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B0RIP8 (SYE_CLAMS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:CMS1428
OrganismClavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum) [Complete proteome] [HAMAP]
Taxonomic identifier31964 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter

Protein attributes

Sequence length506 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 – 506506Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000074318

Regions

Motif23 – 3311"HIGH" region HAMAP-Rule MF_00022
Motif267 – 2715"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2701ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0RIP8 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: D9316DC3517A73A2

FASTA50656,148
        10         20         30         40         50         60 
MTETTAHPVT TATGTDVRVR FCPSPTGTPH VGLIRTALFN WAYARHTGGK LVFRVEDTDA 

        70         80         90        100        110        120 
ARDSEESYEQ LIEALRWLEI DWDEGEGVGG PHAPYRQSQR TDLYLDVIAK LTASGHLYES 

       130        140        150        160        170        180 
FATAEEIEAR NRAAGRDPKM GYDNFERDLT EEERQAFRDE GRSPALRLRV PDTDLSFDDL 

       190        200        210        220        230        240 
VRGTVTFPAG SFPDFVLVRP NGAPLYTLVN PVDDALMGIT HVLRGEDLLS STPRQIALYH 

       250        260        270        280        290        300 
ALIDIGVADA IPRFGHLPYV MGEGNKKLSK RDPESNLFHH RDRGFIPEGL INYLALLGWS 

       310        320        330        340        350        360 
LTHDRDVFSR MEMVTAFDVA DVNPNPARFD LKKAESLNGD HIRLLALDDF AQRLVPYLQA 

       370        380        390        400        410        420 
ADVVGAELTH DQRRMLEAAA PLVQERMQLL GEAPDLLSFL FTTADELPYD DAAVQALKDD 

       430        440        450        460        470        480 
APEVLAASRG ALSGVPHTQW DIDLVQEVLQ NTLITGMGMK PRLAYGPLRV GISGRRISPP 

       490        500 
LFESMVLLGK DETIARLDRL AGMLGE 

« Hide

References

[1]"Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp. sepedonicus suggests recent niche adaptation."
Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., Parkhill J., Ishimaru C.A.
J. Bacteriol. 190:2150-2160(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM849034 Genomic DNA. Translation: CAQ01539.1.
RefSeqYP_001710155.1. NC_010407.1.

3D structure databases

ProteinModelPortalB0RIP8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING31964.CMS_1428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ01539; CAQ01539; CMS1428.
GeneID6157258.
KEGGcms:CMS_1428.
PATRIC21459870. VBIClaMic4666_1492.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAAMGWEVP.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCMIC31964:GJBN-1436-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.
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.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYE_CLAMS
AccessionPrimary (citable) accession number: B0RIP8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 41 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