ID   MUTT4_MYCTO             Reviewed;         248 AA.
AC   P9WIX6; L0TFL7; O05437; Q8VIR0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Putative mutator protein MutT4;
DE            EC=3.6.1.-;
GN   Name=mutT4; OrderedLocusNames=MT4027;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: May be involved in the GO system responsible for removing an
CC       oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-
CC       dGTP) from DNA and the nucleotide pool. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48392.1; -; Genomic_DNA.
DR   PIR; E70600; E70600.
DR   RefSeq; WP_003400124.1; NZ_KK341228.1.
DR   AlphaFoldDB; P9WIX6; -.
DR   SMR; P9WIX6; -.
DR   EnsemblBacteria; AAK48392; AAK48392; MT4027.
DR   GeneID; 45427908; -.
DR   KEGG; mtc:MT4027; -.
DR   PATRIC; fig|83331.31.peg.4333; -.
DR   HOGENOM; CLU_037162_14_3_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Mutator protein.
FT   CHAIN           1..248
FT                   /note="Putative mutator protein MutT4"
FT                   /id="PRO_0000427928"
FT   DOMAIN          62..198
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           103..124
FT                   /note="Nudix box"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   248 AA;  27171 MW;  270A5193861EADD3 CRC64;
     MSDGEQAKSR RRRGRRRGRR AAATAENHMD AQPAGDATPT PATAKRSRSR SPRRGSTRMR
     TVHETSAGGL VIDGIDGPRD AQVAALIGRV DRRGRLLWSL PKGHIELGET AEQTAIREVA
     EETGIRGSVL AALGRIDYWF VTDGRRVHKT VHHYLMRFLG GELSDEDLEV AEVAWVPIRE
     LPSRLAYADE RRLAEVADEL IDKLQSDGPA ALPPLPPSSP RRRPQTHSRA RHADDSAPGQ
     HNGPGPGP