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B3CST4 (SYE2_ORITI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:OTT_0973
OrganismOrientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi) [Complete proteome] [HAMAP]
Taxonomic identifier334380 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeOrientia

Protein attributes

Sequence length474 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.

Sequence caution

The sequence BAG40431.1 differs from that shown. Reason: Erroneous initiation.

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 – 474474Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367728

Regions

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

Sites

Binding site2451ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3CST4 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 3ACE63C5EB0C601A

FASTA47453,576
        10         20         30         40         50         60 
MTNIVTRFAP SPTGFLHIGG ARTALFNYLF ARHHKGKFLL RIEDTDAARS TEEYKLGIID 

        70         80         90        100        110        120 
SLKWLKINWD NDIFYQSANL QRHVNVALEL VKSGKAYYCF TSQEEIDLQR QLAIAQKQSF 

       130        140        150        160        170        180 
IFRSPWRNNI PSSLSLKNNN KAYVIRFKAP NHGTTIINDY VQGKVVFQNQ QIDDMILVRS 

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

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

       310        320        330        340        350        360 
ARLDFDKMLY LNGYYIRSTD NSILAKLVIE ILSKQYILSN ESCNLIQKGM SGLKSRANLL 

       370        380        390        400        410        420 
TDLAENAKIY VLENQLTFVN EALNIIQKTP SMLITEVIDI INNLQELNCE SVKQSLTEFA 

       430        440        450        460        470 
KVKHMKLGQL MDPIRALLTG NTKSPSIFEV IPILGKIHAV KRLADIEAIK SNNQ 

« Hide

References

[1]"The whole-genome sequencing of the obligate intracellular bacterium Orientia tsutsugamushi revealed massive gene amplification during reductive genome evolution."
Nakayama K., Yamashita A., Kurokawa K., Morimoto T., Ogawa M., Fukuhara M., Urakami H., Ohnishi M., Uchiyama I., Ogura Y., Ooka T., Oshima K., Tamura A., Hattori M., Hayashi T.
DNA Res. 15:185-199(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ikeda.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008981 Genomic DNA. Translation: BAG40431.1. Different initiation.
RefSeqYP_001937665.1. NC_010793.1.

3D structure databases

ProteinModelPortalB3CST4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING334380.OTT_0973.

Proteomic databases

PRIDEB3CST4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG40431; BAG40431; OTT_0973.
GeneID6337729.
KEGGott:OTT_0973.
PATRIC22828164. VBIOriTsu129072_1103.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycOTSU334380:GC7O-991-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.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_ORITI
AccessionPrimary (citable) accession number: B3CST4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 38 of the entry and version 2 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