Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q0AR08 (SYE1_MARMM)

Last modified November 3, 2009. Version 28. 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: Mmar10_0986
OrganismMaricaulis maris (strain MCS10) [Complete proteome] [HAMAP]
Taxonomic identifier394221 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeMaricaulis

Protein attributes

Sequence length445 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 – 445445Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367703

Regions

Motif8 – 1811"HIGH" region HAMAP MF_00022
Motif239 – 2435"KMSKS" region HAMAP MF_00022

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AR08-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 950A30EC7BEEBB0C

FASTA44548,719
        10         20         30         40         50         60 
MTKVRFAPSP TGKLHVGNVR TAIFNYLFAR KAGGTFVLRI DDTDVERSTK AYEDGIRADL 

        70         80         90        100        110        120 
TWLGISWDET FKQSDRFDRY EAAAETLKAK GLLYPCYETG EDLDRKRRLQ MANGRPPVYD 

       130        140        150        160        170        180 
RAALDLTDAE KAGFEAEGRK PHWRFKLSGN PVQWDDMVRG HVSIETSSLS DPILIREDGS 

       190        200        210        220        230        240 
FLYTLPSVLD DIESEITHII RGEDHTTNSG AQIEIFEALG GKAPIFGHQA LLVGADGGKL 

       250        260        270        280        290        300 
SKRTGSLGIA DLRDVDGLEP MAIMSLLARI GTSDPVEAFA DVEGILEGFD LGKLSRSPAR 

       310        320        330        340        350        360 
FDDEELKRVN AKLLHAMPYD VAQPKLAVLG ADKGEAVWEA VRPNLETLAD AKAWAVLIDG 

       370        380        390        400        410        420 
PVTPVIEEPD YAAAAAQHLP AGELDGDSWS VWTNALKEAT GRKGKQLFMP LRLMLTGEAR 

       430        440 
GPEMAVLLPL IGRDKVLKRL AGEAA 

« Hide

References

[1]"Complete sequence of Maricaulis maris MCS10."
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., Stephens C., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000449 Genomic DNA. Translation: ABI65279.1.
RefSeqYP_756217.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ0AR08.

Genome annotation databases

GeneID4285284.
GenomeReviewsGene locus Mmar10_0986 in contig CP000449_GR.
KEGGmmr:Mmar10_0986.
NMPDRfig|394221.5.peg.963.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0AR08.
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. 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.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_MARMM
AccessionPrimary (citable) accession number: Q0AR08
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 17, 2006
Last modified: November 3, 2009
This is version 28 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