ID A0A078L1M5_9GAMM Unreviewed; 551 AA.
AC A0A078L1M5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Glutamine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00126};
DE EC=6.1.1.18 {ECO:0000256|HAMAP-Rule:MF_00126};
DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00126};
DE Short=GlnRS {ECO:0000256|HAMAP-Rule:MF_00126};
GN Name=glnS {ECO:0000256|HAMAP-Rule:MF_00126,
GN ECO:0000313|EMBL:CDZ79126.1};
GN ORFNames=BN59_03443 {ECO:0000313|EMBL:CDZ79126.1};
OS Legionella massiliensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ79126.1, ECO:0000313|Proteomes:UP000044071};
RN [1] {ECO:0000313|EMBL:CDZ79126.1, ECO:0000313|Proteomes:UP000044071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000948, ECO:0000256|HAMAP-
CC Rule:MF_00126};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00126}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00126}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00126,
CC ECO:0000256|RuleBase:RU363037}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00126}.
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DR EMBL; CCSB01000004; CDZ79126.1; -; Genomic_DNA.
DR RefSeq; WP_044012285.1; NZ_CCVW01000004.1.
DR AlphaFoldDB; A0A078L1M5; -.
DR STRING; 1034943.BN59_03443; -.
DR eggNOG; COG0008; Bacteria.
DR OrthoDB; 9801560at2; -.
DR Proteomes; UP000044071; Unassembled WGS sequence.
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 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; 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00126};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00126}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00126};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00126};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00126};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00126}; Reference proteome {ECO:0000313|Proteomes:UP000044071}.
FT DOMAIN 27..336
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 339..439
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 455..526
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT MOTIF 267..271
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 35..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 67
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 211
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 260..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
SQ SEQUENCE 551 AA; 64078 MW; CF720A101FC48187 CRC64;
MTESSEKRTH FIRQLVTEDL ASGKHQEVIT RFPPEPNGYL HVGHAKSICL NFGLAEEFKG
RCFLRFDDTN PIKEEEEYVN AIIEDVRWLG FEWCDMTHSS DYYHELYDFA VDLIKQGKAY
VDSLSMEEIR AYRGTLQEPG KESPYRNRSV EENLDLFARM KAGEFADGTH VLRAKIDMQS
GNVNMRDPVL YRIRHAHHQR TGDEWCIYPM YDYAHPISDA LEMISHSLCT LEFQDHRPLY
DWCIENLTLP AQPEQTEFAR LNLSHTVTSK RKLRLLVEEK VVEGWDDPRL PTLRGMRKRG
YPPAAIKQFC ELIGISRSDS VIDMSILEEC VRAELNNSAK RAMGVLEPLK VVIENYPDDK
VEQLTAQYHP QDPTAGSRTL PFAREIYIER SDFMEDPPKK YFRLAPGTEV RLRHAYVIRC
TEVIKDSKGE VIELRCTYDE NTLGKNPEDR KVKGVIHWVS CQHAHPIKIY QYDRLFNDAN
PAREDDFLQF LNKNSLTTQD AFCEPSLVEQ PLHEVFQFER LGYYAVNQLE QGKVSAFHRV
VGLKDTWEKI S
//
