ID   CYC_THELA               Reviewed;         111 AA.
AC   P00047;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Cytochrome c;
OS   Thermomyces lanuginosus (Humicola lanuginosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Thermomyces.
OX   NCBI_TaxID=5541;
RN   [1]
RP   PROTEIN SEQUENCE, AND METHYLATION AT LYS-80 AND LYS-94.
RC   STRAIN=ATCC 16455 / CBS 632.91;
RX   PubMed=4342602; DOI=10.1016/s0021-9258(19)44728-5;
RA   Morgan W.T., Hensley C.P. Jr., Riehm J.P.;
RT   "Proteins of the thermophilic fungus Humicola lanuginosa. I. Isolation and
RT   amino acid sequence of a cytochrome C.";
RL   J. Biol. Chem. 247:6555-6565(1972).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-37.
RX   PubMed=4363050; DOI=10.1016/0006-291x(74)90844-4;
RA   Lederer F., Simon A.M.;
RT   "Neurospora crassa and Humicola lanuginosa cytochromes c: more homology in
RT   the heme region.";
RL   Biochem. Biophys. Res. Commun. 56:317-323(1974).
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   -!- PTM: Lys-94 was found to be 95% trimethylated.
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; A92114; CCHL.
DR   AlphaFoldDB; P00047; -.
DR   SMR; P00047; -.
DR   iPTMnet; P00047; -.
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..111
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000108334"
FT   BINDING         22
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:4342602"
FT   BINDING         25
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:4342602"
FT   BINDING         26
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         88
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         80
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:4342602"
FT   MOD_RES         94
FT                   /note="N6,N6,N6-trimethyllysine; partial"
FT                   /evidence="ECO:0000269|PubMed:4342602"
FT   CONFLICT        11..12
FT                   /note="AS -> SA (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24
FT                   /note="Q -> E (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27..34
FT                   /note="SVEQGGAN -> GEGANVSQ (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   111 AA;  12076 MW;  123501124E3CF317 CRC64;
     AKGGSFEPGD ASKGANLFKT RCAQCHSVEQ GGANKIGPNL HGLFGRKTGS VEGYSYTDAN
     KQAGITWNED TLFEYLENPK KFIPGTKMAF GGLKKNKDRN DLITYLKEAT K