ID   CYC_THEAN               Reviewed;         115 AA.
AC   Q4UEA0;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cytochrome c;
GN   ORFNames=TA12950;
OS   Theileria annulata.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ankara;
RX   PubMed=15994557; DOI=10.1126/science.1110418;
RA   Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA   Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA   Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA   Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA   McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA   Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA   Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA   Shiels B., Tait A., Barrell B.G., Hall N.;
RT   "Genome of the host-cell transforming parasite Theileria annulata compared
RT   with T. parva.";
RL   Science 309:131-133(2005).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}.
CC       Note=Loosely associated with the inner membrane. {ECO:0000250}.
CC   -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000250}.
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   EMBL; CR940348; CAI74589.1; -; Genomic_DNA.
DR   RefSeq; XP_952321.1; XM_947228.1.
DR   AlphaFoldDB; Q4UEA0; -.
DR   SMR; Q4UEA0; -.
DR   STRING; 5874.XP_952321.1; -.
DR   GeneID; 3862479; -.
DR   KEGG; tan:TA12950; -.
DR   VEuPathDB; PiroplasmaDB:TA12950; -.
DR   eggNOG; KOG3453; Eukaryota.
DR   InParanoid; Q4UEA0; -.
DR   OMA; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   Proteomes; UP000001950; Chromosome 2.
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   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW   Reference proteome; Respiratory chain; Transport.
FT   CHAIN           1..115
FT                   /note="Cytochrome c"
FT                   /id="PRO_0000273192"
FT   BINDING         26
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         29
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         30
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         91
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"
SQ   SEQUENCE   115 AA;  12573 MW;  BFC23A603865F717 CRC64;
     MAKPEPDVVV PEGDPAKGAK LFKSKCAQCH TINKGGSVKQ GPNLFGFYGR KSGSTDYAYS
     DANKNSGIVW SDKHLFVYLV NPKQYIPGTK MVFAGLKKEQ DRADLIAYLK EASSK