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Database: UniProt
Entry: L8IBT2_9CETA
LinkDB: L8IBT2_9CETA
Original site: L8IBT2_9CETA 
ID   L8IBT2_9CETA            Unreviewed;       297 AA.
AC   L8IBT2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=5'-nucleotidase {ECO:0000256|RuleBase:RU361276};
DE            EC=3.1.3.5 {ECO:0000256|RuleBase:RU361276};
DE   Flags: Fragment;
GN   ORFNames=M91_17159 {ECO:0000313|EMBL:ELR53940.1};
OS   Bos mutus (wild yak).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR53940.1, ECO:0000313|Proteomes:UP000011080};
RN   [1] {ECO:0000313|EMBL:ELR53940.1, ECO:0000313|Proteomes:UP000011080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX   PubMed=22751099; DOI=10.1038/ng.2343;
RA   Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA   Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA   Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA   Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA   Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA   Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA   Wang J., Liu J.;
RT   "The yak genome and adaptation to life at high altitude.";
RL   Nat. Genet. 44:946-949(2012).
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   EMBL; JH881506; ELR53940.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8IBT2; -.
DR   STRING; 72004.ENSBMUP00000022645; -.
DR   Proteomes; UP000011080; 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   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:UP000011080}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ELR53940.1"
SQ   SEQUENCE   297 AA;  34419 MW;  9225923C500FB418 CRC64;
     QVSTLMKATV LMRQPGRVQE IVGALRKGGE DRLQVISDFD MTLSRFAYNG IRCPSSYNIL
     DNSKIISEEC RKELKALFHH YYPIEIDPHR TIKEKLPHMV EWWTKAHDLL CQQKIQKFQI
     AQVVRESNAM LRDGYKTFFN TLSQNNIPLF IFSAGIGDVL EEMIRQRKVF HPNIHIMSNY
     MEFDEDGFLN GFKGQLIHTY NKNSSVFENS NYFQQLQGKT NILLLGDSMG DLTMADGVPG
     VENILKIGFL NDKVEERRER YMDSYDIVLE RDETLDVVNG LLQHILQQGD WTEMQGS
//
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