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Database: UniProt
Entry: A0A0W1SJ34_9GAMM
LinkDB: A0A0W1SJ34_9GAMM
Original site: A0A0W1SJ34_9GAMM 
ID   A0A0W1SJ34_9GAMM        Unreviewed;       203 AA.
AC   A0A0W1SJ34;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   18-JUL-2018, entry version 15.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AUR68_17870 {ECO:0000313|EMBL:KTG26211.1};
OS   Idiomarina sp. H105.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=1766622 {ECO:0000313|EMBL:KTG26211.1, ECO:0000313|Proteomes:UP000054149};
RN   [1] {ECO:0000313|EMBL:KTG26211.1, ECO:0000313|Proteomes:UP000054149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H105 {ECO:0000313|EMBL:KTG26211.1,
RC   ECO:0000313|Proteomes:UP000054149};
RA   Zhang G., Stingl U., Rashid M.;
RT   "The draft genome sequence of Idiomarina sp., isolated from Erba
RT   brine-seawater interface of Red Sea.";
RL   Submitted (DEC-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KTG26211.1}.
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DR   EMBL; LOPZ01000152; KTG26211.1; -; Genomic_DNA.
DR   EnsemblBacteria; KTG26211; KTG26211; AUR68_17870.
DR   Proteomes; UP000054149; Unassembled WGS sequence.
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:UP000054149};
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:UP000054149}.
FT   DOMAIN        3     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    197       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       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   203 AA;  22656 MW;  B87C31EF7B61D887 CRC64;
     MAHTLPELPY AYDALEPNID AMTMEIHHSR HHNTYVTNLN GALEGTGLED VPVEELVANL
     DRVPEEKRQA VINNGGGHAN HSMFWQMMSP NGGGQPHGDV AKAIDAELGG FDAFKDAFKK
     AALGRFGSGW AWLSVTPEKK LVVENTLNQD SPLMHGNTPV LGLDVWEHAY YLKFQNKRPD
     YVDAFFNVVN WEDVERRYQA AIA
//
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