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Q2KVX0 (SYQ_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:BAV2787
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length586 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 – 586586Glutamine--tRNA ligase HAMAP-Rule MF_00126
PRO_1000095478

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_00126
Motif301 – 3055"KMSKS" region HAMAP-Rule MF_00126

Sites

Binding site3041ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KVX0 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 0791D6E9BCC7E191

FASTA58666,544
        10         20         30         40         50         60 
MTQTTAPHAA SNYLRNIIED DLAANRFQGK RWAGKPGPAS MQASGLPDPA RIRTRFPPEP 

        70         80         90        100        110        120 
NGYLHIGHAK SICVNFGIAK EFGGVCHLRF DDTNPEKEDQ EYVDAIIEAV RWLGFDWNTD 

       130        140        150        160        170        180 
GNNNLYFASD YFEFMYEFAE ALIEAGHAFV DEQSADDIRA QRGTLTEPGR NSPFRDRPAA 

       190        200        210        220        230        240 
ESLTRLREMR DGKHPDGSLV LRARIDMASP NINLRDPVMY RVRHAAHHRT GDKWCIYPMY 

       250        260        270        280        290        300 
SWAHPVEDAL EGITHSICTL EFEDQRPFYD WILARLADLG KLARPLPRQY EFSRLNMSYI 

       310        320        330        340        350        360 
VTSKRKLLQL VREGYVDGWD DPRMPTLFGL RRRGYTASAI RLFCDRTAVS KSDSRIDYSL 

       370        380        390        400        410        420 
LEQAVRDDLD PGTTRSVAVL DPLKLVITNY PKDQTEVCKA PRNPHDPEAG QREFPFSREL 

       430        440        450        460        470        480 
WIERDDFREE APKKYFRLFP GNLVRLKYGY VVRCTGFTKD EAGNITEVQA EYLPDTKSGT 

       490        500        510        520        530        540 
PGADSVKVKG NITWVSAAHA VPAEVRLYDR LFADPHPDGG DKDFLACLNP NSIQTVQAWL 

       550        560        570        580 
EPGTRAEPGA TWQFERLGYF TVDSKDSSPE APVLNRIVTL KDSWAA 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ50398.1.
RefSeqYP_787285.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2KVX0.
SMRQ2KVX0. Positions 11-583.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360910.BAV2787.

Proteomic databases

PRIDEQ2KVX0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6266199.
KEGGbav:BAV2787.
PATRIC21131863. VBIBorAvi43433_2819.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000259232.
KOK01886.
OMAVTHSICT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK05347.

Enzyme and pathway databases

BioCycBAVI360910:GCKI-2852-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_BORA1
AccessionPrimary (citable) accession number: Q2KVX0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 7, 2006
Last modified: February 19, 2014
This is version 61 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