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Q8ZU33 (SYE_PYRAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:PAE2969
OrganismPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827) [Reference proteome] [HAMAP]
Taxonomic identifier178306 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length570 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 – 570570Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119726

Regions

Motif107 – 11711"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q8ZU33 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 767FCEE299A3064C

FASTA57065,837
        10         20         30         40         50         60 
MNVEEIAFKY ALANAVKYGG KADVKAVMAK LMAEVPELRA RAREVKQIVD AVVARVNSMP 

        70         80         90        100        110        120 
LEEQRRILRE RWPELLEERR AEQRRPGLEG LPELPNVRGG VVVRFAPNPD FVLHLGSARP 

       130        140        150        160        170        180 
AILNYAYRIK YGGKFILRFE DTDPRIKSPL VTEEVNAYES IREDLRWLGV RWDEEYIQSQ 

       190        200        210        220        230        240 
RMEIYYEHAK KLLEMGAAYV DLCKPEEWRR LRNEKKACPH REQPPEVNLE LWDKMLEGRF 

       250        260        270        280        290        300 
KEGEAVLRIK TDLTHPDPSV RDWVAFRIID TSKTPHPLTG DKYIVWPTYN FAVSIDDHLM 

       310        320        330        340        350        360 
GVTHVLRAQE HSVNTIKQSY VFRHFGWEQP VTIHFGRLRI EGATLSKSKL KAMRIKYDDL 

       370        380        390        400        410        420 
TLPTLAGLRN RGIVPEAIWD LILSVGIKPS DSTVALANLF AFNRKHIEPI ADRYMYVADP 

       430        440        450        460        470        480 
VKLVFEADKE LTAHVPFHPS FKERGERTYR LGPGRVEVYI QRRDAVAGKV VRLMELANVE 

       490        500        510        520        530        540 
IVRVEGDVAY GRIHSYSLDE AKKIGAPIIQ WVWDPVEITV IKPAGVGRKE VEVGLGEGWL 

       550        560        570 
ERVEVGKYVQ FFRYGYLKKR GPREFVFLHD 

« Hide

References

[1]"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009441 Genomic DNA. Translation: AAL64575.1.
RefSeqNP_560393.1. NC_003364.1.

3D structure databases

ProteinModelPortalQ8ZU33.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING178306.PAE2969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL64575; AAL64575; PAE2969.
GeneID1463740.
KEGGpai:PAE2969.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAAFRIIDT.

Enzyme and pathway databases

BioCycPAER178306:GCEO-2147-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
2.40.240.10. 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.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
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_PYRAE
AccessionPrimary (citable) accession number: Q8ZU33
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 72 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