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Entry: A0A2H0ZZB5_CANAR
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ID   A0A2H0ZZB5_CANAR        Unreviewed;       154 AA.
AC   A0A2H0ZZB5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   16-JAN-2019, entry version 8.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=B9J08_001381 {ECO:0000313|EMBL:PIS56836.1};
OS   Candida auris (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Metschnikowiaceae; Clavispora;
OC   Clavispora/Candida clade.
OX   NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS56836.1, ECO:0000313|Proteomes:UP000230249};
RN   [1] {ECO:0000313|EMBL:PIS56836.1, ECO:0000313|Proteomes:UP000230249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B8441 {ECO:0000313|EMBL:PIS56836.1,
RC   ECO:0000313|Proteomes:UP000230249};
RX   PubMed=27988485; DOI=10.1093/cid/ciw691;
RA   Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J.,
RA   Chowdhary A., Govender N.P., Colombo A.L., Calvo B., Cuomo C.A.,
RA   Desjardins C.A., Berkow E.L., Castanheira M., Magobo R.E., Jabeen K.,
RA   Asghar R.J., Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT   "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT   continents confirmed by whole-genome sequencing and epidemiological
RT   analyses.";
RL   Clin. Infect. Dis. 64:134-140(2017).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PIS56836.1}.
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DR   EMBL; PEKT02000003; PIS56836.1; -; Genomic_DNA.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000230249; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000230249};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230249};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
SQ   SEQUENCE   154 AA;  15989 MW;  F2FE032D32E99869 CRC64;
     MVKAVAVVRG DSKVCGVVNF EQENENDPTT ISWDISGNDP NALRGMHIHQ FGDNTNGCTS
     AGPHFNPFSK THGAPEDDNR HVGDLGNITT DASGVAKGTR KDLLVKLLGP NSVIGRSVVV
     HSGTDDLGKG GNEESLKTGN AGTRPACGVI GVTN
//
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