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Reviewed, UniProtKB/Swiss-Prot Q8KA47 (SYE_BUCAP)

Last modified December 15, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase
      Short name=GluRS
Gene names
Name: gltX
Ordered Locus Names: BUsg_065
OrganismBuchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]
Taxonomic identifier98794 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm HAMAP 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Glutamyl-tRNA synthetase HAMAP MF_00022
PRO_0000119527

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022
Motif238 – 2425"KMSKS" region HAMAP MF_00022

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8KA47-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 07D3789761DEDFA2

FASTA47455,412
        10         20         30         40         50         60 
MKVKTRFAPS PTGNLHIGSI RTALYSWLFA RHYHGKFILR IEDTDFERFD SKSVESILYG 

        70         80         90        100        110        120 
LKWLGLNWDE GPYFQSKRLE RYKEVIKMML ESGNAYKCFC SVKELEDERI RQVSKGKKPR 

       130        140        150        160        170        180 
YSGICRNLHY RNYIANENYV VRFKNPISGQ VTFEDKIRGK ITFQNEELDD LVIQRSNGIP 

       190        200        210        220        230        240 
TYNFCVVIDD LDMNITHVIR GEDHINNTPR QINILKSLNA KIPIYAHVSM IFNEDGHKFS 

       250        260        270        280        290        300 
KRQDALNILE YCKDGFLPEA LLNYVIRLGW SCGNQEIFSI SEMKELFDLR KISKSSSAVS 

       310        320        330        340        350        360 
MKKLFWLNKY YINNLPLSYI SNLLKDHMNH EKINLKNGPD LESVLTLLKN RHHTLKEIAQ 

       370        380        390        400        410        420 
SSRYFYEEFA NFDKSAADEY LIPENHFILK NLYKNIKKIS IWSNETLSSL IKNDCIKLKI 

       430        440        450        460        470 
TLRKISMLLR VVLTGNIFSP SISSVIFLIG KEKTLLRLKK AILFIDNKIK NINN 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE013218 Genomic DNA. Translation: AAM67635.1.
RefSeqNP_660424.2.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1005881.
GenomeReviewsGene locus BUsg_065 in contig AE013218_GR.
KEGGbas:BUsg065.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.

Enzyme and pathway databases

BioCycBAPH198804:BUSG065-MON.

Family and domain databases

HAMAPMF_00022.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
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. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_BUCAP
AccessionPrimary (citable) accession number: Q8KA47
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: December 15, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents