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P56927 (SYQ_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 92. 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:NMB1560
OrganismNeisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]
Taxonomic identifier122586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length562 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
Reference 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 – 562562Glutamine--tRNA ligase HAMAP-Rule MF_00126
PRO_0000195839

Regions

Motif35 – 4511"HIGH" region HAMAP-Rule MF_00126
Motif271 – 2755"KMSKS" region HAMAP-Rule MF_00126

Sites

Binding site2741ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P56927 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: 52F3C71FA22DE36D

FASTA56264,650
        10         20         30         40         50         60 
MLNKDQFADN HFIRTIIEED LESGKHTAVQ TRFPPEPNGY LHIGHAKSIC LNFGLAYIYD 

        70         80         90        100        110        120 
GLCNLRFDDT NPEKENDEYV NAIKEDVEWL GFHWAGEPRF ASNYFDQLYD YAVGLIKDGK 

       130        140        150        160        170        180 
AYVDDLTPEE MREYRGTLTE AGKNSPYRDR SVEENLDLFT RMKNGEFPDG SKTLRLKIDM 

       190        200        210        220        230        240 
ASGNINMRDP VIYRIRRAHH HNTGDKWCIY PMYDYTHCIS DAIEGITHSL CTLEFEAHRP 

       250        260        270        280        290        300 
LYDCVLDNIP APHATRPRQY EFSRLELLYT ITSKRKLNQL VVEKHVSGWD DPRMPTISGM 

       310        320        330        340        350        360 
RRRGYTPEGL RLFAKRAGIS KSENIVDMSV LEGAIREELE NSAPRLMAVL NPLKVTLTNF 

       370        380        390        400        410        420 
ETGRTQSRRA AFHPNHEEMG EREVPISQTI YIEADDFAEN PPKGFKRLIP GGEVRLRHGY 

       430        440        450        460        470        480 
VIKCDEVVKD EAGNVVELKC SIDHDTLGKN PEGRKVKGVI HWVSAEHAAE IKVRLYDRLF 

       490        500        510        520        530        540 
TVERPDAVRG EDGEYLPFTD FLNPESVKEI TAYAEPAAKD LPAESRWQFE RIGYFVTDRK 

       550        560 
DHGKDTPVFN RTVTLKDSWQ PK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002098 Genomic DNA. Translation: AAF41914.1.
PIRE81069.
RefSeqNP_274567.2. NC_003112.2.

3D structure databases

ProteinModelPortalP56927.
SMRP56927. Positions 11-557.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122586.NMB1560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF41914; AAF41914; NMB1560.
GeneID904126.
KEGGnme:NMB1560.
PATRIC20358976. VBINeiMen85645_2007.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000259232.
KOK01886.
OMASREIYID.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycNMEN122586:GHGG-1601-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.
InterProIPR004514. 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_NEIMB
AccessionPrimary (citable) accession number: P56927
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: May 14, 2014
This is version 92 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