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C6DBY6 (SYQ_PECCP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 34. 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:PC1_1205
OrganismPectobacterium carotovorum subsp. carotovorum (strain PC1) [Complete proteome] [HAMAP]
Taxonomic identifier561230 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length552 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 – 552552Glutamine--tRNA ligase HAMAP-Rule MF_00126
PRO_1000203124

Regions

Motif34 – 4411"HIGH" region HAMAP-Rule MF_00126
Motif268 – 2725"KMSKS" region HAMAP-Rule MF_00126

Sites

Binding site2711ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C6DBY6 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: C0362E3B192C4B31

FASTA55263,140
        10         20         30         40         50         60 
MSEAEARPTN FIRQIIDEDL ASGKHDHIQT RFPPEPNGYL HIGHAKSICL NFGIARDYQG 

        70         80         90        100        110        120 
QCNLRFDDTN PVKEDIEYVE SIKRDVEWLG FSWSGDVRYS SDYFDQLHAY AVELIGKGLA 

       130        140        150        160        170        180 
YVDELTPEQI REYRGTLTAP GKNSPYRDRT VQENLALFEK MRNGGFAEGT ACLRAKIDMA 

       190        200        210        220        230        240 
SSFIVMRDPV LYRIKFADHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL 

       250        260        270        280        290        300 
YDWVLDNITI PCHPRQYEFS RLNLEYAIMS KRKLNQLVVE NVVEGWDDPR MPTISGLRRR 

       310        320        330        340        350        360 
GYSASSIREF CVRIGVTKQD NNVEMAALES CIRDDLNENA PRAMAVLDPV KVVIENLPAG 

       370        380        390        400        410        420 
HEEFVAMPNH PNKPEMGSRQ VAFSREVYID RADFREEANK QYKRLVLGKE VRLRNAYVIK 

       430        440        450        460        470        480 
ADRIEKDEQG TITTIYCSYD AETLSKDPAD GRKVKGVIHW VSAAHAVPAE FRLYDRLFSV 

       490        500        510        520        530        540 
ANPGAAEDFL STINPDSLKI TQGFVEASLA QAEAEKAYQF EREGYFCADR VYSSAEHLVF 

       550 
NRTVGLRDTW VG 

« Hide

References

[1]"Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Balakrishnan V., Glasner J., Perna N.T.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001657 Genomic DNA. Translation: ACT12253.1.
RefSeqYP_003016789.1. NC_012917.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561230.PC1_1205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT12253; ACT12253; PC1_1205.
GeneID8132140.
KEGGpct:PC1_1205.
PATRIC20487026. VBIPecCar70489_1208.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000259232.
KOK01886.
OMASREIYID.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPCAR561230:GKCK-1241-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_PECCP
AccessionPrimary (citable) accession number: C6DBY6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: May 14, 2014
This is version 34 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