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Database: UniProt/TrEMBL
Entry: S0AS08_FERAC
LinkDB: S0AS08_FERAC
Original site: S0AS08_FERAC 
ID   S0AS08_FERAC            Unreviewed;       207 AA.
AC   S0AS08;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   07-JUN-2017, entry version 23.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=FACI_IFERC00001G0925 {ECO:0000313|EMBL:AGO60905.1};
OS   Ferroplasma acidarmanus fer1.
OC   Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales;
OC   Ferroplasmaceae; Ferroplasma.
OX   NCBI_TaxID=333146 {ECO:0000313|EMBL:AGO60905.1, ECO:0000313|Proteomes:UP000014660};
RN   [1] {ECO:0000313|EMBL:AGO60905.1, ECO:0000313|Proteomes:UP000014660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fer1 {ECO:0000313|EMBL:AGO60905.1};
RX   PubMed=17267615; DOI=10.1073/pnas.0604851104;
RA   Allen E.E., Tyson G.W., Whitaker R.J., Detter J.C., Richardson P.M.,
RA   Banfield J.F.;
RT   "Genome dynamics in a natural archaeal population.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1883-1888(2007).
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; CP004145; AGO60905.1; -; Genomic_DNA.
DR   RefSeq; WP_019841539.1; NC_021592.1.
DR   STRING; 333146.Faci_050500004780; -.
DR   EnsemblBacteria; AGO60905; AGO60905; FACI_IFERC00001G0925.
DR   GeneID; 31677301; -.
DR   KEGG; fac:FACI_IFERC01G0925; -.
DR   PATRIC; fig|333146.12.peg.942; -.
DR   eggNOG; arCOG04147; Archaea.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OrthoDB; POG093Z0AKF; -.
DR   BioCyc; FACI333146:G1367-948-MONOMER; -.
DR   Proteomes; UP000014660; 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; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000014660};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN       20     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   207 AA;  24105 MW;  E79A8883C594AD06 CRC64;
     MATETWEVKE NAKPRGLDGI SDKQIDYHFD VHYKGYVSKL NEIWSKLPDV DLTKANQNYS
     DLREMKLEET FNYDGSMLHE YYFESLSKDH VAMPESVKAQ IEKDFGSYEK FVALFKATGT
     AFRGWAHLVF DLNCGKLRVL GADIHNASAI WNALMILPLD VYEHAYYTDY GAKRAPYLDA
     FMNNVNWKVV EKRLDRAKRT YEAFKKD
//
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