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Database: UniProt/TrEMBL
Entry: B5G0D0_TAEGU
LinkDB: B5G0D0_TAEGU
Original site: B5G0D0_TAEGU 
ID   B5G0D0_TAEGU            Unreviewed;       224 AA.
AC   B5G0D0;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   25-OCT-2017, entry version 54.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea;
OC   Estrildidae; Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|EMBL:ACH44741.1};
RN   [1] {ECO:0000313|EMBL:ACH44741.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole brain {ECO:0000313|EMBL:ACH44741.1};
RX   PubMed=17018643; DOI=10.1073/pnas.0607098103;
RA   Wada K., Howard J.T., McConnell P., Whitney O., Lints T., Rivas M.V.,
RA   Horita H., Patterson M.A., White S.A., Scharff C., Haesler S.,
RA   Zhao S., Sakaguchi H., Hagiwara M., Shiraki T., Hirozane-Kishikawa T.,
RA   Skene P., Hayashizaki Y., Carninci P., Jarvis E.D.;
RT   "A molecular neuroethological approach for identifying and
RT   characterizing a cascade of behaviorally regulated genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15212-15217(2006).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; DQ214962; ACH44741.1; -; mRNA.
DR   EMBL; DQ214963; ACH44742.1; -; mRNA.
DR   EMBL; DQ214966; ACH44744.1; -; mRNA.
DR   EMBL; DQ214969; ACH44746.1; -; mRNA.
DR   EMBL; EF192002; ACH46435.1; -; mRNA.
DR   RefSeq; NP_001232398.1; NM_001245469.2.
DR   UniGene; Tgu.10867; -.
DR   GeneID; 100190330; -.
DR   KEGG; tgu:100190330; -.
DR   CTD; 6648; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   HOVERGEN; HBG004451; -.
DR   KO; K04564; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN       27    108       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      115    218       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        52     52       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       100    100       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       185    185       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       189    189       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   224 AA;  24919 MW;  1922770D94B7C1F9 CRC64;
     MLRRFAAASR SSAKLVAPLG CLVSRQKHTL PDLPYDYGAL EPHINAEIMQ LHHSKHHATY
     VNNLNVAEEK YKEALAKGDV TTQVSLQPAL KFNGGGHINH TIFWTNLSPN GGGEPKGELM
     EAIKRDFGSF ANFKEKLTAV SVGVQGSGWG WLGYNKEQGR LQIAACANQD PLQGTTGLIP
     LLGIDVWEHA YYLQYKNVRP DYLKAIWNVI NWENVSSRYA TCKK
//
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