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CYF_ARATH
ID   CYF_ARATH               Reviewed;         320 AA.
AC   P56771;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Cytochrome f;
DE   Flags: Precursor;
GN   Name=petA; OrderedLocusNames=AtCg00540;
OS   Arabidopsis thaliana (Mouse-ear cress).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA   Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT   "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL   DNA Res. 6:283-290(1999).
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; AP000423; BAA84398.1; -; Genomic_DNA.
DR   RefSeq; NP_051072.1; NC_000932.1.
DR   AlphaFoldDB; P56771; -.
DR   SMR; P56771; -.
DR   BioGRID; 29952; 1.
DR   STRING; 3702.ATCG00540.1; -.
DR   PaxDb; P56771; -.
DR   PRIDE; P56771; -.
DR   ProteomicsDB; 240407; -.
DR   EnsemblPlants; ATCG00540.1; ATCG00540.1; ATCG00540.
DR   GeneID; 844748; -.
DR   Gramene; ATCG00540.1; ATCG00540.1; ATCG00540.
DR   KEGG; ath:ArthCp035; -.
DR   Araport; ATCG00540; -.
DR   TAIR; locus:504954677; ATCG00540.
DR   eggNOG; ENOG502QPT8; Eukaryota.
DR   HOGENOM; CLU_033498_0_0_1; -.
DR   InParanoid; P56771; -.
DR   OMA; FWAQQNY; -.
DR   OrthoDB; 826802at2759; -.
DR   PRO; PR:P56771; -.
DR   Proteomes; UP000006548; Chloroplast.
DR   ExpressionAtlas; P56771; baseline and differential.
DR   Genevisible; P56771; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0009512; C:cytochrome b6f complex; TAS:TAIR.
DR   GO; GO:0031361; C:integral component of thylakoid membrane; IEA:InterPro.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
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:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0009767; P:photosynthetic electron transport chain; TAS:TAIR.
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:0000250"
FT   CHAIN           36..320
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000023804"
FT   TRANSMEM        286..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
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:0000250"
FT   BINDING         56
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
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:0000250"
SQ   SEQUENCE   320 AA;  35357 MW;  F7D44DD5A0D708E6 CRC64;
     MQTRNTFSWI REEITRSISV SLIIYIITWA SISSAYPIFA QQNYENPREA TGRIVCANCH
     LANKPVDIEV PQTVLPDTVF EAVVKIPYDM QLKQVLANGK KGALNVGAVL ILPEGFELAP
     PDRISPEMKE KIGNLSFQNY RPNKKNILVI GPVPGQKYSE ITFPILAPDP ATNKDVHFLK
     YPIYVGGNRG RGQIYPDGSK SNNTVYNATA GGIISKILRK EKGGYEITIV DASNGREVID
     IIPRGLELLV SEGESIKLDQ PLTSNPNVGG FGQGDAEIVL QDPLRVQGLL FFLGSVVLAQ
     IFLVLKKKQF EKVQLSEMNF
 
 
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