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Database: UniProt/TrEMBL
Entry: A0A088A933_APIME
LinkDB: A0A088A933_APIME
Original site: A0A088A933_APIME 
ID   A0A088A933_APIME        Unreviewed;       152 AA.
AC   A0A088A933;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 19.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=Sod1 {ECO:0000313|EnsemblMetazoa:GB47880-PA};
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Apoidea; Apidae; Apis.
OX   NCBI_TaxID=7460 {ECO:0000313|EnsemblMetazoa:GB47880-PA, ECO:0000313|Proteomes:UP000005203};
RN   [1] {ECO:0000313|EnsemblMetazoa:GB47880-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DH4 {ECO:0000313|EnsemblMetazoa:GB47880-PA};
RA   Wu J.L., Liu J.H., Yuan Y.N., Qiao L.Y., Liu W.Z.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GB47880-PA}
RP   IDENTIFICATION.
RC   STRAIN=DH4 {ECO:0000313|EnsemblMetazoa:GB47880-PA};
RG   EnsemblMetazoa;
RL   Submitted (JAN-2017) to UniProtKB.
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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   RefSeq; NP_001171498.1; NM_001178027.1.
DR   UniGene; Ame.178; -.
DR   ProteinModelPortal; A0A088A933; -.
DR   STRING; 7460.GB10133-PA; -.
DR   PaxDb; A0A088A933; -.
DR   EnsemblMetazoa; GB47880-RA; GB47880-PA; GB47880.
DR   GeneID; 409398; -.
DR   KEGG; ame:409398; -.
DR   CTD; 6647; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   PhylomeDB; A0A088A933; -.
DR   Proteomes; UP000005203; Unplaced.
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:UP000005203};
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:UP000005203};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       10    147       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   152 AA;  15634 MW;  2FF58A50B59313B1 CRC64;
     MTKAVCVLQG EVKGTIFFEQ PESTNSVKVT GQVTGLKKGL HGFHVHEFGD NTNGCTSAGA
     HFNPLGKDHG GPDSDIRHVG DLGNIEADAS GVANVNITDK TIQLQGPHSV IGRTLVVHAD
     PDDLGKGGVE LSKTTGNAGA RLACGVIGIT KV
//
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