SYQ_LUPLU
ID SYQ_LUPLU Reviewed; 794 AA.
AC P52780;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glutamine--tRNA ligase;
DE EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897};
DE AltName: Full=Glutaminyl-tRNA synthetase;
DE Short=GlnRS;
OS Lupinus luteus (European yellow lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3873;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ventus;
RA Siatecka M., Rozek M., Barciszewski J.;
RT "Isolation and characterization of a cDNA clone encoding a plant gene of
RT aminoacyl-tRNA synthetase.";
RL (er) Plant Gene Register PGR95-103(1995).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X91787; CAA62901.1; -; mRNA.
DR PIR; T09643; T09643.
DR AlphaFoldDB; P52780; -.
DR SMR; P52780; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
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.
FT CHAIN 1..794
FT /note="Glutamine--tRNA ligase"
FT /id="PRO_0000195864"
FT REGION 192..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 277..287
FT /note="'HIGH' region"
FT MOTIF 505..509
FT /note="'KMSKS' region"
FT COMPBIAS 192..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 278..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 284..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 310
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 450
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 498..499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 506..508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
SQ SEQUENCE 794 AA; 90483 MW; 4C7D02C0795268E1 CRC64;
MPAKDDTSSD KEKSLELFLK IGLDERTAKN TVANNKVTTN LTSVINDAGV TDGCSRTVGN
LLYTVATKYP ANALPHRPTL LQYIVNSKVK TTAQLDAALS FLSATGSENL DLNKFEEACG
VGVEVSTEDI KHAVDEVVEE NKATILELRY RVNVGELLGH VRKRLPWADA KVVKQLVDAK
LYEILGDRTA ADNEKPKKKK EKPAKVEDKA APVATSEKPL EEDLNPYLIF PNPEDNFKVH
TEVPFSDGNI LRCCNTKALL EKHLKATGGK VLTRFPPEPN GYLHIGHAKA MFVDFGLAKD
RNGGCYLRFD DTNPEAEKKE YIDHIEEIVQ WMGWEPFKIT YTSNYFQELY EFAVELIRRG
HAYVDHQTAD EIKEYREKKL NSPWRDRPIS ESLKLFEDMR RGFIEEGKAT LRMKQDMQSD
NYNMYDLIAY RIKFTPHPHA GDKWCIYPSY DYAHCIVDSI ENVTHSLCTL EFETRRASYY
WLLHALGIYQ PYVWEYSRLN VSNTVMSKRK LNRLVTEKWV DGWDDPRLMT LAGLRRRGMT
PTAINAFVRG MGITRSDGTL ISVERLEYHV REELNKTAPR AMVVLHPLKV VITNLEAKSA
IEVDAKKWPD AQADDASAFY KIPFSNVVYI ERSDFRMQDS KDYYGLAPGK SVILRYAFPI
KCTEVILADD NETILEIRAE YDPSKKTKPK GVLHWVSQPS PGVDPLKVEV RLFERLFLSE
NPAELDNWLG DLNPHSKVEI SNAYGVSLLK DAKLGDRFQF ERLGYFAVDQ DSTPEKLVFN
RTVTLKDSYG KGGK
