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Q5WVE0

- SYE_LEGPL

UniProt

Q5WVE0 - SYE_LEGPL

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Protein

Glutamate--tRNA ligase

Gene
gltX, lpl1875
Organism
Legionella pneumophila (strain Lens)
Status
Reviewed - 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) By similarity.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 – 2391ATP By similarity

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

BioCyciLPNE297245:GJD4-2021-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Gene namesi
Name:gltX
Ordered Locus Names:lpl1875
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000002517: Chromosome

Organism-specific databases

LegioListilpl1875.

Subcellular locationi

Cytoplasm By similarity 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 – 470470Glutamate--tRNA ligaseUniRule annotationPRO_0000119588Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi297245.lpl1875.

Structurei

3D structure databases

ProteinModelPortaliQ5WVE0.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 1911"HIGH" regionUniRule annotationAdd
BLAST
Motifi236 – 2405"KMSKS" regionUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252722.
KOiK01885.
OMAiWINGYYL.
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.

Q5WVE0-1 [UniParc]FASTAAdd to Basket

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MTVRTRFAPS PTGFLHVGGV RTALFSWLYA KHHNGQFILR IEDTDRERST    50
QESVQAILDG MAWLGLNFDE GPYYQTERYA RYQQVAQQLL EEGKAYRCQC 100
SKERLEALRE AQLAAKEKPR YDGHCRNQSL PDSGIPYVIR FRNPDGGIVS 150
FHDEVYGDIH VDNSELDDLI LVRSDGHPTY NFAVVIDDWD MKITHVIRGD 200
DHINNTPRQI NLFKALDAPV PVFAHLPMIL GEDGKRLSKR HGAVSVLQFK 250
ELGVLPHALL NYLVRLGWSH GDQEIFSVQE MITSFDLKNV SRGVSSFNYD 300
KLYWLNQHYQ KSDSPESVAN ALQWHFEQAG IDLNQGPDLK DLVAVQAERC 350
KSLAEMCQIS QYFYTDTIEY NEDAVKKHLR PVVLEPLMVL HERLKALDEW 400
KNDKIQECIN DVSLQFDLNL GKIAQPLRVA VTGSGTSPSI DMTLALLGKN 450
KSIKRLEDAL EKIRARASVV 470
Length:470
Mass (Da):53,548
Last modified:November 23, 2004 - v1
Checksum:iEACE7D81A3A3DBBC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH16114.1.
RefSeqiWP_011215873.1. NC_006369.1.
YP_127213.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH16114; CAH16114; lpl1875.
GeneIDi3113956.
KEGGilpf:lpl1875.
PATRICi22317493. VBILegPne33733_2064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH16114.1 .
RefSeqi WP_011215873.1. NC_006369.1.
YP_127213.1. NC_006369.1.

3D structure databases

ProteinModelPortali Q5WVE0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 297245.lpl1875.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAH16114 ; CAH16114 ; lpl1875 .
GeneIDi 3113956.
KEGGi lpf:lpl1875.
PATRICi 22317493. VBILegPne33733_2064.

Organism-specific databases

LegioListi lpl1875.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252722.
KOi K01885.
OMAi WINGYYL.
OrthoDBi EOG6DRPF7.

Enzyme and pathway databases

BioCyci LPNE297245:GJD4-2021-MONOMER.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi IPR008925. 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 ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF00749. tRNA-synt_1c. 1 hit.
[Graphical view ]
PRINTSi PR00987. TRNASYNTHGLU.
SUPFAMi SSF48163. SSF48163. 1 hit.
TIGRFAMsi TIGR00464. gltX_bact. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
    Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
    Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Lens.

Entry informationi

Entry nameiSYE_LEGPL
AccessioniPrimary (citable) accession number: Q5WVE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: November 23, 2004
Last modified: September 3, 2014
This is version 67 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

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