ADAT1_DICDI
ID ADAT1_DICDI Reviewed; 545 AA.
AC Q54XP3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=DDB_G0278943;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(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; AAFI02000024; EAL68073.1; -; Genomic_DNA.
DR RefSeq; XP_641987.1; XM_636895.1.
DR AlphaFoldDB; Q54XP3; -.
DR SMR; Q54XP3; -.
DR STRING; 44689.DDB0230177; -.
DR PaxDb; Q54XP3; -.
DR EnsemblProtists; EAL68073; EAL68073; DDB_G0278943.
DR GeneID; 8621719; -.
DR KEGG; ddi:DDB_G0278943; -.
DR dictyBase; DDB_G0278943; -.
DR eggNOG; KOG2777; Eukaryota.
DR HOGENOM; CLU_005382_5_2_1; -.
DR InParanoid; Q54XP3; -.
DR OMA; PVNQTHP; -.
DR PhylomeDB; Q54XP3; -.
DR PRO; PR:Q54XP3; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0006400; P:tRNA modification; 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 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..545
FT /note="tRNA-specific adenosine deaminase 1"
FT /id="PRO_0000328176"
FT DOMAIN 59..541
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT REGION 171..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 89
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 318
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
SQ SEQUENCE 545 AA; 62484 MW; E3A9A77A3A8C50A8 CRC64;
MSWKLDKQFS DKICNFSHDF FNKKLIKKGK PISGEWTVLA TLVLVVENTS SYEIKQVLSL
GTGNRCLGKS SLSNQGDVLN DSHAEIICKR SFQKFCYNEI LNLLQSKYYN SILFNIEYHD
SNNNNKDNDN NGSLPTISIK KGHSLHFYVN QTPCGDCSIF PFKKETQPEN FIEKEKLEKD
GKDKIENHEK KEQKDIIKQV DKDKDEENYE DEESKRKLKK VKDDNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NINNNNNQYD DIQRTGAKTV FGEPEDKKLI GVDYHQIGVL
RVKPGRGDPT VSMSCSDKIA RWNVLGIQGS LLSHFIKEQI FLSSITIGDL FNHSSIYRGL
IGRLLPNPTT TTTETSSSSS SSSSSSNTIP NFKLNSDLEI FSTNIQFQFS KLLLESDQQN
NNKSTSSGLA ISFCYPNQHE VTIAINGKKM GTNQKNFNAI SQRSSICKFN LFKLFHQLVL
IIKNKNSNEE NEKNNQIVLI DSLFNYYECK HLSKKYYQEY EKLKEFKFKN WLTNSSDLEN
FVLDN
