Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q47BG6 (SYV_DECAR)

Last modified June 16, 2009. Version 26. 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:
    Valyl-tRNA synthetase
    EC=6.1.1.9
Alternative name(s):
    Valine--tRNA ligase
      Short name=ValRS
Gene names
Name: valS
Ordered Locus Names: Daro_3085
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length943 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner By similarity.

Catalytic activity

ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP MF_02004

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site By similarity.

The C-terminal coiled-coil domain is crucial for aminoacylation activity By similarity.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processvalyl-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

valine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 943943Valyl-tRNA synthetase HAMAP MF_02004
PRO_0000224470

Regions

Coiled coil875 – 93460 Potential
Motif45 – 5511"HIGH" region HAMAP MF_02004
Motif541 – 5455"KMSKS" region HAMAP MF_02004

Sites

Binding site5441ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47BG6-1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 9CB7A2DAC73D3442

FASTA943106,500
        10         20         30         40         50         60 
MELAKAFEPA DIERRWYPEW ETQNYFAAGV DASKADNFCI LLPPPNVTGT LHMGHGFNQT 

        70         80         90        100        110        120 
IMDALTRYYR MRGHNTLWQP GTDHAGIATQ IVVERQLDAQ GISRHDLGRE KFLEKVWEWK 

       130        140        150        160        170        180 
EYSGNTITKQ MRRMGTSPDW KRERFTMDAG LNKVVTETFV RLFNEGLIYR GKRLVNWDPK 

       190        200        210        220        230        240 
LNTAVSDLEV VQEEEDGFMW HIRYPLADGS DSLVVATTRP ETMLGDTAVM VHPEDERYKH 

       250        260        270        280        290        300 
MIGQMVKLPL TDREIPIIAD SYVDLEFGTG CVKVTPAHDF NDYAVGQRHG LPMISILTLD 

       310        320        330        340        350        360 
AKVNENAPEK YRGLDRFDAR KAVVADLEAL GILEKTDKHK LKVPRGDRTN VVIEPMLTDQ 

       370        380        390        400        410        420 
WFVAMSKPGD DGKSITEKAL DVVHSGEIKF YPENWVNTYN QWLNNIQDWC ISRQLWWGHQ 

       430        440        450        460        470        480 
IPAWYGDNGQ IFVAHSEAEA KAEAAKQGYT GTLKRDEDVL DTWFSSALWP FSTLDWTGDE 

       490        500        510        520        530        540 
AIDAANPLLK QYLPSSVLVT GFDIIFFWVA RMVMMTKQIT GQIPFKHVYV HGLIRDGEGQ 

       550        560        570        580        590        600 
KMSKSKGNVL DPIDLIDGIG LEALIEKRTT GLMNPKQAES IAKKTKKEFP EGIASFGTDA 

       610        620        630        640        650        660 
LRFTFASLAS PGRDIKFDLN RCDGYRNFCN KLWNATRFVL MNVEGHDLAL EHQQNGPACG 

       670        680        690        700        710        720 
GSAPLEFSFA DRWIVSQLQR VEQEVEQHFT DYRFDLIAQA IYKFIWDEFC DWYLEIAKVE 

       730        740        750        760        770        780 
IQTGNDAQQR GARRTLVRTL EAVLRLAHPL IPFITEELWQ TVAPIAGRKT HDSIMLAAYP 

       790        800        810        820        830        840 
RAEEYKIDAA SEAKVERLKA LAYACRNLRG EMNVSPALRM PLLVAGGGAE ISEFAAILQA 

       850        860        870        880        890        900 
LGKLSEVQIV DDMPADAMAP VAVVGETRLM LKVEIDVAAE RIRLAKEIEK LEKQISIAQG 

       910        920        930        940 
KLANEGFVAR APAAVIDQEK QRVADFTATL EQLKPQLAKL GQA 

« Hide

References

[1]"Complete sequence of Dechloromonas aromatica RCB."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000089 Genomic DNA. Translation: AAZ47815.1.
RefSeqYP_286285.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3566514.
GenomeReviewsGene locus Daro_3085 in contig CP000089_GR.
KEGGdar:Daro_3085.
NMPDRfig|159087.4.peg.3070.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ47BG6.
OMAQ47BG6. WPDETPE.

Enzyme and pathway databases

BioCycDARO159087:DARO_3085-MON.

Family and domain databases

HAMAPMF_02004.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR014729. Rossmann-like_a/b/a_fold.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR002303. Val-tRNA_synth_Ia.
IPR019754. Val-tRNA_synth_Ia_N.
IPR019499. Val-tRNA_synth_Ia_tRNA-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF5. tRNA-synt_val. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF10458. Val_tRNA-synt_C. 1 hit.
[Graphical view]
PRINTSPR00986. TRNASYNTHVAL.
TIGRFAMsTIGR00422. valS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYV_DECAR
AccessionPrimary (citable) accession number: Q47BG6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 13, 2005
Last modified: June 16, 2009
This is version 26 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