Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7NX86 (SYQ_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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
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:CV_1742
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length560 AA.
Sequence statusComplete.
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

Chain1 – 560560Glutamine--tRNA ligase HAMAP MF_00126
PRO_0000195830

Regions

Motif36 – 4611"HIGH" region HAMAP MF_00126
Motif270 – 2745"KMSKS" region HAMAP MF_00126

Sites

Binding site2731ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NX86 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 2E23F03ECAB9CEF5

FASTA56064,372
        10         20         30         40         50         60 
MSTENNAPVV NNFIRSIIDE DLATGRRSSV VTRFPPEPNG FAHIGHAKAI CINFGLAEDY 

        70         80         90        100        110        120 
NGQCNLRMDD TNPEKESDEF VEAFKQDISW LGFKWNGEVR YASDYFDRLY DYAVELIQAG 

       130        140        150        160        170        180 
KAYVDDLSAE EMRQYRGNLT EPGKNSPYRD RTPEENLDLF TRMKNGEFPD GSKTLRLKID 

       190        200        210        220        230        240 
MASGNINLRD PAIYRIRRVH HHRTGDKWCI YPMYDYTHCI SDAIEGITHS LCSLEFEDHR 

       250        260        270        280        290        300 
PLYDWVLDNI SIEHHPQQIE FSRLELLYAL TSKRKLQALV NDGAVTGWDD PRMPTIAGMR 

       310        320        330        340        350        360 
RRGYSPAGIK LFAQRIGVSK SENIIDMAIL EGAVRETLEN DSPRVMAVVN PLKVTLTNYD 

       370        380        390        400        410        420 
AAVTASRSAP FHPHHPEFGE RDVPIAREIW IERDDFAETP PPKWQRLTAG GEVRLRYSYV 

       430        440        450        460        470        480 
IKCDEVVKDA ADEIVELKCS IDHDTLGKNP EGRKVKGVIH WVSAEHAIQA DVRWYERLFT 

       490        500        510        520        530        540 
EQRPDAVRGE DGEYVDFRQF LNPESLKLVP AYVEASVLQA EPESRFQFER LGYFVTDRYE 

       550        560 
HRKGDKAVFN RTVGLKDSWK

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016825 Genomic DNA. Translation: AAQ59416.2.
RefSeqNP_901412.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NX86.
SMRQ7NX86. Positions 11-558.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2551030.
GenomeReviewsGene locus CV_1742 in contig AE016825_GR.
KEGGcvi:CV_1742.
NMPDRfig|243365.1.peg.1742.
PATRIC21438290. VBIChrVio67196_1706.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG334108.
OMARMPTIAG.
PhylomeDBQ7NX86.
ProtClustDBPRK05347.

Enzyme and pathway databases

BioCycCVIO243365:CV_1742-MONOMER.

Family and domain databases

HAMAPMF_00126. Gln_tRNA_synth.
[Tree]
InterProIPR004514. 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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYQ_CHRVO
AccessionPrimary (citable) accession number: Q7NX86
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: December 15, 2003
Last modified: January 25, 2012
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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents