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Database: UniProt/TrEMBL
Entry: G2SJI5_RHOMR
LinkDB: G2SJI5_RHOMR
Original site: G2SJI5_RHOMR 
ID   G2SJI5_RHOMR            Unreviewed;       209 AA.
AC   G2SJI5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 33.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Rhom172_1946 {ECO:0000313|EMBL:AEN73857.1};
OS   Rhodothermus marinus SG0.5JP17-172.
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=762570 {ECO:0000313|EMBL:AEN73857.1, ECO:0000313|Proteomes:UP000001280};
RN   [1] {ECO:0000313|EMBL:AEN73857.1, ECO:0000313|Proteomes:UP000001280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG0.5JP17-172 {ECO:0000313|EMBL:AEN73857.1,
RC   ECO:0000313|Proteomes:UP000001280};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Chertkov O., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I.,
RA   Gladden J., Woyke T.;
RT   "Complete sequence of chromosome of Rhodothermus marinus SG0.5JP17-
RT   172.";
RL   Submitted (AUG-2011) 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; CP003029; AEN73857.1; -; Genomic_DNA.
DR   RefSeq; WP_012843426.1; NC_015966.1.
DR   ProteinModelPortal; G2SJI5; -.
DR   EnsemblBacteria; AEN73857; AEN73857; Rhom172_1946.
DR   KEGG; rmg:Rhom172_1946; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; RMAR762570:GJAN-1946-MONOMER; -.
DR   Proteomes; UP000001280; 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:UP000001280};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AEN73857.1}.
FT   DOMAIN        3     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   209 AA;  23658 MW;  0D6E9BD2478A4817 CRC64;
     MAFTLPPLPY PYDALEPYVD AQTMEIHHTK HHQGYVNNLN KALEGYPELQ NKSIEELLRG
     INEIPEAIRT AVRNNGGGHA NHSLFWTIMK PNGGGEPTGE LAEAIKATFG SFEAFKEKFS
     AEAAGRFGSG WAWLVVDENG KLQVYSTPNQ DSPYMQGHTP ILGLDVWEHA YYLKYQNRRA
     EYIQNWWNVV NWDQVAQYYK EALAKVAAA
//
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