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Database: UniProt
Entry: W3RST0_9BRAD
LinkDB: W3RST0_9BRAD
Original site: W3RST0_9BRAD 
ID   W3RST0_9BRAD            Unreviewed;       229 AA.
AC   W3RST0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Cytochrome C oxidase {ECO:0000313|EMBL:ETR79359.1};
GN   ORFNames=X566_00145 {ECO:0000313|EMBL:ETR79359.1};
OS   Afipia sp. P52-10.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=1429916 {ECO:0000313|EMBL:ETR79359.1, ECO:0000313|Proteomes:UP000018975};
RN   [1] {ECO:0000313|Proteomes:UP000018975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P52-10 {ECO:0000313|Proteomes:UP000018975};
RX   PubMed=25874801;
RA   Pickering B.S., Tyler S., Smith G., Burton L., Li M., Dallaire A.,
RA   Weingartl H.;
RT   "Identification of a novel afipia species isolated from an Indian flying
RT   fox.";
RL   PLoS ONE 10:E0121274-E0121274(2015).
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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:ETR79359.1}.
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DR   EMBL; AZSJ01000001; ETR79359.1; -; Genomic_DNA.
DR   RefSeq; WP_034462630.1; NZ_AZSJ01000001.1.
DR   AlphaFoldDB; W3RST0; -.
DR   STRING; 1429916.X566_00145; -.
DR   PATRIC; fig|1429916.3.peg.25; -.
DR   eggNOG; COG1999; Bacteria.
DR   OrthoDB; 5296507at2; -.
DR   Proteomes; UP000018975; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR12151:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018975}.
FT   DOMAIN          41..208
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         79
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         83
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         172
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        79..83
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   229 AA;  25573 MW;  04283A57C0F5D36B CRC64;
     MELLKSVALA FALVTTIIAP VLAHSLEEVD QDLRDKDKYF QPVDSEAPSF SLQDADGRVV
     SLAGLRGKVV VLNFIYTNCP DVCPLHAERI AELQVMINQT PMKAMVEFVT ITTDPKRDTG
     EVLRDYGKAH GLDPVNWVFL TATPDQPEDS TRKIAEAYGL KFTQGDDGMQ MHGIVTHVID
     QDGRLRARFH GLKFEPVNLV IFVNALTNRA QRPHGHQQPG LWEKLKGLF
//
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