ID SYQ_SODGM Reviewed; 556 AA. AC Q2NUP0; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=Glutamine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00126}; DE EC=6.1.1.18 {ECO:0000255|HAMAP-Rule:MF_00126}; DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00126}; DE Short=GlnRS {ECO:0000255|HAMAP-Rule:MF_00126}; GN Name=glnS {ECO:0000255|HAMAP-Rule:MF_00126}; OrderedLocusNames=SG0860; OS Sodalis glossinidius (strain morsitans). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Bruguierivoracaceae; Sodalis. OX NCBI_TaxID=343509; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=morsitans; RX PubMed=16365377; DOI=10.1101/gr.4106106; RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., RA Aksoy S.; RT "Massive genome erosion and functional adaptations provide insights into RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."; RL Genome Res. 16:149-156(2006). 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00126}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00126}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00126}. 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; AP008232; BAE74135.1; -; Genomic_DNA. DR RefSeq; WP_011410697.1; NZ_LN854557.1. DR AlphaFoldDB; Q2NUP0; -. DR SMR; Q2NUP0; -. DR STRING; 343509.SG0860; -. DR KEGG; sgl:SG0860; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_001882_2_3_6; -. DR OrthoDB; 9801560at2; -. DR BioCyc; SGLO343509:SGP1_RS07430-MONOMER; -. DR Proteomes; UP000001932; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00807; GlnRS_core; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00126; Gln_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004514; Gln-tRNA-synth. DR InterPro; IPR022861; Gln_tRNA_ligase_bac. 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; IPR020061; Glu_tRNA_lig_a-bdl. DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N. DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR049437; tRNA-synt_1c_C2. DR NCBIfam; TIGR00440; glnS; 1. DR PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1. DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR Pfam; PF03950; tRNA-synt_1c_C; 1. DR Pfam; PF20974; tRNA-synt_1c_C2; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..556 FT /note="Glutamine--tRNA ligase" FT /id="PRO_0000242878" FT MOTIF 34..44 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT MOTIF 268..272 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 35..37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 41..47 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 67 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 212 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 231 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 261..262 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 269..271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" SQ SEQUENCE 556 AA; 64007 MW; A43F55CB61E0E88B CRC64; MSEAEARPTN FIRQIIDDDL ASGKHTSVHT RFPPEPNGYL HIGHAKSIYL NFGIAQDYQG QCNLRFDDTN PVKEDMEYVD SIKHDVQWLG FNWSGDIHYS SDYFDKLHDY ALELIDKGLA YVDQLSPDQI RDYRGTLTRP GKNSPYRDRS VEENRALFAS MRQGEFAEGS ACLRAKIDMA SPFMVMRDPV LYRIKFADHH QTGSKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL YDWVLDNITI NVHPRQYEFS RLNLEYAIMS KRKLNLLVTE KIVEGWDDPR MPTISGLRRR GYTAASIREF CRRIGVTKQD NNVEMAALEA CIREDLNDRA PRAMAVIDPV RVVIESLPMG YEQDIAMPNH PNRPEMGTRQ VAFSREIYID RADFREEANK QYKRLVLGKE VRLRNAFVIK AEHVEKDPQG QITTIFCRHD PDTLSKDPAD GRKVKGVIHW VSANRSLAAE FRLYDRLFSE ANPAAAEDFL STLNPDSLVI RQGFVEAGVP AANTGEPFQF EREGYFCADS RYFSPTHPVF NRTVGLRDTW AQRAAM //