ID A0A1F5A9E9_9BACT Unreviewed; 568 AA.
AC A0A1F5A9E9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=A2V47_09160 {ECO:0000313|EMBL:OGD14816.1};
OS Candidatus Atribacteria bacterium RBG_19FT_COMBO_35_14.
OC Bacteria; Atribacterota.
OX NCBI_TaxID=1797291 {ECO:0000313|EMBL:OGD14816.1, ECO:0000313|Proteomes:UP000177701};
RN [1] {ECO:0000313|EMBL:OGD14816.1, ECO:0000313|Proteomes:UP000177701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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|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:OGD14816.1}.
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DR EMBL; MEYH01000074; OGD14816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5A9E9; -.
DR STRING; 1797291.A2V47_09160; -.
DR Proteomes; UP000177701; 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; 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.
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}.
FT DOMAIN 30..339
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 343..443
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 460..538
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT MOTIF 36..46
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT MOTIF 270..274
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 37..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 43..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 69
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 214
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 263..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
FT BINDING 271..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00126"
SQ SEQUENCE 568 AA; 66136 MW; 5F548147B568517C CRC64;
MDFQESKVTV NFIQEIIDQD KKTNKYHGRI HLRFPPEPNG YLHIGHAKSI CLNFGLAAQN
DGLCNLRFDD TNPSKEDVEY IDSIINDVRW LGFTWDDRLF YASDYFEKMY DYAVRLIKAG
KAYVCDLSPE EIRKYRGGFK EPGKESPYLS RSVEDNLDLF KRMRAGEFAD GSRVLRAKID
MSSPNLNMRD PVLYRILRAA HHRTGDKWCI YPMYDYAHPL EDYYEKITHS VCTLEFEDHR
PLYDWVLNTL NLPDPPQQIE FARLSLTNTV MSKRKLRRLV EEGYTAGWDD PRMPTIAGLR
RRGYTPESIQ NFCDRIGVSK SNSMVDVRFL EHCIREDLNL RVSRVMGVLH PLKLFIDNYP
GDMVEEMESE NNPEDPAAGT RKIPFSRILY IEREDFHEDP PKKYFRLAPG CEVRLKNAYI
IKCERFVRDE KTGEIEEVHC TYDPESKSGK PGAKRKVKGT LHWVSAGHAV KAEVRLYDHL
LLDQNEGIEG QEEEKDFRKQ LNPSSLEVLT YCLVEPSLAG AAPGSRYQFM RKGYFCVDPD
SRSDKLVFNR IVSLRDTWDR ILKAEKIE
//
