing complexes; however, causes a slight decrease in the association of the GRBC complex with the RECC complex (PubMed:26769962). No defect in mitochondrial mRNA editing (PubMed:26769962).
Porphobilinogen deaminase, C-terminal domain
Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain
Porphobilinogen deaminase, chloroplastic
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Binds 1 dipyrromethane group covalently.
The porphobilinogen subunits are added to the dipyrromethane group.
Coproporphyrinogen III oxidase from Leishmania major.
Structural genomics of pathogenic protozoa consortium (SGPP)
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1-301
Leishmania major coproporphyrinogen III oxidase with bound ligand.
X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 1-301 IN COMPLEX WITH SUBSTRATE ANALOG
COPROPORPHYRINOGEN III OXIDASE, MITOCHONDRIAL
OXYGEN-DEPENDENT COPROPORPHYRINOGEN-III OXIDASE, MITOCHONDRIAL
Oxygen-dependent coproporphyrinogen-III oxidase
Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX (By similarity).
Belongs to the aerobic coproporphyrinogen-III oxidase family.
MUTAGENESIS OF TYR-134; TYR-137 AND ARG-142
PROTOPORPHYRINOGEN IX DEHYDROGENASE [MENAQUINONE]
PROTOPORPHYRINOGEN IX DEHYDROGENASE [QUINONE]
Protoporphyrinogen IX dehydrogenase [ubiquinone]
In E.coli extracts under anerobic conditions catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX, transferring electrons to fumarate reductase, presumably via menaquinone. In vitro under aerobic conditions forms protoporphyrin IX using ubiquinone as an electron acceptor. Complements an E.coli hemG deletion, allowing normal growth in vivo.
Leishmania is not able to completely synthesize heme; it is thought that the amastigote form localized in macrophages utilizes coproporphyrinogen from the host to produce heme via the successive action of HemF, HemG and HemH.
Greatly reduced formation of protoporphyrin IX.
Oxygen-binding protein. The oxygen-binding site contains two iron atoms (By similarity).
ZINC FINGER CCHC DOMAIN CONTAINING PROTEIN
Binds to single-stranded DNA located in the 5' hexanucleotide repeat region of the L.major leishmanolysin (GP63) gene.
High mobility group protein homolog TDP-1
Unknown. May play a role in transcription and/or DNA replication. It is not known whether this protein is DNA sequence binding-specific or not.
HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE
Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity).
Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED
ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU
ATP-dependent protease ATPase subunit HslU1
Mitochondrial proteasome-like protease HslVU ATPase subunit 1
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (By similarity). The HslVU protease complex functions in mitochondrial DNA replication by regulating DNA helicase PIF2 protein levels.
A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex (HslVU) is dependent on binding of ATP (By similarity).
Belongs to the ClpX chaperone family. HslU subfamily.
ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU2
Mitochondrial proteasome-like protease HslVU ATPase subunit 2
MUTAGENESIS OF THR-20; THR-21 AND LYS-53
Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Mitochondrial proteasome-like protease HslVU protease subunit
Protease subunit of a proteasome-like degradation complex. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins (By similarity). The HslVU protease complex functions in mitochondrial DNA replication by regulating DNA helicase PIF2 protein levels.
Belongs to the peptidase T1B family. HslV subfamily.
HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED
Heat shock protein 70kD (HSP70), C-terminal subdomain
Heat shock protein 70kD (HSP70), peptide-binding domain
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-249
Heat shock 70-related protein 1, mitochondrial
Heat shock 70 kDa protein, mitochondrial
May participate in eukaryotic mitochondrial DNA replication.
Associated with kinetoplast DNA in the mitochondrion, in the region where kdna replication occurs.
HEAT SHOCK COGNATE 70-KD PROTEIN, TANDEM DUPLICATE 2-RELATED
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Facilitative glucose transporter. Binds D-fructose and cytochalasin-B, but not D-galactose.
On the 2D-gel the determined pI of this protein is: 6.8, its MW is: 32.3 kDa.
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Characterization of a 'gamma' form of initiation factor 2 from Euglena gracilis chloroplast.
Translation initiation factor IF- 2, domain 3
TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL
TRANSLATION INITIATION FACTOR IF-2-RELATED
Translation initiation factor IF-2, chloroplastic
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity).
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
Translation initiation factor 3 (IF-3), C-terminal domain
Translation initiation factor 3 (IF-3), N-terminal domain
TRANSLATION INITIATION FACTOR IF-3, MITOCHONDRIAL
Translation initiation factor IF3, C-terminal domain
Translation initiation factor IF3, N-terminal domain
Translation initiation factor IF-3, chloroplastic
Involved in chloroplast protein synthesis. It enhances the poly(A,U,G)-dependent binding of the initiator tRNA to chloroplast 30S subunits.
Probable eukaryotic initiation factor 4A
ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G (By similarity).
Belongs to the DEAD box helicase family. eIF4A subfamily.
EUKARYOTIC TRANSLATION INITIATION FACTOR 5A
TRANSLATION INITIATION FACTOR 5A FAMILY MEMBER
Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (By similarity). Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity).
Lys-53 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain, leading to the formation of the unusual amino acid hypusine. eIF-5As are the only known proteins to undergo this modification, which is essential for their function.
Structural analysis of Leishmania mexicana eukaryotic initiation factor 5a.
Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (PubMed:26082486). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (PubMed:26082486). Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Required for cell growth during both bloodstream (BF) and insect procyclic (PF) life cycle stages and for survival of the bloodstream form (PubMed:26082486).
Localizes to the cytoplasm in the procyclic insect (PF) life cycle stage.
Lys-52 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain, leading to the formation of the unusual amino acid hypusine. eIF-5As are the only known proteins to undergo this modification, which is essential for their function. Hypusination is mediated by the consecutive action of deoxyhypusine synthase DHSc and deoxyhypusine hydroxylase DOHH (PubMed:26082486).
RNAi-mediated knockdown at the bloodstream life cycle stage causes a growth arrest followed by death. Cells become abnormally round, the number of cells with 1N1K and 2N2K genetic content is decreased whereas the number of cells with more than 2N2K genetic content is increased. RNAi-mediated knockdown at the insect procyclic life cycle stage causes a growth arrest without cell death. Cells become abnormally round and about 40 percent have lost their flagella. The number of cells with 2N1K and 2N2K genetic content is increased whereas the number of cells with 1N1K and 1N2K genetic content is reduced. The number of cells without nuclear DNA (0N1K), known as zoids, is increased. In addition, protein expression levels of formin (Tb927.5.2300) and CAP/Srv2p (Tb10.6k15.1160) are severely reduced.
EUKARYOTIC TRANSLATION INITIATION FACTOR 6
Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. May also be involved in ribosome biogenesis.
Monomer. Associates with the 60S ribosomal subunit.
Shuttles between cytoplasm and nucleus/nucleolus.
Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. May also be involved in ribosome biogenesis (By similarity).
Monomer. Associates with the 60S ribosomal subunit (By similarity).
ColocaliZes with intraflagellar transport (IFT) proteins at the basal body and in the flagellum matrix.
Belongs to the small GTPase superfamily. Rab family.
Intraflagellar transport protein 27 homolog
Small GTPase-like component of the intraflagellar transport (IFT) complex B required for both anterograde and retrograde intraflagellar transport. May be involved in cargo loading of the retrograde transport.
GDP-locked, leading to impaired flagellum assembly. Unable to enter the flagellum and to interact with other IFT-B proteins.
Intraflagellar transport protein 56 homolog
Component of the intraflagellar transport (IFT) complex required for transport of proteins in the motile cilium.
Localizes around the basal bodies and the flagellum base.
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. Potently inhibited by MPA. Inhibited by XMP and GMP.
Heterotetramer. Interacts with glycosomal protein sorting receptor PEX5.
ligand shared between two tetrameric partners
Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.
Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner (PubMed:16824097, PubMed:16246027). Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity). De novo-synthesized myo-inositol is essential for incorporation into GPI (glycosylphosphatidylinositol) glycolipids in the bloodstream form (PubMed:16246027).
0.58 mM for D-glucose 6-phosphate (at 37 degrees Celsius and pH 8.0)
Expressed in both the bloodstream form and the insect-form procyclic cells.
Inviable in the bloodstream form; viability is not restored by addition of extracellular myo-inositol (PubMed:16246027, PubMed:16824097). Levels of glycosylphosphatidylinositol (GPI) glycolipids are decreased (PubMed:16246027, PubMed:16824097).
Belongs to the myo-inositol 1-phosphate synthase family.
RdgB/HAM1 family non-canonical purine NTP pyrophosphatase
INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN
Non-canonical purine NTP pyrophosphatase 1
Non-standard purine NTP pyrophosphatase 1
Nucleoside-triphosphate pyrophosphatase 1
Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Non-canonical purine NTP pyrophosphatase 2
Non-standard purine NTP pyrophosphatase 2
Nucleoside-triphosphate pyrophosphatase 2
Non-canonical purine NTP pyrophosphatase
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND CALCIUM IONS
INOSINE-URIDINE PREFERRING NUCLEOSIDE HYDROLASE
Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, but has a preference for inosine and uridine as substrates. Is not active on thymidine and 2'-deoxynucleosides. Functions in purine salvage from the blood of the host, a fundamental pathway since protozoan parasites such as C.fasciculata are incapable of de novo purine biosynthesis.
kcat is 32 sec(-1) with inosine as substrate. kcat is 243 sec(-1) with 5-methyluridine as substrate.
50 umol/min/mg enzyme with inosine as substrate
7.6 umol/min/mg enzyme with adenosine as substrate
70 umol/min/mg enzyme with guanosine as substrate
0.03 umol/min/mg enzyme with purine riboside as substrate
380 umol/min/mg enzyme with 5-methyluridine as substrate
255 umol/min/mg enzyme with uridine as substrate
36 umol/min/mg enzyme with cytosine as substrate
Isolation and sequencing of nonspecific nucleoside hydrolase (nsnh) from Leishmania.
Catalyzes the hydrolysis of the N-glycosidic bond of all of the commonly occurring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substrates. Likely functions in purine salvage from the host, a fundamental pathway since protozoan parasites such as L.major are incapable of de novo purine biosynthesis.
Is potently inhibited by immucillin A and immucillin ACAP, which are transition state inhibitors.
kcat is 119 sec(-1) with inosine as substrate. kcat is 32 sec(-1) with uridine as substrate. kcat is 0.6 sec(-1) with guanosine as substrate. kcat is 0.6 sec(-1) with adenosine as substrate. kcat is 0.4 sec(-1) with cytidine as substrate.
Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Also specifically binds to base J-containing DNA (J-DNA). Involved in propagation and maintenance of DNA base J synthesis initiated by JBP2 by specifically binding already synthesized DNA base J and propagating J synthesis. Thymine dioxygenase activity and J-DNA-binding are independent functions (By similarity).
Monomer. Binds to DNA as a monomer (By similarity).
The DNA-binding JBP1 domain (DB-JBP1) is necessary and sufficient for binding to J-DNA.
Belongs to the TET family. JBP1 subfamily.
Involved in J base recognition, conferring specificity towards J-DNA
MUTAGENESIS OF HIS-189; ASP-191; HIS-239; ARG-255 AND VAL-259
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 392-561
Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Also specifically binds to base J-containing DNA (J-DNA). Involved in propagation and maintenance of DNA base J synthesis initiated by JBP2 by specifically binding already synthesized DNA base J and propagating J synthesis. Thymine dioxygenase activity and J-DNA-binding are independent functions.
Localizes to discrete spots in the nucleus, probably the J-rich telomeres.
Involved in J base recognition and binding, conferring specificity towards J-DNA
Decreases binding affinity for both J-DNA and normal DNA.
Slightly decreases binding affinity for both J-DNA and normal DNA.
Expressed in bloodstream form and significantly less in procyclic form.
Does not affect growth, gene expression or the stability of some repetitive DNA sequences. The genome contains only about 5% of the wild-type level of J in their DNA. Cells lacking both JBP1 and JBP2 show a complete absence of base J.
DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED
Bifunctional helicase and thymine dioxygenase JBP2
Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Probably also acts as a DNA helicase. Recognizes and binds specific regions of the genome, hydrolyzes ATP and allows the DNA base J de novo synthesis. Involved in initial synthesis of DNA base J, JBP1 being able to act via the basal level of DNA base J and propagate further synthesis. In contrast to JBP1, it does not specifically bind DNA base J, however it binds chromatin (By similarity).
In the C-terminal section; belongs to the SNF2/RAD54 helicase family.
In the N-terminal section; belongs to the TET family. JBP2 subfamily.
catalytic; for thymine dioxygenase activity
MUTAGENESIS OF HIS-415; ASP-417; HIS-465; ARG-479; VAL-483 AND LEU-548
Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Probably also acts as a DNA helicase. Recognizes and binds specific regions of the genome, hydrolyzes ATP and allows the DNA base J de novo synthesis. Involved in initial synthesis of DNA base J, JBP1 being able to act via the basal level of DNA base J and propagate further synthesis. In contrast to JBP1, it does not specifically bind DNA base J, however it binds chromatin.
Does not lead to death. The genome contains reduced level of DNA base J in the DNA.
MUTAGENESIS OF LYS-550 AND 657-ASP-GLU-658
MUTAGENESIS OF HIS-391; ASP-393; HIS-441; ARG-455 AND VAL-459
The genome contains reduced level of DNA base J in the DNA. Cells lacking both JBP1 and JBP2 show a complete absence of base J.
Induces a slight reduction in DNA base J biosynthesis.
Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Histone H1-like DNA-binding protein involved in the organization and segregation of kinetoplast DNA (kDNA). The mitochondrial DNA of kinetoplastid protozoa consists of about 5,000 minicircles and 20 to 30 maxicircles. These circular DNAs are held together by catenation into a highly organized compact disk structure referred to as a kinetoplast DNA (kDNA) network. Binds preferentially to a specific fragment of minicircle DNA and is able to compact kDNA networks through DNA charge neutralization and condensation (By similarity).
Associates with the kinetoplast DNA network.
Present at a constant level throughout the cell cycle.
DNA-ASSOCIATED PROTEIN, PUTATIVE-RELATED
Histone H1-like DNA-binding protein involved in the organization and segregation of kinetoplast DNA (kDNA). The mitochondrial DNA of kinetoplastid protozoa consists of about 5,000 minicircles and 20 to 30 maxicircles. These circular DNAs are held together by catenation into a highly organized compact disk structure referred to as a kinetoplast DNA (kDNA) network. Binds preferentially to a specific fragment of minicircle DNA and is able to compact kDNA networks through DNA charge neutralization and condensation.
Expression varies periodically during the cell cycle in the same manner as transcripts of several kinetoplast and nuclear DNA replication genes.
Present both within the kDNA disk and in the mitochondrial matrix at opposite edges of the kDNA disk.
ATP:guanido phosphotransferase, N-terminal domain
Glutamine synthetase/guanido kinase, catalytic domain
Belongs to the ATP:guanido phosphotransferase family.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.
May be involved in the regulation of the cytoskeleton through interaction with the subpellicular microtubules. May be involved in parasite mobility and attachment to the surface of the host cell. Behaves as a strong immunogen during infection.
Associated with microtubules. Associated with the flagellum and flagellar pocket.
Expressed abundantly in logarithmic phase promastigotes, and to a lesser extent in stationary phase promastigotes and amastigotes.
May be involved in the regulation of the cytoskeleton through interaction with the subpellicular microtubules. May be involved in parasite mobility and attachment to the surface of the host cell. Strongly stimulates T-cell proliferation and is thought to play a role in the immunology of leishmaniasis.
Present in both promastigotes and amastigotes.
A minor in vivo processed fragment (IVP) also exists, probably as a result of proteolysis.
Probably O-glycosylated. Contains equimolar amounts of galactosamine, galactose, glucose and mannose.
May be involved in the regulation of the cytoskeleton through interaction with the subpellicular microtubules. May be involved in parasite mobility and attachment to the surface of the host cell. Behaves as a strong immunogen during infection (By similarity).
There are four copies of the KMP-11 gene in T.b.brucei.
Abundantly expressed in amastigotes and trypomastigotes. In epimastigotes, KMP-11 is expressed at a high level during the logarithmic growth phase but is down-regulated during the stationary phase of growth.
There are four copies of the KMP-11 gene in T.cruzi.
Activated by fructose 2,6-bisphosphate, activated by the effector in a cooperative manner.
SEQUENCE REVISION TO SER-383; TYR-390; ARG-405 AND SER-406
Activated by fructose 2,6-bisphosphate, activated by the effector in a non cooperative manner.
Light-harvesting complex I LH35 proteins
The LH35 protein is synthesized as a 100 kDa polyprotein and is entirely imported into the chloroplast where it is subsequently cleaved into 5 mature 20 kDa LH35 proteins.
Light-harvesting complex I LH38 proteins
The LH38 protein is synthesized as a 100 kDa polyprotein and is entirely imported into the chloroplast where it is subsequently cleaved into 5 mature 20 kDa LH38 proteins.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Expressed in all life-cycle stages but at higher levels in the amastigote stage in the mammal and in stationary phase promastigote cultures which contain the infective metacyclic form of the parasite.
Glycosyltransferase that may be responsible for the addition of galactofuranosyl residues to the nascent lipophosphoglycan (LPG) chain. It could alternatively be involved in the synthesis of the galactofuranosyl donor.
Expressed throughout the life cycle with a two-fold decrease in amastigotes (LPG is 1000-fold less abundant in amastigotes than in promastigotes).
Belongs to the glycosyltransferase 2 family.
Helical; Signal-anchor for type II membrane protein
LEUCINE-RICH REPEAT-CONTAINING PROTEIN 56
Leucine-rich repeat-containing protein 56 homolog
Required for the assembly of dynein arms in the distal portion of flagellum axoneme.
Localizes to the distal portion of the flagellum.
Gene knockout results in significant reduction of flagellar beating and cell swimming, and absence of outer dynein arms in the distal region of flagellum axoneme. Cell motility is characterized by an erratic swimming pattern with altered propagation of the tip-to-base wave, increased frequency of base-to-tip waves, and frequent tumbling typical of outer dynein arm mutants.
Reduced cell motility and reduced number of outer dynein arms. Localizes normally to the distal portion of the flagellum.
IDENTIFICATION IN A COMPLEX WITH PBP1; XAC1 AND MKT1 OR MKT1L
Involved in post-transcriptional regulation of gene expression.
Forms a complex composed of at least MKT1, PBP1, XAC1 and LSM12 (PubMed:24470144). Forms a complex composed of at least MKT1L, PBP1, XAC1 and LSM12 (PubMed:32532821). Within the complex, interacts with PBP1; the interaction is direct (PubMed:24470144, PubMed:32532821).
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115
Membrane antigen containing repeating peptides
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44
GROUP II INTRON-ASSOCIATED OPEN READING FRAME
NUCLEAR INTRON MATURASE 1, MITOCHONDRIAL-RELATED
Could be required for group III intron excision.
NUCLEAR INTRON MATURASE 4, MITOCHONDRIAL
MUTAGENESIS OF LYS-55; CYS-212; CYS-213 AND LYS-268
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF MUTANTS GLY-213 AND ALA-213
MUTAGENESIS OF TYR-31; CYS-92; ASP-95; SER-156; 189-ASP--ASP-190 AND ASP-211
Cysteine protease that cleaves specifically after arginine or lysine residues.
Activated by Ca(2+) (PubMed:18005666, PubMed:23506317, PubMed:28089596, PubMed:22529389). In response to calcium binding, the 280-loop, a disordered loop consisting of residues 269-275, undergoes a conformational change which stabilizes substrates in the active site (PubMed:22529389). The binding to the substrate triggers the release of the N-terminal region resulting in the activation of the enzyme (PubMed:22529389). Proteolytic cleavage is required for catalytic activity towards large protein substrates (PubMed:28089596).
Optimum temperature is 20-25 degrees Celsius.
There are 2 calcium binding sites with high and low affinity, respectively.
Auto-proteolytic cleavage of the propeptide after Lys-55 and between the large and small subunits after Lys-268 is required for catalytic activity towards large protein substrates but is dispensable towards small oligopeptide substrates (PubMed:18005666, PubMed:28089596, PubMed:22529389). After processing, the propeptide and the large and small subunits remain associated by non-covalent bonds (PubMed:18005666). In vivo, the unprocessed enzyme appears to be the predominant form (By similarity).
Regulates substrate access to the active site
Important for Arg/Lys-specific substrate specificity
Increases autoprocessing resulting in the degradation of the enzyme.
Loss of autoprocessing. Loss of catalytic activity towards large protein substrates, no effect on catalytic activity towards short oligopeptide substrates, reduces affinity of the high affinity Ca(2+) binding site, shifts optimum pH for activity towards basic pH; when associated with G-268.
Reduced autoprocessing and 50% loss of catalytic activity towards substrates.
Loss of autoprocessing and catalytic activity towards substrates.
3-fold increase in catalytic activity towards substrates.
Loss of autoprocessing. Loss of catalytic activity towards large protein substrates, no effect on catalytic activity towards short oligopeptide substrates, reduces affinity of the high affinity Ca(2+) binding site, shift optimum pH for activity towards basic pH; when associated with G-55.
Activated by Ca(2+). In response to calcium binding, the 280-loop, the 280-loop, a disordered loop consisting of residues 269-275, undergoes a conformational change which stabilizes substrates in the active site. The binding to the substrate triggers the release of the N-terminal region resulting in the activation of the enzyme. Proteolytic cleavage is required for catalytic activity towards large protein substrates.
Specifically expressed in the mammalian blood stage form (at protein level).
Auto-proteolytic cleavage of the propeptide after Lys-55 and between the large and small subunits after Lys-268 is required for catalytic activity towards large protein substrates but is dispensable towards small oligopeptide substrates. After processing, the propeptide and the large and small subunits remain associated by non-covalent bonds (By similarity). In vivo, the unprocessed enzyme appears to be the predominant form (PubMed:16507595).
RNAi-mediated knockdown causes no defect in the growth of the bloodstream stage form (PubMed:16507595). Simultaneous RNAi-mediated knockdown of MCA2, MCA3 and MCA5 in the bloodstream stage form causes a growth arrest resulting from a block prior to cytokinesis; DNA replication and mitosis are normal (PubMed:16507595). Has no effect on VSG protein recycling (PubMed:16507595). Triple knockout of MCA2, MCA3 and MCA5 in the bloodstream form causes an initial slower growth rate in vitro which reaches wild-type levels after several weeks of culture (PubMed:16507595). Triple knockouts have a normal growth rate and virulence in infected mice (PubMed:16507595).
Unlike in strain 927/4 GUTat10.1, there is a Glu instead of a Lys residue at position 55. Lys-55 is predicted to be conserved between strains as the enzyme undergoes auto-processing at this site. It is not clear if the presence of a Glu residue is due to a sequencing error.
Cysteine protease that cleaves specifically after arginine or lysine residues (PubMed:21949125). In the bloodstream form, may cleave inactive metacaspase-4 MCA4 prior to MCA4 secretion (PubMed:21949125).
Cysteine protease that cleaves specifically after arginine or lysine residues (PubMed:22402587). In epimastigotes, may play a role in cell cycle G1/S transition (PubMed:22402587).
Localizes to cytoplasm in epimastigotes (PubMed:16213036). Translocates to the nucleus following apoptosis induced by human serum (PubMed:16213036).
Expressed in epimastigotes, amastigotes and cell derived trypomastigotes and in metacyclic trypomastigotes (at protein level).
In epimastigotes, the unprocessed enzyme appears to be the main form (PubMed:22402587). Auto-processing is dispensable for catalytic activity towards small oligopeptide substrates (PubMed:22402587).
Inactive metacaspase which plays a role in parasite bloodstream form growth and in parasite virulence within the mammalian host.
Secreted by the parasite bloodstream form (PubMed:21949125). Membrane localization is required for MCA4 processing but is dispensable for MCA4 secretion, and parasite growth and virulence in the mammalian host (PubMed:21949125).
Specifically expressed in the bloodstream form (at protein level).
Proteolytic cleavage by MCA3 occurs prior or during secretion and requires MCA4 membrane localization (PubMed:21949125). Cleavage is dispensable for secretion and parasite growth and virulence in the mammalian host (PubMed:21949125). In vitro, can be cleaved by MCA2 but specifically cleaved by MCA3 in vivo (PubMed:21949125).
Knockouts in the bloodstream form have an initial slower growth rate in vitro which reaches wild-type levels after several weeks of culture (PubMed:21949125). Knockouts in the bloodstream form have a reduced growth rate and virulence in infected mice (PubMed:21949125). RNAi-mediated knockdown at the bloodstream stage results in a more severe phenotype characterized by a growth arrest due to a failure to undergo cytokinesis (PubMed:21949125).
In contrast to other metacaspases (MCA) of the peptidase C14B family, contains a serine residue at the position of the canonical catalytic cysteine and has been shown to lack protease activity.
Loss of flagellum membrane localization. No defect in MCA4 secretion, however processing of the secreted form is impaired. No defect in growth rate and virulence in infected mice.
Restores calcium-dependent auto-processing activity and catalytic activity towards substrates.
Clan CD cysteine peptidases of parasitic protoza.
Localizes to RAB11-positive recycling endosomes.
Expressed in the mammalian blood stage form and insect procyclic form (at protein level).
RNAi-mediated knockdown causes no defect in the growth of the bloodstream stage form (PubMed:16507595). Knockout has no defect in the growth of the procyclic form (PubMed:16507595). Simultaneous RNAi-mediated knockdown of MCA2, MCA3 and MCA5 in the bloodstream stage form causes a growth arrest resulting from a block prior to cytokinesis; DNA replication and mitosis are normal (PubMed:16507595). Has no effect on VSG protein recycling (PubMed:16507595). Triple knockout of MCA2, MCA3 and MCA5 in the bloodstream form causes an initial slower growth rate in vitro which reaches wild-type levels after several weeks of culture (PubMed:16507595). Triple knockouts have a normal growth rate and virulence in infected mice (PubMed:16507595).
Cysteine protease that cleaves specifically after arginine or lysine residues (PubMed:22402587). May play a role in apoptosis (PubMed:22402587).
Specifically expressed in epimastigotes (at protein level).
ABC transporter type 1, transmembrane domain
MYCOBACTIN IMPORT ATP-BINDING/PERMEASE PROTEIN IRTB
Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Confers vinblastine resistance.
Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
the atp-binding cassette (abc) superfamily
In this organism, this protein is encoded by a gene, located in 'H circle', a 68 kb duplex DNA circle containing a 30 kb inverted repeat. Acquired resistance to methotrexate in the organism is associated with the amplification of h circles with increasing level of LTPGPA gene transcription.
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
Highly expressed in the insect stage (Promastigote).
FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA
Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.
Strongly inhibited by FK506 and L-685,818.
MUTAGENESIS OF LYS-102 AND 2-PRO--VAL-64
DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1
Putative mitogen-activated protein kinase kinase 4
Protein kinase which regulates promastigote proliferation in host macrophages, thereby playing an essential role in parasite virulence.
Can use both Mg(2+) and Mn(2+) in vitro and shows higher activity with Mn(2+) but Mg(2+) is likely to be the in vivo cofactor.
Active between 21 and 40 degrees Celsius.
Expressed at promastigote stage but not in lesion-derived amastigotes (at protein level). Expressed during the differentiation of promastigotes to amastigotes in vitro.
Homozygous deletion mutants grow slightly slower, but have no significant morphological abnormalities. In BALB/c mice, has reduced infectivity, which is characterized by a delayed and decelerated development of footpad lesions.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.
No loss of catalytic activity. In BALB/c mice, has reduced infectivity which is characterized by a delayed and decelerated development of footpad lesions. Complete loss of catalytic activity; when associated with R-102.
Severe loss of catalytic activity. In BALB/c mice, has reduced infectivity which is characterized by a delayed and decelerated development of footpad lesions. Complete loss of catalytic activity; when associated with 2-P--V-64 DEL.
DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 5-RELATED
DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE DSOR1
Mitogen-activated protein kinase kinase 5
Protein kinase which phosphorylates and activates MPK4 in vitro.
Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely to be the in vivo cofactor.
IDENTIFICATION IN A COMPLEX WITH PBP1; LSM12 AND XAC1
Forms a complex composed of at least MKT1L, PBP1, XAC1 and LSM12.
Expressed in the procyclic and bloodstream forms (at protein level).
RNAi-mediated knockdown in both the procyclic and the bloodstream form is lethal.
Belongs to the XPG/RAD2 endonuclease family.
Although it belongs to the XPG/RAD2 endonuclease family, only one of the seven Asp residues involved in Mg(2+) binding is conserved suggesting that it has no nuclease activity.
INTERACTION WITH ZC3H11; CFB1; CFB2; PBP1 AND EIF4G5
Involved in post-transcriptional regulation of gene expression (PubMed:24470144). Promotes mRNA stabilization by recruiting a complex containing PBP1, LSM12 and XAC1 to mRNAs (PubMed:24470144, PubMed:32532821). Recruited to mRNAs by sequence-specific RNA binding proteins (PubMed:24470144). May regulate translation through interactions with the EIF4E6-EIF4G5 translation initiation complex (PubMed:32532821).
Forms a complex composed of at least MKT1, PBP1, XAC1 and LSM12 (PubMed:32532821). Within the complex, interacts (via C-terminus) with PBP1; the interaction is direct (PubMed:32532821, PubMed:24470144). Interacts with RNA-binding protein ZC3H11 (via MKT1-binding motif); the interaction is direct (PubMed:32532821, PubMed:24470144). May interact with RNA-binding proteins CFB1 and CFB2 (PubMed:32532821). Interacts with the EIF4E6-EIF4G5 translation initiation complex via EIF4G5; the interaction with EIF4G5 is direct (PubMed:32532821).
Localizes to polysomes (PubMed:24470144). Partially localizes to starvation-induced stress granules but not to heat shock-induced stress granules (PubMed:24470144).
RNAI-mediated knockdown in the bloodstream form is lethal (PubMed:24470144). RNAi-mediated knockdown in the procyclic form has no effect on viability (PubMed:24470144).
Although it belongs to the XPG/RAD2 endonuclease family, only two of the seven Asp residues involved in Mg(2+) binding are conserved suggesting that it has no nuclease activity.
PHOSPHORYLATION AT SER-186; SER-187; THR-190 AND TYR-192
Essential for the two main proliferating life stages, the promastigotes and amastigotes, of the parasite.
Expressed in promastigotes and to a lower extent in axenic amastigotes (at protein level) (PubMed:14636673, PubMed:16384531). Low expression levels in lesion-derived amastigotes (at protein level) (PubMed:14636673, PubMed:16384531).
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Dually phosphorylated on Thr-190 and Tyr-192, which activates the enzyme.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
As part of the mitochondrial 3' processome (MPsome), involved in the maturation of guided RNA (gRNA) precursors.
Component of the mitochondrial 3' processome (MPsome) complex composed at least of terminal uridylyltransferase KRET1/TUT1, 3'-5' exonuclease DSS1, MPSS1, MPSS2 and MPSS3 (PubMed:26833087). Within the complex, interacts with KRET1 (PubMed:26833087).
RNAi-mediated knockdown at the procyclic stage causes moderate growth defect and reduces production of guided RNAs (gRNA) due to a block in the processing of gRNA precursors.
Component of the mitochondrial 3' processome (MPsome) complex composed at least of terminal uridylyltransferase KRET1/TUT1, 3'-5' exonuclease DSS1, MPSS1, MPSS2 and MPSS3 (PubMed:26833087). Within the complex, interacts with DSS1 (PubMed:26833087).
RNAi-mediated knockdown at the procyclic stage causes moderate growth defect without affecting the production of guided RNAs (gRNA).
translation initiation factor eif-2b, domain 1
Methylthioribose-1-phosphate isomerase 1
S-methyl-5-thioribose-1-phosphate isomerase 1
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein 1
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Methylthioribose-1-phosphate isomerase 2
S-methyl-5-thioribose-1-phosphate isomerase 2
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein 2
S-methyl-5-thioribose-1-phosphate isomerase
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein
Class II aldolase/adducin N-terminal domain
METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE
Probable methylthioribulose-1-phosphate dehydratase
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Belongs to the aldolase class II family. MtnB subfamily.
1,2-DIHYDROXY-3-KETO-5-METHYLTHIOPENTENE DIOXYGENASE
Acireductone dioxygenase (Fe(2+)-requiring)
Acireductone dioxygenase (Ni(2+)-requiring)
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
Belongs to the acireductone dioxygenase (ARD) family.
for iron-dependent acireductone dioxygenase activity
for nickel-dependent acireductone dioxygenase activity
CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 1
S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1).
MUTAGENESIS OF LYS-95; ASP-207; LYS-248 AND GLU-285
S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of spliced leader and U1 small nuclear RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped RNA to produce m(7)GpppNmp (cap1). Cap1 modification is linked to higher levels of translation. Recognizes a guanosine cap on RNA independent of its N(7) methylation status.
Component of a complex composed of CBF5, GAR1, NHP2, MTR1, NOP10 and Tb11.01.8210.
Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport (By similarity).
The vault ribonucleoprotein particle is a huge (400 A x 670 A) cage structure of 12.9 MDa. It consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains, PARP4 and one or more vault RNAs (vRNAs) (By similarity).
NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL
Formate dehydrogenase/DMSO reductase, domains 1-3
NADH-ubiquinone oxidoreductase 75 kDa subunit
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized (By similarity).
Complex I is composed of about 30 different subunits.
Matrix and cytoplasmic side of the mitochondrial inner membrane.
Belongs to the complex I 75 kDa subunit family.
NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL
NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Component of the iron-sulfur (IP) fragment of the enzyme. Component of the iron-sulfur (IP) fragment of the enzyme.
Belongs to the complex I 49 kDa subunit family.
COMPLEX1_49KDA DOMAIN-CONTAINING PROTEIN
NADH-ubiquinone oxidoreductase 49 kDa subunit homolog
NADH:ubiquinone oxidoreductase, 30kDa subunit
NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 3, MITOCHONDRIAL
NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 3
NADH-ubiquinone oxidoreductase subunit 9
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Belongs to the complex I 30 kDa subunit family.
NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL
NADH-ubiquinone oxidoreductase 20 kDa subunit
Belongs to the complex I 20 kDa subunit family.
Complex I is composed of 45 different subunits This is a component of the iron-sulfur (IP) fragment of the enzyme.
NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8, MITOCHONDRIAL
NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL
NADH-ubiquinone oxidoreductase subunit 8
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). May donate electrons to ubiquinone.
Belongs to the complex I 23 kDa subunit family.
Fully edited transcripts more abundant in the bloodstream form of T.brucei than in the procyclic forms.
GLYCOSYLATION AT ASN-4; ASN-7; SER-9 AND SER-11
This peptide displays a high degree of glycan microheterogeneity resulting mainly from a variable number of mannose residues in each glycan. Both N-linked and O-linked glycans are high mannose.
The measured mass is that of a major glycosylated and GPI-anchored form.
The measured mass is that of the peptide after removal by PNGase F of all glycans and the GPI anchor.
N-linked (GlcNAc...) (high mannose) asparagine
On the 2D-gel the determined pI of this protein is: 7.1, its MW is: 46.4 kDa.
On the 2D-gel the determined pI of this unknown protein is: 6.7, its MW is: 30.0 kDa.
On the 2D-gel the determined pI of this unknown protein is: 6.7, its MW is: 34.5 kDa.
On the 2D-gel the determined pI of this unknown protein is: 6.7, its MW is: 23.0 kDa.
On the 2D-gel the determined pI of this unknown protein is: 6.5, its MW is: 30.8 kDa.
On the 2D-gel the determined pI of this protein is: 6.5, its MW is: 24.1 kDa.
On the 2D-gel the determined pI of this unknown protein is: 6.9, its MW is: 19.8 kDa.
On the 2D-gel the determined pI of this protein is: 7.2, its MW is: 92.4 kDa.
On the 2D-gel the determined pI of this unknown protein is: 6.7, its MW is: 28.3 kDa.
SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE
May be required but is not sufficient for increased virulence.
On the 2D-gel the determined pI of this unknown protein is: 6.5, its MW is: 33.2 kDa.
On the 2D-gel the determined pI of this unknown protein is: 5.1, its MW is: 20.9 kDa.
On the 2D-gel the determined pI of this unknown protein is: 5.9, its MW is: 47.0 kDa.
On the 2D-gel the determined MW of this unknown protein is: 25.0 kDa.
On the 2D-gel the determined pI of this unknown protein is: 6.0, its MW is: 33.0 kDa.
ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE
ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER
Bifunctional NAD(P)H-hydrate repair enzyme
ADP-dependent (S)-NAD(P)H-hydrate dehydratase
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity).
In the N-terminal section; belongs to the NnrE/AIBP family.
In the C-terminal section; belongs to the NnrD/CARKD family.
Involved in the biogenesis of the 60S ribosomal subunit.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.
Cloning and characterization of the gene encoding the putative Nop10 protein in Trypanosoma cruzi.
H/ACA ribonucleoprotein complex, subunit Nop10
H/ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT 3
H/ACA ribonucleoprotein complex subunit 3-like protein
Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (By similarity).
Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs).
Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Putative serine/threonine-protein kinase A
Putative serine/threonine-protein kinase B
Probable flavin mononucleotide-dependent alkene reductase
Flavin mononucleotide-dependent nitroreductase
May function as a flavin mononucleotide (FMN)-dependent alkene reductase on substrates carrying alpha,beta-unsaturated carbonyl groups (ketones, aldehydes, carboxylic acids, esters, lactones or cyclic imides). The catalysis depends on NAD(P)H, which acts as hydride donor for the reduction. Seems to be involved in metabolic pathways required for efficient replication of amastigotes within macrophages.
Acts as a FMN-dependent nitroreductase that activates anti-leishmanial bicyclic nitroaromatic prodrugs including delamanid, DNDI-VL-2098 and (R)-PA-824, forming toxic products that kill the parasites.
Detected in all developmental stages: log phase promastigotes, metacyclic promastigotes and axenic amastigotes.
Knockout parasites show reduced replication within macrophages, but are resistant to bicyclic nitro-drugs including delamanid and DNDI-VL-2098. Sensitivity to bicyclic nitro-drugs is fully restored on expression of this reductase.
Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.
Belongs to the complex I subunit 1 family.
NADH:ubiquinone/plastoquinone oxidoreductase, chain 3
Belongs to the complex I subunit 3 family.
Belongs to the complex I subunit 5 family.
Made of tandem repeats of a 38 amino acid segment.
Photoactivated adenylate cyclase subunit alpha-like protein 1224-5/1F
Heterotetramer of two alpha and two beta subunits.
Paraxonemal body. And paraxonemal bodies (PABs).
The 1224-5/1F strain is deficient in phototaxis. It is not known if this is due to defective adenylate cyclase activity or defective BLUF domains in this protein.
Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2
SOLUBLE GUANYLATE CYCLASE GCY-32-RELATED
Photoactivated adenylate cyclase subunit alpha-like protein FB
The FB strain is deficient in phototaxis. It is not known if this is due to defective adenylate cyclase activity or defective BLUF domains in this protein. In wild-type E.gracilis, photoactivated adenylate cyclase is found in the paraxonemal bodies (PABs). PABs are not visible in all cells in this strain, and are smaller than in wild-type.
Photoactivated adenylate cyclase subunit alpha-like protein ST-
The ST- strain is deficient in phototaxis. It is not known if this is due to defective adenylate cyclase activity or defective BLUF domains in this protein. In wild-type E.gracilis, photoactivated adenylate cyclase is found in the paraxonemal bodies (PABs). PABs are absent from this strain.
Procyclic form-specific polypeptide B1-alpha
Major surface antigen of procyclic forms.
Expressed only at a certain stage during differentiation in the insect vector.
31 X 2 approximate tandem repeats of E-P
Procyclic form-specific polypeptide A-alpha
Procyclic form-specific polypeptide A-beta
Procyclic form-specific polypeptide B-alpha
Photoactivated adenylate cyclase subunit beta-like protein 1224-5/1F
Photoactivated adenylate cyclase subunit beta-like protein 1224-5/9F
The 1224-5/9F strain is deficient in phototaxis. It is not known if this is due to defective adenylate cyclase activity or defective BLUF domains in this protein.
Photoactivated adenylate cyclase subunit beta-like protein FB
Photoactivated adenylate cyclase subunit beta-like protein ST-
IDENTIFICATION IN A COMPLEX WITH LSM12; XAC1 AND MKT1 OR MKT1L
Involved in post-transcriptional regulation of gene expression (PubMed:24470144). Promotes mRNA stabilization by bridging poly(A)-binding protein to mRNAs (PubMed:24470144).
Forms a complex composed of at least MKT1, PBP1, XAC1 and LSM12 (PubMed:32532821). Forms a complex composed of at least MKT1L, PBP1, XAC1 and LSM12 (PubMed:32532821). Within the complex, interacts with MKT1 (via C-terminus); the interaction is direct (PubMed:24470144, PubMed:32532821). Interacts (via C-terminus) with ZC3H11; the interaction is direct (PubMed:24470144).
Localizes to polysomes (PubMed:24470144). Localizes to starvation-induced stress granules but not heat shock-induced stress granules (PubMed:24470144).
Phosphoenolpyruvate Carboxykinase, domain 1
Phosphoenolpyruvate Carboxykinase, domain 2
Phosphoenolpyruvate carboxykinase (ATP), glycosomal
P60 has the capability to bind to microtubules and membrane vesicles in vitro.
Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.
Photoactivated adenylate cyclase subunit alpha
Photoactivated adenylyl cyclase subunit alpha
Acts as a blue light photoreceptor for the step-up photophobic response. Mediates photoavoidance.
Activity increased by up to 80-fold under blue light.
Paraflagellar body, flagellum and paraxonemal bodies (PABs).
The 1224-5/9F strain is deficient in phototaxis. It is not known if this is due to defective adenylate cyclase activity or defective BLUF domains in the beta subunit of this protein.
Acts as a photoreceptor for the step-up photophobic response.
Photoactivated adenylate cyclase subunit beta
Photoactivated adenylyl cyclase subunit beta
Cytochrome b6-f complex subunit 4, chloroplastic
The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).
Belongs to the cytochrome b family. PetD subfamily.
PetG subunit of the cytochrome b6f complex
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' sub-subfamily.
Important for substrate specificity; cannot use PPi as phosphoryl donor
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 481-487
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ATP
PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE
PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 2
6-phosphofructokinase, pyrophosphate dependent
Pyrophosphate-dependent 6-phosphofructose-1-kinase
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Activated by AMP. Probably promotes oligomerization of the enzyme.
Optimum pH is 6 for the forward reaction and 7.5 for the reverse reaction.
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily.
Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP
Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
69 KDA PARAFLAGELLAR ROD PROTEIN-RELATED
Major component of the paraflagellar rod (PFR). The PFR is a highly ordered lattices of fibrous proteins that are located inside the flagellum and assume a fixed orientation with respect to the microtubular axoneme.
Heterodimer of a 69 kDa and a 73 kDa protein.
Coded by two tandemly repeated genes with identical ORF: PFRA and PFRB.
Coded by two tandemly repeated genes with almost identical ORF: PFRC and PFRD.
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH COBALT
BPG-independent phosphoglycerate mutase, domain B
2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE
2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain
Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA).
Binds 2 manganese ions per subunit (Probable). May also use Mg(2+) and Zn(2+) (Probable).
0.15 mM for 3-phosphoglycerate (at pH 7.4 and 25 degrees Celsius)
0.1 mM for 3-phosphoglycerate (at pH 7.4, 30 degrees Celsius and in the presence of Co(2+))
0.05 mM for 3-phosphoglycerate (at pH 7.4, 30 degrees Celsius and in the presence of Mn(2+))
0.148 mM for 3-phosphoglycerate (at pH 7.4, 37 degrees Celsius and in the presence of Mn(2+) and Co(2+))
0.16 mM for 2-phosphoglycerate (at pH 7.4 and 25 degrees Celsius)
Expressed in the procyclic and bloodstream stages (at protein level).
RNAi-mediated knockdown causes a severe reduction in phosphoglycerate mutase activity and reduces the growth of the procyclic form of the parasite.
Belongs to the BPG-independent phosphoglycerate mutase family.
X-ray crystal structure of apo prostaglandin F synthase from Leishmania major Friedlin.
Seattle structural genomics center for infectious disease (SSGCID)
9,11-endoperoxide prostaglandin H2 reductase
Catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. Has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
270 nmol/min/mg enzyme toward prostaglandin H2
4780 nmol/min/mg enzyme toward 9,10-phenanthrenequinone
7280 nmol/min/mg enzyme toward p-nitrobenzaldehyde
P110/11E abundance is markedly elevated in promastigotes relative to amastigotes.
Belongs to the aldo/keto reductase family.
The crystal structure of prostaglandin F synthase from Trypanosoma brucei.
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NADP
Nicotinamide adenine dinucleotide phosphate
Catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. Has also aldo/ketoreductase activity towards the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
2 umol/min/mg enzyme toward prostaglandin H2
22 umol/min/mg enzyme toward p-nitrobenzaldehyde
48 umol/min/mg enzyme toward 9,10-phenanthrenequinone
crystal structure of prostaglandin F synthase from Trypanosoma cruzi.
Phosphoglycerate kinase, N-terminal domain
PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED
Belongs to the phosphoglycerate kinase family.
In T.brucei, three genes code for phosphoglycerate kinase isozymes, which are transported to different cell compartments.
This cytosolic PGK lacks a C-terminal extension of 38 AA which is present in the glycosomal isoenzyme.
This glycosomal PGK has a C-terminal extension of 38 AA which is not present in the cytosolic isoenzyme. This domain most likely serves as topogenic signal to direct the glycosomal PKG to the glycosome.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES 2 AND 4)
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 5-417 IN COMPLEX WITH ATP AND SUBSTRATE
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 5-419 IN COMPLEX WITH ADP AND SUBSTRATE
Phosphatidylinositol (PI) phosphodiesterase
Variant-surface-glycoprotein phospholipase C
Glycosylphosphatidylinositol-specific phospholipase C
By hydrolysis of the attached glycolipid, releases soluble variant surface glycoprotein containing phosphoinositol from the cell wall of T.brucei after cell lysis. It also cleaves similar membrane anchors on some mammalian proteins. VSG lipase may play a role in processes such as parasite differentiation or antigenic variation.
By hydrolysis of the attached glycolipid, releases soluble variant surface glycoprotein containing phosphoinositol from the cell wall of T.brucei after cell lysis. It also cleaves similar membrane anchors on some mammalian proteins. VSG lipase may play a role in processes such as parasite differentiation or antigenic variation (By similarity).
DNA repair and recombination helicase PIF1
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of mitochondrial (kinetoplast) genome stability. Essential for replication of kinetoplast minicircles. Involved in the segregation of minicircle progeny.
Localizes to the antipodal sites flanking the kDNA disk.
Belongs to the helicase family. PIF1 subfamily.
DNA repair and recombination helicase PIF2
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of mitochondrial (kinetoplast) genome stability. Essential for replication of kinetoplast maxicircles, but not minicircles.
Localizes throughout the tubular structure of the single mitochondrion.
Protein level is regulated by mitochondrial proteasome-like protease HslVU.
Abolishes enzymatic activity, toxic for trypanosome cell growth.
DNA repair and recombination helicase PIF3
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of genome stability.
DNA repair and recombination helicase PIF4
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of mitochondrial (kinetoplast) genome stability.
Localizes predominantly to the kDNA disk.
DNA repair and recombination helicase PIF5
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of mitochondrial (kinetoplast) genome stability. Involved in processing of minicircle Okazaki fragments.
Enriched in the antipodal sites flanking the kDNA disk.
DNA repair and recombination helicase PIF6
DNA repair and recombination helicase PIF7
DNA repair and recombination protein PIF8
Required for the maintenance of mitochondrial (kinetoplast) genome stability. Essential for cell viability. Has probably no helicase activity, missing at least two of seven conserved helicase motifs.
Localizes primarily to the distal face of the kDNA disk. Localization varies with different kDNA replication stages.
Phosphatidylinositol-glycan biosynthesis class M protein
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-PI during GPI precursor assembly (By similarity).
In T.brucei, PIGM has a different substrate specificity compared to mammalian. Given that the protozoan parasite evades the immune response of mammalian hosts and digestion in the gut of the insect vector by means of its coat proteins tethered to the cell surface via GPI-anchors, it may be a good candidate for chemotherapy against African trypanosomiasis.
Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module
Pyruvate-ferredoxin oxidoreductase, PFOR, domain III
Pyruvate-flavodoxin oxidoreductase, EKR domain
PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED
Ferredoxin reductase-like, C-terminal NADP-linked domain
Thiamin diphosphate-binding fold (THDP-binding)
Pyruvate dehydrogenase [NADP(+)], mitochondrial
Pyruvate dehydrogenase [NADP(+)] is one of three enzymes participating in respiratory metabolism. The enzyme is also active with 2-oxobutyrate and oxaloacetate. The enzyme is oxygen sensitive.
Optimum temperature is 40 degrees Celsius.
Expressed in both aerobic and anaerobic conditions.
Arose from gene fusion of pyruvate:ferredoxin oxidoreductase and cytochrome-P450 reductase. Gene fusion has only been found in Euglena and Cryptosporidium.
Euglena cells absolutely require thiamine for growth due to the lack of a pyrimidine formation biosynthetic pathway. Thiamine is actively taken up into the cells and is used as a cofactor after being converted to TPP (thiamine pyrophosphate).
In the N-terminal section; belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family.
Serine/threonine-protein phosphatase PP1(4.8)
Trypanosoma brucei contains two PP1 genes which are highly similar.
Belongs to the PPP phosphatase family. PP-1 subfamily.
Serine/threonine-protein phosphatase PP1(5.9)
Binds 2 magnesium or manganese ions per subunit.
Found in infective promastigote and in tissue amastigote stages.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 32-393 IN COMPLEX WITH SUBSTRATE ANALOG
TRANS-3-HYDROXY-L-PROLINE DEHYDRATASE-RELATED
Catalyzes the interconversion of L- and D-proline. Secreted isoform 1 contributes to parasite immune evasion by acting as a B-cell mitogen. Probably involved in parasite differentiation and infectivity.
Inhibited by maleic acid, iodoacetamide, iodoacetate and, most particularly, pyrrole-2-carboxylic acid.
Membrane-bound and secreted upon differentiation of the parasite into non-dividing infective forms, suggesting that isoform 1 appears upon differentiation (PubMed:16164548).
Cytoplasmic in replicative non-infective forms (PubMed:16164548).
Loss of enzyme activity, without abrogating mitogenic properties.
Catalyzes the interconversion of L- and D-proline.
MUTAGENESIS OF CYS-53; CYS-114 AND CYS-172
Protein tyrosine phosphatase from Leishmania major.
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 4-165 IN COMPLEX WITH SUBSTRATE ANALOG THIOSULFATE
Protein tyrosine phosphatase superfamily
TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE
(Phosphotyrosine protein) phosphatases II
Has protein tyrosine phosphatase activity and may act as a virulence factor to support intracellular survival in host macrophages.
Activated in a reduced environment which promotes the reduction of the disulfide bond between the regulatory Cys-53 and catalytic Cys-114 residues.
Expressed at the promastigote life cycle stage during the logarithmic growth and the stationary phase (at protein level). Expressed at lower levels at the amastigote life cycle stage (at protein level).
Belongs to the protein-tyrosine phosphatase family.
Probable loss of farnesylation. Loss of kinetoplast localization. Does not affect exosome localization.
MUTAGENESIS OF CYS-107 AND 173-CYS--MET-176
Has protein tyrosine phosphatase activity.
Activated in a reduced environment which promotes the reduction of the disulfide bond between the regulatory Cys-52 and the catalytic Cys-107 residues (By similarity). Inhibited by sodium orthovanadate (PubMed:16151248).
In epimastigotes, localizes close to flagellar pocket, cytostome and to reservosomes. Reservosomes are prelysosomal-like acidic organelles found at the cell posterior end which contain the protease cruzipain and ingested proteins and lipids. In amastigotes and trypomastigotes partially co-localizes with concavalin A, a marker of the endocytic pathway.
Expressed at the amastigote life cycle stage (at protein level). Expressed at the epimastigote, amastigote and trypomastigote life cycle stages.
Loss of farnesylation. Localizes to the cytoplasm and loses localization to reservosomes.
SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.
Isolation and characterization of a Naegleria fowleri Tat-binding protein cDNA.
26S proteasome regulatory subunit 8 homolog
The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel (By similarity).
Identification and isolation of three proteasome subunits and their encoding genes from Trypanasoma brucei.
T. cruzi 29 kDa proteasome subunit class II mRNA.
The 29 kDa subunit genomic sequence of Trypanosoma cruzi proteasome.
PROTEASOME SUBUNIT ALPHA TYPE-7-1-RELATED
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-398
PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2
Photosystem I P700 chlorophyll a apoprotein A1
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.
P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The eukaryotic PSI reaction center is composed of at least 11 subunits.
PHOTOSYSTEM I IRON-SULFUR CENTER-RELATED
Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.
Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.
The eukaryotic PSI reaction center is composed of at least 11 subunits.
PHOTOSYSTEM I REACTION CENTER SUBUNIT IX
Subunit IX of photosystem I reaction centre, PsaJ
May help in the organization of the PsaE and PsaF subunits.
Subunit XII of photosystem I reaction centre, PsaM
Photosystem I reaction center subunit XII
Evolution of genetic elements in Euglena species.
Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Bacterial photosystem II reaction centre, L and M subunits
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes.
Tyr-162 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.
2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water.
Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer.
Belongs to the reaction center PufL/M/PsbA/D family.
ligand shared with heterodimeric partner
Photosystem II CP47 reaction center protein
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Binds multiple chlorophylls. PSII binds additional chlorophylls, carotenoids and specific lipids.
Belongs to the PsbB/PsbC family. PsbB subfamily.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-119
photosystem ii from thermosynechococcus elongatus
Photosystem II CP43 reaction center protein
Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids.
Belongs to the PsbB/PsbC family. PsbC subfamily.
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
Photosystem II cytochrome b559, alpha subunit
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Heterodimer of an alpha subunit and a beta subunit. PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes.
With its partner (PsbE) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Photosystem II reaction center protein H
Photosystem II 10 kDa phosphoprotein PsbH
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, numerous small proteins, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes.
PHOTOSYSTEM II REACTION CENTER PROTEIN I
Photosystem II reaction center protein I, PsbI
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-42
PHOTOSYSTEM II REACTION CENTER PROTEIN J
Photosystem II reaction center protein J, PsbJ
This protein is a component of the reaction center of photosystem II.
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
PHOTOSYSTEM II REACTION CENTER PROTEIN K
Photosystem II reaction center protein K, PsbK
Photosystem II reaction center protein L, PsbL
Photosystem II reaction center protein L
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization.
May play a role in photosystem I and II biogenesis.
Originally thought to be a component of PSII; based on experiments in Synechocystis, N.tabacum and barley, and its absence from PSII in T.elongatus and T.vulcanus, this is probably not true.
photosynthetic oxygen evolving center domain
Photosystem II, cytochrome c-550 precursor
OXYGEN-EVOLVING ENHANCER PROTEIN 1-1, CHLOROPLASTIC
OXYGEN-EVOLVING ENHANCER PROTEIN 1-2, CHLOROPLASTIC
Oxygen-evolving enhancer protein 1, chloroplastic
Stabilizes the manganese cluster which is the primary site of water splitting.
Associated with the photosystem II complex.
23 kDa subunit of oxygen evolving system of photosystem II
May be involved in the regulation of photosystem II.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8
PHOTOSYSTEM II REACTION CENTER PROTEIN T
Photosystem II reaction center protein T, PsbT
Seems to play a role in the dimerization of PSII.
Photosystem II reaction center protein Z
Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE
OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870)
H region methotrexate resistance protein
Exhibits a NADPH-dependent biopterin reductase activity. Has good activity with folate and significant activity with dihydrofolate and dihydrobiopterin, but not with quinonoid dihydrobiopterin. Confers resistance to methotrexate (MTX).
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) IN COMPLEX WITH NADP
Adenylosuccinate Synthetase, subunit A, domain 1
Adenylosuccinate Synthetase, subunit A, domain 2
Adenylosuccinate Synthetase, subunit A, domain 3
Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Parasitic protozoa lack the de novo purine biosynthesis pathway and rely exclusively on the salvage pathway for their purine nucleotide requirements.
Belongs to the adenylosuccinate synthetase family.
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH FMN AND OROTATE
DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED
Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro.
Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DHOD1)
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DHOD1)
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DHOD1; DHOD2 AND DHOD3)
X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH FMN; DIHYDROOROTATE; OROTATE; FUMARATE AND SUCCINATE
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 3-314 IN COMPLEX WITH FMN
Optimum temperature is 37 degrees Celsius.
Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b, cytochrome c1 and Rieske protein, 2 core protein subunits, and additional low-molecular weight protein subunits. The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with cytochrome c oxidase (complex IV, CIV).
Belongs to the peptidase M16 family. UQCRC1/QCR1 subfamily.
PROCESSING PEPTIDASE ALPHA SUBUNIT, PUTATIVE-RELATED
Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial
Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
Does not seem to have protease activity as it lacks the zinc-binding site.
Medium-chain alcohol dehydrogenases, catalytic domain
Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.
Ribulose bisphosphate carboxylase, large subunit, C-terminal domain
RuBisCO large subunit, N-terminal domain
RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
RuBisCO, large subunit, small (N-terminal) domain
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.
The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'.
Belongs to the RuBisCO large chain family. Type I subfamily.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-204
SHOWS THAT UTEX 364 IS FROM E.GRACILIS AND NOT E.MUTABILIS
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity).
Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers (By similarity).
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel' (By similarity).
This organism being non-photosynthetic, the role of this protein is uncertain.
Heterohexadecamer of 8 large chains and 8 small chains.
Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway. Specifically phosphorylates D-ribose. Fails to phosphorylate 4, 5 or 6 D-carbon sugars (erythrose, threose, xylulose, arabinose, fructose and glucose).
Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity.
kcat is 10.2 sec(-1) with ATP as substrate and 10.8 sec(-1) with ribose as substrate.
Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Ribulose bisphosphate carboxylase, small subunit
RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC
Ribulose bisphosphate carboxylase small subunit, chloroplastic
Ribulose bisphosphate carboxylase small chain P1, chloroplastic
Ribulose bisphosphate carboxylase small chain P2, chloroplastic
Ribulose bisphosphate carboxylase small chain P3, chloroplastic
Ribulose bisphosphate carboxylase small chain P4, chloroplastic
Ribulose bisphosphate carboxylase small chain P5, chloroplastic
Ribulose bisphosphate carboxylase small chain P6, chloroplastic
Ribulose bisphosphate carboxylase small chain P7, chloroplastic
Ribulose bisphosphate carboxylase small chain P8, chloroplastic
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
Heterohexadecamer of 8 large and 8 small subunits.
In this organism the chloroplast is within a membrane system that is probably derived from the endoplasmic reticulum. The first half of the transit peptide resembles a signal sequence while the second half has the hallmarks of a transit peptide.
Eight small subunits are processed from a large polyprotein (Probable). All start with the same sequence but there is more heterogeneity at the C-terminus (PubMed:24302307).
Belongs to the RuBisCO small chain family.
MUTAGENESIS OF 1026-LYS--LEU-1092 AND 1366-GLY-LYS-1367
MUTAGENESIS OF LYS-1078; ALA-1086 AND 1366-GLY-LYS-1367
INTERACTION WITH THE GRBC COMPLEX; RECC COMPLEX; REMC COMPLEX AND H2F1
ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays an important role in mitochondrial mRNA editing, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA (PubMed:19850921, PubMed:26769962, PubMed:31034523). As part of the RET2-containing gRNA-binding (RET2-GRBC) complex, acts as a scaffold for the assembly of mRNA-gRNA hybrids and the recruitment of the RNA editing core (RECC) complex (PubMed:25928631, PubMed:26769962). Regulates several steps of mRNA editing by the MRBC3010/GRBC6 containing gRNA-binding (MRBC3010-GRBC) complex including loading of unedited mRNA, editing in the first sequence block and subsequent editing progression across multiple sequence blocks (PubMed:25928631). Also, regulates the RNA substrate content of the MRBC3010-GRBC complex as well as the association of this complex with mitoribosomes (PubMed:25928631).
Component of the REH2-associated complex (REH2C) composed of helicase REH2, associated factors H2F1 and H2F2, and mRNAs at various editing stages; the formation of the complex is RNA-independent (PubMed:26769962, PubMed:31034523). Within the complex, interacts with H2F1; the interaction is direct (PubMed:26769962, PubMed:31034523). Interacts transiently, in a RNA-dependent manner, with various editing complexes including the RNA editing core (RECC) complex, the gRNA-binding (GRBC) complex (also known as the MRB1 complex) and the RNA editing mediator (REMC) complex (PubMed:19850921, PubMed:25928631, PubMed:26769962, PubMed:31034523). Interacts with GAP1/GRBC2 via RNA forming a variant of the GRBC complex known as REH2-GRBC complex (PubMed:19850921, PubMed:25928631, PubMed:26769962, PubMed:31034523). Interacts with mitochondrial ribosomes (PubMed:19850921).
The DRBM domain is required for binding to guide RNAs (gRNA) and mRNAs which facilitates the association with the GRBC complex.
RNAi-mediated knockdown at the procyclic stage causes a loss of RNA unwinding activity (PubMed:26769962). Reduces association of H2F1 and abolishes H2F2 association with components of various editing complexes (PubMed:26769962). RNAi-mediated knockdown at the procyclic stage inhibits editing at early 3' sites on pre-mRNA substrates without affecting the interactions between MRB3010/GRBC6, GAP1/GRBC2, RGG2, REL1 and gRNA (PubMed:25928631). Decreases the ratio of unedited mRNA substrates in the MRB3010/GRBC6-MRB complex and the association of never-edited mRNA and 9SrRNA with the MRB3010-MRB complex (PubMed:25928631). Also, causes a decrease in the steady-state levels of guide RNA (gRNA) (PubMed:19850921).
Belongs to the DEAD box helicase family. DEAH subfamily.
Severe reduction in the interaction with H2F1 and GAP1/GRBC2.
Loss of RNA helicase activity. Loss of binding to gRNA. Impaired association with several mRNA editing complexes.
Loss of interaction with gRNA, unedited mRNAs, edited mRNAs at block 1 or at 5' distal blocks, and GAP1/GRBC2 but not with H2F1; when associated with D-1086.
Loss of interaction with gRNA, unedited mRNAs, edited mRNAs at block 1 or at 5' distal blocks, and GAP1/GRBC2 but not with H2F1; when associated with A-1078.
Loss of RNA helicase activity. Loss of interaction with gRNA, unedited mRNAs and edited mRNAs at block 1 or at 5' distal blocks. Loss of interaction with GAP1/GRBC2.
Does not affect the interaction with H2F1 and GAP1/GRBC2.
Moderate reduction in the interaction with GAP1/GRBC2. Interaction with H2F1 is normal. Severe reduction in the interaction with H2F1 and GAP1/GRBC2; when associated with E-1999.
Reduction in the interaction with H2F1 and GAP1/GRBC2. Severe reduction in the interaction with H2F1 and GAP1/GRBC2; when associated with E-1998.
Moderate reduction in the interaction with GAP1/GRBC2. Interaction with H2F1 is normal.
Single-stranded DNA-binding protein P51 subunit
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage.
Component of the heterotrimeric canonical replication protein A complex (RPA).
Belongs to the replication factor A protein 1 family.
Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Heterotrimer of 51, 28, and 14 kDa chains.
Also present in PML nuclear bodies. Redistributes to discrete nuclear foci upon DNA damage (By similarity).
Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). Phosphorylated upon DNA damage, which promotes its translocation to nuclear foci (By similarity).
Belongs to the replication factor A protein 2 family.
Transporter involved in riboflavin (vitamin B2) uptake. Also transports FMN and FAD.
Belongs to the major facilitator superfamily. RibJ family.
RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN
RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT
R1 subunit of ribonucleotide reductase, N-terminal domain
Provides the precursors necessary for DNA synthesis. Catalyzes the rate limiting step in the de novo synthesis of deoxyribonucleotides by directly reducing ribonucleotides to the corresponding deoxyribonucleotides.
Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the large subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site.
Heterodimer of a large and a small subunit.
Belongs to the ribonucleoside diphosphate reductase large chain family.
allosteric effector that controls substrate specificity
RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN
RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2
Ribonucleoside-diphosphate reductase small subunit
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Belongs to the ribonucleoside diphosphate reductase small chain family.
39S RIBOSOMAL PROTEIN L12, MITOCHONDRIAL
Ribosomal protein L7/12, oligomerisation (N-terminal) domain
50S ribosomal protein L12, chloroplastic
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Homodimer. Part of the ribosomal stalk of the 50S ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 forms an elongated spine to which 2 to 4 L12 dimers bind in a sequential fashion. Binds GTP-bound translation factors.
Belongs to the bacterial ribosomal protein bL12 family.
54S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL
50S ribosomal protein L14, chloroplastic
Belongs to the universal ribosomal protein uL14 family.
39S RIBOSOMAL PROTEIN L16, MITOCHONDRIAL
50S ribosomal protein L16, chloroplastic
Belongs to the universal ribosomal protein uL16 family.
50S RIBOSOMAL PROTEIN L20, CHLOROPLASTIC
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity).
Belongs to the bacterial ribosomal protein bL20 family.
50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC
CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED
This protein binds specifically to 23S rRNA.
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
Belongs to the universal ribosomal protein uL22 family.
50S ribosomal protein L23, chloroplastic
Belongs to the universal ribosomal protein uL23 family.
Belongs to the universal ribosomal protein uL2 family.
50S ribosomal protein L32, chloroplastic
Belongs to the bacterial ribosomal protein bL32 family.
50S RIBOSOMAL PROTEIN L36, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL36 family.
Binds 5S rRNA, forms part of the central protuberance of the 50S subunit.
Part of the 50S ribosomal subunit; contacts the 5S rRNA.
Belongs to the universal ribosomal protein uL5 family.
Belongs to the universal ribosomal protein uL1 family.
Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (25S, 5.8S and 5S) (By similarity).
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Component of the large ribosomal subunit.
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Belongs to the eukaryotic ribosomal protein eL14 family.
Molecular cloning and expression in E.coli of a Leishmanial cell surface protein homolog in African trypanosomes.
Belongs to the eukaryotic ribosomal protein eL18 family.
RIBOSOMAL_L23EN DOMAIN-CONTAINING PROTEIN
This protein binds to a specific region on the 26S rRNA.
Belongs to the universal ribosomal protein uL15 family.
Belongs to the eukaryotic ribosomal protein eL28 family.
Sequence of a cDNA from Leishmania major encoding a protein homologous with the human ribosomal protein L30.
Belongs to the eukaryotic ribosomal protein eL30 family.
Ribosomal protein L37 in Leishmania is encoded by duplicate genes.
Belongs to the eukaryotic ribosomal protein eL37 family.
There are two genes for L37 in L.infantum.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78
Ubiquitin-ribosomal protein eL40 fusion protein
Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Component of the 60S subunit of the ribosome.
Ubiquitin is synthesized as a polyubiquitin precursor with 5 or 6 exact head to tail repeats. Some ubiquitin genes contain a single copy of ubiquitin fused to a ribosomal protein. This gene is an exception, since it contains for 4 copies of the ubiquitin fused to the ribosomal protein eL40.
For a better understanding, features related to ubiquitin are only indicated for the first chain.
In the N-terminal section; belongs to the ubiquitin family.
In the C-terminal section; belongs to the eukaryotic ribosomal protein eL40 family.
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UB-EP52)
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (UB-EP52 AND LMJF31.2030)
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77
Ubiquitin is synthesized as a polyubiquitin precursor with 5 or 6 exact head to tail repeats. Some ubiquitin genes contain a single copy of ubiquitin fused to a ribosomal protein.
Belongs to the eukaryotic ribosomal protein eL42 family.
Belongs to the universal ribosomal protein uL4 family.
Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
P0 forms a pentameric complex by interaction with dimers of P1 and P2.
Belongs to the universal ribosomal protein uL10 family.
ACIDIC RIBOSOMAL PROTEIN P2, PUTATIVE-RELATED
Plays an important role in the elongation step of protein synthesis.
P1 and P2 exist as dimers at the large ribosomal subunit.
Belongs to the eukaryotic ribosomal protein P1/P2 family.
Characterization of the ribosomal P2 beta protein from Leishmania (V.) braziliensis.
60S ACIDIC RIBOSOMAL PROTEIN FAMILY MEMBER
High levels are present in the logarithmic growth phase of the promastigote stage.
It is uncertain whether Met-1 or Met-3 is the initiator.
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 51-324 IN COMPLEX WITH ATP
DNA ligase/mRNA capping enzyme, catalytic domain
Essential for RNA editing. RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
Component of the RNA editing complex (editosome), a 1600 kDa complex composed of at least 20 proteins (By similarity). Interacts with terminal uridylyltransferase MEAT1 (By similarity).
Component of the RNA editing complex (editosome), a 1600 kDa complex composed of at least 20 proteins (PubMed:11134327, PubMed:19465686). Interacts with terminal uridylyltransferase MEAT1 (PubMed:19465686).
RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
Component of the RNA editing complex, a 1600 kDa complex composed of at least 20 proteins.
Belongs to the universal ribosomal protein uL6 family.
Ribosomal protein L11, C-terminal domain
Ribosomal protein L11/L12, N-terminal domain
39S RIBOSOMAL PROTEIN L11, MITOCHONDRIAL
60S ribosomal protein L11, mitochondrial
Belongs to the universal ribosomal protein uL11 family.
60S ribosomal protein L14, mitochondrial
60S ribosomal protein L18, mitochondrial
Belongs to the universal ribosomal protein uL18 family.
39S RIBOSOMAL PROTEIN L19, MITOCHONDRIAL
60S ribosomal protein L19, mitochondrial
Belongs to the bacterial ribosomal protein bL19 family.
39S RIBOSOMAL PROTEIN L27, MITOCHONDRIAL
60S ribosomal protein L27, mitochondrial
Belongs to the bacterial ribosomal protein bL27 family.
60S ribosomal protein L32, mitochondrial
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2)
The protein migrates at 80 kDa in SDS-PAGE gels.
DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1
beta and beta-prime subunits of DNA dependent RNA-polymerase
DNA-directed RNA polymerase I largest subunit
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity).
Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits.
Belongs to the RNA polymerase beta' chain family.
IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX
DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1
DNA-directed RNA polymerase II subunit RPB1-A
DNA-directed RNA polymerase II largest subunit A
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates (By similarity).
Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.
The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion temporarily coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits. The ribonucleoside triphosphate is transferred by a rotation to the nucleotide addition (A) site for pairing with the template DNA. The catalytic A site involves three conserved aspartate residues of the RNA Pol II largest subunit which permanently coordinate a second magnesium ion.
Trypanosoma brucei contains two genes for the Pol II largest subunit. The presence of both, polIIA and polIIB genes, is not essential for viability and neither of the genes seem not to confer to alpha-amanitin-resistant transcription.
Protein purification and mass spectrometry by PubMed:16962183 do not differentiate between the TRP4.8/polIIA and TRP5.9/polIIB gene products.
DNA-directed RNA polymerase II subunit RPB1-B
DNA-directed RNA polymerase II largest subunit B
DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1
DNA-directed RNA polymerase III largest subunit
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity).
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.
DNA-directed RNA polymerase, insert domain
Insert subdomain of RNA polymerase alpha subunit
DNA-directed RNA polymerase subunit alpha
Plastid-encoded RNA polymerase subunit alpha
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription (By similarity).
Belongs to the RNA polymerase alpha chain family.
The C-terminal domain thought to be required for interaction with some regulatory factors is missing from this protein.
DNA-directed RNA polymerase subunit alpha, mitochondrial
DNA-directed RNA polymerase, beta subunit, external 1 domain
DNA-directed RNA polymerase, subunit 2, domain 6
RNA polymerase alpha subunit dimerisation domain
DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA
Plastid-encoded RNA polymerase subunit beta
In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
Belongs to the RNA polymerase beta chain family.
PRELIMINARY NUCLEOTIDE SEQUENCE OF 1-524
DNA-directed RNA polymerase subunit beta'
Plastid-encoded RNA polymerase subunit beta'
Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 586-830
DNA-directed RNA polymerase subunit beta''
Plastid-encoded RNA polymerase subunit beta''
Belongs to the RNA polymerase beta' chain family. RpoC2 subfamily.
28S RIBOSOMAL PROTEIN S11, MITOCHONDRIAL
40S RIBOSOMAL PROTEIN S14/30S RIBOSOMAL PROTEIN S11
30S ribosomal protein S11, chloroplastic
Belongs to the universal ribosomal protein uS11 family.
30S RIBOSOMAL PROTEIN S12, CHLOROPLASTIC
With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits (By similarity).
Belongs to the universal ribosomal protein uS12 family.
The ribosomal protein gene rps12 from the plastid genome of the nonphotosynthetic flagellate Astasia longa.
28S RIBOSOMAL PROTEIN S14, MITOCHONDRIAL
Glucocorticoid receptor-like (DNA-binding domain)
30S ribosomal protein S14, chloroplastic
Binds 16S rRNA, required for the assembly of 30S particles.
Belongs to the universal ribosomal protein uS14 family.
28S RIBOSOMAL PROTEIN S18C, MITOCHONDRIAL
30S ribosomal protein S18, chloroplastic
Belongs to the bacterial ribosomal protein bS18 family.
37S RIBOSOMAL PROTEIN S19, MITOCHONDRIAL
30S ribosomal protein S19, chloroplastic
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS19 family.
30S RIBOSOMAL PROTEIN S2 PROKARYOTIC AND ORGANELLAR
Belongs to the universal ribosomal protein uS2 family.
Prokaryotic type KH domain (KH-domain type II)
Belongs to the universal ribosomal protein uS3 family.
37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
With S5 and S12 plays an important role in translational accuracy.
Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity (By similarity).
Belongs to the universal ribosomal protein uS4 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
Belongs to the universal ribosomal protein uS7 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Belongs to the universal ribosomal protein uS8 family.
Belongs to the universal ribosomal protein uS9 family.
An evolutionary study of ycf65 in Euglena chloroplasts.
30S RIBOSOMAL PROTEIN 3-1, CHLOROPLASTIC
Probably a ribosomal protein or a ribosome-associated protein.
Belongs to the chloroplast-specific ribosomal protein cS23 family.
Belongs to the eukaryotic ribosomal protein eS12 family.
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (RPS25 AND LINJ25.1230)
Belongs to the eukaryotic ribosomal protein eS25 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Plays a role in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Belongs to the universal ribosomal protein uS5 family.
Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (25S, 5.8S and 5S).
Belongs to the eukaryotic ribosomal protein eS1 family.
Component of the 40S small ribosomal subunit. Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome.
Component of the small ribosomal subunit. Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3.
Ribosomal protein S6 is the major substrate of protein kinases in eukaryote ribosomes.
Belongs to the eukaryotic ribosomal protein eS6 family.
Component of the 40S small ribosomal subunit (By similarity). Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA (By similarity).
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (RPS8A AND RPS8B)
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (RPS8A AND RPS8B)
Belongs to the eukaryotic ribosomal protein eS8 family.
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.
Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (25S, 5.8S and 5S). Interacts with ribosomal protein S21.
One of the primary rRNA binding proteins, it binds directly to the small rRNA where it nucleates assembly of the head domain of the small subunit.
37S RIBOSOMAL PROTEIN S10, MITOCHONDRIAL
Belongs to the universal ribosomal protein uS10 family.
Protein S12 is involved in the translation initiation step.
In the completely edited RNA, 117 uridines are added at 49 sites and 32 uridines are deleted at 13 sites.
Some positions are modified by RNA editing via nucleotide insertion and deletion. 133 U's are added and 32 U's are deleted at 66 sites.
Retrotransposable element SLACS 45 kDa protein
Retrotransposable element SLACS 132 kDa protein
VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE
Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase
Belongs to the class II ribonucleoside-triphosphate reductase family.
Formate/glycerate dehydrogenase catalytic domain-like
Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
Belongs to the adenosylhomocysteinase family.
SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL
SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit.
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
Probable GTP-binding protein that may be involved in cell development.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-2
NAD-dependent protein deacetylase SIR2rp1
NAD-dependent deacetylase, which probably acts as a regulator of gene expression believed to help form modified chromatin structures on the genes it regulates.
Belongs to the sirtuin family. Class I subfamily.
Cloning of a Trypanosoma brucei Sir2 homolog.
NAD-dependent protein deacetylase, which is involved in repression of RNA polymerase I-mediated expression immediately adjacent to telomeres. It is however not involved in antigenic variation and subtelomeric variant surface glycoprotein (VSG) gene silencing. Plays a role in DNA damage response. Also has ADP-ribosylation activity in vitro.
Co-localizes with telomeres and minichromosomes.
NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues.
Belongs to the sirtuin family. Class II subfamily.
NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL
NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo.
In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-56 and Arg-59) that bind to malonylated and succinylated substrates and define the specificity.
Belongs to the sirtuin family. Class III subfamily.
In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-57 and Arg-60) that bind to malonylated and succinylated substrates and define the specificity.
Delta(8)-fatty-acid desaturase which introduces a double bond at the 8-position in 20-carbon chain length fatty acids (C20) that have an existing delta-11 unsaturation (double bond) (PubMed:10328826). Whether it acts on CoA-linked substrates (as in animals) or phospholipid-linked substrates (as in plants and fungi) is still not clear (Probable).
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Euglena gracilis exhibits the metabolic behavior of a plant in the light and of an animal in the dark. Grown in the dark, this organism contains large amounts of 20-carbon chain length (C20) polyunsaturated fatty acids (PUFA), including arachidonic acid (C20:4n-6), and little or no C18 PUFAs (such as linolenic acid, C18:3). On the other hand, when grown under photoauxotrophic conditions, this organism is rich in linolenic acid and contain relatively small amounts of the C20 PUFAs.
SPHINGOMYELIN SYNTHASE-RELATED PROTEIN 1
Phosphatidylinositol:ceramide inositolphosphotransferase
Bidirectional lipid inositolphosphotransferase capable of converting phosphatidylinositol (PI) and ceramide to inositol-phosphorylceramide (IPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoinositol acceptors. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target.
Belongs to the sphingomyelin synthase family.
Bidirectional lipid inositolphosphotransferase capable of converting phosphatidylinositol (PI) and ceramide to inositol-phosphorylceramide (IPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoinositol acceptors. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target (By similarity).
Predominantly synthesizes inositol phosphorylceramide (IPC), with minimal sphingomyelin (SM)/ethanolamine phosphorylceramide (EPC) synthase activity (PubMed:20457606, PubMed:19545591, PubMed:21899277). Specificity is likely to be defined by residues in the lumenal catalytic domain that interact with the polar head groups of the phospholipid donors (PubMed:21899277). IPC is synthesized by transferring the phosphoinositol from a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) to an N-acylsphing-4-enine (ceramide) or an N-acylsphinganine (dihydroceramide) (PubMed:20457606). SM is synthesized by both stages of the parasite life cycle, bloodstream forms (BSF) and procyclic forms (PCF), by transferring the phosphocholine from a 1,2-diacyl-sn-glycero-3-phosphocholine to an N-acylsphing-4-enine (ceramide) or an N-acylsphinganine (dihydroceramide) (By similarity). Similarly, EPC is synthesized by transferring phosphoethanolamine from a 1,2-diacyl-sn-glycero-3-phosphoethanolamine to ceramide or dihydroceramide by BSF and PCF, while IPC is confined to PCF (By similarity). The ceramide/dihydroceramide ratios are skewed towards dihydroceramide in PCF parasites and ceramide in BSF parasites, this is likely due to differential expression and/or regulation of dihydroceramide desaturase, the enzyme responsible for converting dihydroceramide to ceramide (PubMed:18699867).
Elevated ceramide levels and growth arrest; cells were arrested in division but replication of DNA and organelles continued giving rise to cells containing multiple nuclei, kinetoplasts and flagella.
Phosphatidylethanolamine:ceramide ethanolaminephosphotransferase
Ethanolamine-phosphorylceramide synthase
Bidirectional lipid ethanolaminephosphotransferase capable of converting phosphatidylethanolamine (PE) and ceramide to ethanolamine-phosphorylceramide (EPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoethanolamine acceptors. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target (By similarity).
Predominantly synthesizes ethanolamine-phosphorylceramide (EPC), with minimal sphingomyelin (SM)/inositol phosphorylceramide (IPC) synthase activity (PubMed:20457606, PubMed:21899277). Specificity is likely to be defined by residues in the lumenal catalytic domain that interact with the polar head groups of the phospholipid donors (PubMed:21899277). EPC is synthesized by both stages of the parasite life cycle, bloodstream forms (BSF) and procyclic forms (PCF), by transferring the phosphoethanolamine from a 1,2-diacyl-sn-glycero-3-phosphoethanolamine to an N-acylsphing-4-enine (ceramide) or an N-acylsphinganine (dihydroceramide) (By similarity). Similarly, SM is synthesized by transferring the phosphocholine from a 1,2-diacyl-sn-glycero-3-phosphocholine to ceramide or dihydroceramide by BSF and PCF, while IPC is confined to PCF (By similarity). The ceramide/dihydroceramide ratios are skewed towards dihydroceramide in PCF parasites and ceramide in BSF parasites, this is likely due to differential expression and/or regulation of dihydroceramide desaturase, the enzyme responsible for converting dihydroceramide to ceramide (PubMed:18699867).
Expressed in both bloodstream and procyclic stage parasites.
Phosphatidylcholine:ceramide cholinephosphotransferase 3
Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target (By similarity).
Bifunctional sphingomyelin (SM)/ethanolamine phosphorylceramide (EPC) synthase with minimal inositol phosphorylceramide (IPC) synthase activity (PubMed:20457606, PubMed:21899277). Specificity is likely to be defined by residues in the lumenal catalytic domain that interact with the polar head groups of the phospholipid donors (PubMed:21899277). SM is synthesized by both stages of the parasite life cycle, bloodstream forms (BSF) and procyclic forms (PCF), by transferring the phosphocholine from a 1,2-diacyl-sn-glycero-3-phosphocholine to an N-acylsphing-4-enine (ceramide) or an N-acylsphinganine (dihydroceramide) (By similarity). Similarly, EPC is synthesized by transferring phosphoethanolamine from a 1,2-diacyl-sn-glycero-3-phosphoethanolamine to ceramide or dihydroceramide by BSF and PCF, while IPC is confined to PCF (By similarity). The ceramide/dihydroceramide ratios are skewed towards dihydroceramide in PCF parasites and ceramide in BSF parasites, this is likely due to differential expression and/or regulation of dihydroceramide desaturase, the enzyme responsible for converting dihydroceramide to ceramide (PubMed:18699867).
Enhanced inositol-phosphorylceramide (IPC) synthesis without affecting SM or EPC activity creating a trifunctional enzyme.
Phosphatidylcholine:ceramide cholinephosphotransferase 4
Bifunctional sphingomyelin (SM)/ethanolamine phosphorylceramide (EPC) synthase with minimal inositol phosphorylceramide (IPC) synthase activity (PubMed:18699867, PubMed:20457606, PubMed:19545591, PubMed:21899277). Specificity is likely to be defined by residues in the lumenal catalytic domain that interact with the polar head groups of the phospholipid donors (PubMed:21899277). SM is synthesized by both stages of the parasite life cycle, bloodstream forms (BSF) and procyclic forms (PCF), by transferring the phosphoryl headgroup from a 1,2-diacyl-sn-glycero-3-phosphocholine to an N-acylsphing-4-enine (ceramide) or an N-acylsphinganine (dihydroceramide) with release of 1,2-diacyl-sn-glycerol (PubMed:18699867). Also catalyzes the reverse reaction, production of ceramide from sphingomyelin (PubMed:21899277). EPC is synthesized by transferring phosphoethanolamine from a 1,2-diacyl-sn-glycero-3-phosphoethanolamine to ceramide or dihydroceramide by BSF and PCF, while IPC is confined to PCF (PubMed:18699867). The ceramide/dihydroceramide ratios are skewed towards dihydroceramide in PCF parasites and ceramide in BSF parasites, this is likely due to differential expression and/or regulation of dihydroceramide desaturase, the enzyme responsible for converting dihydroceramide to ceramide (PubMed:18699867).
STRUCTURE-SPECIFIC ENDONUCLEASE SUBUNIT SLX1
Structure-specific endonuclease subunit SLX1 homolog 1
Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Forms a heterodimer with a member of the SLX4 family.
Structure-specific endonuclease subunit SLX1 homolog 2
Structure-specific endonuclease subunit SLX1 homolog
O-PHOSPHOSERYL-TRNA(SEC) SELENIUM TRANSFERASE
SOLUBLE LIVER ANTIGEN/LIVER PANCREAS ANTIGEN
Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Homotetramer composed of two homodimers.
Impaired selenocysteine incorporation into proteins, such as SelT, SelK and SelTryp (PubMed:26586914). No defect in promastigote growth rate and in their capacity to infect host macrophages (PubMed:26586914).
May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate
Crystal Structure of N-terminus truncated selenophosphate synthetase from Leishmania major.
INACTIVE SELENIDE, WATER DIKINASE-LIKE PROTEIN-RELATED
Synthesizes selenophosphate from selenide and ATP.
Expressed at the promastigote and amastigote stages.
Belongs to the selenophosphate synthase 1 family. Class I subfamily.
RNAi-mediated knock down in procyclic and blood stream forms (strain 29-13) impairs growth following prolonged exposure to oxidative stress.
RNA-EDITING COMPLEX PROTEIN MP42-RELATED
Uncharacterized protein Tb927.8.680, mitochondrial
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.
Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity).
Present in the nuclei and mitotic spindle-fibers but absent in flagellar axonemes or cytoskeletal microtubules.
Expressed in actively growing cells and repressed quickly when these cells were induced to differentiate.
Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8 AND 442-451
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8 AND 433-442
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-299
Developmentally regulated neuraminidase implicated in parasite invasion of cells.
Maximal activity in trypomastigotes, minimum in epimastigotes and not detectable in amastigotes.
The variable lengths of the long tandem repeat domain could account in part for the polymorphism of the TCNA protein.
YJGF_ENDORIBONC DOMAIN-CONTAINING PROTEIN
Expressed in epimastigotes (at protein level). Expressed in epimastigote, trypomastigote and amastigote stages.
Translationally-controlled tumor protein homolog
Binds calcium; exact function not known.
Thioredoxin-dependent peroxide reductase
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Homodimer; disulfide-linked, upon oxidation.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Cysteine sulfenic acid (-SOH) intermediate
ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH]
Catalyzes reduction of trans-2-enoyl-CoA to acyl-CoA, an important step in the fatty acid biosynthesis pathway, which is performed in mitochondria under anaerobiosis. Preferably catalyzes the reduction of short chain length substrates such as crotonyl-CoA ((2E)-butenoyl-CoA) and (2E)-hexenoyl-CoA. Can use both NADH and NADPH as electron donor, with 2-3-fold higher specific activities for NADH relative to NADPH. Originally thought to contribute to wax ester production under anaerobic conditions (PubMed:15569691). Later shown to be dispensable for wax ester production under anaerobic conditions, but involved in the greening process (chlorophyll synthesis and/or chloroplast development) (PubMed:30650145).
68 uM for (2E)-butenoyl-CoA (crotonyl-CoA) (in the presence of NADH)
91 uM for trans-2-hexenoyl-CoA (in the presence of NADH)
109 uM for NADH (in the presence of (2E)-butenoyl-CoA (crotonyl-CoA))
119 uM for NADPH (in the presence of (2E)-butenoyl-CoA (crotonyl-CoA))
Expressed under aerobic and anaerobic conditions.
Severe bleaching phenotype concomitant with negligible levels of chlorophylls and glycolipids. The levels of alanine, glycine, tryptophan, and arginine, as well as those for glycerophospholipids were highly impacted in the mutant under anaerobic conditions.
Euglena gracilis exhibits the metabolic behavior of a plant in the light and of an animal in the dark.
X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) IN COMPLEX WITH MANGANESE; SUBSTRATE ANALOG N-OXALYLGLYCINE AND 5-METHYLCYTOSINE DNA
MUTAGENESIS OF ASN-147; ASP-234; HIS-297 AND GLN-310
X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 57-321 IN COMPLEX WITH MANGANESE; 2-OXOGLUTARATE AND 5-METHYLCYTOSINE DNA
Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), and thereby plays a role in active DNA demethylation. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC).
Has good structural similarity to 2-oxoglutarate-dependent dioxygenases of the TET and the alkB families, in spite of very low overall sequence similarity.
Reduced enzyme activity with DNA containing 5-methylcytosine.
Decreases enzyme activity with DNA containing 5-hydroxymethylcytosine.
Nearly abolishes enzyme activity with DNA containing 5-methylcytosine.
Strongly reduced enzyme activity with DNA containing 5-methylcytosine.
Expressed specifically in bloodstream forms.
Expressed in both bloodstream and procyclic forms.
Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.
Belongs to the type II topoisomerase family.
O-(5'-phospho-DNA)-tyrosine intermediate
Important for DNA bending; intercalates between base pairs of target DNA
Isolation of a gene encoding a DNA topoisomerase II of Leishmania (Leishmania) chagasi.
LYSOSOMAL-ASSOCIATED TRANSMEMBRANE PROTEIN
Complement C2 receptor inhibitor tetraspanning
Complement C2 receptor inhibitor trispanning
Cell surface receptor that binds to human complement C2a protein. This results in inhibition of the classical and lectin pathways of complement activation, probably due to interference with binding of C2a to C4b and interference with cleavage by C1 or MASP2 such that C3 convertase cannot be formed. This infers resistance to complement-mediated cell lysis, allowing parasite survival and infection.
Interacts (via N-terminal extracellular domain) with human C2a.
Located on the surface tegumental plasma membrane of metacyclic trypomastigote so in contact with host blood plasma.
In Y strain, expression is seen in metacyclic trypomastigote form and in stationary, but not logarithmic-phase epimastigote forms. In Colombiana strain, expression is seen in metacyclic trypomastigote form only.
The C-sensitive epimastigote form of the Colombiana strain is more susceptible to lysis than the Y strain at all human serum concentrations. Potential vaccine candidate molecule.
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG
X-RAY CRYSTALLOGRAPHY (0.83 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG
Belongs to the triosephosphate isomerase family.
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS IN COMPLEX WITH SUBSTRATE ANALOGS
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG
The enzyme contains a high proportion of positively-charged residues in beta-barrels V and VII (compared to the homologous regions in other triose isomerase sequences). Since 2 clusters of positive charges located at precise distances on the molecular surface are common to 4 glycosomal enzymes, it has been speculated that this might represent a signal for entry into glycosomes (PubMed:3015595).
3-(2-Benzothiazolylthio)-1-Propanesulfonic Acid
tRNA (guanine(37)-N1)-methyltransferase 1
Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Predominantly in the mitochondria and in the nucleus.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family.
tRNA (guanine(37)-N1)-methyltransferase 2
Conjugates glutathione (gamma-Glu-Cys-Gly) and glutathionylspermidine to form trypanothione (N(1),N(8)-bis(glutathionyl)spermidine), which is involved in maintaining intracellular thiol redox and in defense against oxidants.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES TRS-1 AND TRS-2)
Trypanosoma cruzi (Tulahuen 0): expression, purification and functional characterization of an enzyme catalyzing trypanothione synthesis.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE TRS-1)
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES TRS-1 AND TRS-2)
Bifunctional enzyme which catalyzes the formation of trypanothione (N(1),N(8)-bis(glutathionyl)spermidine) from glutathione and spermidine. Converts spermidine or glutathionylspermidine into trypanothione. Can also convert aminopropylcadaverine into glutothionylaminopropylcadaverine and homotrypanothione. Also has low amidase activity, hydrolyzing trypanothione, homotrypanothione or glutathionylspermidine to form glutathione and the corresponding polyamine.
Subject to high-substrate inhibition by glutathione.
570 uM for glutathione with spermidine as cosubstrate
190 uM for glutathione with glutathionylspermidine as cosubstrate
Optimum pH is 8.1 with spermidine as substrate. Optimum pH is 8.5 with glutathionylspermidine as substrate.
In allele TRS-2 and strain Silvio X10/7.
INTERACTION WITH P45 AND P50 RNA LIGASES
RNA EDITING 3' TERMINAL URIDYLYL TRANSFERASE 1
RNA editing terminal uridylyltransferase 1
Terminal uridylyltransferase which is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA. Specifically, catalyzes the addition of Us to the 3'-hydroxyl group of guided RNA (gRNA), with a preference for RNAs terminating in 6 Us, but also can add Us to RNAs terminating in 6 adenines (A), 6 cytosines (C), or 6 guanines (G) (PubMed:11893335, PubMed:15060068). Can mediate RNA-independent UTP polymerization in vitro (PubMed:15060068). Can mediate pyrophosphate-dependent degradation of synthetic RNA ending with U residues in vitro (PubMed:15060068).
Binds 1 Mg(2+) or Mn(2+) per subunit (PubMed:11893335). The type of divalent cation used by the enzyme affects the nucleotide specificity; Mg(2+) induces predominantly uridine (U) incorporation while Mn(2+) induces also substantial incorporation of both adenine (A) and cytosine (C) (PubMed:11893335).
Zinc-binding is required for catalytic activity.
KM is 45-65 uM for UTP (at 27 degrees Celsius) (PubMed:15060068). KM is 18-30 uM for RNA (at 27 degrees Celsius) (PubMed:15060068).
Homotetramer (PubMed:11893335, PubMed:15060068). Part of a 700kDa complex (PubMed:11893335). Interacts with p45 and p50 RNA ligases (PubMed:11893335).
Belongs to the DNA polymerase type-B-like family.
Important for catalytic activity and RNA binding
3-fold reduction in affinity for RNA. Does not affect affinity for UTP.
50-fold reduction in affinity for RNA and 7-fold increase in affinity for UTP.
Loss of catalytic activity. Does not affect tetramerization.
Loss of catalytic activity. Does not affect gRNA binding.
6-fold reduction in affinity for UTP. Does not affect affinity for RNA.
Does not affect affinity for RNA and UTP.
25-fold reduction in affinity for RNA. 2-fold increase in affinity for UTP.
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 189-699 AND MUTANT ALA-473 IN COMPLEX WITH ZINC; MAGNESIUM AND UTP
RNA editing 3' terminal uridylyltransferase 1
Terminal uridylyltransferase which is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-RNA (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351). Specifically, catalyzes the addition of Us to the 3'-hydroxyl group of guided RNA (gRNA), ribosomal RNA (rRNA) and some mRNAs (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351). As part of the mitochondrial 3' processome (MPsome), catalyzes the primary 3' uridylation of gRNA precursors to facilitate their recognition and to induce their processive 3'-5' degradation by DSS1, and the secondary 3' uridylation of mature gRNAs (PubMed:26833087). Involved in the 3' uridylylation of the long A/U tail of some edited and never-edited mRNAs (PubMed:20086102). Promotes 3' uridylylation-mediated decay of some never-edited mRNAs (PubMed:20086102). Does not mediate RNA-independent UTP polymerization (PubMed:27744351).
Binds 1 Mg(2+) or Mn(2+) per subunit (PubMed:27744351). The type of divalent cation used by the enzyme affects the nucleotide specificity; Mg(2+) induces predominantly uridine (U) incorporation while Mn(2+) induces also substantial incorporation of both adenine (A) and cytosine (C) (By similarity).
KM is 18-28 mM for UTP (at 27 degrees Celsius and 12 (U) single-stranded RNA as substrate) (PubMed:15304317). kcat is 100 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.0012 min(-1) with UTP and double-stranded RNA as substrates (PubMed:19465686). kcat is 15.5 min(-1) with UTP as substrate (PubMed:27744351). kcat is 23.5 min(-1) with RNA as substrate (PubMed:27744351).
17 uM for UTP (with 6(U) single-stranded RNA as substrate)
1.5 uM for UTP (with double-stranded RNA as substrate)
Oligomer (PubMed:27744351). Component of the mitochondrial 3' processome (MPsome) complex composed at least of terminal uridylyltransferase KRET1/TUT1, 3'-5' exonuclease DSS1, MPSS1, MPSS2 and MPSS3 (PubMed:26833087, PubMed:27744351). Within the complex, interacts with DSS1, MPSS1 and MPSS3 (PubMed:26833087).
The C2H2-type zinc finger domain is required for the proper folding of the catalytic domain, but is dispensable for uridylation of single strand RNA substrate.
RNAi-mediated knockdown at the procyclic stage causes severe growth defect and a severe reduction in mRNA editing (PubMed:11893335, PubMed:20086102, PubMed:26833087, PubMed:27744351). Reduced production of guided RNAs (gRNA) and rRNAs due to a block in the processing of gRNA and rRNA precursors (PubMed:20086102, PubMed:26833087). Accumulation of unprocessed precursors for some pre-edited and never-edited mRNAs (PubMed:20086102).
Required for oligomerization and may contribute to the incorporation into the MPsome complex
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 20-487 OF MUTANT TRP-94; TRP-122 AND TRP-207 IN COMPLEX WITH MAGNESIUM; MANGANESE AND UTP
MUTAGENESIS OF TRP-94; TRP-122 AND TRP-207
RNA EDITING 3' TERMINAL URIDYLYL TRANSFERASE 2
RNA editing 3' terminal uridylyltransferase 2
Terminal uridylyltransferase which, as part of the mitochondrial RNA editing core complex (RECC), is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA (PubMed:12820966, PubMed:19465686, PubMed:20362585). Specifically, catalyzes the addition of one U to single-stranded RNA with a preference for a 3'-terminal A or G and adds the number of Us specified by a guide RNA (gRNA) to precleaved double-stranded RNA editing substrates (PubMed:12820966, PubMed:19465686, PubMed:20362585, PubMed:16281058). Essential for the survival of the bloodstream form (PubMed:16281058).
kcat is 0.0007 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.002 min(-1) with UTP and double-stranded RNA as substrates (PubMed:19465686). kcat is 0.02 min(-1) with UTP and with RNA with no U in 3' position as substrates (PubMed:20362585). kcat is 0.2 min(-1) with UTP and double-stranded RNA with one U in 3' position as substrates (PubMed:20362585).
1.2 uM for UTP (with 6(U) single-stranded RNA as substrate)
3.4 uM for UTP (with double-stranded RNA as substrate)
2.5 uM for UTP (with RNA with no U in 3' position as substrate)
12.6 uM for UTP (with double-stranded RNA with one U in 3' position as substrate)
Component of the mitochondrial RNA editing core complex (RECC), also known as the editosome complex (PubMed:12820966, PubMed:12649499, PubMed:19465686, PubMed:20362585). Interacts (via middle domain) with MP81; the interaction enhances MP57 catalytic activity and probably recruits MP57 to the RECC complex (PubMed:12820966, PubMed:20362585).
RNAi-mediated knockdown in the procyclic form causes growth arrest.
Middle domain (MD); important for the incorporation into the RECC complex, for catalytic activity and possibly RNA binding
No effect on catalytic activity; when associated with R-122 and R-207.
No effect on catalytic activity; when associated with R-94 and R-207.
No effect on catalytic activity; when associated with R-94 and R-122.
RNA editing 3' terminal uridylyltransferase 3
Terminal uridylyltransferase which catalyzes the addition of Us to the 3'-hydroxyl group of single-stranded RNAs (PubMed:15304317). Does not mediate RNA-independent UTP polymerization (PubMed:15304317).
KM is 36-48 uM for UTP (at 27 degrees Celsius and with 12(U) single-stranded RNA as substrate).
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH UTP AND MAGNESIUM
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH UTP; RNA ANALOG AND MAGNESIUM
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH UTP; RNA ANALOG AND MAGNESIUM
RNA editing 3' terminal uridylyltransferase 4
Terminal uridylyltransferase which, specifically, catalyzes the addition of Us to the 3'-hydroxyl group of single-stranded RNAs with a 3'-terminal U.
Binds 1 Mg(2+) or Mn(2+) per subunit (PubMed:17189640, PubMed:17785418). The type of divalent cation used by the enzyme affects the nucleotide specificity; Mg(2+) induces predominantly uridine (U) incorporation while Mn(2+) induces also substantial incorporation of both adenine (A) and cytosine (C) (PubMed:17189640).
The 3' uridylated RNA substrate is involved in the selective incorporation of UTP; UTP binding is favored due to the constraint posed on the positioning of the NTP base by the continuous stacking interactions between Tyr-189 side chain, the bound NTP, and the terminal nucleoside base of the RNA substrate.
kcat is 0.5 min(-1) with UTP (PubMed:17189640). kcat is 0.3 min(-1) with 6(U) single-stranded RNA (PubMed:17189640).
1 uM for UTP (at 27 degrees Celsius and with 6(U) single-stranded RNA as substrate)
0.2 uM for 6(U) single-stranded RNA (at 27 degrees Celsius)
Loss of catalytic activity. Moderate decrease in UTP binding.
Loss of catalytic activity. Does not affect UTP binding.
Loss of catalytic activity. Partial reduction in UTP binding.
2-fold decrease in affinity for UTP. 660-fold decrease in affinity for RNA.
Does not affect UTP binding. 360-fold decrease in affinity for RNA.
Severe decrease in UTP binding without affecting RNA binding.
Loss of catalytic activity. Severe decrease in UTP binding.
50-fold decrease in affinity for RNA. Does not affect UTP binding.
X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 3-385 IN COMPLEX WITH UTP AND MAGNESIUM
MITOCHONDRIAL EDITOSOME-LIKE COMPLEX ASSOCIATED TUTASE
Terminal uridylyltransferase which, as part of the mitochondrial RNA editing core-like complex (RECC-like), is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA (PubMed:19465686). Specifically, catalyzes the addition of U to single-stranded RNA with a preference for a 3'-terminal U and adds the number of Us specified by a guide RNA (gRNA) to precleaved double-stranded RNA editing substrates (PubMed:19465686, PubMed:20403364). Essential for insect and bloodstream developmental forms viability (PubMed:19465686).
kcat is 0.18 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.04 min(-1) with UTP and double-stranded RNA as substrates (PubMed:19465686).
3.6 uM for UTP (with 6(U) single-stranded RNA as substrate)
1 uM for UTP (with double-stranded RNA as substrate)
Component of the mitochondrial RNA editing core complex-like (RECC-like), also known as the editosome-like complex; only a small proportion of MEAT1 associates with the complex (PubMed:19465686). Interacts with RNA-editing ligase REL1 (PubMed:19465686).
RNAi-mediated knockdown in the procyclic form causes growth arrest (PubMed:19465686). Moderately increases the abundance of mitochondrial RNAs without causing defects in RNA editing (PubMed:19465686).
The submitted sequence corresponds to a mutated form and contains an Ala residue at position 67 instead of an Asp residue.
No effect on catalytic activity. However, shows a moderate lengthening in the extension of the product at longer incubation time. Complete loss of catalytic activity; when associated with A-67; A-181; D-181; F-183; A-335 and A-345. Partial loss of catalytic activity; when associated with A-141; A-338 and R-344. No loss of catalytic activity; when associated with A-344.
Causes growth arrest of the procyclic form. Complete loss of catalytic activity; when associated with 2-N--H-25 DEL.
Partial loss of catalytic activity; when associated with 2-N--H-25 DEL.
Complete loss of catalytic activity; when associated with 2-N--H-25 DEL.
No effect on catalytic activity; when associated with 2-N--H-25 DEL.
Acts as a thiol-disulfide oxidoreductase. It is spontaneously reduced by trypanothione.
N(1),N(8)-bis(glutathionyl)spermidine reductase
Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 2-492
Ubiquinol-cytochrome-C reductase complex subunit IX, mitochondrial
This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain.
Plants bc1 complex contains 10 subunits; 3 respiratory subunits, 2 core proteins and 5 low-molecular weight proteins.
A bifunctional UMP synthase gene from Naegleria gruberi expresses OMP decarboxylase activity in bacteria and in yeast.
Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine monophosphate (UMP).
In the N-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
In the C-terminal section; belongs to the OMP decarboxylase family.
U3 SMALL NUCLEOLAR RNA-ASSOCIATED PROTEIN 11
U3 SMALL NUCLEOLAR RNA-ASSOCIATED PROTEIN 11-RELATED
Probable U3 small nucleolar RNA-associated protein 11
Involved in nucleolar processing of pre-18S ribosomal RNA.
Component of the ribosomal small subunit (SSU) processome.
V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A
Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein).
ATP-SYNT_AB DOMAIN-CONTAINING PROTEIN-RELATED
Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-416
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-344
Variant Surface Glycoprotein, subunit A, domain 2
VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
A soluble form is released from ruptured cells by the action of a PI-PLC.
Variant surface glycoprotein MITAT 1.2, VSG 221, C-terminal domain
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-381
Variant surface glycoprotein ILTAT 1.1BC
Variant surface glycoprotein MITAT 1.1000BC
NUCLEOTIDE SEQUENCE [MRNA] OF 1-59 AND 452-476
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 27-390
N-glycosylated; glycan is composed of 6 to 9 mannose residues.
VACUOLAR TRANSPORTER CHAPERONE 1-RELATED
Vacuolar transporter chaperone complex subunit 1
SPX-dependent polyphosphate polymerase VTC subunit 1
Vacuolar membrane polyphosphate polymerase accessory subunit 1
Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. VTC1 contributes only 3 transmembrane domains to the complex. The VTC complex also plays a role in vacuolar membrane fusion.
The VTC core complex is an integral membrane heterooligomer composed of at least the catalytic subunit vtc4 and the accessory subunits vtc1 and vtc2. vtc1 is a small membrane protein without hydrophilic domain. Vtc2 and vtc4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in vtc4 is the catalytic domain.
Causes an abnormal morphology of acidocalcisomes, a significant decrease in the amount of polyP and a deficient response to hyposmotic stress.
Vacuolar transporter chaperone complex subunit 4
SPX-dependent polyphosphate polymerase VTC subunit 4
Vacuolar membrane polyphosphate polymerase catalytic subunit
Component of a polyphosphate synthase complex that utilizes ATP to synthesize and translocate polyphosphate to acidocalcisomes in epimastigotes, insect-stages of Trypanosoma brucei (PubMed:24386955). Catalytic subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. The VTC complex also plays a role in vacuolar membrane fusion (By similarity). Essential for infection and parasite survival in the mammalian host (PubMed:24114837).
Activity of the enzyme is Mn(2+)-dependent and enhanced in the presence of pyrophosphate (PPi).
Localizes to acidocalcisomes of procyclic (PCF) and bloodstream (BSF) forms of T.brucei.
The SPX domain has very high affinity for inositol polyphosphates. SPX domains may integrate inositol pyrophosphates (PP-InsP)-dependent signaling to adapt cytosolic phosphate concentrations to different metabolic situations.
Is considerably less virulent in mice (PubMed:24114837). Reduces short chain polyP levels and results in accumulation of PPi (PubMed:24386955).
Component of a polyphosphate synthase complex that utilizes ATP to synthesize and translocate polyphosphate to acidocalcisomes in epimastigotes, insect-stages of Trypanosoma brucei (PubMed:24386955). Catalytic subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. The VTC complex also plays a role in vacuolar membrane fusion (By similarity). Essential for infection and parasite survival in the mammalian host (By similarity).
Results in growth defects in procyclic forms (PCF) and changes in acidocalcisome morphology and number. The mean number of acidocalcisomes drops by approximately 2-fold, but individual acidocalcisomes are considerably larger and less circular. Also affects cellular polyP and PPi content. Short chain polyP drops almost 2-fold, while PPi nearly doubles.
X92 crossreacts with PFR-antiserum (PFR = major structural protein of paraflagellar rod).
X92 most likely represents a silent open reading frame in the genome of T.brucei.
IDENTIFICATION IN A COMPLEX WITH PBP1; LSM12 AND MKT1 OR MKT1L
Forms a complex composed of at least MKT1, PBP1, XAC1 and LSM12 (PubMed:32532821). Forms a complex composed of at least MKT1L, PBP1, XAC1 and LSM12 (PubMed:32532821).
RNAi-mediated knockdown in the bloodstream form abolishes cell population growth.
GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB
ATP-dependent 3'-5' DNA helicase involved in nucleotide excision repair (NER) of damaged DNA. XPB-R is a paralog of XBP, but is not a component of the TFIIH basal transcription factor and is dispensable for RNA polymerase II transcription.
Mutants are much less tolerant than wild-type cells to UV light- and cisplatin-induced DNA damage.
Belongs to the helicase family. RAD25/XPB subfamily.
TFIIH BASAL TRANSCRIPTION FACTOR COMPLEX HELICASE XPB SUBUNIT
ATP-dependent 3'-5' DNA helicase, component of the general transcription factor IIH (TFIIH) core complex, involved in spliced leader RNA (SL RNA) gene transcription by RNA polymerase II (PubMed:17259543). TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB is required for promoter opening and promoter escape (By similarity).
Component of the 7-subunit TFIIH core complex composed of XPB, XPD, SSL1, TFB1, TFB2, TFB4 and TFB5.
Uncharacterized 1.9 kDa protein in aldolase locus
Uncharacterized 21 kDa protein in aldolase locus
Uncharacterized 22 kDa protein in aldolase locus
Uncharacterized 25.6 kDa protein in aldolase locus
Photosystem II reaction center protein Ycf12
A core subunit of photosystem II (PSII).
Seems to be required for the assembly of the photosystem I complex.
Uncharacterized 33.0 kDa protein in psbD intron 8
Uncharacterized 7.2 kDa protein in rps2-rps9 intergenic region
Uncharacterized 59.8 kDa protein in psbD intron 8
Uncharacterized 15.6 kDa protein in rps12-trnP intergenic region
Uncharacterized 20.0 kDa protein in rps12-trnP intergenic region
Uncharacterized 8.7 kDa protein in rpl22-rpl23 intergenic region
Uncharacterized 32.3 kDa protein in rbcL-atpE intergenic region
Uncharacterized 13.3 kDa protein in rpl23-rpl2 intergenic region
Uncharacterized 35.4 kDa protein in rbcL-atpE intergenic region
Uncharacterized 9.2 kDa protein in rpl23-rpl2 intergenic region
Uncharacterized 33.1 kDa protein in rbcL-atpE intergenic region
Uncharacterized 15.7 kDa protein in rpl14-rpl12 intergenic region
Uncharacterized 46.2 kDa protein in 16S rRNA 5'region
Uncharacterized 15.0 kDa protein in rpl12-rps7 intergenic region
Uncharacterized 40.9 kDa protein in 16S rRNA 3'region
Uncharacterized 66.5 kDa protein in trnI-trnV intergenic region
Uncharacterized 12.4 kDa protein in rps4-rps11 intergenic region
Uncharacterized 51.9 kDa protein in rps4-rps11 intergenic region
Uncharacterized protein in rps2-rps9 intergenic region
Belongs to the A.longa ORF167/ORF288 family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-287
Uncharacterized 34.5 kDa protein in rps12-trnP intergenic region
Uncharacterized 32.5 kDa protein in rpl14-rpl12 intergenic region
Uncharacterized 30.8 kDa protein in rpl12-rps7 intergenic region
Uncharacterized 25.9 kDa protein in rpl12-rps7 intergenic region
Uncharacterized 20.3 kDa protein in rpl12-rps7 intergenic region
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (1.0-KB KINETOPLAST)
Uncharacterized kinetoplast minicircle 201 polypeptide
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (0.98-KB KINETOPLAST)
Uncharacterized kinetoplast minicircle 51 polypeptide
SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC
SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC, CHLOROPLASTIC-RELATED
RNA-binding protein involved in regulation of mRNA stability (PubMed:23592996). Binds AU-rich regions in the 3'-UTR of mRNAs and promotes their stabilization by recruiting a MKT1-containing complex (PubMed:23592996, PubMed:24470144). Stabilizes chaperone mRNAs during stress that causes an accumulation of misfolded or unfolded proteins in the cytoplasm (PubMed:23592996, PubMed:24470144, PubMed:27002830).
Interacts (via MKT1-binding motif) with MKT1 (PubMed:23592996, PubMed:24470144). Interacts with PBP1 (via C-terminus); the interaction is direct (PubMed:23592996, PubMed:24470144).
Expressed in the procyclic form and the bloodstream form at low levels.
Induced during the response to misfolded or unfolded cytoplasmic proteins; including during thermal stress, sodium arsenite, or acidic pH (at protein level) (PubMed:23592996, PubMed:27002830). Not induced by endoplasmic reticulum stress (PubMed:27002830).
The zinc finger domain binds AU-rich regions in the 3'-UTR of mRNAs.
Phosphorylated at the N-terminus (PubMed:23592996, PubMed:27002830). CK1.2-dependent phosphorylation may lead to proteasome-dependent degradation of ZC3H11 in absence of stress (PubMed:27002830).
RNAi-mediated knockdown in the bloodstream form is lethal and causes a reduction in chaperone mRNA levels in response to heat-induced stress (PubMed:23592996). RNAi-mediated knockdown in the procyclic form causes sensitivity to cytoplasmic protein folding stress (induced by high temperature, puromycin, arsenite, MG132 or ethanol), characterized by a reduction in chaperone mRNA levels (PubMed:23592996, PubMed:27002830).
RNA-binding protein involved in regulation of mRNA stability (PubMed:31743541). Promotes mRNA stabilization by recruiting MKT1 and PBP1 (By similarity). Stabilizes mRNA required for differentiation from the bloodstream form to the procyclic form, and maintenance of the procyclic form (PubMed:31743541). Stabilizes transcripts encoding membrane and mitochondrial proteins, including AQP1 and GPEET2 procyclin (PubMed:31743541).
Interacts (via MKT1-binding motif) with MKT1.
Expressed at low levels in the bloodstream form (at protein level) (PubMed:31743541, PubMed:32532821). Expressed in the procyclic form (PubMed:31743541).
Induced during differentiation of bloodstream form to procyclic form.
RNAi-mediated knockdown causes abnormal differentiation of the bloodstream form into the procyclic form, a reduction in the expression of several mRNA including differentiation protein PAD1, and premature death (PubMed:31743541). RNAi-mediated knockdown at the procyclic stage causes a decrease in growth rate (PubMed:31743541). Simultaneous RNAi-mediated knockdown of ZC3H20 and ZC3H21 at the bloodstream stage is lethal (PubMed:31743541). Simultaneous RNAi-mediated knockdown of ZC3H20 and ZC3H21 at the procyclic stage causes a severe growth defect and a shift towards a bloodstream form (PubMed:31743541).
Abolishes MKT1 binding. Abolishes positive regulation of protein expression.
RNA-binding protein involved in regulation of mRNA stability (PubMed:31743541). Promotes mRNA stabilization by recruiting MKT1 and PBP1 (By similarity). Stabilizes transcripts encoding mitochondrial proteins (PubMed:31743541).
Induced during the differentiation of the bloodstream form to the procyclic form.
RNAi-mediated knockdown in procyclic form does not affect growth rate (PubMed:31743541). Simultaneous knockdown of ZC3H20 and ZC3H21 in the procyclic form results in a severe population growth defect and a shift towards the bloodstream form transcriptome (PubMed:31743541). Simultaneous knockdown of ZC3H20 and ZC3H21 in the bloodstream form is lethal (PubMed:31743541).