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Q2GHQ1 (SYE1_EHRCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase 1
EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Synonyms:gltX-1
Ordered Locus Names:ECH_0208
OrganismEhrlichia chaffeensis (strain Arkansas) [Complete proteome] [HAMAP]
Taxonomic identifier205920 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia

Protein attributes

Sequence length443 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 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 – 443443Glutamate--tRNA ligase 1 HAMAP MF_00022_B
PRO_0000237362

Regions

Motif7 – 1711"HIGH" region HAMAP MF_00022_B
Motif236 – 2405"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2GHQ1 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 715A3468A7CA1085

FASTA44351,094
        10         20         30         40         50         60 
MITRFAPSPT GYLHVGNVRT ALVCWLYARK QNGKFLLRFD DTDTQRSKDE YIREIENDLV 

        70         80         90        100        110        120 
WLNINWDSSF RQSSRFDRYE DVFNYLLKEG LIYPCYESKE ELEFKRKMKL KLGLPPIYDR 

       130        140        150        160        170        180 
SALNLTQAEK DKYSERAPYF RFKIDQNQLI SWNDEVRGKV SFNSENISDP IIRRVDGTYT 

       190        200        210        220        230        240 
YMLPSIIDDM DFNVTHIIRG EDHISNTAVQ IQMLHALKAS IPIFSHLSLL YSDDNKISKR 

       250        260        270        280        290        300 
VGGSSVKDMQ SYGLEPMAIN SYFAKIGTSN PVSVHTRMCG LIDSFDITTF SQAPTKFNID 

       310        320        330        340        350        360 
DVLKLNPKVL CSMSFDDVRN RLQSFNITSP SFWNFVCGNI DKFSDIEGWA KICSGDMIPV 

       370        380        390        400        410        420 
IGQDDKDFIM LALNMLPQGE VRDNTWNLWI SNIKQHTDRR AKNLFTPLRL ALTGLSTGPE 

       430        440 
LAKLLPLIGR VEIVRRLSYS EVQ

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000236 Genomic DNA. Translation: ABD45168.1.
RefSeqYP_507032.1. NC_007799.1.

3D structure databases

ProteinModelPortalQ2GHQ1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2GHQ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3927352.
GenomeReviewsGene locus ECH_0208 in contig CP000236_GR.
KEGGech:ECH_0208.
PATRIC20575951. VBIEhrCha103583_0179.
TIGRECH_0208.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMAARTALIC.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycECHA205920:ECH_0208-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.
IPR001412. aa-tRNA-synth_I_CS.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_EHRCR
AccessionPrimary (citable) accession number: Q2GHQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 21, 2006
Last modified: January 25, 2012
This is version 41 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

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