GenomeNet

Database: UniProt
Entry: A0A1B9IU65_9TREE
LinkDB: A0A1B9IU65_9TREE
Original site: A0A1B9IU65_9TREE 
ID   A0A1B9IU65_9TREE        Unreviewed;       162 AA.
AC   A0A1B9IU65;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   05-DEC-2018, entry version 10.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=L486_03571 {ECO:0000313|EMBL:OCF59072.1};
OS   Kwoniella mangroviensis CBS 10435.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1331196 {ECO:0000313|EMBL:OCF59072.1, ECO:0000313|Proteomes:UP000092583};
RN   [1] {ECO:0000313|EMBL:OCF59072.1, ECO:0000313|Proteomes:UP000092583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10435 {ECO:0000313|EMBL:OCF59072.1,
RC   ECO:0000313|Proteomes:UP000092583};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Kwoniella mangroviensis CBS10435.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10435 {ECO:0000313|Proteomes:UP000092583};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S.,
RA   Birren B.;
RT   "Evolution of pathogenesis and genome organization in the
RT   Tremellales.";
RL   Submitted (DEC-2013) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; KI669461; OCF59072.1; -; Genomic_DNA.
DR   EnsemblFungi; OCF59072; OCF59072; L486_03571.
DR   Proteomes; UP000092583; 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:UP000092583};
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:UP000092583};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       19    158       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   162 AA;  16246 MW;  C3E5C7E6518089EE CRC64;
     MTVPRDGTLL GAIAVLKGDS SVSGVITFTQ EKDGAPVTVS GDIKNLSPNA ERGFHVHEFG
     DNSNGCTSAG PHFNPHGKNH GGPDASERHV GDLGNVKTDG SGTAAVGITD KSISLFGPYS
     IIGRTVVVHE GTDDFGKGGH ADSLKTGNAG GRAACGVIGI AA
//
DBGET integrated database retrieval system