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Database: UniProt
Entry: A0A0A7KH49_9DEIO
LinkDB: A0A0A7KH49_9DEIO
Original site: A0A0A7KH49_9DEIO 
ID   A0A0A7KH49_9DEIO        Unreviewed;       207 AA.
AC   A0A0A7KH49;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   28-MAR-2018, entry version 18.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=QR90_11190 {ECO:0000313|EMBL:AIZ45527.1};
OS   Deinococcus swuensis.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=1182571 {ECO:0000313|EMBL:AIZ45527.1, ECO:0000313|Proteomes:UP000030634};
RN   [1] {ECO:0000313|Proteomes:UP000030634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA   Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT   "Hymenobacter sp. DG25B genome submission.";
RL   Submitted (NOV-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; CP010028; AIZ45527.1; -; Genomic_DNA.
DR   RefSeq; WP_039684590.1; NZ_CP010028.1.
DR   EnsemblBacteria; AIZ45527; AIZ45527; QR90_11190.
DR   KEGG; dsw:QR90_11190; -.
DR   KO; K04564; -.
DR   Proteomes; UP000030634; 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:UP000030634};
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:UP000030634}.
FT   DOMAIN        3     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    202       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       173    173       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   207 AA;  23012 MW;  631434D0B44854EC CRC64;
     MAYQVPPLPY AYDALAPHID ARTMEIHHDK HHQAYVDNAN KALEGTEFAD LPVEELITRL
     DSVPADKKTA LRNNAGGHAN HSLFWTVMGP QGSTQPGGEL MTAINDAFGS FEDFKKKFED
     AAKTRFGSGW AWLVVQNGKL AVVSTANQDS PLMGEAISGT SGTPILGVDV WEHAYYLNYQ
     NKRPDYLEAF WNVVNWDEVA RRYADAK
//
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