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Q28L59 (SYE2_JANSC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:Jann_3636
OrganismJannaschia sp. (strain CCS1) [Complete proteome] [HAMAP]
Taxonomic identifier290400 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeJannaschia

Protein attributes

Sequence length449 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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Glutamate--tRNA ligase 2 HAMAP MF_00022_B
PRO_0000367693

Regions

Motif17 – 2711"HIGH" region HAMAP MF_00022_B
Motif248 – 2525"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28L59 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 4BFCEB83BCAA718F

FASTA44949,517
        10         20         30         40         50         60 
MSAPMSASTS VVTRFAPSPT GFLHVGNLRT ALFNFLIAKK AGGEFILRLD DTDPERSTQA 

        70         80         90        100        110        120 
FADAIQEDME WLGLTWDRIE RQSDRFDRYA AAADELRAKN RFYEAWETPT ELDLKRKKQL 

       130        140        150        160        170        180 
NMHQPPVYDR AALALTDDQK EALRAERGQG VWRFKLDHQR IEWTDGILGD LSIDAASVSD 

       190        200        210        220        230        240 
PVLIRADGQV LYTIASVVDD TDMGVTHVVR GSDHVTNTAT QIQIMEALGK SAPSFAHHSL 

       250        260        270        280        290        300 
LTGPQGEALS KRLGTLALRD LREAGMEPMA LLSHMARIGS SQPVELAGSV EELAEGFDLN 

       310        320        330        340        350        360 
HFGSAPTKFD VEDLWPLTAS VLHGTAFEDV AGEIAALGVP ADIAPAFWEV ARANIGKRAE 

       370        380        390        400        410        420 
IADWWALFRD GATPLVADED REFVAQAFAM LPDLPYDETT WSNWTSAVKE ATGRKGKGLF 

       430        440 
MPLRKAVTGR ERGPEMADVM RLMQVKPTL 

« Hide

References

[1]"Complete sequence of chromosome of Jannaschia sp. CCS1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J., Larimer F. expand/collapse author list , Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000264 Genomic DNA. Translation: ABD56553.1.
RefSeqYP_511578.1. NC_007802.1.

3D structure databases

ProteinModelPortalQ28L59.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ28L59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3936114.
GenomeReviewsGene locus Jann_3636 in contig CP000264_GR.
KEGGjan:Jann_3636.
PATRIC22151178. VBIJanSp43325_3834.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADQERIEW.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycJSP290400:JANN_3636-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_JANSC
AccessionPrimary (citable) accession number: Q28L59
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 4, 2006
Last modified: January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families