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P47576 (SYV_MYCGE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Valine--tRNA ligase
EC=6.1.1.9
Alternative name(s):
Valyl-tRNA synthetase
Short name=ValRS
Gene names
Name:valS
Ordered Locus Names:MG334
OrganismMycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195) [Complete proteome] [HAMAP]
Taxonomic identifier243273 [NCBI]
Taxonomic lineageBacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma ›

Protein attributes

Sequence length837 AA.
Sequence statusComplete.
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. HAMAP-Rule MF_02004

Catalytic activity

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

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02004

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02004.

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. HAMAP-Rule MF_02004

The C-terminal coiled-coil domain is crucial for aminoacylation activity By similarity. HAMAP-Rule MF_02004

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_processregulation of translational fidelity

Inferred from electronic annotation. Source: GOC

valyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

valine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 837837Valine--tRNA ligase HAMAP-Rule MF_02004
PRO_0000106230

Regions

Coiled coil767 – 83771 Potential
Motif46 – 5611"HIGH" region HAMAP-Rule MF_02004
Motif514 – 5185"KMSKS" region HAMAP-Rule MF_02004

Sites

Binding site5171ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P47576 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 7F2FD1FE95D3D8C5

FASTA83797,464
        10         20         30         40         50         60 
MKDKFSFQKN YDFNLVSDGL YEIWNNAGFF KPKDKNNSFT AILPPPNLTG TLHIGHAFEV 

        70         80         90        100        110        120 
SITDQIMRFK KMQGFSINWI PGFDHAGIAT QTKYEKIALK ENQKYFDADD DKKSEMIMNW 

       130        140        150        160        170        180 
ALNQSEIIKN QLKSLGVCLN WSETKFTLSE QANKIVNNCF KNLYENGFIY QAYTLVNWDT 

       190        200        210        220        230        240 
KLNTAISNIE VINKPVNQHL HYVVYKLAND SKQELIVATT RPETIFADVC LLVNPKDKRY 

       250        260        270        280        290        300 
TNFWNKLVVN PLTGKQIPVV TDSYVDIKFG TGILKCTPAH DFNDYEINTK YKFDFLSCID 

       310        320        330        340        350        360 
SNGILNQNAS KFQGLSVLQA RNKIVKWLEK NKLLVKSIPL TSNVGFSERS GTVVEPMLSK 

       370        380        390        400        410        420 
QWFVDLPKLK DHLYLKKYPD FIPKRFNKQV SNWLNKLKPW CISRQLIWGH KIPVWFENNT 

       430        440        450        460        470        480 
GEIVVGEKPS KNLQNYTRSK DVLDTWFSSS LWPLICLNWE QDDSFHETEL LVTGYDILFF 

       490        500        510        520        530        540 
WVLRMLFNSF FETKKLPFKT VLIHGLVRDE QNRKMSKSLN NGIDPVDLIR NYGADAVRLF 

       550        560        570        580        590        600 
LCSNHTPGDD LIFSEQKIKS AWNFLNKLWN VTKFVIQLEN DQEISYDLDK LSLSETWILA 

       610        620        630        640        650        660 
KLDKVIQKIT KLLDKFQLAL ANQILVKFVW DDFCNTFIEA IKKEPNQLKP QLFYTAKSVL 

       670        680        690        700        710        720 
SNIAILLSIT VPFLSERIYQ QFNNKSVMQA TWPLATKIKI PKLFDLVLAA INDLRNYRKQ 

       730        740        750        760        770        780 
YMLNSQQKLV VILSGKNAVD VKQYFNFSWI ELKIETNKKV SFKYQIVDDT TQRLKSLQKQ 

       790        800        810        820        830 
QAFFESEVKR SQAIVKNKSF LEKAPKEKVK SEFLKLEEYQ KKLTETNQLI AKLTKAH

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L43967 Genomic DNA. Translation: AAC71557.1.
U02249 Genomic DNA. Translation: AAD12537.1.
PIRI64236.
RefSeqNP_073002.1. NC_000908.2.

3D structure databases

ProteinModelPortalP47576.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243273.MG_334.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC71557; AAC71557; MG_334.
GeneID875510.
KEGGmge:MG_334.
PATRIC20010224. VBIMycGen98045_0389.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0525.
KOK01873.
OMAIHDWTIS.
OrthoDBEOG644ZM1.
ProtClustDBPRK05729.

Enzyme and pathway databases

BioCycMGEN243273:GH2R-382-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02004. Val_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR014729. Rossmann-like_a/b/a_fold.
IPR010978. tRNA-bd_arm.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR019499. Val-tRNA_synth_tRNA-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
IPR002303. Valyl-tRNA_ligase.
[Graphical view]
PANTHERPTHR11946:SF5. PTHR11946:SF5. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF10458. Val_tRNA-synt_C. 1 hit.
[Graphical view]
PRINTSPR00986. TRNASYNTHVAL.
SUPFAMSSF46589. SSF46589. 1 hit.
SSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00422. valS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYV_MYCGE
AccessionPrimary (citable) accession number: P47576
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Mycoplasma genitalium

Mycoplasma genitalium (strain G-37): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

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