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Database: UniProt/TrEMBL
Entry: A0A1V8MSK8_VIBVL
LinkDB: A0A1V8MSK8_VIBVL
Original site: A0A1V8MSK8_VIBVL 
ID   A0A1V8MSK8_VIBVL        Unreviewed;       170 AA.
AC   A0A1V8MSK8;
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 [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=XM78_c20300 {ECO:0000313|EMBL:OQK60702.1};
OS   Vibrio vulnificus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=672 {ECO:0000313|EMBL:OQK60702.1, ECO:0000313|Proteomes:UP000192157};
RN   [1] {ECO:0000313|EMBL:OQK60702.1, ECO:0000313|Proteomes:UP000192157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VN-0112 {ECO:0000313|EMBL:OQK60702.1,
RC   ECO:0000313|Proteomes:UP000192157};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-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:RU000393}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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:OQK60702.1}.
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DR   EMBL; MVKT01000114; OQK60702.1; -; Genomic_DNA.
DR   RefSeq; WP_011151698.1; NZ_MVKU01000121.1.
DR   GeneID; 2621413; -.
DR   KEGG; vvl:VV93_v1c32800; -.
DR   KO; K04565; -.
DR   Proteomes; UP000192157; 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   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000192157};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    170       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010726967.
FT   DOMAIN       32    169       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   170 AA;  17613 MW;  5AA2C93F1176704A CRC64;
     MNKHTLLAAI LLYSTSSFAQ SLSVDMKDLS SNQTLGTVTI SSSDYGTVFT PDLKGLPSGL
     HGFHLHANGS CESSNKDGKV VLGGAAGGHY DPQNSGKHGY PWTEDNHLGD LPALFVDASG
     NASQPVLAPR VALKDVQGRA LMIHAGADNH SDHPMPLGGG GARIVCGVIK
//
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