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Database: UniProt
Entry: SODC_NPVAC
LinkDB: SODC_NPVAC
Original site: SODC_NPVAC 
ID   SODC_NPVAC              Reviewed;         151 AA.
AC   P24705;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   16-JAN-2019, entry version 98.
DE   RecName: Full=Putative superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=SOD;
OS   Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC   Viruses; dsDNA viruses, no RNA stage; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=46015;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=L1;
RX   PubMed=1871962; DOI=10.1016/0042-6822(91)90831-U;
RA   Tomalski M.D., Eldridge R., Miller L.K.;
RT   "A baculovirus homolog of a Cu/Zn superoxide dismutase gene.";
RL   Virology 184:149-161(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6;
RX   PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA   Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT   "The complete DNA sequence of Autographa californica nuclear
RT   polyhedrosis virus.";
RL   Virology 202:586-605(1994).
CC   -!- FUNCTION: Nonessential for normal virus replication. Could be
CC       either non-functional or with a low activity.
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   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; M96361; AAA66799.1; -; Genomic_DNA.
DR   EMBL; M68862; AAA46746.1; -; Genomic_DNA.
DR   EMBL; L22858; AAA66661.1; -; Genomic_DNA.
DR   PIR; A40564; DSNVAC.
DR   RefSeq; NP_054060.1; NC_001623.1.
DR   ProteinModelPortal; P24705; -.
DR   SMR; P24705; -.
DR   GeneID; 1403863; -.
DR   KEGG; vg:1403863; -.
DR   OrthoDB; 11973at10239; -.
DR   Proteomes; UP000008292; Genome.
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   Antioxidant; Complete proteome; Copper; Disulfide bond; Late protein;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN         1    151       Putative superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164162.
FT   METAL        43     43       Copper; catalytic. {ECO:0000250}.
FT   METAL        45     45       Copper; catalytic. {ECO:0000250}.
FT   METAL        60     60       Copper; catalytic. {ECO:0000250}.
FT   METAL        60     60       Zinc; structural. {ECO:0000250}.
FT   METAL        68     68       Zinc; structural. {ECO:0000250}.
FT   METAL        77     77       Zinc; structural. {ECO:0000250}.
FT   METAL        80     80       Zinc; structural. {ECO:0000250}.
FT   METAL       118    118       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     54    144       {ECO:0000250}.
SQ   SEQUENCE   151 AA;  16182 MW;  BD6A6AB0C8FFA1E9 CRC64;
     MKAICIISGD VHGKIYFQQE SANQPLKISG YLLNLPRGLH GFHVHEYGDT SNGCTSAGEH
     FNPTNEDHGA PDAEIRHVGD LGNIKSAGYN SLTEVNMMDN VMSLYGPHNI IGRSLVVHTD
     KDDLGLTDHP LSKTTGNSGG RLGCGIIAIC K
//
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