5NT3B_CHICK
ID 5NT3B_CHICK Reviewed; 289 AA.
AC Q5ZKF6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=7-methylguanosine phosphate-specific 5'-nucleotidase {ECO:0000250|UniProtKB:Q9W197};
DE Short=7-methylguanosine nucleotidase;
DE EC=3.1.3.91 {ECO:0000250|UniProtKB:Q9W197};
DE AltName: Full=Cytosolic 5'-nucleotidase 3B;
DE AltName: Full=Cytosolic 5'-nucleotidase III-like protein {ECO:0000250|UniProtKB:Q9W197};
DE Short=cN-III-like protein;
DE EC=3.1.3.5 {ECO:0000250|UniProtKB:Q9W197};
DE AltName: Full=N(7)-methylguanylate 5'-phosphatase;
GN Name=NT5C3B; Synonyms=NT5C3L; ORFNames=RCJMB04_11c18;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Specifically hydrolyzes 7-methylguanosine monophosphate
CC (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific
CC activity for m(7)GMP may protect cells against undesired salvage of
CC m(7)GMP and its incorporation into nucleic acids. Also has weak
CC activity for CMP. UMP and purine nucleotides are poor substrates (By
CC similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q9W197};
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:0000250|UniProtKB:Q9W197};
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:0000250|UniProtKB:Q9W197};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC {ECO:0000305}.
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DR EMBL; AJ720128; CAG31787.1; -; mRNA.
DR RefSeq; NP_001006334.1; NM_001006334.1.
DR RefSeq; XP_015155089.1; XM_015299603.1.
DR RefSeq; XP_015155090.1; XM_015299604.1.
DR AlphaFoldDB; Q5ZKF6; -.
DR SMR; Q5ZKF6; -.
DR STRING; 9031.ENSGALP00000005776; -.
DR PaxDb; Q5ZKF6; -.
DR Ensembl; ENSGALT00000005786; ENSGALP00000005776; ENSGALG00000003651.
DR Ensembl; ENSGALT00000095514; ENSGALP00000069538; ENSGALG00000003651.
DR GeneID; 420034; -.
DR KEGG; gga:420034; -.
DR CTD; 115024; -.
DR VEuPathDB; HostDB:geneid_420034; -.
DR eggNOG; KOG3128; Eukaryota.
DR GeneTree; ENSGT00390000012959; -.
DR HOGENOM; CLU_048584_0_2_1; -.
DR InParanoid; Q5ZKF6; -.
DR OrthoDB; 1171042at2759; -.
DR PhylomeDB; Q5ZKF6; -.
DR TreeFam; TF314663; -.
DR Reactome; R-GGA-429958; mRNA decay by 3' to 5' exoribonuclease.
DR PRO; PR:Q5ZKF6; -.
DR Proteomes; UP000000539; Chromosome 27.
DR Bgee; ENSGALG00000003651; Expressed in granulocyte and 13 other tissues.
DR ExpressionAtlas; Q5ZKF6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07504; HAD_5NT; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
DR Pfam; PF05822; UMPH-1; 1.
DR SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01544; HAD-SF-IE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..289
FT /note="7-methylguanosine phosphate-specific 5'-
FT nucleotidase"
FT /id="PRO_0000328951"
FT ACT_SITE 38
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 85
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 85
FT /ligand="N(7)-methyl-GMP"
FT /ligand_id="ChEBI:CHEBI:58285"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
FT BINDING 153..154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0P0"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0P0"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9W197"
SQ SEQUENCE 289 AA; 33109 MW; 9DF06DC1F6EF099E CRC64;
MVPELQKSTV RIQQPERVMG VIRAIKEQGC SKLQVISDFD MTLSRFGCNG RRCPTSHNIL
DNSHVISEDG KKKLKDLLHH YYPIEIDPNR TLEEKRPLMV EWWTRAHELL SQQKIQKGDI
AQIVRESDVM LRDGFNELFD QLHKYSVPMF IFSAGVGDVL EEIIRQANVF YPNVNVVSNY
MDFDDSGVLK CFKSPLIHTY NKNNSVLQGT AYFQQLSTRT SIILLGDSMG DLTMADGVPS
VENILKIGFL NDKVEEQRGR YLDAYDIVLE SDETLDVVNG ILRYILMET
