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Q8X9H8 (SYQ_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Z0827, ECs0710
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subunit structure

Monomer By similarity. HAMAP MF_00126

Subcellular location

Cytoplasm HAMAP 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

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 554553Glutamine--tRNA ligase HAMAP MF_00126
PRO_0000195835

Regions

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

Sites

Binding site2711ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X9H8 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A484939DB8B4EC67

FASTA55463,510
        10         20         30         40         50         60 
MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG 

        70         80         90        100        110        120 
QCNLRFDDTN PVKEDIEYVD SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA 

       130        140        150        160        170        180 
YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRTGGFEEGK ACLRAKIDMA 

       190        200        210        220        230        240 
SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL 

       250        260        270        280        290        300 
YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR 

       310        320        330        340        350        360 
GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE 

       370        380        390        400        410        420 
GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR SDFREEANKQ YKRLVLGKEV RLRNAYVIKA 

       430        440        450        460        470        480 
ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP 

       490        500        510        520        530        540 
NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN 

       550 
RTVGLRDTWA KVGE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG55002.1.
BA000007 Genomic DNA. Translation: BAB34133.1.
PIRF85567.
F90717.
RefSeqNP_286394.1. NC_002655.2.
NP_308737.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X9H8.
SMRQ8X9H8. Positions 9-548.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000025181; EBESCP00000024074; EBESCG00000024235.
EBESCT00000057634; EBESCP00000055462; EBESCG00000056682.
GeneID917079.
957752.
GenomeReviewsGene locus Z0827 in contig AE005174_GR.
Gene locus ECs0710 in contig BA000007_GR.
KEGGece:Z0827.
ecs:ECs0710.
PATRIC18350431. VBIEscCol44059_0727.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009048.
HOGENOMHBG334108.
OMARMPTIAG.
ProtClustDBPRK05347.

Enzyme and pathway databases

BioCycECOL83334:ECS0710-MONOMER.

Family and domain databases

HAMAPMF_00126. Gln_tRNA_synth.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth_Ib.
IPR022861. Gln_tRNA_synth_bac.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:2.40.240.10. Rbsml_L25/Gln-tRNA_synth_b-brl. 2 hits.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01886.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. Ribosomal_L25rel. 1 hit.
TIGRFAMsTIGR00440. GlnS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYQ_ECO57
AccessionPrimary (citable) accession number: Q8X9H8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 68 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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