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A5IMM2 (SYE2_THEP1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:Tpet_1432
OrganismThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995) [Complete proteome] [HAMAP]
Taxonomic identifier390874 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length469 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

Subunit structure

Monomer By similarity. 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

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367791

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5IMM2 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: F27D3AB4FE070BD8

FASTA46954,607
        10         20         30         40         50         60 
MVRVRFAPSP TGFLHVGGAR TALFNFLFAR KEKGKFILRI EDTDLERSER EYEEKLMESL 

        70         80         90        100        110        120 
RWLGLLWDEG PDVGGDHGPY RQSERVEIYR EHAERLVKEG KAYYVYAYPE EIEEMREKLL 

       130        140        150        160        170        180 
SEGKAPHYSQ EMFEKFDTPE RRREYEEKGL RPAVFFKMPR KDYVLNDVVK GEVVFKTGAI 

       190        200        210        220        230        240 
GDFVIMRSNG LPTYNFACVV DDMLMEITHV IRGDDHLSNT LRQLALYEAF EKAPPVFAHV 

       250        260        270        280        290        300 
STILGPDGKK LSKRHGATSV EAFRDMGYLP EALVNYLALL GWSHPEGKEL LTLEELISSF 

       310        320        330        340        350        360 
SLDRLSPNPA IFDPQKLKWM NGYYLRNMPI EKLAELAKPF FEKAGIKIID EEYFKKVLEI 

       370        380        390        400        410        420 
TKERVEVLSE FPEESRFFFE DPAPVEIPEE MKEVFSQLKE ELQNVRWTME EITPVFKKVL 

       430        440        450        460 
KQHGVKPKEF YMTLRRVLTG REEGPELVNI IPLLGKEIFL RRIERSLGG 

« Hide

References

[1]"Complete sequence of Thermotoga petrophila RKU-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RKU-1 / ATCC BAA-488 / DSM 13995.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000702 Genomic DNA. Translation: ABQ47445.1.
RefSeqYP_001245021.1. NC_009486.1.

3D structure databases

ProteinModelPortalA5IMM2.
SMRA5IMM2. Positions 1-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390874.Tpet_1432.

Proteomic databases

PRIDEA5IMM2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ47445; ABQ47445; Tpet_1432.
GeneID5170216.
KEGGtpt:Tpet_1432.
PATRIC23945711. VBIThePet65348_1452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAPEGMLNY.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycTPET390874:GHJI-1478-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_THEP1
AccessionPrimary (citable) accession number: A5IMM2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 26, 2007
Last modified: May 14, 2014
This is version 50 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