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Q2FTH6 (SYE_METHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:Mhun_2885
OrganismMethanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) [Reference proteome] [HAMAP]
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length561 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
Reference 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 – 561561Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237424

Regions

Motif107 – 11711"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q2FTH6 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 0621797F09CB5DE0

FASTA56162,639
        10         20         30         40         50         60 
MDDVRSVLLI AALSNAVKHK SVPAAGAVMG AILGTHPELR SKAGEIKGLL GSVLEEVSSL 

        70         80         90        100        110        120 
SAEDREEKLK TIAPDQYASL FEKKEKKKIG LPDLPKAEGG VVMRFAPNPS GPLHLGHARA 

       130        140        150        160        170        180 
AFLNDEYIRR YGGKYILRIE DTDPKRVDPD AYDMVREDIA WMGLSIAETI FQSDRFSKYY 

       190        200        210        220        230        240 
EVGKELIQKG HAYVCRCDNE KFKDLKMHKT ACPCRSQSPE EALDLFDQML DGAFTEGEVG 

       250        260        270        280        290        300 
VRLKTDLSHP DPAMRDYPLF RVLTSTPHQR VDAIVYPLMN LSVAVDDHLL GMTHVIRGKD 

       310        320        330        340        350        360 
HIANTKRQEF IFRYMGWETP VYRHYGRMGI EGVVLSTSQM RAGIQSGEYS GWDDVRLGTL 

       370        380        390        400        410        420 
RAMARRGIQP QAVRNAVVEI GIGETDIQFS WENLYAKNKE IIDSQADRFF FVPDPVLVPV 

       430        440        450        460        470        480 
SGSDPVVAKA MRYPGDESRG YREIPFAGSL YLPKAELESG AAYIRLKDLF NIKVLYEGDI 

       490        500        510        520        530        540 
IRGEYAGDDL QEARSKKAPI IQWLPENHAN PCTLKTPDGD VSGVCEPEAV TTQDRIVQFE 

       550        560 
RVGFARIDAA GNPAVAYFTH R 

« Hide

References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27890 / DSM 864 / NBRC 100397 / JF-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000254 Genomic DNA. Translation: ABD42577.1.
RefSeqYP_504296.1. NC_007796.1.

3D structure databases

ProteinModelPortalQ2FTH6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323259.Mhun_2885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD42577; ABD42577; Mhun_2885.
GeneID3924180.
KEGGmhu:Mhun_2885.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAYLGWDDP.

Enzyme and pathway databases

BioCycMHUN323259:GH0L-2928-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 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.
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_METHJ
AccessionPrimary (citable) accession number: Q2FTH6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 21, 2006
Last modified: May 14, 2014
This is version 53 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