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Database: UniProt
Entry: G0QHB0_NANS0
LinkDB: G0QHB0_NANS0
Original site: G0QHB0_NANS0 
ID   G0QHB0_NANS0            Unreviewed;       200 AA.
AC   G0QHB0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   05-DEC-2018, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=J07AB43_16720 {ECO:0000313|EMBL:EGQ43681.1};
OS   Nanosalina sp. (strain J07AB43).
OC   Archaea; Euryarchaeota; Stenosarchaea group;
OC   Candidatus Nanohaloarchaeota; Nanohaloarchaea; Candidatus Nanosalina.
OX   NCBI_TaxID=889948 {ECO:0000313|EMBL:EGQ43681.1, ECO:0000313|Proteomes:UP000009379};
RN   [1] {ECO:0000313|EMBL:EGQ43681.1, ECO:0000313|Proteomes:UP000009379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J07AB43 {ECO:0000313|Proteomes:UP000009379};
RA   Narasingarao P., Podell S., Ugalde J.A., Brochier-Armanet C.,
RA   Emerson J.B., Brocks J.J., Heidelberg K.B., Banfield J.F., Allen E.E.;
RT   "De novo metagenomic assembly reveals abundant novel major lineage of
RT   Archaea in hypersaline microbial communities.";
RL   ISME J. 0:0-0(2011).
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; GL982576; EGQ43681.1; -; Genomic_DNA.
DR   ProteinModelPortal; G0QHB0; -.
DR   SMR; G0QHB0; -.
DR   OMA; YEGWKGE; -.
DR   Proteomes; UP000009379; 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:UP000009379};
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:UP000009379}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    190       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   COILED       33     53       {ECO:0000256|SAM:Coils}.
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;  23343 MW;  3490184BE222305A CRC64;
     MTEYSLIELP YEYDALSPKI SEQVMEWHHD VHHQGYINGV NDAEQKLQEQ REEGDFSNTA
     SLLNQFTHNY CGNVLHEMFW NNMSPTGGGK PEGQLMEKIQ EDFGSYENWK KEFKQAAKSA
     SGWALLVYIP YTNELHNVPV DNHDEGAVWG AHPVLALDVW EHSYYHDYGP ERGEFIDNFF
     DLIEWSDVQQ NFDEMAEKFE
//
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