CYF_ANTAG
ID CYF_ANTAG Reviewed; 322 AA.
AC Q85AR2;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cytochrome f;
DE Flags: Precursor;
GN Name=petA;
OS Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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 -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 19 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 53 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 74 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 96 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 195 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 246 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 275 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 282 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 292 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 295 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The initiator methionine is created
CC by RNA editing. The nonsense codons at positions 74, 96, 195 and 275
CC are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
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DR EMBL; AB086179; BAC55362.1; -; Genomic_DNA.
DR EMBL; AB087454; BAC55458.1; -; mRNA.
DR RefSeq; NP_777426.1; NC_004543.1.
DR AlphaFoldDB; Q85AR2; -.
DR SMR; Q85AR2; -.
DR PRIDE; Q85AR2; -.
DR GeneID; 2553510; -.
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 2: Evidence at transcript level;
KW Chloroplast; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Photosynthesis; Plastid; RNA editing; Signal; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..37
FT /evidence="ECO:0000250"
FT CHAIN 38..322
FT /note="Cytochrome f"
FT /id="PRO_0000023803"
FT TRANSMEM 285..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 38
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 58
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 62
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 322 AA; 35745 MW; BB0F5A136DB20FEF CRC64;
MQNRKTYAYD WIKKWMIKSI STLIIINTMV WSSVSEAYPI FAQQGYENPR EATGRIVCAN
CHLAKKPVDI EVPQSVLPDT VFEAVVKIPY DTQVKQVLAN GKKGALNVGA VLILPEGFEL
APSNRVPPEM KEKIGNLYFQ SYRPDKKNIL VVGPVPGKKY SEIIFPILAP NPATNKDAHF
LKYPIYVGGN RGRGQIYPDG SKSNNTVYNA STTGIIKKVL RKEKGGYEII IDNTLDGRQV
IDIVPPGPEL IISEGESIKV DQPLTNNPNV GGFGQGDAEI VLQDVLRVQG LLLFFASVIL
AQIFLVLKKK QFEKVQLAEM NF
