ID   A0A1I8ANL9_9BILA        Unreviewed;       502 AA.
AC   A0A1I8ANL9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=5'-nucleotidase domain-containing protein 3 {ECO:0000313|WBParaSite:L893_g758.t1};
OS   Steinernema glaseri.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g758.t1};
RN   [1] {ECO:0000313|WBParaSite:L893_g758.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR017434-2};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR017434-2};
CC   -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00009589}.
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DR   AlphaFoldDB; A0A1I8ANL9; -.
DR   WBParaSite; L893_g758.t1; L893_g758.t1; L893_g758.
DR   Proteomes; UP000095287; Unplaced.
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; HAD superfamily/HAD-like; 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   NCBIfam; TIGR02244; HAD-IG-Ncltidse; 1.
DR   PANTHER; PTHR12103; 5'-NUCLEOTIDASE DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR12103:SF39; FI20020P1; 1.
DR   Pfam; PF05761; 5_nucleotid; 1.
DR   PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR017434-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR017434-2}.
FT   ACT_SITE        64
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT   ACT_SITE        66
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT   BINDING         64
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         66
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         341
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
SQ   SEQUENCE   502 AA;  58362 MW;  51BF9EFFDF1324EA CRC64;
     MAVLSRTLYC CKRIASAQTL HNAYKKAQEL VSHHRPSYPP RIDPRGVFAN NELNLHKIGV
     YGFDYDYTLA VYTRELSPLI YSLAINRLVT RLKYPEGLLK IAYDPIFAIR GLHFDVDHCC
     LLKVDAFNQI QKGTVYRGRK KLTDDEVVEL YGGSSLSDEK GRSLPQLIDL FSLPWAGLLA
     TVVQFFDDNN IMFDPVCLYQ DVAEAVRQVH VTGEMYASVS ANMEKYVHQN VGLKEYLERL
     HNNGKELFMV TNSPFSFMNI GMCYMLGDDW RRLFKYIVVS AKKPNFFQGK APFRLYLEQE
     DTLWYERVTD LKPGRIYAGG NITDFSKKAK FQNSGVLYFG DHIYTDLADP MLQLGWHTAA
     IVPELAREIR AQNHEEFRSA IMWLEMLTSL IEAYQCYELT DDKAKYEFKK WILERRALRE
     KTKAMFNPQF GSMFRTYHNM TYFSRRLGRL SDIYTSRLPN MLKYSDEHTF FPRRNALPHE
     THLHIQHVQA PVDGDDLILD AD
//