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Database: UniProt/TrEMBL
Entry: C3ZM91_BRAFL
LinkDB: C3ZM91_BRAFL
Original site: C3ZM91_BRAFL 
ID   C3ZM91_BRAFL            Unreviewed;       156 AA.
AC   C3ZM91;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   25-OCT-2017, entry version 58.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=BRAFLDRAFT_264030 {ECO:0000313|EMBL:EEN46347.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae;
OC   Branchiostoma.
OX   NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554};
RN   [1] {ECO:0000313|EMBL:EEN46347.1, ECO:0000313|Proteomes:UP000001554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN46347.1,
RC   ECO:0000313|Proteomes:UP000001554};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN46347.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J.,
RA   Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J.,
RA   Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E.,
RA   Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y.,
RA   Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A.,
RA   Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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; GG666644; EEN46347.1; -; Genomic_DNA.
DR   RefSeq; XP_002590336.1; XM_002590290.1.
DR   UniGene; Bfl.12884; -.
DR   ProteinModelPortal; C3ZM91; -.
DR   SMR; C3ZM91; -.
DR   STRING; 7739.JGI264030; -.
DR   GeneID; 7205783; -.
DR   KEGG; bfo:BRAFLDRAFT_264030; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   InParanoid; C3ZM91; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   Proteomes; UP000001554; Partially assembled 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; 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:UP000001554};
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:UP000001554};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   156 AA;  15827 MW;  1E396DE429F0D90D CRC64;
     MSLKAVCVLV GETVKGTVTF TQASSDSPVE VTGTISNLTP PGKHGFHIHE FGDTTNGCTS
     AGSHFNPAKK NHGGPQDAER HVGDLGNVEV GDDGVATINI TDSQLQLTGP NSIVGRAVVV
     HAGEDDLGKG GFEDSLTTGH AGGRLACGVI GITKQA
//
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