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Q1LQ72 (SYQ_RALME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine--tRNA ligase

EC=6.1.1.18
Alternative name(s):
Glutaminyl-tRNA synthetase
Short name=GlnRS
Gene names
Name:glnS
Ordered Locus Names:Rmet_0818
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length582 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). HAMAP-Rule MF_00126

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00126

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00126.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutaminyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 582582Glutamine--tRNA ligase HAMAP-Rule MF_00126
PRO_1000095506

Regions

Motif50 – 6011"HIGH" region HAMAP-Rule MF_00126
Motif296 – 3005"KMSKS" region HAMAP-Rule MF_00126

Sites

Binding site2991ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LQ72 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 688FBD9447623404

FASTA58266,121
        10         20         30         40         50         60 
MSHDTKPNDT PAASNFLRSI IDQDLATGTY AGRADKQGDP LPTVITRFPP EPNGYLHIGH 

        70         80         90        100        110        120 
AKSICVNFGL ARDYAGRCHL RFDDTNPVKE DTEYVDSIID AVHWLGFSWD SAQAGSTPHL 

       130        140        150        160        170        180 
YFASDYFDQL YKFAETLIER GVAYVDSQSA EQIAAMRGNF SEPGKPSPFR DRSVEENLKL 

       190        200        210        220        230        240 
FREMRDGKYA DGEHVLRAKI DMTAPNIVMR DPVLYRIRHA HHHRTGDKWC IYPMYDFTHC 

       250        260        270        280        290        300 
ISDAIENITH SLCTLEFENN RPLYDWVLEH LRDAGVFANP LPHQYEFARL NLTYAITSKR 

       310        320        330        340        350        360 
RLKQLVDEQR VTGWDDPRMP TIVGIRRRGY TPESIQLFCD RVGVSKADSW IDMSTLEGAV 

       370        380        390        400        410        420 
RDDLDARAPR SVAVLDPLKL ILDNYPEGQS EECSAPVHPK QPEMGRRVFP LSRELWIERE 

       430        440        450        460        470        480 
DFNENPPKGY FRLFPGNKVR LRYGYVIECT GVDKDADGNV IAVHANYLPE TKSGTPGADS 

       490        500        510        520        530        540 
VKVKGNIHWV SAPHACEAEV RLYDRLFNDP NPDAGGKNFL DALNPESKKV VTAYLEPGLR 

       550        560        570        580 
DAKPEDRFQF ERHGYFVADR VDSQPGKPVF NRTVGLKDSW GK 

« Hide

References

[1]"Complete sequence of the chromosome of Ralstonia metallidurans CH34."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH34 / ATCC 43123 / DSM 2839.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000352 Genomic DNA. Translation: ABF07704.1.
RefSeqYP_582973.1. NC_007973.1.

3D structure databases

ProteinModelPortalQ1LQ72.
SMRQ1LQ72. Positions 14-579.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266264.Rmet_0818.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF07704; ABF07704; Rmet_0818.
GeneID4037609.
KEGGrme:Rmet_0818.
PATRIC20286178. VBIRalMet4734_1202.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000259232.
KOK01886.
OMASREIYID.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCMET266264:GJ5G-849-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
HAMAPMF_00126. Gln_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth.
IPR022861. Gln_tRNA_ligase_bac.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. SSF50715. 1 hit.
TIGRFAMsTIGR00440. glnS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYQ_RALME
AccessionPrimary (citable) accession number: Q1LQ72
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 30, 2006
Last modified: May 14, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries