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

Q9X2I8 (SYE2_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:TM_1875
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete 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

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000119681

Regions

Motif31 – 4111"HIGH" region HAMAP-Rule MF_00022
Motif254 – 2585"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2571ATP By similarity

Secondary structure

.................................................................................... 487
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X2I8 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 5E15A2E9E1580791

FASTA48757,382
        10         20         30         40         50         60 
MFITGAFFDI LEVGPKKIRR CFELVRVRFA PSPTGHLHVG GARTALFNWM FARKEGGKFI 

        70         80         90        100        110        120 
LRIEDTDTER SSREYEQQIL ESLRWCGLDW DEGPDIGGDF GPYRQSERLE IYREYAEKLV 

       130        140        150        160        170        180 
EDKRAYYVVY DKEDPSKELF TTYEYPHEYK EKGHPVTIKF KVLPGKTSFE DLLKGYMEFD 

       190        200        210        220        230        240 
NSTLEDFIIM KSNGFPTYNF AVVVDDHLMR ISHVFRGEDH LSNTPKQLMI YEAFGWEAPV 

       250        260        270        280        290        300 
FMHIPLILGS DRTPLSKRHG ATSVEHFRRE GILSRALMNY LALLGWRVEG DEIFTIEEKL 

       310        320        330        340        350        360 
QSFDPKDISN KGVIFDYQKL EWVNGKHMRR IDLEDLKREF IEWAKYAGKE IPSVDERYFS 

       370        380        390        400        410        420 
ETLRICREKV NTLSQLYDIM YPFMNDDYEY EKDYVEKFLK REEAERVLEE AKKAFKDLNS 

       430        440        450        460        470        480 
WNMEEIEKTL RDLSEKGLAS KKVVFQLIRG AVTGKLVTPG LFETIEVLGK ERTLKRLERT 


LQFLKKT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36937.1.
PIRF72200.
RefSeqNP_229671.1. NC_000853.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AFHX-ray2.00A2-487[»]
3AKZX-ray2.90A/B/C/D1-487[»]
3AL0X-ray3.37C1-487[»]
ProteinModelPortalQ9X2I8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59231N.
STRING243274.TM1875.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36937; AAD36937; TM_1875.
GeneID897796.
KEGGtma:TM1875.
PATRIC23938739. VBITheMar51294_1896.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAEIFDMEY.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycTMAR243274:GC6P-1926-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
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...

Other

EvolutionaryTraceQ9X2I8.

Entry information

Entry nameSYE2_THEMA
AccessionPrimary (citable) accession number: Q9X2I8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 97 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries