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Q1AS60 (SYE2_RUBXD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Rxyl_2856
OrganismRubrobacter xylanophilus (strain DSM 9941 / NBRC 16129) [Complete proteome] [HAMAP]
Taxonomic identifier266117 [NCBI]
Taxonomic lineageBacteriaActinobacteriaRubrobacteridaeRubrobacteralesRubrobacterineaeRubrobacteraceaeRubrobacter

Protein attributes

Sequence length496 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 – 496496Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367768

Regions

Motif13 – 2311"HIGH" region HAMAP-Rule MF_00022
Motif255 – 2595"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1AS60 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: C10F241670F45A88

FASTA49656,617
        10         20         30         40         50         60 
MEASRQVRVR YAPSPTGRLH VGGVRTALFN WLFARKHGGV FILRIEDTDL ERSTEESVEQ 

        70         80         90        100        110        120 
LKRSLRWIGL DWDEGPDVGG PHAPYRQTER LELYRRAARR LLESGAAYYD FATPEELTRF 

       130        140        150        160        170        180 
RQRARAEGRP PIYTGGPYRE MDPEEALRRV RMGEPHTVRF KTPREGRTVF EDIIRGPVGF 

       190        200        210        220        230        240 
ENATIEDFVL LKSTGTPTYN FAAAVDDAEM QITHVIRGDD HISNTPRQIM IHRALGHELP 

       250        260        270        280        290        300 
AFAHVPQVLG PDRKKLSKRH GAASVEDFAE QGILPEALFN YLALLGAGYA ADEEIFAPEE 

       310        320        330        340        350        360 
LAERFRLEKV SGNPAIFDEQ KLLAINAVYI RRKSPEELAM LAAPMLSERG VADAGELERD 

       370        380        390        400        410        420 
MPRLVRIMEL LRERLQRTTD IPEAAGYFYG ERLDYDREQF EKQFGKEFVR ENLPELYRRL 

       430        440        450        460        470        480 
KALPEWTADA IESCVRGLAA EKEKGARHLI HPLRFATTGR TVSAGLFETM ELIGRERCLL 

       490 
RIADVLERLQ SPERSL 

« Hide

References

[1]"Complete sequence of Rubrobacter xylanophilus DSM 9941."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9941 / NBRC 16129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000386 Genomic DNA. Translation: ABG05768.1.
RefSeqYP_645580.1. NC_008148.1.

3D structure databases

ProteinModelPortalQ1AS60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266117.Rxyl_2856.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG05768; ABG05768; Rxyl_2856.
GeneID4115833.
KEGGrxy:Rxyl_2856.
PATRIC23372512. VBIRubXyl52678_2828.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAEMQITH.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycRXYL266117:GH8O-2916-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...

Entry information

Entry nameSYE2_RUBXD
AccessionPrimary (citable) accession number: Q1AS60
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 11, 2006
Last modified: February 19, 2014
This is version 60 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