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Reviewed, UniProtKB/Swiss-Prot A5CD02 (SYE1_ORITB)

Last modified January 19, 2010. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 1
      Short name=GluRS 1
Gene names
Name: gltX1
Ordered Locus Names: OTBS_0573
OrganismOrientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi) [Complete proteome] [HAMAP]
Taxonomic identifier357244 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeOrientia

Protein attributes

Sequence length478 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 MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022

Subunit structure

Monomer By similarity. HAMAP MF_00022

Subcellular location

Cytoplasm By similarity HAMAP 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 478478Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367725

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022
Motif242 – 2465"KMSKS" region HAMAP MF_00022

Sites

Binding site2451ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5CD02-1 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 142483D2A096C22B

FASTA47853,883
        10         20         30         40         50         60 
MTNIVTRFAP SPTGFLHIGG ARTALFNYLF ARHHKGKFLL RIEDTDAARS TEEYKISIID 

        70         80         90        100        110        120 
SLKWLKINWD NDIFYQSANL QRHVNIALEL VKSGKAYYCF TSPEEIDLQR QLAITQKQSF 

       130        140        150        160        170        180 
IFRSPWRNNI PSSLSLKNNN KAYVIRFKAP DYGTTIINDH VQGEVVFQNQ QIDDMILVRS 

       190        200        210        220        230        240 
DGTPTYMLAV VVDDHDMGIT HIIRGDDHLT NAAKQIALYD ALGWAAPAMV HIPLIYGPDG 

       250        260        270        280        290        300 
TKLSKRHGAI GVDAYQKMGY LPEALCNYLL RLGWSYQDEE IISHERAIKL FDIDGLGGKS 

       310        320        330        340        350        360 
AARLDFDKML YLNGYYIRST DNSILAKLVI EILSKQYILS NESCNLIQKG MSGLKSRANL 

       370        380        390        400        410        420 
LTDLAENAKI YVLESQLTFI NEALNIIQKT PSMLITEVID IINNLQELNC ESVKQALTEF 

       430        440        450        460        470 
AKTKKMKLGQ LMDPIRALLT GNTKSPSIFE VIPILGKIHT IKRLAGIKAI KSNNQTLV 

« Hide

References

[1]"The Orientia tsutsugamushi genome reveals massive proliferation of conjugative type IV secretion system and host-cell interaction genes."
Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y., Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S., Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.
Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007) [PubMed: 17483455] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM494475 Genomic DNA. Translation: CAM79639.1. Different initiation.
RefSeqYP_001248424.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5CD02.

Genome annotation databases

GeneID5218910.
GenomeReviewsGene locus OTBS_0573 in contig AM494475_GR.
KEGGots:OTBS_0573.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_ORITB
AccessionPrimary (citable) accession number: A5CD02
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: January 19, 2010
This is version 21 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents