ID A0A120GQA7_9BACI Unreviewed; 550 AA.
AC A0A120GQA7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=AS888_15520 {ECO:0000313|EMBL:KWW21029.1};
OS Peribacillus simplex.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1478 {ECO:0000313|EMBL:KWW21029.1};
RN [1] {ECO:0000313|EMBL:KWW21029.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VanAntwerpen02 {ECO:0000313|EMBL:KWW21029.1};
RA Couger M.B.;
RT "Genome Sequence of Bacillus simplex strain VanAntwerpen2.";
RL Submitted (NOV-2015) 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|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00126}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_00126, ECO:0000256|RuleBase:RU363037}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00126}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KWW21029.1}.
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DR EMBL; LNNH01000012; KWW21029.1; -; Genomic_DNA.
DR RefSeq; WP_061141382.1; NZ_LNNH01000012.1.
DR AlphaFoldDB; A0A120GQA7; -.
DR Proteomes; UP000064189; 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 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 {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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}.
FT DOMAIN 25..333
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 336..436
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 453..527
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT MOTIF 31..41
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT MOTIF 264..268
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 32..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 38..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 64
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 208
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 257..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 265..267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
SQ SEQUENCE 550 AA; 63955 MW; C7B4BB3278EB43F5 CRC64;
MENNASNFIK TIIKDDLETG KHDHIITRFP PEPNGYLHIG HAKSIILNFG VADDFNGKTN
LRFDDTNPLK EDIEYVNSIK EDVKWLGYDW DNLFFASDYF DEMFKRAVLL INKGLAYVDD
LNADQIREYR GSLTEPGKDS PYRNRTVEEN LELFEKMRNG EFENGEKVLR AKIDMSSPNI
NLRDPVIYRI SHTEHHNTGN KWCIYPMYAF AHPIEDAIEG VTHSICTLEF EDQRPLYDWI
VEHCEMESKP QQYEFGRLNL TNTVMSKRKL KQLVDERFVD GWDDPRMPTI SGLRRRGYTP
EAIRAFCQEI GVAKTSGVVD SQMLDHFVRE DLKLKAPRTM AVLNPLKVVI TNYPEGEVEW
LDAEVNPEVP EMGMRKIPFS REIYIEQDDF MENPPKKYFR LFPGNEVRLK HAYFIKCEEV
IKDDNGNVIE LRCTYDVETK SGSGFTGRKV KGTLHWVEAS QAISAEFRNY QPLILDSAAE
DEEEKSFLER VNPDSIEILQ GFVEPNMKDV QPQDKFQFFR HGYYNVDTKL TKADRLVFNQ
IVGLKSSFKL
//
