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A8LIP0 (SYE2_DINSH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Dshi_2748
OrganismDinoroseobacter shibae (strain DFL 12) [Complete proteome] [HAMAP]
Taxonomic identifier398580 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Dinoroseobacter

Protein attributes

Sequence length440 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 – 440440Glutamate--tRNA ligase 2 HAMAP MF_00022_B
PRO_0000367666

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
A8LIP0 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 1711E9B9F83B7C2C

FASTA44048,289
        10         20         30         40         50         60 
MTTTRFAPSP TGYLHVGNLR TALFNYMIAR KAGGTFILRI DDTDPERSKP EYVDAIQEDL 

        70         80         90        100        110        120 
TWLGLTWDRI EYQSRRLDRY AEAADALRAA GRFYEAFETP TELDLKRKKQ LNMGRPPVYD 

       130        140        150        160        170        180 
RAALALSEDE KAALRAERGQ GVWRFKLDHE RITWTDGILG DISIDAASVS DPVLIRGDGQ 

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

       250        260        270        280        290        300 
SKRLGTLALR DLRAEGIEPM ALLSLMARLG SSQPVEVAGS LEALIEGFDL STFGAAPTKF 

       310        320        330        340        350        360 
DRADLFPLTA RLLHATPFAE VADEIAALGV PAAQAELFWE VARANITTRA DLAGWWQLFR 

       370        380        390        400        410        420 
DGGAPLVAEE DRAFVADAFA RLPEPPYGPE TWGAWTAEVK AASGRKGKGL FMPLRKAVTG 

       430        440 
LERGPEMADV MRLLQKKPTL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000830 Genomic DNA. Translation: ABV94481.1.
RefSeqYP_001534082.1. NC_009952.1.

3D structure databases

ProteinModelPortalA8LIP0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8LIP0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5713647.
GenomeReviewsGene locus Dshi_2748 in contig CP000830_GR.
KEGGdsh:Dshi_2748.
PATRIC21818261. VBIDinShi9476_2862.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAARTALIC.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycDSHI398580:DSHI_2748-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_DINSH
AccessionPrimary (citable) accession number: A8LIP0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 4, 2007
Last modified: January 25, 2012
This is version 29 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

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