Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A8ABI5 (SYE_IGNH4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:Igni_1110
OrganismIgnicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125) [Complete proteome] [HAMAP]
Taxonomic identifier453591 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeIgnicoccus

Protein attributes

Sequence length562 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

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
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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 562562Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000070998

Regions

Motif104 – 11411"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
A8ABI5 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 1416697F0F34CB10

FASTA56264,685
        10         20         30         40         50         60 
MDVRELALKH ALRNAYLHGG KAQLKPVVTA VLAESPELRP KVKEIIPIIK EVVEEVNRMS 

        70         80         90        100        110        120 
LEEQERILKE RFPEALEERK KETRKGLPPL PNAERGKVKT RFAPNPDFYM TLGNARPAII 

       130        140        150        160        170        180 
SYEYAKAYEG RFVLRFEDTD PRTKRPLPEA YEAIKEDLSW LGIGWDEEYY QSQRMEVYYG 

       190        200        210        220        230        240 
LLRELVRRGG AYVCTCPPEE WRKLRDEGKP CPHRDLPPEE QEELLDQVLE GKFGEGEAVV 

       250        260        270        280        290        300 
RVKTDLRHPD PSVRDWVAFR IIDTSKHPHP LTGDKYVLWP TYNFAAGVDD YLMGITHVLR 

       310        320        330        340        350        360 
AREHRQNTVK QEFLYKHLGW TMPTVIHFGR LKLEGFVLSK SKMREAGFKG DDPRAATIRG 

       370        380        390        400        410        420 
LRRRGFAPEA IREVMLSVGI KSSDASISFA NLAAENKKVI DKKAYRVMAV EDPAPAKLLA 

       430        440        450        460        470        480 
PEPLEAELPW HPTEGLGSRK YSVEPGEVVY LERADLRRAK RRGGLRLMEL ANFKYKGFDE 

       490        500        510        520        530        540 
DEGVYLLEFE SKELDKEKGY DIVQWVKDPK GAIVWRPGER KSFALVEPEA LKLEGWVQLI 

       550        560 
RKGYAKVDGV EEDTLNLIYL HE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000816 Genomic DNA. Translation: ABU82287.1.
RefSeqYP_001435694.1. NC_009776.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING453591.Igni_1110.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU82287; ABU82287; Igni_1110.
GeneID5562106.
KEGGiho:Igni_1110.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAAFRIIDT.

Enzyme and pathway databases

BioCycIHOS453591:GHYN-1141-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_A. Glu_tRNA_synth_A.
InterProIPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR022888. Glu_tRNA_synth_arc.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. SSF50715. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYE_IGNH4
AccessionPrimary (citable) accession number: A8ABI5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 46 of the entry and version 1 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries