ID   CYF_VITVI               Reviewed;         320 AA.
AC   Q0ZJ07;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE   Flags: Precursor;
GN   Name=petA {ECO:0000255|HAMAP-Rule:MF_00610};
OS   Vitis vinifera (Grape).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Maxxa;
RX   PubMed=16603088; DOI=10.1186/1471-2148-6-32;
RA   Jansen R.K., Kaittanis C., Lee S.-B., Saski C., Tomkins J., Alverson A.J.,
RA   Daniell H.;
RT   "Phylogenetic analyses of Vitis (Vitaceae) based on complete chloroplast
RT   genome sequences: effects of taxon sampling and phylogenetic methods on
RT   resolving relationships among rosids.";
RL   BMC Evol. Biol. 6:32-32(2006).
CC   -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC       electron transfer between photosystem II (PSII) and photosystem I
CC       (PSI), cyclic electron flow around PSI, and state transitions.
CC       {ECO:0000255|HAMAP-Rule:MF_00610}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00610};
CC       Note=Binds 1 heme group covalently. {ECO:0000255|HAMAP-Rule:MF_00610};
CC   -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC       cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and
CC       the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and
CC       PetN. The complex functions as a dimer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00610}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00610}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000255|HAMAP-
CC       Rule:MF_00610}.
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DR   EMBL; DQ424856; ABE47547.1; -; Genomic_DNA.
DR   RefSeq; YP_567089.1; NC_007957.1.
DR   AlphaFoldDB; Q0ZJ07; -.
DR   SMR; Q0ZJ07; -.
DR   STRING; 29760.VIT_11s0016g02030.t01; -.
DR   PRIDE; Q0ZJ07; -.
DR   EnsemblPlants; Vitvi00g04187_t001; Vitvi00g04187_P001; Vitvi00g04187.
DR   GeneID; 4025050; -.
DR   Gramene; Vitvi00g04187_t001; Vitvi00g04187_P001; Vitvi00g04187.
DR   KEGG; vvi:4025050; -.
DR   eggNOG; ENOG502QPT8; Eukaryota.
DR   InParanoid; Q0ZJ07; -.
DR   OrthoDB; 826802at2759; -.
DR   Proteomes; UP000009183; Chloroplast.
DR   ExpressionAtlas; Q0ZJ07; baseline and differential.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031361; C:integral component of thylakoid membrane; IEA:InterPro.
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; 2.60.40.830; -; 1.
DR   HAMAP; MF_00610; Cytb6_f_cytF; 1.
DR   InterPro; IPR024058; Cyt-f_TM.
DR   InterPro; IPR002325; Cyt_f.
DR   InterPro; IPR024094; Cyt_f_lg_dom.
DR   InterPro; IPR036826; Cyt_f_lg_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF01333; Apocytochr_F_C; 1.
DR   Pfam; PF16639; Apocytochr_F_N; 1.
DR   PRINTS; PR00610; CYTOCHROMEF.
DR   SUPFAM; SSF103431; SSF103431; 1.
DR   SUPFAM; SSF49441; SSF49441; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   PROSITE; PS51010; CYTF; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Photosynthesis; Plastid; Reference proteome; Signal; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   CHAIN           36..320
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000275459"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         36
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         56
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         59
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         60
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
SQ   SEQUENCE   320 AA;  35318 MW;  AFF38A881C4619B1 CRC64;
     MQTRNTFSWI KEQITRSISV SLMIYIITRT SISNAYPIFA QQGYENPREA TGRIVCANCH
     LANKPVDIEV PQAVLPDTVF EAVVRIPYDM QMKQVLANGK RGALNVGAVL ILPEGFELAP
     PDRISPEMKE KIGNLSFQNY RPTKKNILVI GPVPGQKYSE ITFPILSPDP ATKKDVHFLK
     YPIYVGGNRG RGQIYPDGSK SNNTVYNATA AGIVSKIIRK EKGGYEITIA DASDGRQVVD
     IIPPGPELLV SEGESIKLDQ PLTSNPNVGG FGQGDAEIVL QDPLRIQGLL FFLSSVILAQ
     IFLVLKKKQF EKVQLSEMNF