ID A0A3Q2D611_CYPVA Unreviewed; 292 AA.
AC A0A3Q2D611;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=5'-nucleotidase {ECO:0000256|RuleBase:RU361276};
DE EC=3.1.3.5 {ECO:0000256|RuleBase:RU361276};
GN Name=NT5C3B {ECO:0000313|Ensembl:ENSCVAP00000013892.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000013892.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000013892.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP + H2O = cytidine + phosphate; Xref=Rhea:RHEA:29367,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17562, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:60377; EC=3.1.3.91;
CC Evidence={ECO:0000256|ARBA:ARBA00036362};
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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 AlphaFoldDB; A0A3Q2D611; -.
DR Ensembl; ENSCVAT00000021561.1; ENSCVAP00000013892.1; ENSCVAG00000000420.1.
DR GeneTree; ENSGT00390000012959; -.
DR OMA; CHIFITL; -.
DR Proteomes; UP000265020; Unplaced.
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 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:SF15; 7-METHYLGUANOSINE PHOSPHATE-SPECIFIC 5'-NUCLEOTIDASE; 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:UP000265020}.
SQ SEQUENCE 292 AA; 33429 MW; EFFA4185F4081AE5 CRC64;
MSVSHICLSS GSVLMKDPQR VQEILQSMSK AGINTLQVIS DFDMTLTRFS YNGKRCPTCH
NILDNSKAIS DECRQELDHL LKTYYPIEID TSKPVSEKLP LMVEWWTKAH DLLVEQRIKK
DELAEAVRES DAMLREGYEL FFDRLHEHGI PLLIFSAGIG DILEEVIRQA NVFHSNVKVI
SNYMDFDESG RLKAFKGELI HIYNKREGAL LNTGHFEELR SRPNVLLMGD SLGDLNMADG
VQDMKYILKI GYLNDKVEER KQSYLDSYDI VLVNDESLEV PNAVLHYLTS NK
//