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B1L5U2 (SYE_KORCO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:Kcr_1075
OrganismKorarchaeum cryptofilum (strain OPF8) [Reference proteome] [HAMAP]
Taxonomic identifier374847 [NCBI]
Taxonomic lineageArchaeaKorarchaeotaCandidatus Korarchaeum

Protein attributes

Sequence length569 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
Reference 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 – 569569Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367802

Regions

Motif99 – 10911"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
B1L5U2 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: AD8CCE18820588F2

FASTA56965,142
        10         20         30         40         50         60 
MEDVKELIVR LAAENALKYG KADTKAVIGK ILYMRPDLKQ NVRELIPLVE EAVRAVNEMP 

        70         80         90        100        110        120 
KEALEGIVGE VKKEKKEEVR KWPDLPKAER GKVVTRVAPE PNGYPTLGHA KGLLVPFIYA 

       130        140        150        160        170        180 
RLYDGKFLLR FEDTNPRVER LEYYEAIRNE FSRLLEACEE ELGLSPGRWD EEIIESYHLE 

       190        200        210        220        230        240 
EMYSLAKKLI EAGKAYVCTC PAAEVRKRRK LGISCDHRDQ PIEKNLELWE KMLNGGFREG 

       250        260        270        280        290        300 
EAHLRLKTDM SHPNVTMRDP GIFRVIEAEH PIHGDKYRVY PVYDFSVSVM DSLTGVTHAF 

       310        320        330        340        350        360 
RSKEFEPHVD VQRHIVRALG LREYEMIQFG RITVEGIPLS KRYIRPLVES GILEGWDDPR 

       370        380        390        400        410        420 
IPTLRGLFRR GINPRAIVRF FYELGPSKVD ATVNMEAIAS INRKILDPIA ERYMFVPNPI 

       430        440        450        460        470        480 
KAKIEGLTPP VIAQVEVHPD SKRKREIRLD ESEVFIASSD LEGLKPGDEL RLRGLVNVTI 

       490        500        510        520        530        540 
RSVNPDEVSL RVSEEQRVKG VKIIQWAPVR NGVPARLFVP ESPYSFRMLG GYGEPALRGI 

       550        560 
KEGEIVQFVR VGFARLDRRD PLTFILSHD 

« Hide

References

[1]"A korarchaeal genome reveals new insights into the evolution of the Archaea."
Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L., Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A., Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G., Richardson P., Keller M., Stetter K.O.
Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OPF8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000968 Genomic DNA. Translation: ACB07821.1.
RefSeqYP_001737504.1. NC_010482.1.

3D structure databases

ProteinModelPortalB1L5U2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374847.Kcr_1075.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB07821; ACB07821; Kcr_1075.
GeneID6094352.
KEGGkcr:Kcr_1075.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAMRFAPNP.

Enzyme and pathway databases

BioCycKCRY374847:GH12-1079-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_A. Glu_tRNA_synth_A.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004526. 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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_KORCO
AccessionPrimary (citable) accession number: B1L5U2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 42 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