ADAT2_XENLA
ID ADAT2_XENLA Reviewed; 175 AA.
AC Q4V7V8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=tRNA-specific adenosine deaminase 2;
DE EC=3.5.4.33 {ECO:0000305};
DE AltName: Full=Deaminase domain-containing protein 1;
DE AltName: Full=tRNA-specific adenosine-34 deaminase subunit ADAT2;
GN Name=adat2; Synonyms=deadc1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably participates in deamination of adenosine-34 to
CC inosine in many tRNAs. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT2 subfamily. {ECO:0000305}.
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DR EMBL; BC097698; AAH97698.1; -; mRNA.
DR RefSeq; NP_001089483.1; NM_001096014.1.
DR AlphaFoldDB; Q4V7V8; -.
DR SMR; Q4V7V8; -.
DR DNASU; 734534; -.
DR GeneID; 734534; -.
DR CTD; 734534; -.
DR Xenbase; XB-GENE-963032; adat2.L.
DR OrthoDB; 1616309at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 734534; Expressed in zone of skin and 19 other tissues.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:InterPro.
DR HAMAP; MF_00972; tRNA_aden_deaminase; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR028883; tRNA_aden_deaminase.
DR Pfam; PF14437; MafB19-deam; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..175
FT /note="tRNA-specific adenosine deaminase 2"
FT /id="PRO_0000287656"
FT DOMAIN 8..133
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 61
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 175 AA; 19505 MW; 90F9BD0FFAFFA1EB CRC64;
MEPLQITEEI QNWMHKAFQM AQDALNNGEV PVGCLMVYGN QVVGKGRNEV NETKNATQHA
EMVAIDQVLD WCEMNSKKST DVFENIVLYV TVEPCIMCAG ALRLLKIPLV VYGCRNERFG
GCGSVLNVSG DDIPDTGTKF KCIGGYQAEK AIELLKTFYK QENPNAPKSK VRKKE
