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Database: UniProt
Entry: A0A061QHR8_9PROT
LinkDB: A0A061QHR8_9PROT
Original site: A0A061QHR8_9PROT 
ID   A0A061QHR8_9PROT        Unreviewed;       162 AA.
AC   A0A061QHR8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Cytochrome c {ECO:0000313|EMBL:GAK33779.1};
GN   Name=CYCS {ECO:0000313|EMBL:GAK33779.1};
GN   ORFNames=AQ1_01670 {ECO:0000313|EMBL:GAK33779.1};
OS   alpha proteobacterium Q-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK33779.1, ECO:0000313|Proteomes:UP000027360};
RN   [1] {ECO:0000313|EMBL:GAK33779.1, ECO:0000313|Proteomes:UP000027360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q-1 {ECO:0000313|EMBL:GAK33779.1,
RC   ECO:0000313|Proteomes:UP000027360};
RX   PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA   Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA   Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT   "Iodide oxidation by a novel multicopper oxidase from the
RT   alphaproteobacterium strain Q-1.";
RL   Appl. Environ. Microbiol. 78:3941-3949(2012).
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:GAK33779.1}.
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DR   EMBL; BAYV01000016; GAK33779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061QHR8; -.
DR   STRING; 1492281.AQ1_01670; -.
DR   Proteomes; UP000027360; Unassembled WGS sequence.
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   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
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}; Reference proteome {ECO:0000313|Proteomes:UP000027360};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..162
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001605052"
FT   DOMAIN          46..150
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   162 AA;  18210 MW;  20453CA10414BBCD CRC64;
     MRSDLPFPSS RCAQRSKRRM LYVLLLFAMA FGVSAAADES ISIPGGDAER GRTLFFSCKA
     CHELAPADIR TTDDSKLNLF GLFGRRVGFD PNYNHYSAAL KDADFIWTED RLDQWLKSPN
     SLLPGNKMPF SGIMKAQDRL DLIAYLRQFK ADPPPDALMT IK
//
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