ID A0A0V0X2Y0_9BILA Unreviewed; 335 AA.
AC A0A0V0X2Y0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=5'-nucleotidase {ECO:0000256|ARBA:ARBA00012643, ECO:0000256|RuleBase:RU361276};
DE EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643, ECO:0000256|RuleBase:RU361276};
DE Flags: Fragment;
GN Name=F25B5.3 {ECO:0000313|EMBL:KRX81923.1};
GN ORFNames=T06_14555 {ECO:0000313|EMBL:KRX81923.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81923.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX81923.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX81923.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 ECO:0000256|RuleBase:RU361276};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361276}.
CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC {ECO:0000256|ARBA:ARBA00008389, ECO:0000256|RuleBase:RU361276}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX81923.1}.
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DR EMBL; JYDK01000026; KRX81923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0X2Y0; -.
DR STRING; 92179.A0A0V0X2Y0; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 NCBIfam; TIGR01544; HAD-SF-IE; 1.
DR PANTHER; PTHR13045; 5'-NUCLEOTIDASE; 1.
DR PANTHER; PTHR13045:SF0; CYTOSOLIC 5'-NUCLEOTIDASE 3A; 1.
DR Pfam; PF05822; UMPH-1; 1.
DR SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU361276};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361276};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080,
KW ECO:0000256|RuleBase:RU361276};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361276};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..335
FT /note="5'-nucleotidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006872343"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX81923.1"
SQ SEQUENCE 335 AA; 38622 MW; 87244E94CAFC0666 CRC64;
LSYSFMGIIC LHALFMFRYT SVSFAEMSGY LSITSVAKSL CDSLTKNSSV IIPDPTLFCQ
KWITLKRAFP DKLQVVSDFD KTLSKYQLKN GDLAWSTHDV VEQSIFQTDK EIFAQFKSLR
EKYYPVEFDP HMSDEDKIPS MEHWWKSCHD LIVKSKTKAS SLEAFTAKSK LILRREVSVF
FDILQRNRIP FIIFSAGIGD VITYVLKRHL KSVPENVHLI SNFFELNDEG IVCGFKEPMI
HTFNKNASVI VDEGKCFYEK IRNRDCVLLI GDSLGDVHMD VGVVTERCIL KVGFLNENCE
KLKQRYKSEY DVIICNDQTF RIPNHILQSM LHTTS
//