Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q98LB1 (SYV_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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
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:mll1104
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium

Protein attributes

Sequence length927 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 – 927927Valine--tRNA ligase HAMAP MF_02004
PRO_0000224544

Regions

Coiled coil856 – 91762 Potential
Motif45 – 5511"HIGH" region HAMAP MF_02004
Motif571 – 5755"KMSKS" region HAMAP MF_02004

Sites

Binding site5741ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q98LB1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 0EFAE339A503A00D

FASTA927104,995
        10         20         30         40         50         60 
MLEKTYDAKT VEPKIAKVWE EADAFRAGAG AEEGAEAFTI VIPPPNVTGS LHMGHALNNT 

        70         80         90        100        110        120 
LQDILVRFER MRGKNVLWQP GMDHAGIATQ MVVERQLMEK QIHRRDLTRE QFIEKVWEWK 

       130        140        150        160        170        180 
AESGGTIFNQ LKRLGASADW SRERFTMDEG LSKAVLEVFV TLYKEGLIYK DKRLVNWDPR 

       190        200        210        220        230        240 
LLTAISDLEV EQHEVNGNLW HFRYPLEGET FDPENPKTFI TVATTRPETM LGDTAVAVHP 

       250        260        270        280        290        300 
DDERYRHLVG KNVVLPIVGR KIPVVADEYS DPEKGSGAVK ITPAHDFNDF EVGKRHKLPA 

       310        320        330        340        350        360 
INILTVEAAI KLKDNEDFLA GLDATPERQA VWDELDGLDR FVARKKIVEL MEEGGFLEKV 

       370        380        390        400        410        420 
EPHRHAVPHG DRGGVPIEPF LTEQWYANAA ELAKPAIASV REGRTNFVPK NWEKTYFDWM 

       430        440        450        460        470        480 
ENIQPWCISR QLWWGHQIPA WYGPDGRVFV EKTEEEALSA AIEYYLALEG PWKAWVEDRL 

       490        500        510        520        530        540 
ENFQPGEILT RDEDVLDTWF SSALWPFSTL GWPDQTPELK TYYQTDVLVT GFDIIFFWVA 

       550        560        570        580        590        600 
RMMMMGLHFM DEEPFHTVYV HALVRDKNGA KMSKSKGNVI DPLDLIDEYG ADALRFTLTV 

       610        620        630        640        650        660 
MAAQGRDVKL DPARIAGYRN FGTKLWNATR FAEMNEVARN DDFWLNDAKL AVNRWILTEL 

       670        680        690        700        710        720 
TRAARQITDG ITSYRFNEAA GAAYRFVWNL FCDWYLELLK PVFMGTDEAA KAESRACVAF 

       730        740        750        760        770        780 
VLDEIYKLLH PMMPFMTEEL WAQTAGEGKE RESLLCHAAW PSPDFEDDEA AADINWLVDL 

       790        800        810        820        830        840 
VSGIRSVRSE MNVPPAAIAP LVVVGANGVT RERLVRQDSA IKRLARVGDI SLADAAPKGS 

       850        860        870        880        890        900 
AQIVLNEATI CLPLGSLIDL AAEAARLQKE LAKVTEEIAR LHKKLSNERF VASAPAEIVE 

       910        920 
AEREKLAEYR DAQDKLAVAL TRVRDAG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000012 Genomic DNA. Translation: BAB48552.1.
RefSeqNP_102766.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ98LB1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1225429.
GenomeReviewsGene locus mll1104 in contig BA000012_GR.
KEGGmlo:mll1104.
NMPDRfig|266835.1.peg.871.
PATRIC22475948. VBIMesLot2464_0890.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG577712.
OMATDQWYVS.
ProtClustDBPRK05729.

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_RHILO
AccessionPrimary (citable) accession number: Q98LB1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2001
Last modified: January 25, 2012
This is version 57 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents