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Database: UniProt/TrEMBL
Entry: Q9HM56_THEAC
LinkDB: Q9HM56_THEAC
Original site: Q9HM56_THEAC 
ID   Q9HM56_THEAC            Unreviewed;       205 AA.
AC   Q9HM56;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   25-OCT-2017, entry version 88.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Ta0013 {ECO:0000313|EMBL:CAC11162.1};
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 /
OS   NBRC 15155 / AMRC-C165).
OC   Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075 {ECO:0000313|Proteomes:UP000001024};
RN   [1] {ECO:0000313|EMBL:CAC11162.1, ECO:0000313|Proteomes:UP000001024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165
RC   {ECO:0000313|Proteomes:UP000001024};
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.L., Koretke K.K., Volker C.,
RA   Mewes H.W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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; AL445063; CAC11162.1; -; Genomic_DNA.
DR   RefSeq; WP_010900440.1; NC_002578.1.
DR   ProteinModelPortal; Q9HM56; -.
DR   STRING; 273075.Ta0013; -.
DR   PRIDE; Q9HM56; -.
DR   EnsemblBacteria; CAC11162; CAC11162; CAC11162.
DR   GeneID; 1455683; -.
DR   KEGG; tac:Ta0013; -.
DR   eggNOG; arCOG04147; Archaea.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG093Z0AKF; -.
DR   BioCyc; TACI273075:G13HZ-14-MONOMER; -.
DR   Proteomes; UP000001024; 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   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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001024};
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:UP000001024}.
FT   DOMAIN       19     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    190       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        78     78       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       159    159       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   205 AA;  23799 MW;  96257668FA063E6A CRC64;
     MAETWEIKEK LKPRGLEGIS DVQIDNHFDV HYKGYVNKLN EIWSRLPDVD RSKANQNYSE
     FRALKLEETF NYGGSLLHEL YFEGLTPKHS EVPKEFKDAV AKDFGSYEKW LEDFKATGTA
     FRGWAILVFD LNYGKLRNIG SDAHNVGLIW NSIAILTMDV YEHAYYVDYG AKRAPYLDAF
     LKNVNWPVVL DRLNRAKKAY EAFKS
//
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