SYQ_RHOBA
ID SYQ_RHOBA Reviewed; 601 AA.
AC Q7UX42;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, 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=RB1578;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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}.
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DR EMBL; BX294135; CAD72170.1; -; Genomic_DNA.
DR RefSeq; NP_864489.1; NC_005027.1.
DR AlphaFoldDB; Q7UX42; -.
DR SMR; Q7UX42; -.
DR STRING; 243090.RB1578; -.
DR EnsemblBacteria; CAD72170; CAD72170; RB1578.
DR KEGG; rba:RB1578; -.
DR PATRIC; fig|243090.15.peg.737; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_001882_2_3_0; -.
DR InParanoid; Q7UX42; -.
DR OMA; INNFCAQ; -.
DR OrthoDB; 142899at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 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_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00440; glnS; 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; Reference proteome.
FT CHAIN 1..601
FT /note="Glutamine--tRNA ligase"
FT /id="PRO_0000195847"
FT MOTIF 76..86
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT MOTIF 308..312
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 77..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 83..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 109
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 253
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 301..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 309..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
SQ SEQUENCE 601 AA; 68668 MW; 0C6B526811FF4CD3 CRC64;
MARANRGEHS TLSTFWQSRH NAASFDPLYR RIDVNAPEPS DSATPEKTPS KHFIRQAIDA
DLASGRFDGV ATRFPPEPNG YLHIGHAKSI CLNFGLAKDM GGTCNLRFDD TNPIKEDTEY
VDSIQEDVRW LGFEWDNLHF ASDYFDQLYD WAEQLVKDGK AYVCDLTAEE TREYRGTLTE
PGKNSPHRDR TPEKNLELLR AMKAGKFKDG EKTLRAKIDM ASPNINLRDP VMYRIAHVPH
HRTGDKWCIY PMYDWAHGQS DSLEKITFSI CTLEFEHHRP LYNWYCENLG IHHPRQIEFA
RLNMTFTVMS KRKLLQLVKE NHVTGWDDPR MPTLVGLRRR GYTPESIRSF CADIGVAKFN
STIDVIRLEN SVREHLNSVA PRRMAVLDPI KLTITNWPEG KVEMMNAINN PEDESAGSRE
IPFSGELYIE TEDFREEAPR KFFRLKKGGS VRLRSGYIVD CHDVVKDADG NVTEVLCTYD
PETKSGEDTS GRKVKGTIHW VSREHAQKVT VRNYDRLFKV ENPDASSDTG SFLDHLNPDS
LTTLTAHVEP ALAEAAVGDR VQFERLGYYV VDPDSTDGEI IFNRIVPLRD TWGKIEAKGK
K
