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Database: UniProt
Entry: A0A069JSB4_9ACTN
LinkDB: A0A069JSB4_9ACTN
Original site: A0A069JSB4_9ACTN 
ID   A0A069JSB4_9ACTN        Unreviewed;       153 AA.
AC   A0A069JSB4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=8-oxo-dGTP diphosphatase {ECO:0000256|ARBA:ARBA00038905};
DE            EC=3.6.1.55 {ECO:0000256|ARBA:ARBA00038905};
GN   ORFNames=DT87_10410 {ECO:0000313|EMBL:KDQ67608.1};
OS   Streptomyces sp. NTK 937.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ67608.1, ECO:0000313|Proteomes:UP000027475};
RN   [1] {ECO:0000313|EMBL:KDQ67608.1, ECO:0000313|Proteomes:UP000027475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ67608.1,
RC   ECO:0000313|Proteomes:UP000027475};
RA   Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT   "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT   producer of the benzoxazol antibiotic caboxamycin.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896; EC=3.6.1.55;
CC         Evidence={ECO:0000256|ARBA:ARBA00035861};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC       {ECO:0000256|ARBA:ARBA00005582, ECO:0000256|RuleBase:RU003476}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDQ67608.1}.
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DR   EMBL; JJOB01000001; KDQ67608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A069JSB4; -.
DR   OrthoDB; 9804442at2; -.
DR   Proteomes; UP000027475; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR047127; MutT-like.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR47707; 8-OXO-DGTP DIPHOSPHATASE; 1.
DR   PANTHER; PTHR47707:SF1; NUDIX HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003476};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Mutator protein {ECO:0000256|ARBA:ARBA00022457}.
FT   DOMAIN          22..151
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   153 AA;  16545 MW;  C4D6D332BC988EEB CRC64;
     MNAPVDAALL GNLIHAADAD SITKHVVGAV ISTAEGHVLL LHRSADDYLG GLWELPSGGV
     DAGETLTEAL HREVAEETGL TVAAIGTYLG HFDYLSKSGK TTRQFNFTAR VTRESDTVKL
     TEHDAHLWAD RTEQERVSGA VRDVLAIWRE KTA
//
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