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Reviewed, UniProtKB/Swiss-Prot Q4JWU8 (SYV_CORJK)

Last modified June 16, 2009. Version 30. 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: jk0550
OrganismCorynebacterium jeikeium (strain K411) [Complete proteome] [HAMAP]
Taxonomic identifier306537 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length932 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 – 932932Valyl-tRNA synthetase HAMAP MF_02004
PRO_0000224468

Regions

Coiled coil863 – 92967 Potential
Motif75 – 8511"HIGH" region HAMAP MF_02004
Motif568 – 5725"KMSKS" region HAMAP MF_02004

Sites

Binding site5711ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4JWU8-1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: E67C2E72F2147002

FASTA932104,813
        10         20         30         40         50         60 
MPCLARLLDL ADVSDSSSKA NGSNPIGADR SAQLPAAWDP AAVEENLYQG WVDSGYFKAD 

        70         80         90        100        110        120 
PSSDKPPFSI VLPPPNVTGQ LHMGHALDHT LMDAMARRKR MQGFEVLWLP GSDHAGIATQ 

       130        140        150        160        170        180 
TKVEANLKET EGKDRFDYGR DAFVGKVWEW KDRYGGVIQR QMRAIGDSVD WSRERFTLDD 

       190        200        210        220        230        240 
GLSRAVQTMF KELFDAGLIY RANRMVNWSP VLQTAISDIE VVYSDDEGEL VSIRYGSLED 

       250        260        270        280        290        300 
SEPHVVVATT RVETMLGDVA VAVHPEDERY TDLVGKSLPH PFLPDRQMIV VADDYVDPEF 

       310        320        330        340        350        360 
GTGAVKITPA HDPNDFAMGQ RHDLPMPVIM DETGHIANTG TEFDGMERYE AREKIRLALE 

       370        380        390        400        410        420 
EQGRIVARKF PYVHSVGHSE RSKEAVEPRL SEQWFVKVEE LAKMSGDAIR SGDSVIHPSS 

       430        440        450        460        470        480 
QEPRWFDWVD DMHDWCISRQ LWWGHRIPIW YGPNGEIVCC GPDDEAPTGE GWYQDEDVLD 

       490        500        510        520        530        540 
TWFSSALWPF STMGWPEKTP ELEKFYPTSV LVTGYDILFF WVARMMMFAT FASKHTPEIL 

       550        560        570        580        590        600 
GTGKDGRPQI PFNDIFLHGL VRDEHGRKMS KSLGNGIDPM DWVRDYGADA LRFTLARGAN 

       610        620        630        640        650        660 
PGSDLPVGED AAQSSRNFAT KLYNATKFAL MNGARVGELP ARETLTDADR WILDRLEEVR 

       670        680        690        700        710        720 
QLVDDALDRY EFSLANENLY RFAWGEFCDW YLEIAKVQIP RDWDSATEEQ VQRGIRTQIV 

       730        740        750        760        770        780 
LGRVLDSVLR LLHPAMPFVT ETLWKALTDG EEGYSESLVT ADWPTADLTN GGAQTDADAV 

       790        800        810        820        830        840 
RRMADVDKLV TELRRFRSDQ GVKPSQKVPA KLDFAAADLA NFEEAVRSLV RLETPEEDFA 

       850        860        870        880        890        900 
ETASIEVRLS QATIAVQLDT SGTVDVAAER KRLEKDLAAA QKELDNAAKK LGNENFLAKA 

       910        920        930 
PEKVVEGIRE RQRVAQEEFE RITARLEGLP KA 

« Hide

References

[1]"Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora."
Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., Puehler A.
J. Bacteriol. 187:4671-4682(2005) [PubMed: 15968079] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR931997 Genomic DNA. Translation: CAI36709.1.
RefSeqYP_250327.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3433539.
GenomeReviewsGene locus jk0550 in contig CR931997_GR.
KEGGcjk:jk0550.
NMPDRfig|306537.3.peg.546.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ4JWU8.
OMAQ4JWU8. TDQWYVS.

Enzyme and pathway databases

BioCycCJEI306537:JK0550-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_CORJK
AccessionPrimary (citable) accession number: Q4JWU8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: August 2, 2005
Last modified: June 16, 2009
This is version 30 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