ID   SYQ_CAEEL               Reviewed;         786 AA.
AC   O62431;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Probable glutamine--tRNA ligase;
DE            EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897};
DE   AltName: Full=Glutaminyl-tRNA synthetase;
DE            Short=GlnRS;
GN   Name=qars-1 {ECO:0000312|WormBase:Y41E3.4a};
GN   Synonyms=ers-1 {ECO:0000312|WormBase:Y41E3.4a},
GN   qrs-5 {ECO:0000312|WormBase:Y41E3.4a};
GN   ORFNames=Y41E3.4 {ECO:0000312|WormBase:Y41E3.4a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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; Z95559; CAB08998.1; -; Genomic_DNA.
DR   PIR; T26811; T26811.
DR   RefSeq; NP_001255843.1; NM_001268914.1.
DR   AlphaFoldDB; O62431; -.
DR   SMR; O62431; -.
DR   BioGRID; 43497; 13.
DR   STRING; 6239.Y41E3.4a; -.
DR   iPTMnet; O62431; -.
DR   EPD; O62431; -.
DR   PaxDb; O62431; -.
DR   PeptideAtlas; O62431; -.
DR   EnsemblMetazoa; Y41E3.4a.1; Y41E3.4a.1; WBGene00001336.
DR   GeneID; 178415; -.
DR   KEGG; cel:CELE_Y41E3.4; -.
DR   UCSC; Y41E3.4; c. elegans.
DR   CTD; 178415; -.
DR   WormBase; Y41E3.4a; CE18372; WBGene00001336; qars-1.
DR   eggNOG; KOG1148; Eukaryota.
DR   GeneTree; ENSGT00940000168831; -.
DR   InParanoid; O62431; -.
DR   OMA; INNFCAQ; -.
DR   OrthoDB; 809861at2759; -.
DR   PhylomeDB; O62431; -.
DR   PRO; PR:O62431; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00001336; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; O62431; baseline and differential.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
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: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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..786
FT                   /note="Probable glutamine--tRNA ligase"
FT                   /id="PRO_0000195861"
FT   REGION          181..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           276..286
FT                   /note="'HIGH' region"
FT   MOTIF           499..503
FT                   /note="'KMSKS' region"
FT   COMPBIAS        181..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         277..279
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         283..289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         309
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         444
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         463
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         492..493
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         500..502
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
SQ   SEQUENCE   786 AA;  88262 MW;  D00F343D845F4B47 CRC64;
     MATKEELLSL GLSDSKVAET LKNVKLTETI GSIVKLASES GEISKQKGTL LYQLATKLKP
     QVAAHTPLVV KYIMNDGIKT EPQLSAAIEY LLSHTVKGIQ VPDFEKSCGV GVVVTIDDIE
     AAVTKVIGQH REKIVAERYS FPAGKLLGEL RALLPWADGA ITKKEVDLRF LELLGPKTAE
     DLAPKKKEKK PEGPKPSKDA AAAATAPGTK NQKEASPEEF ADGAETMDEL LRTRAHFHKV
     GENFKQDGYV TTPKTAELLK AHVAAVGGKV VTRFPPEPNG VLHIGHAKAI NINFGYAKAM
     GGVCNLRFDD TNPEKEEEKF FSAIEDIVHW LGYDPARVTH SSDNFQQLYL WAVKLIQKGL
     AFVCHQKVEE MRGFEVQLSP WRERPIEENI QLFEDMKNGK FDEGEATLRL KLTLEEGKVD
     PVAYRIKYVP HHRTGNQWCI YPTYDYTHCL CDSIENITHS LCTKEFQSRR SSYYWLCNAL
     DIYCPVQWEY GRLNVNYTVV SKRKILKLIT TKTVNDWDDP RLFTLTALRR RGIPSEAINR
     FVAKLGLTMS QMVIDPHVLD ATVRDYLNIH APRTMAVLEG LKLTIENFSE LNLPSSVDVP
     DFPSDPTDPR KHSVSVDREI FIEKSDYKPD DSDKSFRRLT PKQAVGLKHI GLVLRFVKEV
     KDAEGHVTEV VVKAEKLSEK DKPKAFIHWV AKPVSCEVRL YDRLFKSKNP EDAQLVPGGF
     LSDINPDSLT VVYNALIDQS IAKSKVYDRF QFERIGFFCV DRDSTSSTLV FNRTVMLKDG
     GASGKN