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Reviewed, UniProtKB/Swiss-Prot Q0VSA8 (SYV_ALCBS)

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

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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: ABO_0492
OrganismAlcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]
Taxonomic identifier393595 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

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Protein attributes

Sequence length931 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 931931Valyl-tRNA synthetase HAMAP MF_02004
PRO_1000022162

Regions

Coiled coil859 – 93173 Potential
Motif42 – 5211"HIGH" region HAMAP MF_02004
Motif523 – 5275"KMSKS" region HAMAP MF_02004

Sites

Binding site5261ATP By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q0VSA8-1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: D41D1B42071748B5

FASTA931105,906
        10         20         30         40         50         60 
MIMDKTYQPD RIEQSWYENW EQAGHFKPSG QGDPFCIMIP PPNVTGSLHM GHAFQDTIMD 

        70         80         90        100        110        120 
TLVRYRRMQG RNTLWQVGTD HAGIATQMVV ERKLAGEGTN RHELGREKFL DKVWEWKRES 

       130        140        150        160        170        180 
GGTITRQLRR MGASVDWTRE RFTMDDGLSN AVREVFVRLH KEGLIYRGKR LVNWDPALHT 

       190        200        210        220        230        240 
AISDLEVENV EEQGHMWHFR YPLSDGSGHL VVATTRPETM LGDTAVAVHP QDPRYKDMIG 

       250        260        270        280        290        300 
KSIRLPLADR NIPIIADDYV DPDFGSGCVK ITPAHDFNDY EVGKRHDLPM INILTIDAAL 

       310        320        330        340        350        360 
NDEVPEGYRG LDRVEARKKV VDDLDALGLL EKVDDHTLQV PRGDRSGVVI EPYLTDQWFV 

       370        380        390        400        410        420 
AVEELAKPAI AAVENGDIQF VPKNYENMYF SWMRDLQDWC ISRQLWWGHR IPAWYDADGN 

       430        440        450        460        470        480 
VYVGRDEEEV RAENNLGDTP LSQDDDVLDT WFSSALWTFS TLGWPDDTDA LRTFHPTDVL 

       490        500        510        520        530        540 
VTGFDIIFFW VARMIMMTLK FTDQVPFKKV YVHGLVRDND GQKMSKSKGN VLDPLDMIDG 

       550        560        570        580        590        600 
ITLDALIDKR TKGLMQPQKE KQITKRTNKD FPDGINPYGT DALRFTFLSL ASTGRDIKWD 

       610        620        630        640        650        660 
MGRIEGYRNF CNKIWNAARY VMMNTEGEDC GIDTDSEVEL SLADRWIISA LQRAELEVSE 

       670        680        690        700        710        720 
ALDSFRFDVA SHAAYEFIWN EYCDWYLELS KPVLWGDEYS DAQKRGTRRT LVTVLEAILR 

       730        740        750        760        770        780 
MAHPFMPFIT EEIWQKVGPL AGKASAAGKG EKTDTIMLQP FPASEPAKID TNAETGAEWV 

       790        800        810        820        830        840 
KAVISAVRNI RGEMGIPLGK ALPIYLHNGK DSDKALLDAN RVFLCKLAKL ESITWLTAED 

       850        860        870        880        890        900 
SAPASATALV GDMEILVPMA GLIDKEAEIE RLSKEIEKLR KEVGRAEGKL KNPKFVDKAP 

       910        920        930 
QAVVDKEKAK LDDYRSQLAK LEEQLEKIKY L

« Hide

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Cross-references

Sequence databases

AM286690 Genomic DNA. Translation: CAL15940.1.
RefSeqYP_692212.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4211958.
GenomeReviewsGene locus ABO_0492 in contig AM286690_GR.
KEGGabo:ABO_0492.
NMPDRfig|393595.12.peg.489.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0VSA8.
OMAQ0VSA8. TDQWYVS.

Enzyme and pathway databases

BioCycABOR393595:ABO_0492-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.
IPR011321. Val-tRNA_synth_Ia_C.
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.
G3DSA:1.10.287.380. Val-tRNA_synth_Ia_C. 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...

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Entry information

Entry nameSYV_ALCBS
AccessionPrimary (citable) accession number: Q0VSA8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
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)

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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