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Database: UniProt/TrEMBL
Entry: W0K3A4_9EURY
LinkDB: W0K3A4_9EURY
Original site: W0K3A4_9EURY 
ID   W0K3A4_9EURY            Unreviewed;       200 AA.
AC   W0K3A4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   25-OCT-2017, entry version 18.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HALDL1_10425 {ECO:0000313|EMBL:AHG03970.1};
OS   Halobacterium sp. DL1.
OC   Archaea; Euryarchaeota; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=751944 {ECO:0000313|EMBL:AHG03970.1, ECO:0000313|Proteomes:UP000004595};
RN   [1] {ECO:0000313|EMBL:AHG03970.1, ECO:0000313|Proteomes:UP000004595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DL1 {ECO:0000313|EMBL:AHG03970.1,
RC   ECO:0000313|Proteomes:UP000004595};
RG   DOE Joint Genome Institute;
RA   Cavicchioli R., Huntemann M., Han J., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Palaniappan K., Ivanova N.,
RA   Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N.,
RA   Hua S.X., Woyke T.;
RL   Submitted (JAN-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; CP007060; AHG03970.1; -; Genomic_DNA.
DR   RefSeq; WP_009761252.1; NZ_CP007060.1.
DR   ProteinModelPortal; W0K3A4; -.
DR   EnsemblBacteria; AHG03970; AHG03970; HALDL1_10425.
DR   GeneID; 25141779; -.
DR   KEGG; hdl:HALDL1_10425; -.
DR   KO; K04564; -.
DR   OrthoDB; POG093Z0AKF; -.
DR   Proteomes; UP000004595; 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:UP000004595};
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:UP000004595}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    190       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       158    158       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   200 AA;  22300 MW;  44569C643FC88490 CRC64;
     MSQHELPPLP YDYDALEPHI SEQVLTWHHD THHQGYVNGL NAAEGTLAEN RESGEYGSTA
     GALGSVTHNG SGHYLHTMFW ENMSENGGGE PSGELADRIE EDFGSYEGWK GEFKAAASAA
     GGWALLVYDP VSKQLRNLAV DKHDQGALWG SHPILALDVW EHSYYYDYGP KRGDFIDAFF
     EVVDWDDVAE NYQKTVSNHE
//
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