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Database: UniProt
Entry: A0A384BQ19_URSMA
LinkDB: A0A384BQ19_URSMA
Original site: A0A384BQ19_URSMA 
ID   A0A384BQ19_URSMA        Unreviewed;       331 AA.
AC   A0A384BQ19;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=5'-nucleotidase {ECO:0000256|RuleBase:RU361276};
DE            EC=3.1.3.5 {ECO:0000256|RuleBase:RU361276};
GN   Name=NT5C3A {ECO:0000313|Ensembl:ENSUMAP00000003310,
GN   ECO:0000313|RefSeq:XP_008684693.1};
OS   Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008684693.1};
RN   [1] {ECO:0000313|Ensembl:ENSUMAP00000003310}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_008684693.1}
RP   IDENTIFICATION.
RC   TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008684693.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(7)-methyl-GMP = N(7)-methylguanosine + phosphate;
CC         Xref=Rhea:RHEA:37107, ChEBI:CHEBI:15377, ChEBI:CHEBI:20794,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58285; EC=3.1.3.91;
CC         Evidence={ECO:0000256|ARBA:ARBA00023710};
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}.
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DR   RefSeq; XP_008684693.1; XM_008686471.2.
DR   STRING; 29073.ENSUMAP00000003310; -.
DR   Ensembl; ENSUMAT00000004067.1; ENSUMAP00000003310.1; ENSUMAG00000002813.1.
DR   GeneID; 103658960; -.
DR   KEGG; umr:103658960; -.
DR   CTD; 51251; -.
DR   OrthoDB; 531581at2759; -.
DR   Proteomes; UP000261680; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
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   CDD; cd07504; HAD_5NT; 1.
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:UP000261680}.
SQ   SEQUENCE   331 AA;  37478 MW;  FB3BF3E82B7CAD8A CRC64;
     MDRAAVARMG AVASASVCVL VAGVVLAQYI FTLKRKTGRK TKIIEMMPEF QRSSVRIKNP
     ARVEEIICGL IKGGAPKLQI ITDFDMTLSR FSYEGKRCPT CHYVIDNSKL VTDECRKKLL
     QLKEKYYAIE IDPGLTMEEK YPYMVEWYTK SHGLLVEQAL PKAKLKEIVA ESDVMLKEGY
     ENFFDKLQEY GIPVFIFSAG IGDILEEVIH QAGVYHPNIT VVSNFMDFDD NGVLKGFKGE
     LIHVFNKHDG ALKNTEYFNR LKDNSNIILL GDSQGDIRMA DGVANVEHIL KIGYLNDRVD
     ELLEKYMDSY DIVLVKDESL DVANSILQKI L
//
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