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Database: UniProt/TrEMBL
Entry: I7CUM7_NATSJ
LinkDB: I7CUM7_NATSJ
Original site: I7CUM7_NATSJ 
ID   I7CUM7_NATSJ            Unreviewed;       200 AA.
AC   I7CUM7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   25-OCT-2017, entry version 28.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=NJ7G_1159 {ECO:0000313|EMBL:AFO56406.1};
OS   Natrinema sp. (strain J7-2).
OC   Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae;
OC   Natrinema.
OX   NCBI_TaxID=406552 {ECO:0000313|EMBL:AFO56406.1, ECO:0000313|Proteomes:UP000006507};
RN   [1] {ECO:0000313|EMBL:AFO56406.1, ECO:0000313|Proteomes:UP000006507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J7-2 {ECO:0000313|EMBL:AFO56406.1,
RC   ECO:0000313|Proteomes:UP000006507};
RX   PubMed=22911826; DOI=10.1371/journal.pone.0041621;
RA   Feng J., Liu B., Zhang Z., Ren Y., Li Y., Gan F., Huang Y., Chen X.,
RA   Shen P., Wang L., Tang B., Tang X.F.;
RT   "The complete genome sequence of Natrinema sp. J7-2, a haloarchaeon
RT   capable of growth on synthetic media without amino acid supplements.";
RL   PLoS ONE 7:E41621-E41621(2012).
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; CP003412; AFO56406.1; -; Genomic_DNA.
DR   RefSeq; WP_014863428.1; NC_018224.1.
DR   EnsemblBacteria; AFO56406; AFO56406; NJ7G_1159.
DR   GeneID; 13351651; -.
DR   KEGG; nat:NJ7G_1159; -.
DR   PATRIC; fig|406552.5.peg.1029; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG093Z0AKF; -.
DR   Proteomes; UP000006507; 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:UP000006507};
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:UP000006507}.
FT   DOMAIN        4     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;  22359 MW;  477913CE796CA2E1 CRC64;
     MTDHELPPLP YDYDALEPAL SEQVLTWHHD THHQGYVNGL NAAEETLAEN REEGDFGSTP
     GALSNVTHNG CGHYLHTLFW ENMSPNGGGE PEGDLADRIE EDFGSYEGWK GEFEAAAGAA
     GGWALLVYDP VSKQLRNVAV DKHDQGALWG AHPVLALDVW EHSYYYDYGP DRGDFIDAFF
     DVVNWEKAEA EYQTCLDHFE
//
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