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Database: UniProt
Entry: A0A1X7U1F6_AMPQE
LinkDB: A0A1X7U1F6_AMPQE
Original site: A0A1X7U1F6_AMPQE 
ID   A0A1X7U1F6_AMPQE        Unreviewed;       248 AA.
AC   A0A1X7U1F6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   16-JAN-2019, entry version 9.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.21481_001, ECO:0000313|Proteomes:UP000007879};
RN   [1] {ECO:0000313|EnsemblMetazoa:Aqu2.1.21481_001, ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E.,
RA   Glavina del Rio T., Bruce D., Barry K., Pitluck S., Srivastava M.,
RA   Simakov O., Chapman J., Mitros T., Hellsten U., Putnam N.H., Fahey B.,
RA   Gauthier M., Larroux C., Richards G.S., Stanke M., Adamska M.,
RA   Darling A., Dacre M., Degnan S.M., Zhai Y., Adamski M., Calcino A.,
RA   Cummins S.F., Goodstein D.M., Harris C., Shu S., Woodcroft B.,
RA   Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The genome of the haplosclerid demosponge Amphimedon queenslandica
RT   and the evolution of animal complexity.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:Aqu2.1.21481_001}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-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:RU000414}.
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:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   RefSeq; XP_011406277.2; XM_011407975.2.
DR   EnsemblMetazoa; Aqu2.1.21481_001; Aqu2.1.21481_001; Aqu2.1.21481.
DR   GeneID; 100637349; -.
DR   KEGG; aqu:100637349; -.
DR   KO; K04564; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000007879; 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   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007879};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    248       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5013390325.
FT   DOMAIN       32    126       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      135    233       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        58     58       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       119    119       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       202    202       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       206    206       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   248 AA;  29224 MW;  318E7F769107EE1A CRC64;
     MEFIRIFSLF SFFTLTLSQS SIYDEMFYPV DEYSFPQLPG YDYHELEPYI DQRTLTVHHK
     KHHQGYTVKM NQALKDWRKQ EPQSDLAKSS IIDILQNLEM VPDKWRTTLQ NNAGGYVNHI
     YYWVTMCPKP GEISKALLKK IKASFPAGMS EFKESFTTAS LSLFGSGYVW LVTDDEGSIS
     IISTKNQDCP ISSNLYPLLV LDVWEHSYYL KHQNLRADYI SDWWNVVCWQ NVETLRQFWI
     NRQIKDEL
//
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