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Q83BL6 (SYE2_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:gltX-2
Ordered Locus Names:CBU_1488
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length465 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.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference 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 – 465465Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000119551

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif249 – 2535"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83BL6 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 66F71C16CF65E449

FASTA46552,763
        10         20         30         40         50         60 
MMKSRFCPSP TGLMHLGNAR TALFNYLFAK SKDGIFLLRI EDTDVERSKE TFDLGLQEDL 

        70         80         90        100        110        120 
RWLNLEWQEG PGADEGNGPY HQSKRQAIYD DYYQRLEEAD QAYPCFCSEE QLRLSRKIQR 

       130        140        150        160        170        180 
SAGKPPRYAG TCRSLSAAEI EKKKAEGLQP ALRFRVPDDE VVVFADLVRG EQRFQTNDIG 

       190        200        210        220        230        240 
DFIIRRANGT SPFMFCNAID DALMGVSHVL RGEDHLTNTP RQLLILQALE LPVPTYAHIA 

       250        260        270        280        290        300 
LIVGPDGSPL SKRHGSRGIK ELRDNGYLPL ALTNYLARLG HYYASDELLS LAELAKGFNV 

       310        320        330        340        350        360 
ESLSKSPAKF NAQQLDYWQK QTVNQLPNDD FWEWAGSELQ SQIPTDKDDL FLTTVKPNVS 

       370        380        390        400        410        420 
FPRDVAYWVN VCFGKTLNLE TAQSELLRAT GNRYFEEAFE AFKKFGKDLN SVVSHLKEKL 

       430        440        450        460 
NLKGKPLYQP LRIALTGAEH GPELAKLILI MDYETIQNRL QEACQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO90985.2.
RefSeqNP_820471.2. NC_002971.3.

3D structure databases

ProteinModelPortalQ83BL6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_1488.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO90985; AAO90985; CBU_1488.
GeneID1209398.
KEGGcbu:CBU_1488.
PATRIC17931739. VBICoxBur82552_1489.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMANKLTWIN.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-1476-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_COXBU
AccessionPrimary (citable) accession number: Q83BL6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 16, 2008
Last modified: February 19, 2014
This is version 73 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

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries