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Database: UniProt
Entry: A0A1D2VDP1_9ASCO
LinkDB: A0A1D2VDP1_9ASCO
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ID   A0A1D2VDP1_9ASCO        Unreviewed;       154 AA.
AC   A0A1D2VDP1;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   16-JAN-2019, entry version 11.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=ASCRUDRAFT_9295 {ECO:0000313|EMBL:ODV59630.1};
OS   Ascoidea rubescens DSM 1968.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Ascoideaceae; Ascoidea.
OX   NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV59630.1, ECO:0000313|Proteomes:UP000095038};
RN   [1] {ECO:0000313|Proteomes:UP000095038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T.,
RA   Goker M., Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K.,
RA   Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K., Lapidus A., Lindquist E.,
RA   Lipzen A., Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KV454485; ODV59630.1; -; Genomic_DNA.
DR   RefSeq; XP_020045937.1; XM_020195114.1.
DR   EnsemblFungi; ODV59630; ODV59630; ASCRUDRAFT_9295.
DR   GeneID; 30968750; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000095038; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001320; P:age-dependent response to reactive oxygen species involved in chronological cell aging; IEA:EnsemblFungi.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0006882; P:cellular zinc ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR   GO; GO:1901856; P:negative regulation of cellular respiration; IEA:EnsemblFungi.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:EnsemblFungi.
DR   GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
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:UP000095038};
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:UP000095038};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       14    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  15789 MW;  9CCDD67BEEFC5E4B CRC64;
     MVKAIAVLKG TVGVGGVVTF EQNSENEPTK ISYKITGNSP NALKGFHIHE FGDNTNGCTS
     AGPHFNPFNN THGAPTETVR HVGDLGNIKT DAQGVATGEI FDSLVKLIGP TSIIGRTVVV
     HDGEDDLGKG GHPDSLKTGN AGGRPACGVI GFAA
//
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