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Database: UniProt/TrEMBL
Entry: A7S2P3_NEMVE
LinkDB: A7S2P3_NEMVE
Original site: A7S2P3_NEMVE 
ID   A7S2P3_NEMVE            Unreviewed;       154 AA.
AC   A7S2P3;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   05-JUL-2017, entry version 65.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=v1g234825 {ECO:0000313|EMBL:EDO42041.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO42041.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J.,
RA   Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V.,
RA   Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E.,
RA   Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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   EMBL; DS469569; EDO42041.1; -; Genomic_DNA.
DR   RefSeq; XP_001634104.1; XM_001634054.1.
DR   UniGene; Nve.8504; -.
DR   ProteinModelPortal; A7S2P3; -.
DR   STRING; 45351.NEMVEDRAFT_v1g234825-PA; -.
DR   EnsemblMetazoa; EDO42041; EDO42041; NEMVEDRAFT_v1g234825.
DR   GeneID; 5513890; -.
DR   KEGG; nve:NEMVE_v1g234825; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   InParanoid; A7S2P3; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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:UP000001593};
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:UP000001593};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  15850 MW;  2749ABAB176577E7 CRC64;
     MVIRGVCCLV GDNEVKGVIH FTQQAPDGPC TLRGRITGLT EGKHGFHIHE FGDNTNGCTS
     AGAHYNPHGK MHGAPEDKDR HLGDLGNIEA DANGIADVSI TDCLVSLTGQ CSIIGRSLVV
     HEGMDDLGAG GHELSLTTGN AGGRVACGVI GIAL
//
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