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PSBI_GRATL
ID   PSBI_GRATL              Reviewed;          38 AA.
AC   Q6B8Q2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Photosystem II reaction center protein I {ECO:0000255|HAMAP-Rule:MF_01316};
DE            Short=PSII-I {ECO:0000255|HAMAP-Rule:MF_01316};
DE   AltName: Full=PSII 4.8 kDa protein {ECO:0000255|HAMAP-Rule:MF_01316};
GN   Name=psbI {ECO:0000255|HAMAP-Rule:MF_01316}; OrderedLocusNames=Grc000152;
OS   Gracilaria tenuistipitata var. liui (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX   NCBI_TaxID=285951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA   Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT   "Comparative analysis of the complete plastid genome sequence of the red
RT   alga Gracilaria tenuistipitata var. liui provides insights into the
RT   evolution of rhodoplasts and their relationship to other plastids.";
RL   J. Mol. Evol. 59:464-477(2004).
CC   -!- FUNCTION: One of the components of the core complex of photosystem II
CC       (PSII), required for its stability and/or assembly. PSII is a light-
CC       driven water:plastoquinone oxidoreductase that uses light energy to
CC       abstract electrons from H(2)O, generating O(2) and a proton gradient
CC       subsequently used for ATP formation. It consists of a core antenna
CC       complex that captures photons, and an electron transfer chain that
CC       converts photonic excitation into a charge separation.
CC       {ECO:0000255|HAMAP-Rule:MF_01316}.
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_01316}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01316}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01316}.
CC   -!- SIMILARITY: Belongs to the PsbI family. {ECO:0000255|HAMAP-
CC       Rule:MF_01316}.
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DR   EMBL; AY673996; AAT79733.1; -; Genomic_DNA.
DR   RefSeq; YP_063658.1; NC_006137.1.
DR   AlphaFoldDB; Q6B8Q2; -.
DR   SMR; Q6B8Q2; -.
DR   GeneID; 2944005; -.
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:0009539; C:photosystem II reaction center; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01316; PSII_PsbI; 1.
DR   InterPro; IPR003686; PSII_PsbI.
DR   InterPro; IPR037271; PSII_PsbI_sf.
DR   PANTHER; PTHR35772; PTHR35772; 1.
DR   Pfam; PF02532; PsbI; 1.
DR   SUPFAM; SSF161041; SSF161041; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; Photosynthesis; Photosystem II; Plastid;
KW   Reaction center; Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..38
FT                   /note="Photosystem II reaction center protein I"
FT                   /id="PRO_0000219627"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01316"
SQ   SEQUENCE   38 AA;  4552 MW;  3549B57DA1EB875B CRC64;
     MFTLKIFVYT TVIFFVSLFF FGFLSNDPSR NPNRKDLE
 
 
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