ID   DNPH1_TRIAD             Reviewed;         144 AA.
AC   B3SAE4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_03036};
DE            EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03036};
GN   ORFNames=TRIADDRAFT_32238;
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Trichoplacidae; Trichoplax.
OX   NCBI_TaxID=10228;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999;
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of
CC       deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate
CC       and a purine or pyrimidine base. {ECO:0000255|HAMAP-Rule:MF_03036}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-
CC         deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase;
CC         Xref=Rhea:RHEA:57852, ChEBI:CHEBI:15377, ChEBI:CHEBI:26432,
CC         ChEBI:CHEBI:62877, ChEBI:CHEBI:142209; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03036};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-
CC         D-ribose 5-phosphate + a purine nucleobase; Xref=Rhea:RHEA:51132,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:26386, ChEBI:CHEBI:62877,
CC         ChEBI:CHEBI:142198; Evidence={ECO:0000255|HAMAP-Rule:MF_03036};
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_03036}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03036}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03036}.
CC   -!- SIMILARITY: Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase
CC       1 family. {ECO:0000255|HAMAP-Rule:MF_03036}.
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DR   EMBL; DS985261; EDV20245.1; -; Genomic_DNA.
DR   RefSeq; XP_002117195.1; XM_002117159.1.
DR   AlphaFoldDB; B3SAE4; -.
DR   SMR; B3SAE4; -.
DR   STRING; 10228.TriadP32238; -.
DR   PRIDE; B3SAE4; -.
DR   EnsemblMetazoa; TriadT32238; TriadP32238; TriadG32238.
DR   GeneID; 6758408; -.
DR   KEGG; tad:TRIADDRAFT_32238; -.
DR   CTD; 6758408; -.
DR   eggNOG; ENOG502S2J2; Eukaryota.
DR   HOGENOM; CLU_100069_1_0_1; -.
DR   InParanoid; B3SAE4; -.
DR   OMA; MHIYFCG; -.
DR   OrthoDB; 1533988at2759; -.
DR   PhylomeDB; B3SAE4; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0070694; F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity; ISS:UniProtKB.
DR   GO; GO:0009159; P:deoxyribonucleoside monophosphate catabolic process; ISS:UniProtKB.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR   HAMAP; MF_03036; Nuc_phosphate_hydrolase; 1.
DR   InterPro; IPR028607; DNPH1.
DR   InterPro; IPR007710; Nucleoside_deoxyribTrfase.
DR   Pfam; PF05014; Nuc_deoxyrib_tr; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosidase; Hydrolase; Nucleotide metabolism; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..144
FT                   /note="Putative 2'-deoxynucleoside 5'-phosphate N-hydrolase
FT                   1"
FT                   /id="PRO_0000379463"
FT   BINDING         7..13
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O35820"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
FT   BINDING         107..109
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
SQ   SEQUENCE   144 AA;  16248 MW;  15645E9DBEB06624 CRC64;
     MAKRSIYFCG SIRGGRNDAQ FYAKIIQHLK QYGDILTEHV GHCGPEEEGL DDKTIHDRDL
     AWLLQSDVIV AEVTQPSLGV GYELGRAIAA DKLVLCLFRP DSGRRLSGMI RGAINSVNFF
     VEDYHQDEYA SKIDQFFTVR VTRP