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Database: UniProt/TrEMBL
Entry: A0A1S3JVI8_LINUN
LinkDB: A0A1S3JVI8_LINUN
Original site: A0A1S3JVI8_LINUN 
ID   A0A1S3JVI8_LINUN        Unreviewed;       154 AA.
AC   A0A1S3JVI8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   30-AUG-2017, entry version 4.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=LOC106176506 {ECO:0000313|RefSeq:XP_013414383.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013414383.1};
RN   [1] {ECO:0000313|RefSeq:XP_013414383.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013414383.1};
RG   RefSeq;
RL   Submitted (FEB-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; XP_013414383.1; XM_013558929.1.
DR   EnsemblMetazoa; g17842.t1; g17842.t1; g17842.
DR   GeneID; 106176506; -.
DR   Proteomes; UP000085678; Genome assembly.
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; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
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:UP000085678};
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:UP000085678};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  15691 MW;  82D073B62D01BFBF CRC64;
     MALKAVCVLK GASDVIGTVY FEQTSADGPC KVTGEVTGLK EGLHGFHVHQ FGDNTNGCTS
     AGPHFNPSGK THGGPDDENR HFGDLGNIKA GSDGKATVAI TDKLVTLTGP NSVIGRTIVV
     HEGQDDLGKG GNEESLKTGN AGGRLACGVI GITH
//
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