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A5CFB7 (SYE2_ORITB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:OTBS_1957
OrganismOrientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi) [Complete proteome] [HAMAP]
Taxonomic identifier357244 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeOrientia

Protein attributes

Sequence length448 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 CAM81052.1 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 – 448448Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367726

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif240 – 2445"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5CFB7 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 27F3179D43E053A6

FASTA44851,389
        10         20         30         40         50         60 
MTVITRFAPS PTGKLHIGNV RVALVNWLYA QKYNGNFILR IDDTDRDRSK VEYHEAIIKD 

        70         80         90        100        110        120 
LQWLGINWNS SFLQSIRFNK YKAAKQYLIS SGRLYECYET PEMLEIERKR QLTSGYPPIY 

       130        140        150        160        170        180 
SRKALELTKA QKVQLQAEGY KVHYRFLIDR NKPIIWNDLI KGEIKYDGSN ISDPIVIKED 

       190        200        210        220        230        240 
GTMIYMLCSV IDDIEYRISH IIRGEDHITN TAIQIQMFEA LGAAIPQLGH LSLIKSDSGK 

       250        260        270        280        290        300 
ISKRIGGFTI DYLRDQLGIE PMAVNNLLAL SGTSNNVDAY FSLESLITKF DLSAFSKSAI 

       310        320        330        340        350        360 
IYNENELVTL NHKLLVNTEY DTIKHRLTAI GLPDVTKEFW LAVRHNLNTL NDIKIWWQIC 

       370        380        390        400        410        420 
YLPTLDKFQE QDAEFLKLAA GLLPSGKLTD NSWDDWVQNI IKATNRRGKA LFMPLRLALT 

       430        440 
GITYGPELKY LLPLIGGEEV KARLLRHQ 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Boryong.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM494475 Genomic DNA. Translation: CAM81052.1. Different initiation.
RefSeqYP_001249147.1. NC_009488.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357244.OTBS_1957.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM81052; CAM81052; OTBS_1957.
GeneID5218997.
KEGGots:OTBS_1957.
PATRIC22825427. VBIOriTsu83812_2120.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycOTSU357244:GCA5-1991-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_ORITB
AccessionPrimary (citable) accession number: A5CFB7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 48 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