ID   NT5D3_XENLA             Reviewed;         499 AA.
AC   Q6GN91;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=5'-nucleotidase domain-containing protein 3;
DE            EC=3.1.3.-;
GN   Name=nt5dc3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC       {ECO:0000305}.
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DR   EMBL; BC073624; AAH73624.1; -; mRNA.
DR   RefSeq; NP_001085970.1; NM_001092501.1.
DR   AlphaFoldDB; Q6GN91; -.
DR   SMR; Q6GN91; -.
DR   DNASU; 444399; -.
DR   GeneID; 444399; -.
DR   KEGG; xla:444399; -.
DR   CTD; 444399; -.
DR   Xenbase; XB-GENE-940467; nt5dc3.S.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 444399; Expressed in spleen and 19 other tissues.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR016695; Pur_nucleotidase.
DR   PANTHER; PTHR12103; PTHR12103; 1.
DR   Pfam; PF05761; 5_nucleotid; 1.
DR   PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR02244; HAD-IG-Ncltidse; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..499
FT                   /note="5'-nucleotidase domain-containing protein 3"
FT                   /id="PRO_0000326249"
FT   ACT_SITE        50
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        52
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         337
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   499 AA;  58786 MW;  ABCC67C9DC8CD623 CRC64;
     MRGYLNSNYK EVKRSINELD PSISSNLLNP DAIFANNEMS LEDIEVYGFD YDYTLAFYSK
     HLHTLIFNTA RDILINEHRY PKEIQRYEYD PNFAIRGLHY DVHKALLMKI DSFHYIQLGT
     VYRGLNVVPD SEVIEMYEGS HVPLEQMSDF YGKSSEGNTM KQFMDIFSLP EMTLLCCVNE
     YFLKNNIDYE PVHLYKDVKE AIRDVHVKGI LYRAVEADIE RYICYGERTQ AVLSKLSNHG
     KKMFLITNSP SSFVNKGMNF IVGKDWRDLF DVVIVQADKP NFFNDKRRPF RKVAERGILL
     WDKIHHLEKG QTYKQGNLFE FLKLTGWRGS KVLYFGDHIY SDLADLTLKH GWRTGAIIPE
     LKSEIEIMNT SHYIKTMAWL QGLTGLLERM QVYRDAESQM VLQDWIKERQ ETRDLTKTMF
     NRQFGSIFRT DHNPTYFLRR LSRFADIYME SLSSLLNYDL HHTFYPKRTP LQHELPVCSE
     QQYANTFRIP LGRETAPIK