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Database: UniProt
Entry: U1MGY5_9EURY
LinkDB: U1MGY5_9EURY
Original site: U1MGY5_9EURY 
ID   U1MGY5_9EURY            Unreviewed;       203 AA.
AC   U1MGY5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   05-DEC-2018, entry version 20.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=J07HX5_00660 {ECO:0000313|EMBL:ERG88514.1};
OS   halophilic archaeon J07HX5.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Halobacteriales.
OX   NCBI_TaxID=1325472 {ECO:0000313|EMBL:ERG88514.1, ECO:0000313|Proteomes:UP000053694};
RN   [1] {ECO:0000313|EMBL:ERG88514.1, ECO:0000313|Proteomes:UP000053694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23637883;
RA   Podell S., Ugalde J.A., Narasingarao P., Banfield J.F.,
RA   Heidelberg K.B., Allen E.E.;
RT   "Assembly-driven community genomics of a hypersaline microbial
RT   ecosystem.";
RL   PLoS ONE 8:E61692-E61692(2013).
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:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={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; KE356559; ERG88514.1; -; Genomic_DNA.
DR   Proteomes; UP000053694; 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   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053694};
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:UP000053694}.
FT   DOMAIN        8     86       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       94    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   COILED       36     56       {ECO:0000256|SAM:Coils}.
FT   METAL        31     31       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   203 AA;  22985 MW;  A09B8510C5C58B19 CRC64;
     MAQRSQPQLP ELPYEYDALE PHISEQVVNW HHDTHHQSYV NNLAAAEETL AENREAGDYD
     GTAAAIRDVT HNTGGHYLHT LFWENMHPDG GGEPSGELRD RIETDFGSYE GWKGEFETAA
     SDASGWALLV YDPVTKQLRN ATVDNHDEGA IWGAHPILSL DVWEHSYYYD YGPDRGGLID
     GFFEVVNWDY VADQYDTVVS RIE
//
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