ADAT1_CHICK
ID ADAT1_CHICK Reviewed; 503 AA.
AC Q5ZI16;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=RCJMB04_31g18;
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 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}.
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DR EMBL; AJ720968; CAG32627.1; -; mRNA.
DR RefSeq; NP_001012797.1; NM_001012779.1.
DR AlphaFoldDB; Q5ZI16; -.
DR SMR; Q5ZI16; -.
DR STRING; 9031.ENSGALP00000001334; -.
DR GeneID; 415886; -.
DR KEGG; gga:415886; -.
DR CTD; 23536; -.
DR VEuPathDB; HostDB:geneid_415886; -.
DR eggNOG; KOG2777; Eukaryota.
DR InParanoid; Q5ZI16; -.
DR OrthoDB; 947117at2759; -.
DR PhylomeDB; Q5ZI16; -.
DR PRO; PR:Q5ZI16; -.
DR Proteomes; UP000000539; 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..503
FT /note="tRNA-specific adenosine deaminase 1"
FT /id="PRO_0000287649"
FT DOMAIN 63..502
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT ACT_SITE 89
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 94
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 303
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
SQ SEQUENCE 503 AA; 55901 MW; A3CD6832D0A18C31 CRC64;
MWTADEIAEL CYEHYRSRLP KQGKPDPSRE WTSLAAVVKV ESAANEAGSA VLGTLQVAKE
VVALGTGTKC IGLNKMRKTG DVLNDSHAEV VAKRSFQRYL LHQMRLATSY QQCSIFIPGT
ETGKWKLKPN IIFIFFCSHT PCGDASIIPI RETENHLSKS VDGHDIAGQS VLCSSSNCDH
RGPEDKRKSE KMASSHMIKR MKNADGGFFS TITEDMAVQQ VFAKPEGNVN PECCESSEEM
QAANKETNAG KLKAVGVYRT GAKFVPGELS DTLIPGIEYH CVGLLRVKPG RGDRTCSMSC
SDKLARWNVL GCQGALLMHF LQYPVYLSAV IVGKCPYSQE AMQRAVIERC RHISLLPDGF
LTQEVQLLQS DLQFEHSRQA IQEGQTSSKR KLVPCSAAIS WSAVPEGPLD VTSDGFRQGT
TKKGIGSPQS RSKICKVELF HEFQKLVTSI SKENLPDTLR MKTLETYWDY KEAALNYQEA
WKALRSQALL GWIKNAQEYL LFM