ID   CYC_EUGVI               Reviewed;         102 AA.
AC   P22342;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Cytochrome c;
OS   Euglena viridis (Cercaria viridis).
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3040;
RN   [1]
RP   PROTEIN SEQUENCE, ACETYLATION AT GLY-1, AND METHYLATION AT LYS-85.
RC   STRAIN=LJ-1;
RX   PubMed=1645532; DOI=10.1042/bj2760047;
RA   Ambler R.P., Kamen M.D., Bartsch R.G., Meyer T.E.;
RT   "Amino acid sequences of Euglena viridis ferredoxin and cytochromes c.";
RL   Biochem. J. 276:47-52(1991).
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}.
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DR   PIR; S15454; S15454.
DR   AlphaFoldDB; P22342; -.
DR   SMR; P22342; -.
DR   iPTMnet; P22342; -.
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   Acetylation; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Metal-binding; Methylation; Mitochondrion; Respiratory chain; Transport.
FT   CHAIN           1..102
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108315"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         17
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         79
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   MOD_RES         1
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:1645532"
FT   MOD_RES         85
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:1645532"
SQ   SEQUENCE   102 AA;  11121 MW;  005A9F285C8A7AB3 CRC64;
     GDAERGKKLF ESRAGQCHSS QKGVNSTGPA LYGVYGRTSG TVPGYAYSNA NKNAAIVWED
     ESLNKFLENP KKYVPGTKMA FAGIKAKKDR LDIIAYMKTL KD