ID   CYF_CERDE               Reviewed;         320 AA.
AC   A8SEB6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE   Flags: Precursor;
GN   Name=petA {ECO:0000255|HAMAP-Rule:MF_00610};
OS   Ceratophyllum demersum (Rigid hornwort) (Coontail).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ceratophyllales; Ceratophyllaceae;
OC   Ceratophyllum.
OX   NCBI_TaxID=4428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18048334; DOI=10.1073/pnas.0708072104;
RA   Moore M.J., Bell C.D., Soltis P.S., Soltis D.E.;
RT   "Using plastid genome-scale data to resolve enigmatic relationships among
RT   basal angiosperms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19363-19368(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF614270; ABQ81463.1; -; Genomic_DNA.
DR   RefSeq; YP_001542460.1; NC_009962.1.
DR   AlphaFoldDB; A8SEB6; -.
DR   SMR; A8SEB6; -.
DR   PRIDE; A8SEB6; -.
DR   GeneID; 5729405; -.
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..35
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   CHAIN           36..320
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000342052"
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;  35323 MW;  F956EC2ACF0724EC CRC64;
     MQNRNTFSWV KDQMSRFISV SIMIYVITRT SISNAYPIFA QQGYENPREA TGRIVCANCH
     LANKPVDIEV PQAVLPDTVF EAVVRIPYDM QLKQVLANGK KGGLNVGAVL ILPEGFELAP
     PDRISPEMKE KIGNLSFQSY RPNKKNILIM GPVPGKKYSQ IVFPILSPDP ATKKDVHFLK
     YPIYVGGNRG RGQIYPDGSK SNNTVYNATA TGIVSKIVRK EKGGYEITIA DTADGHQVVD
     IIPPGPELLV SEGESIKIDQ PLTSNPNVGG FGQGDAEIVL QDPLRVQGLL FFFASVILAQ
     IFLVLKKKQF EKVQLSEMNF