ID G0VQU7_MEGEL Unreviewed; 563 AA.
AC G0VQU7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=MELS_1577 {ECO:0000313|EMBL:CCC73797.1};
OS Megasphaera elsdenii DSM 20460.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1064535 {ECO:0000313|EMBL:CCC73797.1, ECO:0000313|Proteomes:UP000010111};
RN [1] {ECO:0000313|EMBL:CCC73797.1, ECO:0000313|Proteomes:UP000010111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20460 {ECO:0000313|EMBL:CCC73797.1,
RC ECO:0000313|Proteomes:UP000010111};
RX PubMed=21914887; DOI=10.1128/JB.05861-11;
RA Marx H., Graf A.B., Tatto N., Thallinger G.G., Mattanovich D., Sauer M.;
RT "Genome Sequence of the Ruminal Bacterium Megasphaera elsdenii.";
RL J. Bacteriol. 193:5578-5579(2011).
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: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}.
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DR EMBL; HE576794; CCC73797.1; -; Genomic_DNA.
DR RefSeq; WP_014016526.1; NZ_CP027570.1.
DR AlphaFoldDB; G0VQU7; -.
DR STRING; 1064535.MELS_1577; -.
DR KEGG; med:MELS_1577; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_001882_2_3_9; -.
DR Proteomes; UP000010111; 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; 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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000010111}.
FT DOMAIN 27..338
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 341..441
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 459..534
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT MOTIF 33..43
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT MOTIF 269..273
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 34..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 40..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 66
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 262..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
SQ SEQUENCE 563 AA; 65440 MW; 2876BD0F5A8B33BD CRC64;
MDNETTKNFI ENIIDEDNEK NTYGKRVHTR FPPEPNGYLH LGHAKSICLN FGIAKKYGGL
TNLRFDDTNP SKENTEYVES IKRDVKWLGF DWDDRMFYAS DYFDKLYEYA KKLIRLGKAY
VDDLSGDEIR EYRGTFNTPG KESPYRNRSV EENLQLFEEM KDGKYADGEK VLRAKIDMAS
PNLNMRDPVI YRIVHASHHR TGDKWCIYPM YDFAHPVSDA IERITHSICT LEFEAHRPLY
NWVLEDWDDP EGQKPRQIEF ARLNVTNMIT SKRKLRLLVE KGIVSGWDDP RMPTISGIRR
RGYTPESIRD FCERIGVAKA DSLVDISLLE YCIREDLKLK APRLMTVIDP IKVVLTNYPD
GKTETMTADN NQENEAMGTR EMTFSKNLYI ERNDFMEEPV KKFFRLAPGK EVRLKYAYII
KCEEVIKDED GNIVELHCTY DPESKSGSGA NANRKVKGTL QWVNAEDAVD VETRVYDYLL
KDDGSEEEGE SKDFLDQINP HSLDVYHSKA EKALATYHVG DKFQFLRQGY FVIDPDTTAD
HFVVNRIVGL RDTWAKMQKK KNQ
//
