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Database: UniProt
Entry: J5RRJ4_SACK1
LinkDB: J5RRJ4_SACK1
Original site: J5RRJ4_SACK1 
ID   J5RRJ4_SACK1            Unreviewed;       154 AA.
AC   J5RRJ4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   16-JAN-2019, entry version 26.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=YJR104C {ECO:0000313|EMBL:EJT42496.1};
GN   ORFNames=SKUD_179403 {ECO:0000313|EMBL:EJT42496.1};
OS   Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS
OS   8840 / NBRC 1802 / NCYC 2889) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT42496.1, ECO:0000313|Proteomes:UP000002753};
RN   [1] {ECO:0000313|EMBL:EJT42496.1, ECO:0000313|Proteomes:UP000002753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC   {ECO:0000313|Proteomes:UP000002753};
RX   PubMed=12775844; DOI=10.1126/science.1084337;
RA   Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B.,
RA   Majors J., Waterston R., Cohen B.A., Johnston M.;
RT   "Finding functional features in Saccharomyces genomes by phylogenetic
RT   footprinting.";
RL   Science 301:71-76(2003).
RN   [2] {ECO:0000313|Proteomes:UP000002753}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC   {ECO:0000313|Proteomes:UP000002753};
RX   PubMed=22384314; DOI=10.1534/g3.111.000273;
RA   Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA   Rine J., Johnston M., Hittinger C.T.;
RT   "The awesome power of yeast evolutionary genetics: New genome
RT   sequences and strain resources for the Saccharomyces sensu stricto
RT   genus.";
RL   G3 (Bethesda) 1:11-25(2011).
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:EJT42496.1}.
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DR   EMBL; AACI03001431; EJT42496.1; -; Genomic_DNA.
DR   EnsemblFungi; EJT42496; EJT42496; SKUD_179403.
DR   Proteomes; UP000002753; 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:UP000002753};
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:UP000002753};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  15824 MW;  55EA32BE1887CDE1 CRC64;
     MVQAVAVLKG DAGVSGVVQF EQASESEPTT ISYEIAGNSP NALRGFHIHE FGDATNGCVS
     AGPHFNPFKK THGAPTDEVR HVGDMGNLET DANGVARGSF KDSLIKLIGP TSVVGRSVVI
     HAGQDDLGKG DTEESLKTGN AGPRPACGVI GVTN
//
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