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Database: UniProt
Entry: A0A151JMA2_9HYME
LinkDB: A0A151JMA2_9HYME
Original site: A0A151JMA2_9HYME 
ID   A0A151JMA2_9HYME        Unreviewed;       258 AA.
AC   A0A151JMA2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-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=ALC57_03705 {ECO:0000313|EMBL:KYN26890.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Formicoidea; Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN26890.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN26890.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN26890.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN26890.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) 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; KQ978966; KYN26890.1; -; Genomic_DNA.
DR   Proteomes; UP000078492; 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:UP000078492};
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:UP000078492};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN      118    255       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   258 AA;  27590 MW;  03479687FC52676F CRC64;
     MNRVLSFTES AVLSYGPALA IAIIPINIDS RHISRVRSSE GVPERFSSDL VLARSPPSRS
     EDKTARDSST SHDNDLGAVP IKELPPEPPL FKDCFPQRRK RRRRELVAVV HLTSFSSRNV
     TGNLKIVQTP LDGPVTITGT ISGLTGGLHG FHVHEKGDLS EGCKSAGAHF NPENNTHGAP
     EDTVRHVGDL GNIMANPDGE AIINITDNII SLRGSNSIVG RSIVVHSDED DLGKGNHSLS
     STTGNSGDRW ACGVVGIE
//
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