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Database: UniProt/TrEMBL
Entry: F2UJN2_SALR5
LinkDB: F2UJN2_SALR5
Original site: F2UJN2_SALR5 
ID   F2UJN2_SALR5            Unreviewed;       224 AA.
AC   F2UJN2;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   07-JUN-2017, entry version 24.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=PTSG_08425 {ECO:0000313|EMBL:EGD77331.1};
OS   Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC   Eukaryota; Choanoflagellida; Craspedida; Salpingoecidae; Salpingoeca.
OX   NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN   [1] {ECO:0000313|Proteomes:UP000007799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q.,
RA   Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Salpingoeca rosetta.";
RL   Submitted (AUG-2009) 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: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; GL832977; EGD77331.1; -; Genomic_DNA.
DR   RefSeq; XP_004990675.1; XM_004990618.1.
DR   ProteinModelPortal; F2UJN2; -.
DR   EnsemblProtists; EGD77331; EGD77331; PTSG_08425.
DR   GeneID; 16071233; -.
DR   KEGG; sre:PTSG_08425; -.
DR   InParanoid; F2UJN2; -.
DR   KO; K04564; -.
DR   Proteomes; UP000007799; 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   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   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:UP000007799};
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:UP000007799}.
FT   DOMAIN       23    104       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      114    217       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        48     48       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        96     96       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       184    184       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       188    188       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   224 AA;  25189 MW;  A542E81EC5C2664B CRC64;
     MMQCLRTTTR RAFGSVRAAS RLKHTLPDLQ YDYGELEPVI SAEIMQLHHA KHHQTYVNNL
     NVAEEQYGEA VHKGDLSKAI ALQSAIKFNG GGHINHSIFW TNLAPQRLGG GEPPSGELMK
     EIEKTFGSFE SFKEKLNTST AAVQGSGWGW LGYNKTRKTL EIATCPNQDP LEATTGLVPL
     LGIDVWEHAY YLQYKNVRPD YLKAIWEVVN WKNVVERYEA AKSA
//
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