ID A0A151X9L3_9HYME Unreviewed; 311 AA.
AC A0A151X9L3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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};
GN ORFNames=ALC60_03997 {ECO:0000313|EMBL:KYQ57009.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ57009.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ57009.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ57009.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ57009.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-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}.
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DR EMBL; KQ982373; KYQ57009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151X9L3; -.
DR STRING; 64791.A0A151X9L3; -.
DR Proteomes; UP000075809; 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:UP000075809}.
SQ SEQUENCE 311 AA; 35847 MW; D67777B196E10194 CRC64;
MRTSSWLVGR FIATCNARWQ LAFGTKQFPA LRSKHVYIRD KVAVLETINA IRQSGVNNLQ
IVTDFDLTLT KQHIDGRHVL SSFGMFRKCK QLPQQYLDKA KDLYDKYRPI EIDPEMPVNE
KADAMRDWMN AAQNLLKGIE FDPHELEEVA QAFDNILRDG TEEFFEKLYN TKVPIIIFSA
GLGDIVEAVL RYHNALFDNV KIFSNFLKYN GNQLDGFKND MPIHVYNKNE CALEKNYLKI
LQKRQNVLLM GDTVGDANMV EGIEDTKAVL KIGFLYEHVE ASLNSFMENF DIVLIDDQTM
QVPIEIIQNI L
//