ID D2NRH0_ROTMD Unreviewed; 335 AA.
AC D2NRH0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=NTP pyrophosphohydrolase including oxidative damage repair enzyme {ECO:0000313|EMBL:BAI64246.1};
GN OrderedLocusNames=RMDY18_04140 {ECO:0000313|EMBL:BAI64246.1};
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64246.1, ECO:0000313|Proteomes:UP000001883};
RN [1] {ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAI64246.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64246.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT "Isolation and identification of Rothia mucilaginosa from persistent apical
RT periodontitis lesions.";
RL J Osaka Dent Univ 44:93-98(2010).
RN [3] {ECO:0000313|EMBL:BAI64246.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64246.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA Fukushima H.;
RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT Lesion.";
RL Sequencing 2010:457236-457236(2010).
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005582, ECO:0000256|RuleBase:RU003476}.
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DR EMBL; AP011540; BAI64246.1; -; Genomic_DNA.
DR RefSeq; WP_012903002.1; NC_013715.1.
DR AlphaFoldDB; D2NRH0; -.
DR STRING; 680646.RMDY18_04140; -.
DR KEGG; rmu:RMDY18_04140; -.
DR eggNOG; COG1051; Bacteria.
DR eggNOG; COG2062; Bacteria.
DR HOGENOM; CLU_048989_0_0_11; -.
DR Proteomes; UP000001883; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03673; Ap6A_hydrolase; 1.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
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; PTHR21340; DIADENOSINE 5,5-P1,P4-TETRAPHOSPHATE PYROPHOSPHOHYDROLASE MUTT; 1.
DR PANTHER; PTHR21340:SF8; NUDIX HYDROLASE; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003476};
KW Reference proteome {ECO:0000313|Proteomes:UP000001883}.
FT DOMAIN 30..157
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 335 AA; 36866 MW; 49655E3DCDBC105F CRC64;
MAPLDSPSIY YSARRFDAVN SIDRAPANTA DIVASGALIW RMRDGALEVL IIHRPRYDDW
SWPKGKQDPG ESLAETAIRE IREEVGLQVV LGVPLAVTSY PVGGRPKDVF YWAAELPDGA
RALADEGEVD ELRWVTTDVA RALLTNHDDL APLESLEALA EADALRTRPI LIARHAKAKP
RSNWAAAEDD RPLAATGKRQ ALASSRLFAA WAPSRIISSP WLRCVQTVTP YSVDYGVSVK
EKKSLSEAGA QRHPARVART VASLFDKDSS SLLCTHRPVL PRVMDVLREY LFEGSAEVLP
TEDPYLEPGD TLVLQVTEGD DPRIVSVERV RAALD
//
