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Database: UniProt/TrEMBL
Entry: A9A591_NITMS
LinkDB: A9A591_NITMS
Original site: A9A591_NITMS 
ID   A9A591_NITMS            Unreviewed;       206 AA.
AC   A9A591;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   25-OCT-2017, entry version 63.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Nmar_0394 {ECO:0000313|EMBL:ABX12290.1};
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX12290.1, ECO:0000313|Proteomes:UP000000792};
RN   [1] {ECO:0000313|EMBL:ABX12290.1, ECO:0000313|Proteomes:UP000000792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1 {ECO:0000313|EMBL:ABX12290.1,
RC   ECO:0000313|Proteomes:UP000000792};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Stahl D., Richardson P.;
RT   "Complete sequence of Nitrosopumilus maritimus SCM1.";
RL   Submitted (OCT-2007) 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; CP000866; ABX12290.1; -; Genomic_DNA.
DR   ProteinModelPortal; A9A591; -.
DR   STRING; 436308.Nmar_0394; -.
DR   EnsemblBacteria; ABX12290; ABX12290; Nmar_0394.
DR   KEGG; nmr:Nmar_0394; -.
DR   eggNOG; arCOG04147; Archaea.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000000792; 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:UP000000792};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ABX12290.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000792}.
FT   DOMAIN        3     92       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       99    201       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        84     84       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       172    172       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   206 AA;  23313 MW;  FD2F09812CBD0C96 CRC64;
     MGKYTLPEMP YAYDALEPHI DARTMEIHHT KHHQTYTDKL NAALETCPAE IQDKDILDIL
     SDINSVPEDK RGAINFNGGG YDNHRLFWNN MKPNGGGEPG GSIADAINDS FGSFSDFKEK
     FSSTTAVIQG SGWGWLVYNP SSGKVEYKSM PNQTSPRTEG LVPLLGCDVW EHAYYLNYQN
     KRPAYIEAWW NVVNWDEVEN RFSKAK
//
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