SYQ_DROME
ID SYQ_DROME Reviewed; 778 AA.
AC Q9Y105; Q9VBU3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable glutamine--tRNA ligase;
DE EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897};
DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000312|FlyBase:FBgn0027090};
GN Name=GlnRS {ECO:0000312|FlyBase:FBgn0027090};
GN Synonyms=Aats-gln {ECO:0000312|FlyBase:FBgn0027090};
GN ORFNames=CG10506 {ECO:0000312|FlyBase:FBgn0027090};
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 [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 [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC ChEBI:CHEBI:456215; EC=6.1.1.18;
CC Evidence={ECO:0000250|UniProtKB:P47897};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF56434.2; -; Genomic_DNA.
DR EMBL; AF145668; AAD38643.1; -; mRNA.
DR RefSeq; NP_524841.1; NM_080102.5.
DR AlphaFoldDB; Q9Y105; -.
DR SMR; Q9Y105; -.
DR BioGRID; 69882; 8.
DR DIP; DIP-18324N; -.
DR IntAct; Q9Y105; 4.
DR STRING; 7227.FBpp0084240; -.
DR PaxDb; Q9Y105; -.
DR PRIDE; Q9Y105; -.
DR EnsemblMetazoa; FBtr0084866; FBpp0084240; FBgn0027090.
DR GeneID; 45786; -.
DR KEGG; dme:Dmel_CG10506; -.
DR CTD; 45786; -.
DR FlyBase; FBgn0027090; GlnRS.
DR VEuPathDB; VectorBase:FBgn0027090; -.
DR eggNOG; KOG1148; Eukaryota.
DR GeneTree; ENSGT00940000168831; -.
DR HOGENOM; CLU_001882_2_3_1; -.
DR InParanoid; Q9Y105; -.
DR OMA; INNFCAQ; -.
DR OrthoDB; 809861at2759; -.
DR PhylomeDB; Q9Y105; -.
DR BioGRID-ORCS; 45786; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 45786; -.
DR PRO; PR:Q9Y105; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0027090; Expressed in oviduct (Drosophila) and 25 other tissues.
DR Genevisible; Q9Y105; DM.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; TAS:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 1.10.10.2420; -; 1.
DR Gene3D; 1.10.8.1290; -; 1.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth.
DR InterPro; IPR007638; Gln-tRNA-synth_Ib_RNA-bd_2.
DR InterPro; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
DR InterPro; IPR042558; Gln-tRNA-synth_Ib_RNA-bd_N_1.
DR InterPro; IPR042559; Gln-tRNA-synth_Ib_RNA-bd_N_2.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR Pfam; PF04557; tRNA_synt_1c_R2; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00440; glnS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..778
FT /note="Probable glutamine--tRNA ligase"
FT /id="PRO_0000195863"
FT REGION 188..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..283
FT /note="'HIGH' region"
FT MOTIF 496..500
FT /note="'KMSKS' region"
FT COMPBIAS 189..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 280..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 306
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 441
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 489..490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 497..499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
SQ SEQUENCE 778 AA; 87508 MW; 748509EC93E5E43A CRC64;
MAGDDLIAKF QALGMSEQKA KETLKNANVT KNLQLSLAAA GSATLSDGTG MLIYHMATKL
KPQTADHLPL LVRYIVEHKL DNTQRVDAAL EYLLKCGQSL NANIDLQALE KECGVGVVVT
PEQIERTVQA KIKASYKEAL LEQRYHFNSF KILQDVRGEL KWADAKSVKA AIDVEIFDLL
GPKTEADLKP QTKANDKPKA AKPKAEVTPA AQTAEAASDG ATTISELMKT KVHFHAPGEN
FKADGYVVTE HTERLLKEHL ARTGGKVHTR FPPEPNGILH IGHAKAININ FGYAAAHDGV
CYLRYDDTNP EKEEEKFFLA IKEMVEWLGY KPFKITYSSD NFQQLYEWAV VLINKGLAYV
CHQKAEELKG FNPKPSPWRE RPIEESLRLF EDMKRGKIDE GAATLRMKVT LEEGKMDPVA
YRIKFISHHR TGSDWCIYPT YDYTHCLCDS LEDITHSLCT KEFQSRRSSY YWLCNALGIY
CPVQWEYGRL NMNYALVSKR KIAKLITEQI VHDWDDPRLF TLTALRRRGF PAEAINNFCA
QMGVTGAQIA VDPAMLEAAV RDVLNVTAPR RLVVLEPLKV TIKNFPHAAP VQLEVPDFPQ
NPQQGTHKIT LDKVIYIEQG DFKLEPEKGY RRLAPKQSVG LRHAGLVISV DEIVKDPATG
QVVELICTSQ PAEQAEKPKA FVQWVSQPIQ LEVRLYEQLF KHKNPEDPNE VPGGFLSDIS
EQSMSVVVAF ADRALNQAKV YDKFQFERIG FFSVDPDTSA NHLVFNRTVG LKEDAGKK
