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Database: UniProt/TrEMBL
Entry: A0A0E3PP25_9EURY
LinkDB: A0A0E3PP25_9EURY
Original site: A0A0E3PP25_9EURY 
ID   A0A0E3PP25_9EURY        Unreviewed;       246 AA.
AC   A0A0E3PP25;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=MSSAC_2329 {ECO:0000313|EMBL:AKB36919.1};
OS   Methanosarcina siciliae C2J.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434118 {ECO:0000313|EMBL:AKB36919.1, ECO:0000313|Proteomes:UP000033123};
RN   [1] {ECO:0000313|EMBL:AKB36919.1, ECO:0000313|Proteomes:UP000033123}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2J {ECO:0000313|EMBL:AKB36919.1,
RC   ECO:0000313|Proteomes:UP000033123};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) 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; CP009508; AKB36919.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKB36919; AKB36919; MSSAC_2329.
DR   KEGG; msj:MSSAC_2329; -.
DR   PATRIC; fig|1434118.4.peg.2997; -.
DR   KO; K04564; -.
DR   OrthoDB; POG093Z0AKF; -.
DR   Proteomes; UP000033123; 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:UP000033123};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AKB36919.1}.
FT   DOMAIN       49    128       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      138    238       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        73     73       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       121    121       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       207    207       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       211    211       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   246 AA;  28738 MW;  3D97693A41181629 CRC64;
     MFRSIWIPFG FYSGLFRYSD LLGFYSDSGA NSAKQLIVKR VDNMAKDLYK LPPLKYGYAD
     LEPYISEEQL RIHHDKHHQG YVNNTNALLE MMEKARKEGT DFDYKATAKA LSFNLSGHVL
     HDFFWWEMTP ASNASKEPVG EFAEAIKEDF GSFERFKKEF SKVASSVEGS GWAALTFCND
     TKRLGIVQIE KHNVNLVPDF PIIMDLDVWE HAYYIDYKND RGKFIEGFWN IIDWEELDKY
     FKKIQK
//
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