CYC_WICAO
ID CYC_WICAO Reviewed; 109 AA.
AC P00042;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cytochrome c;
OS Wickerhamomyces anomalus (Yeast) (Hansenula anomala).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=4927;
RN [1]
RP PROTEIN SEQUENCE, AND METHYLATION AT LYS-61; LYS-78 AND LYS-79.
RX PubMed=6269851; DOI=10.1111/j.1432-1033.1981.tb06400.x;
RA Becam A.-M., Lederer F.;
RT "Amino-acid sequence of the cytochrome c from the yeast Hansenula anomala.
RT Identification of three methylated positions.";
RL Eur. J. Biochem. 118:295-302(1981).
CC -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome
CC c heme group can accept an electron from the heme group of the
CC cytochrome c1 subunit of cytochrome reductase. Cytochrome c then
CC transfers this electron to the cytochrome oxidase complex, the final
CC protein carrier in the mitochondrial electron-transport chain.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC associated with the inner membrane.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC November 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/076";
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DR PIR; A00035; CCHQ.
DR AlphaFoldDB; P00042; -.
DR SMR; P00042; -.
DR iPTMnet; P00042; -.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002327; Cyt_c_1A/1B.
DR PANTHER; PTHR11961; PTHR11961; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Methylation; Mitochondrion; Respiratory chain; Transport.
FT CHAIN 1..109
FT /note="Cytochrome c"
FT /id="PRO_0000108325"
FT BINDING 20
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:6269851"
FT BINDING 23
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:6269851"
FT BINDING 24
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 86
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT MOD_RES 61
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:6269851"
FT MOD_RES 61
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:6269851"
FT MOD_RES 78
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:6269851"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:6269851"
SQ SEQUENCE 109 AA; 12064 MW; 49CDCB05D9EDBCBB CRC64;
PAPFKKGSEK KGATLFKTRC LQCHTVEKGG PHKVGPNLHG IFGRQSGKAE GYSYTDANIK
KAVEWSEQTM SDYLENPKKY IPGTKMAFGG LKKEKDRNDL VTYLANATK