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A5CPZ8 (SYE_CLAM3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:CMM_1108
OrganismClavibacter michiganensis subsp. michiganensis (strain NCPPB 382) [Complete proteome] [HAMAP]
Taxonomic identifier443906 [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_0000330960

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
A5CPZ8 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: F0F2888DD67DFF66

FASTA50655,936
        10         20         30         40         50         60 
MTETTAHPVT TATGTDVRVR FCPSPTGTPH VGLIRTALFN WAYARHTGGK LVFRVEDTDA 

        70         80         90        100        110        120 
ARDSEESYEQ LIEALRWLEI DWDEGEGVGG PHAPYRQSQR TDLYLDVIRK LTESGHLYES 

       130        140        150        160        170        180 
YATAEEIEAR NRAAGRDPKM GYDNFERDLT EAERQAFRDE 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 DVTPAPARFD LKKAESLNGD HIRLLALDDF AQRLVPYLQA 

       370        380        390        400        410        420 
ADVVGAELTH DEQRMLEAAA PLVQERMQLL GEAPDLLSFL FTTADALPYD DAAVQALKDD 

       430        440        450        460        470        480 
AAAVLAASRG ALAGVPHTQW DIDLVQEVLQ NTLITGMGMK PRLAYGPLRV AVSGRRISPP 

       490        500 
LFESMVLLGK DETIARLDRL AGMLGG 

« Hide

References

[1]"The genome sequence of the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382 reveals a large island involved in pathogenicity."
Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C. expand/collapse author list , Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., Bartels D.
J. Bacteriol. 190:2138-2149(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCPPB 382.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM711867 Genomic DNA. Translation: CAN01151.1.
RefSeqYP_001221849.1. NC_009480.1.

3D structure databases

ProteinModelPortalA5CPZ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING443906.CMM_1108.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAN01151; CAN01151; CMM_1108.
GeneID5175327.
KEGGcmi:CMM_1108.
PATRIC21452961. VBIClaMic82482_1208.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMALMLFGRD.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCMIC443906:GCI2-1140-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_CLAM3
AccessionPrimary (citable) accession number: A5CPZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 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