ID H8GTW8_DEIGI Unreviewed; 312 AA.
AC H8GTW8;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=MutT/nudix family protein {ECO:0000313|EMBL:AFD26608.1};
GN OrderedLocusNames=DGo_CA2681 {ECO:0000313|EMBL:AFD26608.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD26608.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD26608.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(2012).
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|RuleBase:RU003476}.
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DR EMBL; CP002191; AFD26608.1; -; Genomic_DNA.
DR AlphaFoldDB; H8GTW8; -.
DR STRING; 745776.DGo_CA2681; -.
DR KEGG; dgo:DGo_CA2681; -.
DR PATRIC; fig|745776.4.peg.2749; -.
DR eggNOG; COG1051; Bacteria.
DR HOGENOM; CLU_890593_0_0_0; -.
DR Proteomes; UP000007575; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 2.
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; PTHR43046:SF2; 8-OXO-DGTP DIPHOSPHATASE; 1.
DR PANTHER; PTHR43046; GDP-MANNOSE MANNOSYL HYDROLASE; 1.
DR Pfam; PF00293; NUDIX; 2.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; Nudix; 2.
DR PROSITE; PS51462; NUDIX; 2.
DR PROSITE; PS00893; NUDIX_BOX; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003476}.
FT DOMAIN 1..146
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT DOMAIN 171..304
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 312 AA; 33943 MW; FA595A0095FBD342 CRC64;
MAAGLLIENE RGEVLLQRRG DDGLWGLPGG AVESGEDFLA AARRELREET GLECPDLTWL
GLHDGLVSGP DLYGRYPHGD EIYIVDVLFY GTLPARALEH ACPDDSGETL ELGWFAHDSL
PTISGSINVV CLNILRRRAG LPPLALPPRP PRRPDPGYWA DLARLLDGRP WFVPGASVYV
EDDLGRLLLL RDAESGQWTL PGGKLEPGEG LEACARRELR EETGLEAASL EPLHLLAGPE
FRYRDGAGVW DSVGVAYRAQ GVRGELRLPA GEVTEARYVR AAELDGLDLL GPYTRRAVAL
WREAQAGAAS TV
//
