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Database: UniProt/TrEMBL
Entry: U3TC41_9CREN
LinkDB: U3TC41_9CREN
Original site: U3TC41_9CREN 
ID   U3TC41_9CREN            Unreviewed;       214 AA.
AC   U3TC41;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   25-OCT-2017, entry version 20.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=ACAM_0527 {ECO:0000313|EMBL:BAN89996.1};
OS   Aeropyrum camini SY1 = JCM 12091.
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=1198449 {ECO:0000313|EMBL:BAN89996.1, ECO:0000313|Proteomes:UP000016887};
RN   [1] {ECO:0000313|EMBL:BAN89996.1, ECO:0000313|Proteomes:UP000016887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY1 {ECO:0000313|EMBL:BAN89996.1};
RX   PubMed=23872576; DOI=10.1128/AEM.01089-13;
RA   Daifuku T., Yoshida T., Kitamura T., Kawaichi S., Inoue T., Nomura K.,
RA   Yoshida Y., Kuno S., Sako Y.;
RT   "Variation of the Virus-Related Elements within Syntenic Genomes of
RT   the Hyperthermophilic Archaeon Aeropyrum.";
RL   Appl. Environ. Microbiol. 79:5891-5898(2013).
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; AP012489; BAN89996.1; -; Genomic_DNA.
DR   EnsemblBacteria; BAN89996; BAN89996; ACAM_0527.
DR   KEGG; acj:ACAM_0527; -.
DR   PATRIC; fig|1198449.6.peg.532; -.
DR   KO; K04564; -.
DR   OrthoDB; POG093Z0AKF; -.
DR   Proteomes; UP000016887; 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:UP000016887};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:BAN89996.1}.
FT   DOMAIN        6     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    198       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        31     31       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       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   214 AA;  24593 MW;  AD2B80BB2A127E09 CRC64;
     MVSFKRYELP PLPYNYNALE PYIIEEIMRL HHQKHHNTYV KGANAALEKI EKHLRGEAQI
     DVRAVMRDFS FNYAGHIMHT IFWPNMAPPG KGGGTPGGRV ADLIEKQFGG FEKFKSLFSA
     AAKTVEGVGW GVLAFDPLTE ELRILQVEKH NVLMTAGLVP ILVIDVWEHA YYLQYKNDRG
     SYVDNWWNVV NWDDVEKRLE QALNNAKPLY LLPQ
//
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