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Q6YR76 (SYE_ONYPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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:PAM_140
OrganismOnion yellows phytoplasma (strain OY-M) [Complete proteome] [HAMAP]
Taxonomic identifier262768 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeCandidatus PhytoplasmaCandidatus Phytoplasma asteris

Protein attributes

Sequence length449 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

Subunit structure

Monomer By similarity. 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

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119617

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif214 – 2185"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2171ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6YR76 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E3C2C2FD0D9CA4FC

FASTA44952,352
        10         20         30         40         50         60 
MKKIKVRYAP SPTGFLHIGN ARTALFNYLF AKQNQGEFII RIEDTDFSRN VEGGEASQLK 

        70         80         90        100        110        120 
NLRWLGIDWS EGPDIQGPFG PYRQSERLAI YQKYAQKLLD QDLAYKEFQE GHTTFAIRFR 

       130        140        150        160        170        180 
VPTNQTFAFD DLIRGKLTFQ SQEIEDFIIL KSNGYPSYNF AVVIDDHLMQ ISHIFRGEEH 

       190        200        210        220        230        240 
ITNTPKQIMI YQAFQWHLPQ FAHMTLILNE NKKKLSKRDA NIMQFIEQYE KLGYLPQALF 

       250        260        270        280        290        300 
NFLSLLGFSP LSQTEILSPQ ELINLFDVAR LNKAPAMFDK TKLDYLNNQH LRKLLPEVIA 

       310        320        330        340        350        360 
SFILQKKYLA LTTAPTNYKE WMTKFVALFQ DRMHYMQQIT DFYQLFFQST PFLSQEATHF 

       370        380        390        400        410        420 
LQTNPQTTLI LKTFYNVFDV IVFEKDVIAN SIKQVTTQND FAKKTLFMAL RIGTTCKMHG 

       430        440 
PSIALLLELL GKKQVLKNLS YVLEQAQKF 

« Hide

References

[1]"Reductive evolution suggested from the complete genome sequence of a plant-pathogenic phytoplasma."
Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S., Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.
Nat. Genet. 36:27-29(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OY-M.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006628 Genomic DNA. Translation: BAD04225.1.
RefSeqNP_950392.1. NC_005303.2.

3D structure databases

ProteinModelPortalQ6YR76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262768.PAM_140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD04225; BAD04225; PAM_140.
GeneID2673455.
KEGGpoy:PAM_140.
PATRIC22809738. VBIOniYel86799_0197.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAKRDANIM.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycMORG262768:GHF5-142-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 2 hits.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_ONYPE
AccessionPrimary (citable) accession number: Q6YR76
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 77 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