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Q3ZZG9 (SYV_DEHSC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:cbdbA384
OrganismDehalococcoides sp. (strain CBDB1) [Complete proteome] [HAMAP]
Taxonomic identifier255470 [NCBI]
Taxonomic lineageBacteria › Chloroflexi › Dehalococcoidetes › Dehalococcoides

Protein attributes

Sequence length880 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 MF_02004

Catalytic activity

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

Subunit structure

Monomer By similarity. HAMAP MF_02004

Subcellular location

Cytoplasm By similarity HAMAP 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 MF_02004

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

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

valine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 880880Valine--tRNA ligase HAMAP MF_02004
PRO_0000224472

Regions

Coiled coil815 – 85440 Potential
Motif51 – 6111"HIGH" region HAMAP MF_02004
Motif529 – 5335"KMSKS" region HAMAP MF_02004

Sites

Binding site5321ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ZZG9 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: E0A6F24298F69053

FASTA880100,189
        10         20         30         40         50         60 
MAQCSDLPEM AKAYEAAEVE KKWYQYWMEK SYFKPNPNSD KKPFVIIMPP PNVTGELHLG 

        70         80         90        100        110        120 
HALTATLEDI MIRWHRMQGE PTLWLPGVDH AGIAAQVVVE RELAKQGKTR QQLGRELFLE 

       130        140        150        160        170        180 
KMWEWVNPCR EKIRHQHMRL GASCDWDRET FTLDAGPVKA VREIFTNLYE KGLIYKGERI 

       190        200        210        220        230        240 
INWCPRCGTA VSDLEVDHKD LAGHIWHLRY PLEDGSGFVT VATTRPETMQ GDTAVAIHPD 

       250        260        270        280        290        300 
DTRYAGMVGK NVVLPIMNRR IPVIADEAVD MAFGTGAVKV TPAHDPNDFE MGLRHNLPMI 

       310        320        330        340        350        360 
TIQNRDTTMN ENAGPCSGMT AKACREYVVS EMKSLGLLLR IEDYIHSVGH CQRCSAVIEP 

       370        380        390        400        410        420 
MVSKQWFVKM EPLAKPALEA VNSGRIQILP ERFNKVYQNW MENIRDWCIS RQLWWGHRIP 

       430        440        450        460        470        480 
VWYCPCGEMI VAKVDPTVCP KCGGTELEQD PDVLDTWFSS GLWPHSTLGW PDQTEDLKRF 

       490        500        510        520        530        540 
YPGTVMETAY DIIFFWVARM IVMGMEDMNE VPFRTVYLHG LIRDDKGEKM SKTKGNVIDP 

       550        560        570        580        590        600 
LKVIDQYGTD ALRFAVTFGT SPGNDSKLGQ TKLEAARNFA NKLWNASRFV IMNLGEAKEL 

       610        620        630        640        650        660 
TPEAELPLED RWIISRMNRV TADVTRLMEE FQFGEAQRVL QDFIWGEFCD WYIELAKVRL 

       670        680        690        700        710        720 
RDEASVSPRP VLVRVLSSIL RLLHPYMPFI TEELWSYLRP YLPESLRETD IIVAPYPAAD 

       730        740        750        760        770        780 
KTCFDEQAES VMGSLVEIVR SLRNLRAEHN VEISRYIQAN IYAGDMASVL GNYLGAVETL 

       790        800        810        820        830        840 
SRARPVNILP GHYSGASTAT EVVLVLTGIE VVVPMSTMVD LEVEAKRVKA EISELEIQIE 

       850        860        870        880 
RLSTRLSDEQ FLAKAPQAVV DKERIKLEGY IEKVSRLKSA

« Hide

References

[1]"Genome sequence of the chlorinated compound-respiring bacterium Dehalococcoides species strain CBDB1."
Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.
Nat. Biotechnol. 23:1269-1273(2005) [PubMed: 16116419] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CBDB1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ965256 Genomic DNA. Translation: CAI82595.1.
RefSeqYP_307511.1. NC_007356.1.

3D structure databases

ProteinModelPortalQ3ZZG9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3ZZG9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3623827.
GenomeReviewsGene locus cbdbA384 in contig AJ965256_GR.
KEGGdeh:cbdb_A384.
NMPDRfig|255470.3.peg.768.
PATRIC21610947. VBIDehSp125902_0319.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0525.
HOGENOMHBG577712.
OMATDQWYVS.
PhylomeDBQ3ZZG9.
ProtClustDBPRK05729.

Enzyme and pathway databases

BioCycDSP255470:CBDBA384-MONOMER.

Family and domain databases

HAMAPMF_02004. Val_tRNA_synth_type1.
[Tree]
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_Ia_tRNA-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
IPR002303. Valyl-tRNA_synthetase.
[Graphical view]
Gene3DG3DSA:3.90.740.10. G3DSA:3.90.740.10. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01873.
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.
SUPFAMSSF46589. tRNA_binding_arm. 1 hit.
SSF47323. tRNAsyn_1a_bind. 1 hit.
SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMsTIGR00422. ValS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYV_DEHSC
AccessionPrimary (citable) accession number: Q3ZZG9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 27, 2005
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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