ID   CYF_TRICV               Reviewed;         314 AA.
AC   P49476;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Cytochrome f;
DE   Flags: Precursor;
GN   Name=petA;
OS   Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC   Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX   NCBI_TaxID=1514140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kowallik K.V., Stoebe B., Schaffran I., Kroth-Pancic P., Freier U.;
RT   "The chloroplast genome of a chlorophyll a+c-containing alga, Odontella
RT   sinensis.";
RL   Plant Mol. Biol. Rep. 13:336-342(1995).
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:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 heme group covalently. {ECO:0000250};
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:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
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DR   EMBL; Z67753; CAA91736.1; -; Genomic_DNA.
DR   PIR; S78363; S78363.
DR   AlphaFoldDB; P49476; -.
DR   SMR; P49476; -.
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; Signal; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..314
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000023823"
FT   TRANSMEM        280..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         31
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:0000250"
FT   BINDING         51
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
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:0000250"
SQ   SEQUENCE   314 AA;  33855 MW;  CD3131391B584462 CRC64;
     MATNKFFKSL LFTLTIAISL FGLSIENSSA YPVFAQQGYS NPRAANGKLA CANCHLNQKA
     IEIEAPQAVL PNSVFEVTVK VPYDTTRQQV GANGKKADLN VGGIVILPKG FKLAAKNQIP
     AEVKAKNKGV FISPYSTEFD NILIVGPIAG KTHQELIFPV VSPDPEKDSD VKYLTYPLYA
     GGNRGRGQVY PTGEKSNINS FGAVQAGQIS EITTSEKGES NITIINSDGV KTSQIIPAGL
     TLTVKQGDSV KVDQSLNIDP NVGGFGQEET EIVLQNPLRI IGYLGFCFCV LLTQVLLIIK
     KKQFEKVQAA ELNF