ID A0A0N5D882_THECL Unreviewed; 352 AA.
AC A0A0N5D882;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=5'-nucleotidase {ECO:0000256|ARBA:ARBA00012643};
DE EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643};
GN ORFNames=TCLT_LOCUS9294 {ECO:0000313|EMBL:VDN06917.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000930501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000930501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN06917.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000815};
CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC {ECO:0000256|ARBA:ARBA00008389}.
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DR EMBL; UYYF01004767; VDN06917.1; -; Genomic_DNA.
DR STRING; 103827.A0A0N5D882; -.
DR WBParaSite; TCLT_0000930501-mRNA-1; TCLT_0000930501-mRNA-1; TCLT_0000930501.
DR OMA; THFISNM; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.10.150.340; Pyrimidine 5'-nucleotidase (UMPH-1), N-terminal domain; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
DR PANTHER; PTHR13045; 5'-NUCLEOTIDASE; 1.
DR PANTHER; PTHR13045:SF0; CYTOSOLIC 5'-NUCLEOTIDASE 3A; 1.
DR Pfam; PF05822; UMPH-1; 2.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000276776}.
SQ SEQUENCE 352 AA; 39658 MW; 67708AFC7F45904E CRC64;
MVIDILLKND KVRIRDVSTV EWKLNEMINA GKDKLLVISD FDYTLSRFHD AEGKSCCTTH
GVFDVAAQTV SKELETVLKN LKSKYLPIEF DPHMTIAEKM PHMENWWRTS HQHIIKAGFT
KQSIQNFVRE AKLELKTLNI FGFQGAHTVV PKYLVFREGA QEYILALHDY NVPLIIFSAG
VGNVIDFFMQ EAFGQLPNNV HIVSNMMKYN ENDVATAFSE PLIHTFSKNT AVISHYGSLL
NEISSRTSVL LLGDTLGDSN MDSGLKCELV ALKIGFLNYN DETLLNQYLH SYDIVLLDDQ
SLQVPSLILN SIFDGFSDEK NLSTCISCRF ESEDNAAIKE GESVSVESNA RA
//
