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Q14JD8

- SYE_FRAT1

UniProt

Q14JD8 - SYE_FRAT1

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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
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).UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi97 – 971ZincUniRule annotation
Metal bindingi99 – 991ZincUniRule annotation
Metal bindingi124 – 1241ZincUniRule annotation
Metal bindingi126 – 1261ZincUniRule annotation
Binding sitei239 – 2391ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW
  4. 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, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciFTUL393115:GJUT-314-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetaseUniRule annotation
Short name:
GluRSUniRule annotation
Gene namesi
Name:gltXUniRule annotation
Ordered Locus Names:FTF0307
OrganismiFrancisella tularensis subsp. tularensis (strain FSC 198)
Taxonomic identifieri393115 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
ProteomesiUP000001821: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Glutamate--tRNA ligasePRO_1000001900Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi393115.FTF0307.

Structurei

3D structure databases

ProteinModelPortaliQ14JD8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi8 – 1811"HIGH" regionAdd
BLAST
Motifi236 – 2405"KMSKS" region

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252722.
KOiK01885.
OMAiVTGQTHG.
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.

Q14JD8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MITTRFAPSP TGFLHVGGVR TALFSWLYAK NNNGKFILRI EDTDLERSTQ
60 70 80 90 100
EAVDAILDGM SWLGLKNDGE IYYQTKRFDR YKEVIQELIA DGKAYYCSCS
110 120 130 140 150
KERLEELREY QQANNLKTGY DGKCRDANYI PQQGESYVVR FKNPQDGVVS
160 170 180 190 200
WDDAVKGRIS ISNHELDDMI IQRADGSPTY NFCVVVDDID MAITHIIRGD
210 220 230 240 250
DHVNNTPKQI NIYKALNANV PIFAHVPMIL GPDGAKLSKR HGAVNVMQYR
260 270 280 290 300
EDGYLPQAIL NYLVRLGWSH GDQEIFSIEE MIKAFNLEHI NASPSRFDFE
310 320 330 340 350
KLKWLNKHYI KESKFDDIQT EVEYHFAKTG LDISNGPDLK ELVAVMAEKV
360 370 380 390 400
DTLVELAEKS SYFYSDDISY DENAVKKHIK ASTGEIFVKL LENFEALDAQ
410 420 430 440 450
QWQDPDVLHN IVSTTAEQCQ VGMGKVGMPL RVAITGSGQS PDIGITLKLL
460
GKNKVVARLT KALEELCK
Length:468
Mass (Da):52,953
Last modified:August 22, 2006 - v1
Checksum:iB5D3AC570C11C4A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM286280 Genomic DNA. Translation: CAL08323.1.
RefSeqiYP_666488.1. NC_008245.1.

Genome annotation databases

EnsemblBacteriaiCAL08323; CAL08323; FTF0307.
GeneIDi4199800.
KEGGiftf:FTF0307.
PATRICi17959315. VBIFraTul133500_0342.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM286280 Genomic DNA. Translation: CAL08323.1 .
RefSeqi YP_666488.1. NC_008245.1.

3D structure databases

ProteinModelPortali Q14JD8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 393115.FTF0307.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL08323 ; CAL08323 ; FTF0307 .
GeneIDi 4199800.
KEGGi ftf:FTF0307.
PATRICi 17959315. VBIFraTul133500_0342.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci FTUL393115:GJUT-314-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. "Genome sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
    Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
    PLoS ONE 2:E352-E352(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FSC 198.

Entry informationi

Entry nameiSYE_FRAT1
AccessioniPrimary (citable) accession number: Q14JD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: October 29, 2014
This is version 62 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