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Database: UniProt
Entry: A0A2T9Z1G1_9FUNG
LinkDB: A0A2T9Z1G1_9FUNG
Original site: A0A2T9Z1G1_9FUNG 
ID   A0A2T9Z1G1_9FUNG        Unreviewed;       102 AA.
AC   A0A2T9Z1G1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Cytochrome c domain-containing protein {ECO:0000259|PROSITE:PS51007};
GN   ORFNames=BB559_001607 {ECO:0000313|EMBL:PVU98399.1};
OS   Furculomyces boomerangus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX   NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU98399.1, ECO:0000313|Proteomes:UP000245699};
RN   [1] {ECO:0000313|EMBL:PVU98399.1, ECO:0000313|Proteomes:UP000245699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU98399.1,
RC   ECO:0000313|Proteomes:UP000245699};
RX   PubMed=29764946;
RA   Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT   "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT   Symbiosis.";
RL   MBio 9:e00636-e00618(2018).
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       {ECO:0000256|RuleBase:RU004427}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000256|ARBA:ARBA00004569}.
CC   -!- PTM: Binds 1 heme group per subunit. {ECO:0000256|RuleBase:RU004427}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC       {ECO:0000256|ARBA:ARBA00006488, ECO:0000256|RuleBase:RU004426}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PVU98399.1}.
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DR   EMBL; MBFT01000081; PVU98399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T9Z1G1; -.
DR   STRING; 61424.A0A2T9Z1G1; -.
DR   Proteomes; UP000245699; Unassembled WGS sequence.
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; Cytochrome c-like domain; 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; CYTOCHROME C; 1.
DR   PANTHER; PTHR11961:SF12; CYTOCHROME C; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU004427};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Mitochondrion {ECO:0000256|RuleBase:RU004427};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245699};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW   ECO:0000256|RuleBase:RU004427};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU004427}.
FT   DOMAIN          3..102
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   102 AA;  10832 MW;  88E74862410738DE CRC64;
     MSGDPAKGAK LFKTRCATCH NVNPGVNSTG PSLAGIFGRQ SGSVPGYAYT AANKNSGIVW
     DDEVLDKYLT KPTAMIPGTK MVFAGFKKAK DRADMIAYLK TI
//
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