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Database: UniProt
Entry: A0A2B4SYK8_STYPI
LinkDB: A0A2B4SYK8_STYPI
Original site: A0A2B4SYK8_STYPI 
ID   A0A2B4SYK8_STYPI        Unreviewed;       304 AA.
AC   A0A2B4SYK8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   05-DEC-2018, entry version 5.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=SOD1 {ECO:0000313|EMBL:PFX34183.1};
GN   ORFNames=AWC38_SpisGene1020 {ECO:0000313|EMBL:PFX34183.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX34183.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D.,
RA   Flot J.-F., Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and
RT   Acropora digitifera provides evidence for extensive differences
RT   between species of corals.";
RL   bioRxivorg 0:0-0(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PFX34183.1}.
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DR   EMBL; LSMT01000006; PFX34183.1; -; Genomic_DNA.
DR   Proteomes; UP000225706; 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; -; 3.
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; 3.
DR   Pfam; PF00080; Sod_Cu; 2.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 3.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000225706};
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:UP000225706};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       19     90       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
FT   DOMAIN      110    216       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   304 AA;  31925 MW;  E49D494ED57728D5 CRC64;
     MVDNFDISCV VVWEAGAFSG HHGDLGNITA GPDGVAKIDI RDKLVSVVGV DSVVGRTIVV
     HAKQDDLGKG GNDESLKTGN AGARLACGVI GLTKSIFLLV MARAVCHLAG DIQGTITFLQ
     EQPGGPCVIK GMLQGLTEGH HGIHILEFGD ISQGCKSAGA HFNPHNKTHG GPEDNNSRHV
     GDLGNIEAND QGQAEVNFTD SVVSLTGEYS VIGRTLEDLK TLEFRHRSLK ISEKSLKISA
     DESKLKFSFV FSVEISVCEG VDDLGIGGHE LSLTTGNSGA CLACGIIGIS KYSEQTKVPP
     DDPV
//
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