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CYC6_GRATL
ID   CYC6_GRATL              Reviewed;         108 AA.
AC   Q6B941;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Cytochrome c6 {ECO:0000255|HAMAP-Rule:MF_00594};
DE   AltName: Full=Cytochrome c-553 {ECO:0000255|HAMAP-Rule:MF_00594};
DE   AltName: Full=Cytochrome c553 {ECO:0000255|HAMAP-Rule:MF_00594};
DE   AltName: Full=Soluble cytochrome f {ECO:0000255|HAMAP-Rule:MF_00594};
DE   Flags: Precursor;
GN   Name=petJ {ECO:0000255|HAMAP-Rule:MF_00594}; OrderedLocusNames=Grc000012;
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: Functions as an electron carrier between membrane-bound
CC       cytochrome b6-f and photosystem I in oxygenic photosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00594}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00594}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC       {ECO:0000255|HAMAP-Rule:MF_00594}.
CC   -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00594}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00594}.
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DR   EMBL; AY673996; AAT79594.1; -; Genomic_DNA.
DR   RefSeq; YP_063519.1; NC_006137.1.
DR   AlphaFoldDB; Q6B941; -.
DR   SMR; Q6B941; -.
DR   GeneID; 2944073; -.
DR   GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.760.10; -; 1.
DR   HAMAP; MF_00594; Cytc_PetJ; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR023655; Cyt_C6.
DR   InterPro; IPR008168; Cyt_C_IC.
DR   PANTHER; PTHR34688; PTHR34688; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Electron transport; Heme; Iron; Metal-binding; Photosynthesis;
KW   Plastid; Signal; Thylakoid; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00594"
FT   CHAIN           24..108
FT                   /note="Cytochrome c6"
FT                   /id="PRO_0000275347"
FT   BINDING         37
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00594"
FT   BINDING         40
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00594"
FT   BINDING         41
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00594"
FT   BINDING         81
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00594"
SQ   SEQUENCE   108 AA;  11814 MW;  20D9FC01F8B51337 CRC64;
     MRLLFAFFII CHIFTNNVQL TFAADLDAGE QIFSANCSAC HANGNNAIMP DKTLKSDALS
     ENKMNSIEAI TNQVKNGKNA MPAFGGRLAD EDIENVANYV LNKSENGW
 
 
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