NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
P-loop containing nucleotide triphosphate hydrolases
ABC TRANSPORTER I FAMILY MEMBER 6, CHLOROPLASTIC
P-loop containing nucleoside triphosphate hydrolases
Probable ATP-dependent transporter ycf16
Belongs to the ABC transporter superfamily. Ycf16 family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Belongs to the acyl carrier protein (ACP) family.
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.
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).
N-terminal domain of the delta subunit of the F1F0-ATP synthase
ATP SYNTHASE SUBUNIT DELTA, CHLOROPLASTIC
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.
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
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). CF(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.
Belongs to the ATPase delta chain family.
F0F1 ATP synthase delta/epsilon subunit, N-terminal
ATP SYNTHASE EPSILON CHAIN, CHLOROPLASTIC
Epsilon subunit of F1F0-ATP synthase N-terminal domain
Produces ATP from ADP in the presence of a proton gradient 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.
Belongs to the ATPase epsilon chain family.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
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).
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
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.
AAA-TYPE ATPASE FAMILY PROTEIN / ANKYRIN REPEAT FAMILY PROTEIN
Seems to be necessary for the expression of RuBisCO.
CYTOCHROME C BIOGENESIS PROTEIN CCS1, CHLOROPLASTIC
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Belongs to the CcmF/CycK/Ccl1/NrfE/CcsA family.
CHLOROPLAST ENVELOPE MEMBRANE PROTEIN-RELATED
May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts.
Necessary for the expression of RuBisCO.
TCP-1-like chaperonin intermediate domain
60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.
Belongs to the chaperonin (HSP60) family.
Ferredoxin thioredoxin reductase (FTR), catalytic beta chain
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.
ATP-dependent Clp protease ATP-binding subunit ClpA homolog
May interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast.
Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Binds 1 heme c group covalently per subunit.
Part of the oxygen-evolving complex of photosystem II.
Associated with photosystem II at the lumenal side of the thylakoid membrane.
Belongs to the cytochrome c family. PsbV subfamily.
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 groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently.
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.
Cytochrome f subunit of the cytochrome b6f complex, transmembrane anchor
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).
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
Belongs to the bacterial histone-like protein family.
This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.
Belongs to the helicase family. DnaB subfamily.
Probable replicative DNA helicase, 1st part
Probable replicative DNA helicase, 2nd part
Heat shock protein 70kD (HSP70), C-terminal subdomain
Heat shock protein 70kD (HSP70), peptide-binding domain
Belongs to the heat shock protein 70 family.
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.
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.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Forms a complex with heterodimeric ferredoxin-thioredoxin reductase (FTR) and thioredoxin.
Belongs to the 2Fe2S plant-type ferredoxin family.
Ferredoxin thioredoxin reductase catalytic beta subunit
FERREDOXIN-THIOREDOXIN REDUCTASE CATALYTIC CHAIN, CHLOROPLASTIC
Ferredoxin-thioredoxin reductase, catalytic chain
Ferredoxin-thioredoxin reductase subunit B
Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
Heterodimer of subunit A (variable subunit) and subunit B (catalytic subunit). Heterodimeric FTR forms a complex with ferredoxin and thioredoxin (By similarity).
Belongs to the ferredoxin thioredoxin reductase beta subunit family.
Increases the nucleophilicity of the active site Cys
ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1
Acts as a processive, ATP-dependent zinc metallopeptidase.
In the central section; belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.
GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2, CYTOSOLIC
Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
Glyceraldehyde-3-phosphate dehydrogenase, chloroplastic
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
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.
Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae.
HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED
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.
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.
Thiamin diphosphate-binding fold (THDP-binding)
Acetohydroxy-acid synthase large subunit
Binds 1 thiamine pyrophosphate per subunit.
ACETOLACTATE SYNTHASE SMALL SUBUNIT 2, CHLOROPLASTIC
Acetohydroxy-acid synthase small subunit
Belongs to the acetolactate synthase small subunit family.
SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED
Putative septum site-determining protein MinD
ATPase required for the correct placement of the division site.
Belongs to the ParA family. MinD subfamily.
Cell division topological specificity factor MinE
Cell division protein MinE topological specificity domain
Putative cell division topological specificity factor
Prevents the cell division inhibition by proteins minC and minD at internal division sites while permitting inhibition at polar sites.
YVTN repeat-like/Quinoprotein amine dehydrogenase
PHOTOSYSTEM II STABILITY/ASSEMBLY FACTOR HCF136, CHLOROPLASTIC
Oligoxyloglucan reducing end-specific cellobiohydrolase
Essential for photosystem II (PSII) biogenesis; required for assembly of an early intermediate in PSII assembly that includes D2 (psbD) and cytochrome b559.
A 7-bladed beta-propeller torus, about 54 by 55 Angstroms, with a depth of about 25 Angstroms and a central pore.
a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
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.
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. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
PetN subunit of the cytochrome b6f complex
Non-globular alpha+beta subunits of globular proteins
Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.
Heterotetramer of 2 different alpha chains and 2 identical beta chains. The subunit composition could comprise of any combination of 2 out of 4 different alpha units with an invariant beta unit (By similarity).
Contains one covalently linked 15,16-dihydrobiliverdin chromophore.
The light-harvesting system in Cryptophytes contains phycobiliprotein complexes. Unusually they are composed of either phycoerythrin (CPE) or phycocyanin (CPC) but never allophycocyanin (APC), with only one type of biliprotein being present in any one species. Unlike cyanobacteria or red algae these proteins are not arranged into higher-order phycobilisome complexes, and they are found in the thylakoid lumen.
Nuclear-encoded genes of phycoerythrin alpha subunits.
X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 38-104 IN COMPLEX WITH CPEA2; CPEA3 AND 15,16-DIHYDROBILIVERDIN
X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 38-104 IN COMPLEX WITH CPEA2; CPEA3 AND 15,16-DIHYDROBILIVERDIN
Phycoerythrin alpha-2 chain, chloroplastic
Heterotetramer of 2 different alpha chains and 2 identical beta chains. The subunit composition could comprise of any combination of 2 out of 4 different alpha units with an invariant beta unit.
X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 53-128 IN COMPLEX WITH CPEA2; CPEB AND 15,16-DIHYDROBILIVERDIN
X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 53-128 IN COMPLEX WITH CPEA2; CPEB AND 15,16-DIHYDROBILIVERDIN
Phycoerythrin alpha-3 chain, chloroplastic
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 53-132 IN COMPLEX WITH 15,16-DIHYDROBILIVERDIN; MESOBILIVERDIN AND PHYCOCYANOBILIN
Heterotetramer of 2 different alpha chains and 2 identical beta chains which form 2 alpha-beta heterodimers within the heterotetramer.
Contains two phycocyanobilin chromophores, one mesobiliverdin chromophore and one 15,16-dihydrobiliverdin chromophore with binding mediated by both the alpha and beta subunits.
Contains one phycocyanobilin chromophore, one mesobiliverdin chromophore and one 15,16-dihydrobiliverdin chromophore with binding mediated by both the alpha and beta subunits.
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 48-114 IN COMPLEX WITH PHYCOERYTHROBILIN
Heterotetramer of 2 different alpha chains and 2 identical beta chains which form 2 alpha-beta heterodimers within the heterotetramer. The two alpha-beta heterodimers are rotated to an open configuration in contrast to the closed configuration found in other cryptophyte species due to the insertion of a single amino acid, Asp-65, in a conserved region of the alpha chain. In the open form, the central chromophores are not in physical contact but are separated by a water-filled channel.
Contains three phycoerythrobilin chromophores with binding mediated by both the alpha and beta subunits.
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 48-109 IN COMPLEX WITH PHYCOCYANOBILIN
Heterotetramer of 2 identical alpha chains and 2 identical beta chains which form 2 alpha-beta heterodimers within the heterotetramer. The two alpha-beta heterodimers are rotated to an open configuration in contrast to the closed configuration found in other cryptophyte species due to the insertion of a single amino acid, Asp-65, in a conserved region of the alpha chain. In the open form, the central chromophores are not in physical contact but are separated by a water-filled channel.
Contains three phycocyanobilin chromophores with binding mediated by both the alpha and beta subunits.
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 53-132 IN COMPLEX WITH MESOBILIVERDIN AND PHYCOCYANOBILIN
Contains two phycocyanobilin chromophores and one mesobiliverdin chromophore with binding mediated by both the alpha and beta subunits.
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 48-109 IN COMPLEX WITH PHYCOERYTHROBILIN
Contains one phycocyanobilin chromophore and one mesobiliverdin chromophore with binding mediated by both the alpha and beta subunits.
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH 15,16-DIHYDROBILIVERDIN; MESOBILIVERDIN AND PHYCOCYANOBILIN
PHYCOBILISOME 32.1 KDA LINKER POLYPEPTIDE, PHYCOCYANIN-ASSOCIATED, ROD 2-RELATED
CHROMOPHORE BINDING AT CYS-50; CYS-61; CYS-82 AND CYS-158
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.
Heterotetramer of one alpha-1, one alpha-2, and two beta chains.
Contains three covalently linked bilin chromophores.
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH 15,16-DIHYDROBILIVERDIN AND PHYCOERYTHROBILIN
Heterotetramer of 2 different alpha chains and 2 identical beta chains which form 2 alpha-beta heterodimers within the heterotetramer. The two alpha-beta heterodimers are rotated to an open configuration in contrast to the closed configuration found in other cryptophyte species due to the insertion of a single amino acid, 'Asp-65', in a conserved region of the alpha chain. In the open form, the central chromophores are not in physical contact but are separated by a water-filled channel.
Contains three phycoerythrobilin chromophores and one 15,16-dihydrobiliverdin chromophore with binding of the phycoerythrobilin chromophores mediated by both the alpha and beta subunits.
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH 15,16-DIHYDROBILIVERDIN AND PHYCOCYANOBILIN
Heterotetramer of 2 identical alpha chains and 2 identical beta chains which form 2 alpha-beta heterodimers within the heterotetramer. The two alpha-beta heterodimers are rotated to an open configuration in contrast to the closed configuration found in other cryptophyte species due to the insertion of a single amino acid, 'Asp-65', in a conserved region of the alpha chain. In the open form, the central chromophores are not in physical contact but are separated by a water-filled channel.
Contains three phycocyanobilin chromophores and one 15,16-dihydrobiliverdin chromophore with binding of the phycocyanobilin chromophores mediated by both the alpha and beta subunits.
X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH CPEA2; CPEA3 AND PHYCOERYTHROBILIN
X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) IN COMPLEX WITH CPEA2; CPEA3 AND PHYCOERYTHROBILIN
Heterotetramer of 2 different alpha chains and 2 identical beta chains. The subunit composition could comprise any combination of 2 out of 4 different alpha units with an invariant beta unit.
Contains three covalently linked phycoerythrobilin chromophores.
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 PsaD, reaction center subunit II
PHOTOSYSTEM I REACTION CENTER SUBUNIT II
PHOTOSYSTEM I REACTION CENTER SUBUNIT II-1, CHLOROPLASTIC-RELATED
PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center.
PHOTOSYSTEM I REACTION CENTER SUBUNIT IV A, CHLOROPLASTIC-RELATED
Photosystem I reaction center subunit IV
Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Photosystem I PsaF, reaction centre subunit III
PHOTOSYSTEM I REACTION CENTER SUBUNIT III, CHLOROPLASTIC
Subunit III of photosystem I reaction centre, PsaF
Photosystem I reaction center subunit III
Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI.
PHOTOSYSTEM I REACTION CENTER SUBUNIT VIII
Subunit VIII of photosystem I reaction centre, PsaI
May help in the organization of the PsaL subunit.
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.
Photosystem I reaction center subunit X, PsaK
Photosystem I reaction center subunit PsaK
Photosystem I PsaL, reaction centre subunit XI
PHOTOSYSTEM I REACTION CENTER SUBUNIT XI, CHLOROPLASTIC
Photosystem I reaction center subunit XI, PsaL
Photosystem I reaction center subunit XI
Subunit XII of photosystem I reaction centre, PsaM
Photosystem I reaction center subunit XII
PHOTOSYSTEM II REACTION CENTER PSB28 PROTEIN, CHLOROPLASTIC
Photosystem II reaction center Psb28 protein
Photosystem II reaction center W protein
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/PsbA) 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-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.
C-terminally processed by CTPA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth.
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.
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/PsbA) 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
PHOTOSYSTEM II REACTION CENTER PROTEIN J
Photosystem II reaction center protein J, PsbJ
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.
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 X protein
Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.
PSII consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. PSII forms dimeric complexes.
Belongs to the PsbX family. Type 1 subfamily.
Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II.
PHOTOSYSTEM II REACTION CENTER PROTEIN Z
Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Associated with the photosystem II complex.
Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Probable RuBisCO transcriptional regulator
Trans-acting transcriptional regulator of RuBisCO genes (rbcL and rbcS) expression.
Belongs to the LysR transcriptional regulatory family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 470-488
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.
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 1-46
Ribulose bisphosphate carboxylase, small subunit
RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC
RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT
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. Although the small subunit is not catalytic it is essential for maximal activity.
Heterohexadecamer of 8 large and 8 small subunits.
In this alga, in contrast to plants, the small subunit is encoded in the chloroplast.
Belongs to the RuBisCO small chain family.
Ribosomal protein L11, C-terminal domain
Ribosomal protein L11/L12, N-terminal domain
39S RIBOSOMAL PROTEIN L11, MITOCHONDRIAL
50S ribosomal protein L11, chloroplastic
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Belongs to the universal ribosomal protein uL11 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.
39S RIBOSOMAL PROTEIN L13, MITOCHONDRIAL
50S ribosomal protein L13, chloroplastic
Belongs to the universal ribosomal protein uL13 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.
39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL
50S ribosomal protein L18, chloroplastic
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 uL18 family.
39S RIBOSOMAL PROTEIN L19, MITOCHONDRIAL
50S ribosomal protein L19, chloroplastic
Belongs to the bacterial ribosomal protein bL19 family.
Binds directly to 23S rRNA. Might be involved in E site tRNA release (Potential).
Belongs to the universal ribosomal protein uL1 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.
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.
50S RIBOSOMAL PROTEIN L21, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL21 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.
RIBOSOMAL_L23EN DOMAIN-CONTAINING PROTEIN
50S ribosomal protein L23, chloroplastic
Belongs to the universal ribosomal protein uL23 family.
50S RIBOSOMAL PROTEIN L24, CHLOROPLASTIC
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Belongs to the universal ribosomal protein uL24 family.
39S RIBOSOMAL PROTEIN L27, MITOCHONDRIAL
50S ribosomal protein L27, chloroplastic
Belongs to the bacterial ribosomal protein bL27 family.
50S RIBOSOMAL PROTEIN L29, CHLOROPLASTIC
60S RIBOSOMAL PROTEIN L35/50S RIBOSOMAL PROTEIN L29
Belongs to the universal ribosomal protein uL29 family.
Belongs to the universal ribosomal protein uL2 family.
50S RIBOSOMAL PROTEIN L31, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.
50S ribosomal protein L32, chloroplastic
Belongs to the bacterial ribosomal protein bL32 family.
50S RIBOSOMAL PROTEIN L33, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL33 family.
50S ribosomal protein L34, chloroplastic
Belongs to the bacterial ribosomal protein bL34 family.
50S ribosomal protein L35, chloroplastic
Belongs to the bacterial ribosomal protein bL35 family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13
50S ribosomal protein L36, chloroplastic
Belongs to the bacterial ribosomal protein bL36 family.
50S RIBOSOMAL PROTEIN L3-1, CHLOROPLASTIC
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Belongs to the universal ribosomal protein uL3 family.
Belongs to the universal ribosomal protein uL4 family.
Belongs to the universal ribosomal protein uL5 family.
Belongs to the universal ribosomal protein uL6 family.
Involved in intercistronic processing of primary transcripts from chloroplast operons. The endonucleolytic activity of the enzyme depends on the number of phosphates at the 5' end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences.
5' to 3' exonuclease, C-terminal subdomain
DNA-directed RNA polymerase, insert domain
C-terminal domain of RNA polymerase alpha subunit
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.
The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Belongs to the RNA polymerase alpha chain family.
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
beta and beta-prime subunits of DNA dependent RNA-polymerase
Plastid-encoded RNA polymerase subunit beta
Belongs to the RNA polymerase beta chain family.
DNA-directed RNA polymerase subunit beta'
Plastid-encoded RNA polymerase subunit beta'
Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.
DNA-directed RNA polymerase subunit beta''
Plastid-encoded RNA polymerase subunit beta''
Belongs to the RNA polymerase beta' chain family. RpoC2 subfamily.
Putative DNA-directed RNA polymerase subunit omega
Plastid-encoded RNA polymerase omega subunit
May be involved in RNA polymerase activity.
Belongs to the RNA polymerase subunit omega family.
37S RIBOSOMAL PROTEIN S10, MITOCHONDRIAL
30S ribosomal protein S10, chloroplastic
Involved in the binding of tRNA to the ribosomes.
Belongs to the universal ribosomal protein uS10 family.
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.
28S RIBOSOMAL PROTEIN S12, MITOCHONDRIAL
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.
30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18
37S RIBOSOMAL PROTEIN SWS2, MITOCHONDRIAL
30S ribosomal protein S13, chloroplastic
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA.
Belongs to the universal ribosomal protein uS13 family.
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 S16, MITOCHONDRIAL
30S ribosomal protein S16, chloroplastic
Belongs to the bacterial ribosomal protein bS16 family.
37S RIBOSOMAL PROTEIN S17, MITOCHONDRIAL
30S ribosomal protein S17, chloroplastic
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS17 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 S20, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bS20 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.
With S4 and S12 plays an important role in translational accuracy.
Part of the 30S ribosomal subunit. Contacts protein S4 (By similarity).
The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
Belongs to the universal ribosomal protein uS5 family.
Binds together with S18 to 16S ribosomal RNA.
Belongs to the bacterial ribosomal protein bS6 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.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-134
Belongs to the universal ribosomal protein uS9 family.
30S RIBOSOMAL PROTEIN 3-1, CHLOROPLASTIC
Probable 30S ribosomal protein 3, chloroplastic
Probably a ribosomal protein or a ribosome-associated protein.
Belongs to the chloroplast-specific ribosomal protein cS23 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.
Protein transport protein Sec61 subunit alpha
Appears to play a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins.
Heterotrimeric complex composed of SEC61-alpha, SEC61-beta and SEC61-gamma.
Helical scaffold and wing domains of SecA
SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM
Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
A minor fraction is associated with the chloroplast thylakoid membrane.
Probable protein-export membrane protein secG
Involved in protein export. Participates in an early event of protein translocation across the chloroplast thylakoid membrane (Potential).
PREPROTEIN TRANSLOCASE SUBUNIT SCY2, CHLOROPLASTIC
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Component of the plastid Sec protein translocase complex, which is composed of at least SecY, SecE and SecG.
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug.
Component of the plastid Sec protein translocase complex, which is composed of at least SecY and SecE.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-412
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.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-402
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-411
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
Photosystem II reaction center protein Ycf12
A core subunit of photosystem II (PSII).
Possible role in chlorophyll and/or carotenoid binding.
PROTEIN COFACTOR ASSEMBLY OF COMPLEX C SUBUNIT B CCB3, CHLOROPLASTIC-RELATED
UPF0051 PROTEIN ABCI8, CHLOROPLASTIC-RELATED
Probable transcriptional regulator ycf27
Probable promoter-specific protein mediating the interaction between DNA and RNA polymerase.
HTH-TYPE TRANSCRIPTIONAL REGULATOR YHJB-RELATED
Probable transcriptional regulator ycf29
PROTEIN CONSERVED IN THE GREEN LINEAGE AND DIATOMS 27, CHLOROPLASTIC
PROTEIN HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 244, CHLOROPLASTIC
Belongs to the NmrA-type oxidoreductase family. Ycf39 subfamily.
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
LIPA AND NB-ARC DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_3G14650)
TETRATRICOPEPTIDE REPEAT PROTEIN (AFU_ORTHOLOGUE AFUA_6G03870)
SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC
SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC, CHLOROPLASTIC-RELATED
Uncharacterized AAA domain-containing protein ycf46
Belongs to the AAA ATPase family. Highly divergent.
Seems to be required for the assembly of the photosystem I complex.