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CYF_TUPAK
ID   CYF_TUPAK               Reviewed;         329 AA.
AC   Q3ZJ66;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE   Flags: Precursor;
GN   Name=petA {ECO:0000255|HAMAP-Rule:MF_00610};
OS   Tupiella akineta (Green alga) (Pseudendoclonium akinetum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; OUU clade;
OC   Ulotrichales; Tupiellaceae; Tupiella.
OX   NCBI_TaxID=160070;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 1912;
RX   PubMed=15930151; DOI=10.1093/molbev/msi182;
RA   Pombert J.-F., Otis C., Lemieux C., Turmel M.;
RT   "The chloroplast genome sequence of the green alga Pseudendoclonium
RT   akinetum (Ulvophyceae) reveals unusual structural features and new insights
RT   into the branching order of chlorophyte lineages.";
RL   Mol. Biol. Evol. 22:1903-1918(2005).
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; AY835431; AAV80625.1; -; Genomic_DNA.
DR   RefSeq; YP_636201.1; NC_008114.1.
DR   AlphaFoldDB; Q3ZJ66; -.
DR   SMR; Q3ZJ66; -.
DR   GeneID; 4108805; -.
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..44
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   CHAIN           45..329
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000275445"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         45
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         65
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         68
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         69
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   329 AA;  36686 MW;  49CF9C61431D7727 CRC64;
     MKRNIIFLVI HQFENLTMKK KQNIFFIFLL TVFFNFTVNS NVSAYPVFAQ QGYKNPREAN
     GRIVCANCHL AQKPVELEVP QAVLPDTVFE AMVKIPYDQQ IKQVQANGKK GDLNVGMVLI
     LPEGFELAPS DRLPEEMKKK VGNLYYQPYS SEQKNILVIG PIPGKLYNEM VVPLISPNPA
     TNKNVNYLKY PIYLGGNRGR GQLYPDGSKS NNNLYNASAT GKITEITPTG KKGGFDITIQ
     TLNGETVIDK VPAGPELIVT KDQTIQVDQP LTNNPNVGGF GQAEAEIVLQ NPARVQGLII
     FLITIFITQL FLVLKKKQVE KVQLAEMNF
 
 
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