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A8GPB2 (SYE2_RICAH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:A1C_04895
OrganismRickettsia akari (strain Hartford) [Complete proteome] [HAMAP]
Taxonomic identifier293614 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length463 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 – 463463Glutamate--tRNA ligase 2 HAMAP MF_00022_B
PRO_0000367753

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022_B
Motif239 – 2435"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8GPB2 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: D0053298392C2F34

FASTA46352,433
        10         20         30         40         50         60 
MTNVITRFAP SPTGFLHIGS ARTALFNYLF ARHNNGKFLL RIEDTDKERS TKAAVDAIFS 

        70         80         90        100        110        120 
GLKWLGLDWD AEVIFQSKRN DLYKKAALRL LKEGKAYYCF TSQEEIEKQR QKALENKQHF 

       130        140        150        160        170        180 
IFNSEWRDKE PDAYPTDVKP VIRLKTPREG RITIHDTLQG EVVIENSHID DMVLLRADGT 

       190        200        210        220        230        240 
ATYMLAVVAD DHDMGITHII RGDDHLTNAA RQIAIYQALG YEVPSMTHIP LIHGADGAKL 

       250        260        270        280        290        300 
SKRHGALGVD AYKNMGYLPE SLCNYLLRLG WSHGNDEIIS MTQAIEWFNL DSLGKSPSRL 

       310        320        330        340        350        360 
DFAKMNSLNA YYLRMLDNDT LTAKTVEILK QNYKISDKEV SYIKQAMSSL LVRSETLLDL 

       370        380        390        400        410        420 
AQLAQIYLVD SPIVYNQDAK EIIENCNKDL IKQVTEGLNK IEKFDKESVQ NKFKEIAAAN 

       430        440        450        460 
DLKLSDIMKP VRALITGMDA SPSVFAIAEI LGKENILKRL ETI 

« Hide

References

[1]"Complete genome sequence of Rickettsia akari."
Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Dasch G., Eremeeva M.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hartford.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000847 Genomic DNA. Translation: ABV75237.1.
RefSeqYP_001493745.1. NC_009881.1.

3D structure databases

ProteinModelPortalA8GPB2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8GPB2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5645637.
GenomeReviewsGene locus A1C_04895 in contig CP000847_GR.
KEGGrak:A1C_04895.
NMPDRfig|293614.3.peg.915.
PATRIC17876960. VBIRicAka50705_1015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMAIEWFNLD.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycRAKA293614:A1C_04895-MONOMER.

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.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_RICAH
AccessionPrimary (citable) accession number: A8GPB2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 32 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