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B1M0I6 (SYE2_METRJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:Mrad2831_5563
OrganismMethylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831) [Complete proteome] [HAMAP]
Taxonomic identifier426355 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length446 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 – 446446Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367712

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif239 – 2435"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1M0I6 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: B09056FD871CD5FB

FASTA44648,358
        10         20         30         40         50         60 
MTLVRFAPSP TGYLHIGNAR PALLNALFAR RTGGRFLLRL DDTDAERSTE AFAEAIGEDL 

        70         80         90        100        110        120 
AWLGIVPDLF ARQSARTAQH DAAADRLRAA GRLYPCYETP EELERRRRRQ LGRGQPPIYD 

       130        140        150        160        170        180 
RAALRLTGDE RAALEAEGRR PHWRFLLEAR TVGWDDLVRG PAHVDCASLS DPVLIRADGS 

       190        200        210        220        230        240 
YLYTLPSVVD DADLGITHVI RGEDHVTNTG VQVQIFEALG AAVPVFGHHN LLTTADGEGL 

       250        260        270        280        290        300 
SKRLGHLSLR GLREAGYEPA AVRSLAVLTG SAESVRAVPD LDTLAGLVDL GEISRAPARF 

       310        320        330        340        350        360 
DPAELDGLNA RLIHAMPYRE AAARLADLGI PADRAEAFWL AVRANLSRVP EAAPWWRVVT 

       370        380        390        400        410        420 
GPVEPVLTEP AVIAAAVESL PPEPFGPETW NAWTTEIRTR TGAKGRGLFM PLRLALTGLE 

       430        440 
HGPDLAGLLP LIGRERAARR LSGAAA 

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium radiotolerans JCM 2831."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Marx C.J., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27329 / DSM 1819 / JCM 2831.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001001 Genomic DNA. Translation: ACB27508.1.
RefSeqYP_001758191.1. NC_010505.1.

3D structure databases

ProteinModelPortalB1M0I6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING426355.Mrad2831_5563.

Proteomic databases

PRIDEB1M0I6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB27508; ACB27508; Mrad2831_5563.
GeneID6141637.
KEGGmrd:Mrad2831_5563.
PATRIC22579544. VBIMetRad70578_5627.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAAGRLYPC.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycMRAD426355:GJB5-5627-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. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_METRJ
AccessionPrimary (citable) accession number: B1M0I6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 40 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