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O58052 (SYV_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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:PH0314
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length891 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_02005

Catalytic activity

ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP-Rule MF_02005

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02005.

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_02005

Sequence similarities

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

Sequence caution

The sequence BAA29387.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   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 – 891891Valine--tRNA ligase HAMAP-Rule MF_02005
PRO_0000106252

Regions

Motif43 – 5311"HIGH" region HAMAP-Rule MF_02005
Motif536 – 5405"KMSKS" region HAMAP-Rule MF_02005

Sites

Binding site5391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O58052 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 6E3924A940C217FC

FASTA891104,961
        10         20         30         40         50         60 
MLPKNYDPNE IEPKWQKYWL EEKIYKYRLD ENKPSYAIDT PPPFTSGTLH LGHVLSHTWI 

        70         80         90        100        110        120 
DIIARYKRMR GYNVLFPQGF DNHGLPTELK VEKEFGITKD QPEEFLKKCV EWTWQAIEAM 

       130        140        150        160        170        180 
RKQFIRIGYS ADWDLEYHTM DDWYKAAVQR SLLEFYKKGL IYREEHPVYW CPKCRTSLAK 

       190        200        210        220        230        240 
AEVGYVEEEG YLYYIKLPLA DGSGYIPIAT TRPELMPACV AVFVHPDDER YKHLVGKKVK 

       250        260        270        280        290        300 
LPIFEREVPI LADEDVDPNF GTGAVYNCTY GDEQDIVWQK RYNLPVIIVI NEDGTMNENA 

       310        320        330        340        350        360 
GPYAGLKIEE ARKKIAEDLE KMGLLYKKEK IKHRVLRHTE RSSCMAPIEL LPKKQWFIKV 

       370        380        390        400        410        420 
KDLIDEIIKV AKEINWYPED MFLRLKDWAE SMDWDWVISR QRVFGTPFPF WVCKNGHIIP 

       430        440        450        460        470        480 
AREEDLPVDP RFDKPPVDKC PVCGAEIEPV TDVLDCWVDS SITPLIITKW HEAIKGDEEA 

       490        500        510        520        530        540 
KKWFEHNFPT ALRPQGTDII RTWAFYTILR TYVLTGKKPW KDIVINGMVA GPDGRKMSKS 

       550        560        570        580        590        600 
YGNVVSPEEV IPKYGADALR LWTALAPPGE DHPFKWETVD YNYRFLQKVW NIYRFAERHI 

       610        620        630        640        650        660 
KDFDYEKYRD VELEPLDKWI LSRLHRIIKF ATEELERYRF NLITRELITF IWHEVADDYI 

       670        680        690        700        710        720 
EMIKYRLYGE DEESKLKAKV ALYELLYNVM LLLAPFVPHI TEEIYHAIFK EKIGEKSVHL 

       730        740        750        760        770        780 
LSWPEYREDR IDEEAEKIGE LARKIVSEMR KYKNSHGLPL NAKLKHVAIY ALDSYERLKL 

       790        800        810        820        830        840 
IERDIAGTMN IERLEIVKGE PHLEERIVEV KPNYKNIGPK YGKLVPRIVQ YLRENAESIV 

       850        860        870        880        890 
REIKEKGKAE FEVEGKKVEL TKEDITVRKE VFSEGEKVET SVVDDVVIVF F 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA29387.1. Different initiation.
PIRD71457.
RefSeqNP_142298.1. NC_000961.1.

3D structure databases

ProteinModelPortalO58052.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING70601.PH0314.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA29387; BAA29387; BAA29387.
GeneID1444193.
KEGGpho:PH0314.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0525.
HOGENOMHOG000020095.
KOK01873.
OMAWMDSSIS.
ProtClustDBPRK13208.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-295-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02005. Val_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
IPR022874. Valine-tRNA_ligase_type_2.
IPR002303. Valyl-tRNA_ligase.
[Graphical view]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00986. TRNASYNTHVAL.
SUPFAMSSF47323. 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_PYRHO
AccessionPrimary (citable) accession number: O58052
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: February 19, 2014
This is version 89 of the entry and version 2 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries