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B3CRX8 (SYE1_ORITI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:OTT_0777
OrganismOrientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi) [Complete proteome] [HAMAP]
Taxonomic identifier334380 [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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000367727

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022_B
Motif240 – 2445"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3CRX8 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 6D980FEC9C77418E

FASTA44851,379
        10         20         30         40         50         60 
MTVITRFAPS PTGKLHIGNV RVALVNWLYA QKYNGNFILR IDDTDRDRSK VEYHEAIIKD 

        70         80         90        100        110        120 
LQWLGINWNS SFLQSTRFNK YAAAKQYLIS SGRLYECYET PEMLEIERKR QLASGYPPIY 

       130        140        150        160        170        180 
SRKSLELTTA QKVQLQAEGY KVHYRFLIDR NKPIIWNDLI KGEIKYDGSN VSDPIVIKED 

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

       250        260        270        280        290        300 
ISKRIGGFTI DYLKDQLGIE PMAVNNLLAL SGTSNNVDAY FSLESLITKF DLSAFSKSTI 

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

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

       430        440 
GITYGPELKY LLPLIGGDEV RARLLRYQ 

« 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: 18508905] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ikeda.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008981 Genomic DNA. Translation: BAG40235.1.
RefSeqYP_001937469.1. NC_010793.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB3CRX8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6337915.
GenomeReviewsGene locus OTT_0777 in contig AP008981_GR.
KEGGott:OTT_0777.
PATRIC22827698. VBIOriTsu129072_0879.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMALLYPCYE.
ProtClustDBPRK12558.

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_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
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. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_ORITI
AccessionPrimary (citable) accession number: B3CRX8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families