Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B4EV71 (SYQ_PROMH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:PMI0539
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length555 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 – 555555Glutamine--tRNA ligase HAMAP-Rule MF_00126
PRO_1000095498

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
B4EV71 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: B27A127CA7A29829

FASTA55564,124
        10         20         30         40         50         60 
MNEADARPTN FIRQIIDEDL ATGKHNSVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYQG 

        70         80         90        100        110        120 
KCNLRFDDTN PVKEDVEYIN SIQKDVQWLG FQWDGNVHYS SDYFDQLYQY AIELINKGLA 

       130        140        150        160        170        180 
YVDELSAEEI REYRGTLKEP GKNSPYRSRS VEENLALFEK MRAGGFEEGK ACLRAKIDMA 

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

       250        260        270        280        290        300 
YDWVLDNITI PCHPRQYEFS RLNLEYTVMS KRKLNQLVTE NIVDGWDDPR MPTISGLRRR 

       310        320        330        340        350        360 
GYTAESIREF CQRIGVTKQD NNVEMASLEA CIRDDLNENA PRAMAVIDPV RLVIENMPEG 

       370        380        390        400        410        420 
EEILTAPNHP NKPEMGTREV PFSREIYIDR ADFKEEANRQ YKRLVLGKEV RLRNAYVIKA 

       430        440        450        460        470        480 
ERVEKDEQGE ITTIYCTYDP QTLNKDPADG RKVKGVIHWV SIPHAIPAEI RLYDRLFSVP 

       490        500        510        520        530        540 
NPGAEEDFLS TINPESLVIR QGFVEASLKD AAIEKAYQFE REGYFCADKL STADKLVFNR 

       550 
TVGLRDTWAK ISKQG 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI4320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942759 Genomic DNA. Translation: CAR41300.1.
RefSeqYP_002150309.1. NC_010554.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING529507.PMI0539.

Proteomic databases

PRIDEB4EV71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR41300; CAR41300; PMI0539.
GeneID6801487.
KEGGpmr:PMI0539.
PATRIC20515761. VBIProMir120933_0523.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000259232.
KOK01886.
OMASREIYID.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPMIR529507:GJIW-553-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_PROMH
AccessionPrimary (citable) accession number: B4EV71
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 38 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