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A4YIL8 (SYE_METS5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:Msed_2131
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera

Protein attributes

Sequence length566 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 – 566566Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000071001

Regions

Motif104 – 11411"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
A4YIL8 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 9121E10FC443A779

FASTA56665,210
        10         20         30         40         50         60 
MTMELEEIVY KYALWNAVKH NGQAQVGPVV SKVFAERPEL KANAKEVVKL AEKMVAKVNA 

        70         80         90        100        110        120 
MSLEQQTAEL QKYPELLEER KKEEKKTLSP LPNVKGTVVT RFAPNPDGPL HLGNARAAVL 

       130        140        150        160        170        180 
SFEYAKMYKG KFILRFDDTD PKVKKPIKEA YDWIRDDLRW LNITWDLEFK ASERMSAYYN 

       190        200        210        220        230        240 
VAKVMLEKGF AYVDTLSDAE FKAWRDSRNK TVYKPRTNPP EVNLELWEKM LNGDFDEGKA 

       250        260        270        280        290        300 
VVRIKTNPED PDPSKIDWVM LRIIDTKRNP HPIAGDKFRV WPTYNFATAV DDHEFGITHI 

       310        320        330        340        350        360 
LRAKEHTTNT EKQRWVYDYM GWEMPTVLEF GRLKLEGFMM SKSKIRGMLE TGSERDDPRL 

       370        380        390        400        410        420 
PTLAGLRRRG IIPDTVREII IQVGLKVTDA TISFDNIASV NRKLLDPVAK RLMFVREGVL 

       430        440        450        460        470        480 
FKLEIPQEMK AKVPLIPARQ EFREIFVKPG DEIYLDKGDV EEGKVVRLMD LCNVKIEGDR 

       490        500        510        520        530        540 
LRFLSQDLES AKRMGANIIQ WVKKSESKSV NVIKADPNKD VEEIRGYGEG YFETLKPGDI 

       550        560 
VQLVRYGFAR VDSISRGEIT MIFAHE 

« Hide

References

[1]"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000682 Genomic DNA. Translation: ABP96270.1.
RefSeqYP_001192194.1. NC_009440.1.

3D structure databases

ProteinModelPortalA4YIL8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399549.Msed_2131.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP96270; ABP96270; Msed_2131.
GeneID5104424.
KEGGmse:Msed_2131.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAMRFAPNP.
ProtClustDBPRK04156.

Enzyme and pathway databases

BioCycMSED399549:GH1O-2165-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_METS5
AccessionPrimary (citable) accession number: A4YIL8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 47 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