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Protein

Glutamate--tRNA ligase 2

Gene

gltX2

Organism
Ehrlichia canis (strain Jake)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei239 – 2391ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. tRNA binding Source: InterPro

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciECAN269484:GI02-832-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase 2UniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetase 2UniRule annotation
Short name:
GluRS 2UniRule annotation
Gene namesi
Name:gltX2UniRule annotation
Ordered Locus Names:Ecaj_0795
OrganismiEhrlichia canis (strain Jake)
Taxonomic identifieri269484 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia
ProteomesiUP000000435 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Glutamate--tRNA ligase 2PRO_0000237361Add
BLAST

Proteomic databases

PRIDEiQ3YR29.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi269484.Ecaj_0795.

Structurei

3D structure databases

ProteinModelPortaliQ3YR29.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi7 – 1711"HIGH" regionAdd
BLAST
Motifi236 – 2405"KMSKS" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252721.
KOiK01885.
OMAiLYPCYET.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3YR29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITRFAPSPT GYLHVGNVRT ALICWLYVRK QKGKFLLRFD DTDTQRSQEE
60 70 80 90 100
YIKEIENDLK WLNMNWDASF RQSSRFDRYE DVFQYLLKEG FLYPCYESKE
110 120 130 140 150
ELEFKRKMKL KSGLPPIYDR SALNLTQAEK DKYFGRAPYF RFKINQDQLI
160 170 180 190 200
NWDDEIRGKV SFNPKNISDP IIRRVDGTYT YMLPSVIDDM DFNVTHVIRG
210 220 230 240 250
EDHISNTAVQ IQMLDALKAK VPMFAHLSLL YSDDNKISKR VGGSSVKDMQ
260 270 280 290 300
LYELEPMAIN SYFAKIGTSH PIDVHINMLG LINSFDITAF SQAPTKFNID
310 320 330 340 350
DILKLNPKIL HNMSFDDVKD RLKELKIDKP AFWDFVCGNI EKFSDIEEWI
360 370 380 390 400
KICSRDMVPV VKQDDKDFIT LALNMFPQGE VHDSTWNTWV SNIKQQTDRR
410 420 430 440
GKNLFAPLRL ALTGLAAGPE LAKLLPLIGR EEIVRRLSYS VTQ
Length:443
Mass (Da):51,549
Last modified:September 27, 2005 - v1
Checksum:i3508EE2D6663FD3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000107 Genomic DNA. Translation: AAZ68826.1.
RefSeqiYP_303424.1. NC_007354.1.

Genome annotation databases

EnsemblBacteriaiAAZ68826; AAZ68826; Ecaj_0795.
KEGGiecn:Ecaj_0795.
PATRICi20575248. VBIEhrCan118076_0869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000107 Genomic DNA. Translation: AAZ68826.1.
RefSeqiYP_303424.1. NC_007354.1.

3D structure databases

ProteinModelPortaliQ3YR29.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269484.Ecaj_0795.

Proteomic databases

PRIDEiQ3YR29.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ68826; AAZ68826; Ecaj_0795.
KEGGiecn:Ecaj_0795.
PATRICi20575248. VBIEhrCan118076_0869.

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252721.
KOiK01885.
OMAiLYPCYET.
OrthoDBiEOG6DRPF7.

Enzyme and pathway databases

BioCyciECAN269484:GI02-832-MONOMER.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies."
    Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.
    J. Bacteriol. 188:4015-4023(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Jake.

Entry informationi

Entry nameiSYE2_EHRCJ
AccessioniPrimary (citable) accession number: Q3YR29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: September 27, 2005
Last modified: April 29, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.