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Q1GEA9 (SYE2_SILST) 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:TM1040_2275
OrganismSilicibacter sp. (strain TM1040) [Complete proteome] [HAMAP]
Taxonomic identifier292414 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length441 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 – 441441Glutamate--tRNA ligase 2 HAMAP MF_00022_B
PRO_0000367770

Regions

Motif8 – 1811"HIGH" region HAMAP MF_00022_B
Motif239 – 2435"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GEA9 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 189E4DDD5B382C5D

FASTA44148,893
        10         20         30         40         50         60 
MTTTRFAPSP TGYIHVGNLR TALMNYLIAR KAGGTFILRI DDTDPERSKE EYVDAIKQDL 

        70         80         90        100        110        120 
EWLGITWDKV ERQSERLDRY AEAADKLREI GRFYEAFETP TELDLKRKKQ LNMGKPPVYD 

       130        140        150        160        170        180 
RAALALSDAE KESLRAERGN GVWRFKLDQE RIEWTDGILG DISIDAASVS DPVLIRGDGQ 

       190        200        210        220        230        240 
VLYTIASVVD DTDMGVTHVV RGSDHVTNTA TQIQIMAALG HGHPEFAHHS LLTGPQGEAL 

       250        260        270        280        290        300 
SKRLGTLALR DLREAGVKPM ALLSLMARLG SSDPVELRTD MAELVDGFDI NRFGSAPTKF 

       310        320        330        340        350        360 
DAEDLYPLTA RYLQTLPVAT VKSELDAIGV PADTQEAFWA VAKENITTLK DLEGWWILCR 

       370        380        390        400        410        420 
DGAEPLIADE DKEFIAEAMT LLPEGPYDSE SWGKWTAAVK EKTGRKGKGL FMPLRKAVTG 

       430        440 
MERGPDMSAL LALMQTVRAR G 

« Hide

References

[1]"Complete sequence of chromosome of Silicibacter sp. TM1040."
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., Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TM1040.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000377 Genomic DNA. Translation: ABF65007.1.
RefSeqYP_614269.1. NC_008044.1.

3D structure databases

ProteinModelPortalQ1GEA9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1GEA9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4078459.
GenomeReviewsGene locus TM1040_2275 in contig CP000377_GR.
KEGGsit:TM1040_2275.
NMPDRfig|292414.1.peg.637.
PATRIC23388804. VBIRueSp69653_3208.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADQERIEW.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycSSP292414:TM1040_2275-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_SILST
AccessionPrimary (citable) accession number: Q1GEA9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 27, 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