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A4XLI3 (SYE2_CALS8) 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:Csac_2186
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length482 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 – 482482Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367632

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif249 – 2535"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4XLI3 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 3A945617B3EB77D6

FASTA48255,894
        10         20         30         40         50         60 
MVRVRFAPSP TGQLHIGGAR TALFNYLFAK KHNGKFILRI EDTDLERSRE EWAKAIMKSL 

        70         80         90        100        110        120 
KWLGIEWDEG PDIGGEFGPY FQSQRKDIYM EYINKLLEEG KAYYCFCSQE EIEKEREIAK 

       130        140        150        160        170        180 
QNKVSYKYSK KCRNISLEEA KRRIKNGEKA AVRIKAPQDG VTVVHDIIRG DVEFSNDQLD 

       190        200        210        220        230        240 
DFIILKSDGN PTYNFVCVVD DYFMKISHVI RAEEHLSNTP KQLIIYQALN LTPPQFAHVP 

       250        260        270        280        290        300 
MILAPDRSKL SKRHGATSVE EFFENGYLKE AIVNYLLLLG WSPGEDRTII GLDEAIEKFE 

       310        320        330        340        350        360 
LEKVSKNAAI YDVNKLTWIN GHYLKEIHIE DLYERMKYFY SKKGIEIERF DKEYVKSALK 

       370        380        390        400        410        420 
LVREKVKTLV EVVDASTYFF DDSYEYDQKG VEKYLTPENL NIVKSLLDEL KNLEPFSAPE 

       430        440        450        460        470        480 
IESLVRKKAE SLNVKAANII HTIRVCISGR TVTPGLFEMM EVLGKKEVVK RIERTCEKFL 


IK 

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
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., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000679 Genomic DNA. Translation: ABP67768.1.
RefSeqYP_001180959.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XLI3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351627.Csac_2186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP67768; ABP67768; Csac_2186.
GeneID5086758.
KEGGcsc:Csac_2186.
PATRIC21254124. VBICalSac56748_2367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAFLYARHL.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCSAC351627:GJ17-2228-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_CALS8
AccessionPrimary (citable) accession number: A4XLI3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 29, 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