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Database: UniProt
Entry: A0A0D2BFD2_9EURO
LinkDB: A0A0D2BFD2_9EURO
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ID   A0A0D2BFD2_9EURO        Unreviewed;       321 AA.
AC   A0A0D2BFD2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Cytochrome c1, heme protein, mitochondrial {ECO:0000256|ARBA:ARBA00040084};
DE            EC=7.1.1.8 {ECO:0000256|ARBA:ARBA00012951};
DE   AltName: Full=Complex III subunit 4 {ECO:0000256|ARBA:ARBA00041779};
DE   AltName: Full=Complex III subunit IV {ECO:0000256|ARBA:ARBA00041724};
DE   AltName: Full=Cytochrome b-c1 complex subunit 4 {ECO:0000256|ARBA:ARBA00041262};
GN   ORFNames=PV08_04903 {ECO:0000313|EMBL:KIW17708.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW17708.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW17708.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW17708.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC         Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:132124; EC=7.1.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00029351};
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602326-1};
CC       Note=Binds 1 heme c group covalently per subunit.
CC       {ECO:0000256|PIRSR:PIRSR602326-1};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004434}.
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DR   EMBL; KN847494; KIW17708.1; -; Genomic_DNA.
DR   RefSeq; XP_016237924.1; XM_016379247.1.
DR   AlphaFoldDB; A0A0D2BFD2; -.
DR   STRING; 91928.A0A0D2BFD2; -.
DR   GeneID; 27331986; -.
DR   VEuPathDB; FungiDB:PV08_04903; -.
DR   HOGENOM; CLU_040334_1_1_1; -.
DR   OrthoDB; 275461at2759; -.
DR   Proteomes; UP000053328; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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; Cytochrome c-like domain; 1.
DR   Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002326; Cyt_c1.
DR   InterPro; IPR021157; Cyt_c1_TM_anchor_C.
DR   PANTHER; PTHR10266; CYTOCHROME C1; 1.
DR   PANTHER; PTHR10266:SF3; CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF02167; Cytochrom_C1; 1.
DR   PRINTS; PR00603; CYTOCHROMEC1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF81496; Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602326-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602326-1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602326-1};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        278..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          97..268
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          139..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT   BINDING         113
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT   BINDING         114
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT   BINDING         234
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
SQ   SEQUENCE   321 AA;  35330 MW;  E7B6A7E28C0BD50E CRC64;
     MLATSAIRSA PLRTAARTVV RRTTTRAASS SSSEASSSPF YITAGASAAT AATVGSIAWY
     YHLFGQDAYA MTPAEEGLHP TQYPWEHTKW NKTFDHAALR RGFQVYQEVC AACHSLKRIP
     YRSLVGTFMT VDEAKALAEE NEYDTEPNDE GEIEKRPGKL SDYLPSPYKN DEAARAANNG
     ALPPDLSLIV KARHGGCNYI FSLLTGYPEE PPAGATVQSG LNFNPYFPGT GIAMARVLYD
     GLVEYPDGTP ATTSQMAKDV VEFLNWTAEP EMDDRKKMGM KVMIIGVALL AISGWVKRYK
     WSPIKTRKLV YNPPLEGRGR R
//
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