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Database: UniProt/TrEMBL
Entry: W0JR24_9EURY
LinkDB: W0JR24_9EURY
Original site: W0JR24_9EURY 
ID   W0JR24_9EURY            Unreviewed;       200 AA.
AC   W0JR24;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   25-OCT-2017, entry version 20.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HALLA_13985 {ECO:0000313|EMBL:AHF99731.1};
OS   Halostagnicola larsenii XH-48.
OC   Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae;
OC   Halostagnicola.
OX   NCBI_TaxID=797299 {ECO:0000313|EMBL:AHF99731.1, ECO:0000313|Proteomes:UP000019024};
RN   [1] {ECO:0000313|EMBL:AHF99731.1, ECO:0000313|Proteomes:UP000019024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH-48 {ECO:0000313|EMBL:AHF99731.1,
RC   ECO:0000313|Proteomes:UP000019024};
RG   DOE Joint Genome Institute;
RA   Anderson I., Huntemann M., Han J., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Palaniappan K., Ivanova N.,
RA   Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N.,
RA   Hua S.X., Woyke T.;
RL   Submitted (JAN-2014) 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; CP007055; AHF99731.1; -; Genomic_DNA.
DR   RefSeq; WP_049952973.1; NZ_CP007055.1.
DR   EnsemblBacteria; AHF99731; AHF99731; HALLA_13985.
DR   GeneID; 25145540; -.
DR   KEGG; hlr:HALLA_13985; -.
DR   PATRIC; fig|797299.3.peg.1804; -.
DR   KO; K04564; -.
DR   OrthoDB; POG093Z0AKF; -.
DR   Proteomes; UP000019024; Chromosome.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000019024};
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:UP000019024}.
FT   DOMAIN        5     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    190       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       158    158       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   200 AA;  22286 MW;  FE5B0DABDC413879 CRC64;
     MTDNELPPLP YDYDALEPSI SEQVVTWHHD THHQGYVNGL NSAEETLAEN RESGDFGSTP
     GALSNVTHNG CGHYLHTLFW ENMSPNGGGE PSGDLADRIE EDFGSYEAWK GEFEAAAGAA
     GGWALLVYDP VAKQLRNIAV DKHDQGALWG SHPILALDVW EHSYYYDYGP DRGSFIDSFF
     DVVNWDKAAE EYQTCLDHFE
//
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