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Reviewed, UniProtKB/Swiss-Prot A7HS42 (SYE1_PARL1)

Last modified November 3, 2009. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 1
      Short name=GluRS 1
Gene names
Name: gltX1
Ordered Locus Names: Plav_1104
OrganismParvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966) [Complete proteome] [HAMAP]
Taxonomic identifier402881 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeParvibaculum

Protein attributes

Sequence length449 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 By similarity.

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 – 449449Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367730

Regions

Motif11 – 2111"HIGH" region HAMAP MF_00022
Motif242 – 2465"KMSKS" region HAMAP MF_00022

Sites

Binding site2451ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7HS42-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 214F6D8EBB9C309F

FASTA44949,180
        10         20         30         40         50         60 
MSGAPVVRFA PSPTGSLHVG NARAALFNFL FARKNSGKFM LRMDDTDDER STVEFAAGIE 

        70         80         90        100        110        120 
EDLTWLGLRH DLFARQSDRL AAYEAAAAKL KADGRLYPAY ETAAELDRKR KRQMARGLPP 

       130        140        150        160        170        180 
VYDRAALALT DEDRAKLEAE GRKPHWRFRL DRVHTAFDDL VQGAVEVDGA SLSDPVLIRE 

       190        200        210        220        230        240 
DGRFLYTLPS VVDDIDFAVT HVIRGSDHIT NTGVQIQIIR ALGAEPPVYA HYSLLNGPEG 

       250        260        270        280        290        300 
KPLSKRDDAA RFSLRALRDA GFEPMALNSL LARLGTPDAV EPCLSLDELA ARFDISRLGR 

       310        320        330        340        350        360 
ADIRFDPADL AKVNTACLHL MSYEEAKPRL AALGCDLGEA FWEAIKPNLI LFSDAADWAR 

       370        380        390        400        410        420 
VVEGPVEPVI ENPDFAAAAA AALPPEPWDE STWALWTDAV KQATGAKGKA LFMPLRLALT 

       430        440 
GLTHGPELKN LLPLIGRERA SARLGGLTR 

« Hide

References

[1]"Complete genome sequence and annotation of Parvibaculum lavamentivorans DS-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000774 Genomic DNA. Translation: ABS62725.1.
RefSeqYP_001412382.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7HS42.

Genome annotation databases

GeneID5455819.
GenomeReviewsGene locus Plav_1104 in contig CP000774_GR.
KEGGpla:Plav_1104.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMALRLDDTD.

Family and domain databases

HAMAPMF_00022.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR001412. aa-tRNA-synth_I_CS.
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. 2 hits.
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.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_PARL1
AccessionPrimary (citable) accession number: A7HS42
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 11, 2007
Last modified: November 3, 2009
This is version 16 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

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