ID   ADAT1_XENTR             Reviewed;         472 AA.
AC   Q28FE8;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=tRNA-specific adenosine deaminase 1;
DE            EC=3.5.4.34;
DE   AltName: Full=tRNA-specific adenosine-37 deaminase;
GN   Name=adat1; ORFNames=TEgg036c08.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in
CC         tRNA(Ala) + NH4(+); Xref=Rhea:RHEA:50968, Rhea:RHEA-COMP:12855,
CC         Rhea:RHEA-COMP:12856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.34;
CC   -!- COFACTOR:
CC       Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
CC       {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the ADAT1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR762003; CAJ83671.1; -; mRNA.
DR   RefSeq; NP_001037984.1; NM_001044519.1.
DR   AlphaFoldDB; Q28FE8; -.
DR   SMR; Q28FE8; -.
DR   STRING; 8364.ENSXETP00000058713; -.
DR   PaxDb; Q28FE8; -.
DR   GeneID; 733776; -.
DR   KEGG; xtr:733776; -.
DR   CTD; 23536; -.
DR   Xenbase; XB-GENE-1002540; adat1.
DR   eggNOG; KOG2777; Eukaryota.
DR   InParanoid; Q28FE8; -.
DR   OrthoDB; 947117at2759; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; ISS:UniProtKB.
DR   GO; GO:0008033; P:tRNA processing; ISS:UniProtKB.
DR   InterPro; IPR002466; A_deamin.
DR   Pfam; PF02137; A_deamin; 1.
DR   SMART; SM00552; ADEAMc; 1.
DR   PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..472
FT                   /note="tRNA-specific adenosine deaminase 1"
FT                   /id="PRO_0000287650"
FT   DOMAIN          59..471
FT                   /note="A to I editase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   ACT_SITE        85
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         90
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT   BINDING         274
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         405
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   472 AA;  53186 MW;  124B46C760F6487B CRC64;
     MQAKGLWSAD EIAALSYGHY TTQLPKQGLP DPSREWTLMA AVIQIESVED TKVIKKVVAM
     GTGTKCIGQA KLRKTGDVLQ DSHAEIIAKR SFQRYLLHQL SLAVSDTKDC LFIPGTEKGK
     WMLRPEISFV FFTSHTPCGD ASIIPVISHE DELGHPLPSE VTEKDHSSNN VCESVNTTYK
     RKVRSEEDIG FISKKMKHSI DEILTRPENY EEENRHDFPS TCQKALDVHR TGAKCVAGEL
     QDSYSPGVNY HTVGVLRIKP GRGDRTMSMS CSDKMARWNV LGCQGALLMH FLQQPIYLSA
     VVVGKCPFSQ DAMERALYNR CHKVLSLPCA FRLNRVQIIQ SDLEFQHGRH ALTKKDATRK
     LVPCGAAVSW SAVPHHPLDV TANGYRQGTT RKAIGSPQCR SRICKAEIFN TFRELVQRLS
     EKQRSESLSS QGLKTYWDYK AAAITYQEAW NCLRQQAFTS WIQTPRDFLM FS