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Database: UniProt
Entry: A0A0L7L0A6_9NEOP
LinkDB: A0A0L7L0A6_9NEOP
Original site: A0A0L7L0A6_9NEOP 
ID   A0A0L7L0A6_9NEOP        Unreviewed;       119 AA.
AC   A0A0L7L0A6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, 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=OBRU01_17827 {ECO:0000313|EMBL:KOB68704.1};
OS   Operophtera brumata (winter moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia;
OC   Geometroidea; Geometridae; Larentiinae; Operophtera.
OX   NCBI_TaxID=104452 {ECO:0000313|EMBL:KOB68704.1, ECO:0000313|Proteomes:UP000037510};
RN   [1] {ECO:0000313|EMBL:KOB68704.1, ECO:0000313|Proteomes:UP000037510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM2013NL {ECO:0000313|EMBL:KOB68704.1};
RC   TISSUE=Head and thorax {ECO:0000313|EMBL:KOB68704.1};
RX   PubMed=26227816; DOI=10.1093/gbe/evv145;
RA   Derks M.F., Smit S., Salis L., Schijlen E., Bossers A., Mateman C.,
RA   Pijl A.S., de Ridder D., Groenen M.A., Visser M.E., Megens H.J.;
RT   "The Genome of Winter Moth (Operophtera brumata) Provides a Genomic
RT   Perspective on Sexual Dimorphism and Phenology.";
RL   Genome Biol. Evol. 7:2321-2332(2015).
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:KOB68704.1}.
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DR   EMBL; JTDY01004021; KOB68704.1; -; Genomic_DNA.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000037510; 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; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000037510};
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:UP000037510};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN        5    114       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   119 AA;  12380 MW;  DC219F39BBCBDC38 CRC64;
     MDIYKGKHGL HIHEFGDNTN GCTSAGPHFN PQNFDHGSPD ADIRHLGDLG NIESSGAPET
     RVCVEDSQIS LVGPNSIVGR TLVVHADPDD LGMGGHELSK TTGNAGARIA CGVIGLAKI
//
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