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Database: UniProt
Entry: A0A0L8IFP8_OCTBM
LinkDB: A0A0L8IFP8_OCTBM
Original site: A0A0L8IFP8_OCTBM 
ID   A0A0L8IFP8_OCTBM        Unreviewed;       155 AA.
AC   A0A0L8IFP8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   16-JAN-2019, entry version 16.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=OCBIM_22005110mg {ECO:0000313|EMBL:KOG00316.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Cephalopoda; Coleoidea;
OC   Neocoleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae;
OC   Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOG00316.1, ECO:0000313|Proteomes:UP000053454};
RN   [1] {ECO:0000313|Proteomes:UP000053454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Albertin C.B., Simakov O., Mitros T., Wang Z.Y., Pungot J.R.,
RA   Edsinger-Gonzalez E., Brenner S., Ragsdale C.W., Rokhsar D.S.;
RT   "WGS assembly of Octopus bimaculoides.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KQ415813; KOG00316.1; -; Genomic_DNA.
DR   RefSeq; XP_014768917.1; XM_014913431.1.
DR   EnsemblMetazoa; Ocbimv22005110m; Ocbimv22005110m.p; Ocbimv22005110m.g.
DR   GeneID; 106868255; -.
DR   KEGG; obi:106868255; -.
DR   KO; K04565; -.
DR   OMA; MAMKAVC; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000053454; 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; -; 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   Complete proteome {ECO:0000313|Proteomes:UP000053454};
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:UP000053454};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   155 AA;  16133 MW;  CF89B098D09B32D5 CRC64;
     MMQAVCVLGC SDSVSGKIFF KQECSNGPVK VTGEISGMPD GKHGFHIHEF GDNTNGCVSA
     GAHFNPEGKE HGGPTKETRH VGDLGNVESA QNVAKVNIED AVISLNGPNC IVGRTLVVHE
     DVDDLGLGGH KDSKTTGNAG RRLACGVIGI AKLEK
//
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