ID F7V6I6_CLOSS Unreviewed; 159 AA.
AC F7V6I6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN OrderedLocusNames=CXIVA_23980 {ECO:0000313|EMBL:BAK48365.1};
OS Clostridium sp. (strain SY8519).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK48365.1, ECO:0000313|Proteomes:UP000008937};
RN [1] {ECO:0000313|Proteomes:UP000008937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX PubMed=21914882; DOI=10.1128/JB.05637-11;
RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT intestine.";
RL J. Bacteriol. 193:5568-5569(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; AP012212; BAK48365.1; -; Genomic_DNA.
DR RefSeq; WP_013978322.1; NC_015737.1.
DR AlphaFoldDB; F7V6I6; -.
DR STRING; 1042156.CXIVA_23980; -.
DR KEGG; cls:CXIVA_23980; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_037162_11_2_9; -.
DR OrthoDB; 9804563at2; -.
DR Proteomes; UP000008937; Chromosome.
DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd03427; MTH1; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR003562; Mutator_MutX_prot.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR43758; 7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE; 1.
DR PANTHER; PTHR43758:SF2; OXIDIZED PURINE NUCLEOSIDE TRIPHOSPHATE HYDROLASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR01402; MUTATORMUTX.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008937}.
FT DOMAIN 1..128
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 159 AA; 18525 MW; DEFB05F22DB59824 CRC64;
MLMTTLCYIE QNDCYLMLHR TTKKNDINRD KWIGVGGKFE DRESPEECLL REVREETGLT
LTSWQFRGFL TFLAEDYEEE FICLYTADGF TGTLTDCNEG ELEWVPKSRI GSLNLWEGDR
IFLKKLMRQD PFFSMKLSYR GDTLTECRVD GVSVLPVSS
//