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Q6LYI0 (SYE_METMP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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:
Glutamate--tRNA ligase

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:MMP1011
OrganismMethanococcus maripaludis (strain S2 / LL) [Complete proteome] [HAMAP]
Taxonomic identifier267377 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

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_processglutamyl-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

glutamate-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 – 555555Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119720

Regions

Motif100 – 11011"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q6LYI0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: C8B79D519993E177

FASTA55564,095
        10         20         30         40         50         60 
MKDTVMTYLL ENSIKFKGKP NPKAAMGKIL GENPDLRSKV KEVNQVISEV LKEIETMSLE 

        70         80         90        100        110        120 
EQQAKLDELA PEGLGQKTER KRKEIELKNV KGNVVMRFAP NPSGPLHIGH ARASVLNDFF 

       130        140        150        160        170        180 
SKKYNGKLVL RLEDTDAKRV LPEAYEMIQE DLKWLGVKVD EVIVQSERLE TYYEYGRKLI 

       190        200        210        220        230        240 
EMGHAYVCDC DADEFRTLRE QGLPCKCRDT TPEENIALWE KMLAGELDNV AVRLKTDIAH 

       250        260        270        280        290        300 
KNPSIRDFPI FRIERTPHPK NGTKYHVYPL MNLSVTVDDH LLGMTHVLRG KDHIVNTEKQ 

       310        320        330        340        350        360 
EYIYNYFGWE IPEYVHYGIL KIEGPVLSTS KMHAGILSGE YSGWDDARLG TLRALRKRGI 

       370        380        390        400        410        420 
RPEALYKLMV EIGIKQADVR FAWENLYAAN KDIIDKDARR FFFVESPKKL VISGAENRKI 

       430        440        450        460        470        480 
DLRMHPDRSE LGNRELLFDG EIYVSDDLEA GKMYRLMELF NIVVEKVEND IIYAKYDSDD 

       490        500        510        520        530        540 
FKVAKTNKAS IIHWIPVKDS IPVTVIDENA EKIEGFAEKD FAVVKEDDFV QFERFGFVRI 

       550 
DEKLDNKYTC YLTHK 

« Hide

References

[1]"Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis."
Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., Moore B.C. expand/collapse author list , Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A.
J. Bacteriol. 186:6956-6969(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S2 / LL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950229 Genomic DNA. Translation: CAF30567.1.
RefSeqNP_988131.1. NC_005791.1.

3D structure databases

ProteinModelPortalQ6LYI0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267377.MMP1011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF30567; CAF30567; MMP1011.
GeneID2762222.
KEGGmmp:MMP1011.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAMRFAPNP.
ProtClustDBPRK04156.

Enzyme and pathway databases

BioCycMMAR267377:GJ77-1041-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
2.40.240.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_A. Glu_tRNA_synth_A.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_arc/euk.
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.
IPR022888. Glu_tRNA_synth_arc.
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.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_METMP
AccessionPrimary (citable) accession number: Q6LYI0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 64 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