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Reviewed, UniProtKB/Swiss-Prot Q5P9M8 (SYV_ANAMM)

Last modified June 16, 2009. Version 33. 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: AM1170
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length823 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_02005

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.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   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 – 823823Valyl-tRNA synthetase HAMAP MF_02005
PRO_0000224606

Regions

Motif52 – 6211"HIGH" region HAMAP MF_02005
Motif549 – 5535"KMSKS" region HAMAP MF_02005

Sites

Binding site5521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P9M8-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: C8F916707C698F84

FASTA82394,004
        10         20         30         40         50         60 
MNVRVRHFMQ SLDSRYQHKT VEEECNAAWD EHKIYKWKGN VAQSFVIDTP PPTVSGVLHM 

        70         80         90        100        110        120 
GHVFSYCHTD FIARYQRMAG KDVFYPIGFD DNGLPTERLV EKIKKLRAVQ LERAEFTKMC 

       130        140        150        160        170        180 
REVSHEFRTK FRNLFRRLGI SYDWALEYHT VSEEVQRLSQ ASFLDLYAKD KLYRKQQPIL 

       190        200        210        220        230        240 
WDTVDCTAIA HAEVEELDLH SHLNTISFHT VGGEKIDIAT TRPELIPACV ALFFNPEDDR 

       250        260        270        280        290        300 
YTHLHGQFAV VPVGGHKVKI LPDDKVRIDK GTGLVMCCTF GDETDVYWWR THNLDTKTIV 

       310        320        330        340        350        360 
SRTGHIVDLA EDTPDAKIPA AQFDGMHVQK ARKAVCDALE GAGLLVSQEP IVHTVKCAER 

       370        380        390        400        410        420 
SGAPIEILLS HQWFVRVMEH KHELLEQVQK VQWHPDSMRK RMEIWIENLN WDWCISRQRY 

       430        440        450        460        470        480 
FGVPFPVWYS KREGEVGKVL LPDVRDLPVD PLRDLPSGYG RDEVEPDVDV MDTWATSSIS 

       490        500        510        520        530        540 
PQFLTKSVGQ VLRNENLEPL FPTDLRAQSH EIIRSWAFYT MLKSYYHNGE IPWQNIMISG 

       550        560        570        580        590        600 
WCLAEDKTKM SKSKGNAMDP ESTLDLYGAD SVRYWAAKSR LGADTVFSEE VLKTGRRLTT 

       610        620        630        640        650        660 
KLWNASKFVA TFFLRDNPPA GTTAAPTDLW ILSKLHKAVA HNTENLKLFE YCAALNRTEE 

       670        680        690        700        710        720 
FFWKDFCDNY LELVKHRAYN HGSAHGHASA VSTLHHTLKT LLLLFAPFLP YVTEAVYGTL 

       730        740        750        760        770        780 
FSGCIHAQEW PNADEIPYNA SLEQHGDALI KIVEEVRKAK THAQVSVKYP VELITIGGLA 

       790        800        810        820 
TDFPESMLED LKHMCCAEQI KLTAPDSTEL EVAVTLAPTV SSN 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000030 Genomic DNA. Translation: AAV87002.1.
RefSeqYP_154257.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3171649.
GenomeReviewsGene locus AM1170 in contig CP000030_GR.
KEGGama:AM1170.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5P9M8.
OMAQ5P9M8. SGWILDP.

Enzyme and pathway databases

BioCycAMAR234826:AM1170-MON.

Family and domain databases

HAMAPMF_02005.
[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.
[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.
[Graphical view]
PRINTSPR00986. TRNASYNTHVAL.
TIGRFAMsTIGR00422. valS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYV_ANAMM
AccessionPrimary (citable) accession number: Q5P9M8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: January 4, 2005
Last modified: June 16, 2009
This is version 33 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