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PSBC_GUITH
ID   PSBC_GUITH              Reviewed;         473 AA.
AC   O78426;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Photosystem II CP43 reaction center protein {ECO:0000255|HAMAP-Rule:MF_01496};
DE   AltName: Full=PSII 43 kDa protein {ECO:0000255|HAMAP-Rule:MF_01496};
DE   AltName: Full=Protein CP-43 {ECO:0000255|HAMAP-Rule:MF_01496};
DE   Flags: Precursor;
GN   Name=psbC {ECO:0000255|HAMAP-Rule:MF_01496};
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9929392; DOI=10.1007/pl00006462;
RA   Douglas S.E., Penny S.L.;
RT   "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT   sequence and conserved synteny groups confirm its common ancestry with red
RT   algae.";
RL   J. Mol. Evol. 48:236-244(1999).
CC   -!- FUNCTION: One of the components of the core complex of photosystem II
CC       (PSII). It binds chlorophyll and helps catalyze the primary light-
CC       induced photochemical processes of PSII. PSII is a light-driven
CC       water:plastoquinone oxidoreductase, using light energy to abstract
CC       electrons from H(2)O, generating O(2) and a proton gradient
CC       subsequently used for ATP formation. {ECO:0000255|HAMAP-Rule:MF_01496}.
CC   -!- COFACTOR:
CC       Note=Binds multiple chlorophylls and provides some of the ligands for
CC       the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also
CC       provide a ligand for a Cl- that is required for oxygen evolution. PSII
CC       binds additional chlorophylls, carotenoids and specific lipids.
CC       {ECO:0000255|HAMAP-Rule:MF_01496};
CC   -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC       PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC       PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-
CC       evolving complex and a large number of cofactors. It forms dimeric
CC       complexes. {ECO:0000255|HAMAP-Rule:MF_01496}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496}; Multi-pass membrane
CC       protein {ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496}.
CC   -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01496}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC35611.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF041468; AAC35611.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_050677.2; NC_000926.1.
DR   AlphaFoldDB; O78426; -.
DR   SMR; O78426; -.
DR   GeneID; 856963; -.
DR   HOGENOM; CLU_028310_1_1_1; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   Gene3D; 1.10.10.670; -; 1.
DR   HAMAP; MF_01496; PSII_PsbC_CP43; 1.
DR   InterPro; IPR000932; PS_antenna-like.
DR   InterPro; IPR036001; PS_II_antenna-like_sf.
DR   InterPro; IPR005869; PSII_PsbC.
DR   InterPro; IPR044900; PSII_PsbC_sf.
DR   PANTHER; PTHR33180; PTHR33180; 1.
DR   Pfam; PF00421; PSII; 1.
DR   SUPFAM; SSF161077; SSF161077; 1.
DR   TIGRFAMs; TIGR01153; psbC; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chlorophyll; Chloroplast; Chromophore; Manganese; Membrane;
KW   Metal-binding; Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW   Thylakoid; Transmembrane; Transmembrane helix.
FT   PROPEP          1..14
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT                   /id="PRO_0000431220"
FT   CHAIN           15..473
FT                   /note="Photosystem II CP43 reaction center protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT                   /id="PRO_0000077515"
FT   TRANSMEM        73..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        139..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        180..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        262..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        292..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        452..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   BINDING         367
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   MOD_RES         15
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496"
FT   MOD_RES         15
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496"
SQ   SEQUENCE   473 AA;  52010 MW;  C6ACA71784D69CE6 CRC64;
     MKTLYSLRRF YHVETPFNSN VGIAGRDIES TGFAWWSGNS RLINVSGKLL GAHVAHAGLM
     VFWCGAMTLF EVAHYIPEKP LYEQGLILLP HLATLGWGVG PGGEIIDVYP YFVVGVLHLI
     SSAVLGFGGV YHSLIGPDTL EESFPAFGYD WRDKNKITTI LGIHLVILGF GALLLVIKAI
     YVGGLYDTWA PGGGDVRIID NPTLNPAVIF GYVLKSPWGG DGWIVSVNNM EDVVGGHIWI
     GFTCIAGGFW HILTKPFAWA RRAYVWSGEA YLSYSLVAVS LMAFIASQYA WYNNTVYPSE
     FYGPTGPEAS QSQAFTFLVR DQRLGASVSS AQGPTGLGKY LMRSPSGEII LGGETQRFWD
     LRAPWIEPLR GPNGLDLNKI KNDIQPWQER RAAEYMTHAP LGSLNSVGGV ATEINSVNYV
     SPRSWLTTSH FFLGFAFYIG HLWHAGRARA AAAGFEKGIN RENEPVLTLR PID
 
 
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