ADAT1_DROME
ID ADAT1_DROME Reviewed; 394 AA.
AC Q9V3R6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=tRNA-specific adenosine deaminase 1;
DE EC=3.5.4.34;
DE AltName: Full=dADAT1;
DE AltName: Full=tRNA-specific adenosine-37 deaminase;
GN Name=Adat1 {ECO:0000312|FlyBase:FBgn0028658}; Synonyms=adat;
GN ORFNames=CG16889 {ECO:0000312|FlyBase:FBgn0028658};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=10629039; DOI=10.1128/mcb.20.3.825-833.2000;
RA Keegan L.P., Gerber A.P., Brindle J., Leemans R., Gallo A., Keller W.,
RA O'Connell M.A.;
RT "The properties of a tRNA-specific adenosine deaminase from Drosophila
RT melanogaster support an evolutionary link between pre-mRNA editing and tRNA
RT modification.";
RL Mol. Cell. Biol. 20:825-833(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC -!- FUNCTION: Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
CC {ECO:0000269|PubMed:10629039}.
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 Evidence={ECO:0000269|PubMed:10629039};
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 -!- TISSUE SPECIFICITY: Widely expressed in early embryos, and later
CC concentrates in the central nervous system.
CC {ECO:0000269|PubMed:10629039}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:10629039}.
CC -!- SIMILARITY: Belongs to the ADAT1 family. {ECO:0000305}.
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DR EMBL; AF192530; AAF06773.1; -; mRNA.
DR EMBL; AE014134; AAF53333.1; -; Genomic_DNA.
DR RefSeq; NP_001260450.1; NM_001273521.1.
DR RefSeq; NP_609676.1; NM_135832.3.
DR AlphaFoldDB; Q9V3R6; -.
DR SMR; Q9V3R6; -.
DR BioGRID; 60820; 6.
DR STRING; 7227.FBpp0080150; -.
DR PaxDb; Q9V3R6; -.
DR EnsemblMetazoa; FBtr0080573; FBpp0080150; FBgn0028658.
DR EnsemblMetazoa; FBtr0331627; FBpp0304017; FBgn0028658.
DR GeneID; 34787; -.
DR KEGG; dme:Dmel_CG16889; -.
DR UCSC; CG16889-RA; d. melanogaster.
DR CTD; 23536; -.
DR FlyBase; FBgn0028658; Adat1.
DR VEuPathDB; VectorBase:FBgn0028658; -.
DR eggNOG; KOG2777; Eukaryota.
DR GeneTree; ENSGT00940000168020; -.
DR HOGENOM; CLU_005382_5_1_1; -.
DR InParanoid; Q9V3R6; -.
DR OMA; IGRCQNV; -.
DR OrthoDB; 947117at2759; -.
DR PhylomeDB; Q9V3R6; -.
DR BRENDA; 3.5.4.34; 1994.
DR BioGRID-ORCS; 34787; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Adat1; fly.
DR GenomeRNAi; 34787; -.
DR PRO; PR:Q9V3R6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0028658; Expressed in neurectoderm and 14 other tissues.
DR ExpressionAtlas; Q9V3R6; baseline and differential.
DR Genevisible; Q9V3R6; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IDA:FlyBase.
DR GO; GO:0006382; P:adenosine to inosine editing; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IDA:FlyBase.
DR GO; GO:0008033; P:tRNA processing; IMP: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 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..394
FT /note="tRNA-specific adenosine deaminase 1"
FT /id="PRO_0000287651"
FT DOMAIN 54..388
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT ACT_SITE 80
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 84
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 194
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
SQ SEQUENCE 394 AA; 45350 MW; 7EBB8124F1EF9828 CRC64;
MCDNKKPTVK EIAELCLKKF ESLPKTGKPT ANQWTILAGI VEFNRNTEAC QLVSLGCGTK
CIGESKLCPN GLILNDSHAE VLARRGFLRF LYQELKQDRI FHWNSTLSTY DMDEHVEFHF
LSTQTPCGDA CILEEEQPAA RAKRQRLDED SEMVYTGAKL ISDLSDDPML QTPGALRTKP
GRGERTLSMS CSDKIARWNV IGVQGALLDV LISKPIYFSS LNFCCDDAQL ESLERAIFKR
FDCRTFKHTR FQPQRPQINI DPGIRFEFSQ RSDWQPSPNG LIWSQVPEEL RPYEISVNGK
RQGVTKKKMK TSQAALAISK YKLFLTFLEL VKFNPKLSEM FDQQLSDPER IAYASCKDLA
RDYQFAWREI KEKYFLQWTK KPHELLDFNP MSNK
