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Database: UniProt/TrEMBL
Entry: A0A1V0SLW1_SPOUR
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ID   A0A1V0SLW1_SPOUR        Unreviewed;       202 AA.
AC   A0A1V0SLW1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   25-OCT-2017, entry version 5.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SporoP32a_00105 {ECO:0000313|EMBL:ARK20088.1},
GN   SporoS204_00120 {ECO:0000313|EMBL:ARF12710.1};
OS   Sporosarcina ureae.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae;
OC   Sporosarcina.
OX   NCBI_TaxID=1571 {ECO:0000313|EMBL:ARF12710.1, ECO:0000313|Proteomes:UP000192486};
RN   [1] {ECO:0000313|EMBL:ARF12710.1, ECO:0000313|Proteomes:UP000192486, ECO:0000313|Proteomes:UP000193533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P32a {ECO:0000313|EMBL:ARK20088.1,
RC   ECO:0000313|Proteomes:UP000193533}, and S204
RC   {ECO:0000313|EMBL:ARF12710.1, ECO:0000313|Proteomes:UP000192486};
RA   Oliver A.S., Cooper K.K.;
RT   "Comparative Genomics and Epigenetics of Sporosarcina ureae.";
RL   Submitted (APR-2016) 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; CP015108; ARF12710.1; -; Genomic_DNA.
DR   EMBL; CP015348; ARK20088.1; -; Genomic_DNA.
DR   RefSeq; WP_029054514.1; NZ_CP015348.1.
DR   KEGG; sure:SporoP32a_00105; -.
DR   KO; K04564; -.
DR   Proteomes; UP000192486; Chromosome.
DR   Proteomes; UP000193533; 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:UP000192486,
KW   ECO:0000313|Proteomes:UP000193533};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   202 AA;  22969 MW;  CBB7B0FD86480BE1 CRC64;
     MAYTLPELPY AYDALEPHID KETMNIHHTK HHNTYVTNVN NALEGHEELL NMPVDELVAN
     LDKVPEDKRT AVRNNGGGHS NHSLFWTILS PNGGGNPTGE VAEAIDKKFG SFDAFKEEFA
     KAATTRFGSG WAWLVVNNGE IEVTSTPNQD SPYMDGKTPL LGLDVWEHAY YLNYQNRRPD
     YISAFWNVVN WDEVEKRYQD NK
//
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