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Q2NFU2 (SYE_METST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:Msp_0923
OrganismMethanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3) [Complete proteome] [HAMAP]
Taxonomic identifier339860 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanosphaera

Protein attributes

Sequence length563 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 – 563563Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237423

Regions

Motif104 – 11411"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q2NFU2 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 7ECE36266DE04D46

FASTA56364,969
        10         20         30         40         50         60 
MDIEETIYKY ALTNAIEHGN KCQVGSVIGM VMSKNPEMRK DPKTVSQLAG KLVAKVNNLT 

        70         80         90        100        110        120 
PEEQQKEVES LGGLEQHTKK EEKPKGLPEL KNTEDKKVTL RFAPNPSGPL HIGHARAAIL 

       130        140        150        160        170        180 
NKLYQEKYNG KLILRIEDTD PKRVEPDAYD AIPQDIKWLG IEPDEIYTQS DRLEIYYEYA 

       190        200        210        220        230        240 
QKAIEIGAAY MCKCDGGEFK KLKDNCQPCP CRSHTIEENM ELWNNFENME EGEAVLRIKT 

       250        260        270        280        290        300 
DINHKNPAIR DWVAMRIVNQ EHPRLGNKYK IYPMMNFSVT VDDHLMGMTH VLRGKDHLAN 

       310        320        330        340        350        360 
SEKQTYLYKH FGWDVPEFIH YGRLKMDDVE LSTSKAREGI ENKTYTGWDD PRLGTIRAIA 

       370        380        390        400        410        420 
RRGIKKEVLY DLIEEIGTKQ ADATISWKKI YGLNRNIIEE NTNRYFFIPN AVKVDVENLP 

       430        440        450        460        470        480 
SSKTNMTVER ELHYNKPEKG FRNLTFNGSV YIPEDDYKHA QDKNIPLRLM DLINIKIEED 

       490        500        510        520        530        540 
KVIYDSETLE DAQAQHARII QWAPVETSIS ATVVMPDNTH VTGYIECDAS NLEVDDMVQL 

       550        560 
ERFGFARVDK INDNEITFYY THN 

« Hide

References

[1]"The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis."
Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K.
J. Bacteriol. 188:642-658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000102 Genomic DNA. Translation: ABC57311.1.
RefSeqYP_447954.1. NC_007681.1.

3D structure databases

ProteinModelPortalQ2NFU2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING339860.Msp_0923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC57311; ABC57311; Msp_0923.
GeneID3856230.
KEGGmst:Msp_0923.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAMRFAPNP.
ProtClustDBPRK04156.

Enzyme and pathway databases

BioCycMSTA339860:GJEZ-923-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_METST
AccessionPrimary (citable) accession number: Q2NFU2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: February 7, 2006
Last modified: February 19, 2014
This is version 52 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