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Database: UniProt/TrEMBL
Entry: F2KQT8_ARCVS
LinkDB: F2KQT8_ARCVS
Original site: F2KQT8_ARCVS 
ID   F2KQT8_ARCVS            Unreviewed;       198 AA.
AC   F2KQT8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   28-MAR-2018, entry version 34.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Arcve_0629 {ECO:0000313|EMBL:AEA46650.1};
OS   Archaeoglobus veneficus (strain DSM 11195 / SNP6).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=693661 {ECO:0000313|EMBL:AEA46650.1, ECO:0000313|Proteomes:UP000008136};
RN   [1] {ECO:0000313|EMBL:AEA46650.1, ECO:0000313|Proteomes:UP000008136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SNP6;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA   Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Archaeoglobus veneficus SNP6.";
RL   Submitted (MAR-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; CP002588; AEA46650.1; -; Genomic_DNA.
DR   RefSeq; WP_013683324.1; NC_015320.1.
DR   ProteinModelPortal; F2KQT8; -.
DR   STRING; 693661.Arcve_0629; -.
DR   EnsemblBacteria; AEA46650; AEA46650; Arcve_0629.
DR   GeneID; 10393726; -.
DR   KEGG; ave:Arcve_0629; -.
DR   eggNOG; arCOG04147; Archaea.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG093Z0AKF; -.
DR   BioCyc; AVEN693661:G1GSI-628-MONOMER; -.
DR   Proteomes; UP000008136; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
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:UP000008136};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AEA46650.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008136}.
FT   DOMAIN        4     83       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       90    192       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       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   198 AA;  22868 MW;  DD63F349C2E4072E CRC64;
     MSRYVLPELP YEYNALEPYI SEEILKLHHD KHHSAYVKGA NAALEKLEKA RKGEIEVDIK
     AVLKELSFHV GGHILHTIFW NCMTPEKGEP SGVLAEKIKE EFGSVERFKD EFSKAANSVE
     GSGWAALMYC PLTGRLIIQQ IEKHNVNLAP GLHILACIDV WEHAYYLQYK NDRASFVKNW
     WNVVNWNFIE ERLKEAMK
//
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