ID   A0A0N5BXC7_STREA        Unreviewed;       571 AA.
AC   A0A0N5BXC7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=5'-nucleotidase {ECO:0000313|WBParaSite:SPAL_0001045800.1};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001045800.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001045800.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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; A0A0N5BXC7; -.
DR   STRING; 174720.A0A0N5BXC7; -.
DR   WBParaSite; SPAL_0001045800.1; SPAL_0001045800.1; SPAL_0001045800.
DR   Proteomes; UP000046392; Unplaced.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07522; HAD_cN-II; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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:SF15; CYTOSOLIC PURINE 5'-NUCLEOTIDASE; 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        44
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT   ACT_SITE        46
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         46
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         334
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
SQ   SEQUENCE   571 AA;  66968 MW;  DD0B3EF9F4B8EC83 CRC64;
     MEINNNIKQN DSCEFRSLKK RNPDKRVFAN RNLRLEKIKW IGFDMDYTIA MYKSPQFENL
     QFKQIIERLV DVGYPKEFLK FEYDPIFPTR GLWFDYTYGN LLKVDEFGHI LKGMHGLRWL
     TTTEIEEQYP NKFITLTEQR VYVLNTLFNL PETHLIAQVI DYFENHSEFE QNPEKTGIQQ
     GDLTMTYKSI FKDIRKAVDY MHIQGTMKQD VIDNVNHYVD NDPRIAKMLL NLKENDKKIF
     LLTNSDYYYT NAIMKYILGD KWNTYFDITV VDARKPFWFA EGSLFREVDT VTGTIKIGAK
     KGPLASDIVY SGGNCETFSK LVKCKGRDVL YVGDHVYGDV LKSKKSRGWR TFLVVPEIVN
     ELNVWTKGRK YFDTLDKLEE LLSETYKSYD VTTRTKPDNK ELLEKLRRAT IDMESEYGVF
     GSLFRSGSSQ TFFACQLERF ADIYASSCVN LMYYPSFYFF RSPMKLMSHE LTVHHGSILF
     PSGRQGFYHN DTLGEKVRGW NREKRTSECD TFCEDEEDDD ISPQADNSFL LVDRKDSDTN
     QYDTNSEDKL TVKNFPYTDV ISHPNVQIDD L
//