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Q488M6 (SYV_COLP3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:CPS_0738
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Colwelliaceae › Colwellia

Protein attributes

Sequence length973 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 – 973973Valine--tRNA ligase HAMAP MF_02004
PRO_0000224464

Regions

Coiled coil901 – 97070 Potential
Motif57 – 6711"HIGH" region HAMAP MF_02004
Motif569 – 5735"KMSKS" region HAMAP MF_02004

Sites

Binding site5721ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q488M6 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: F2650EE687C39838

FASTA973110,937
        10         20         30         40         50         60 
MLQQNNEQLL NLLPDKMMEK TFNPTDIEQS LYTSWEEQGY FSPTGEGDSY SIAIPPPNVT 

        70         80         90        100        110        120 
GSLHMGHAFQ QTIMDTLIRY QRMQGKNTLW QTGCDHAGIA TQMVVERKIA AEEDKTRHDY 

       130        140        150        160        170        180 
GREGFIDKIW EWKEESGGTI GKQMRRLGNS IDWSRERFTM DDGMSEAVQE VFVRLFEDDL 

       190        200        210        220        230        240 
IYRGKRLVNW DPKFHTAISD LEVENKDKKG HMWHLRYPLA NGAKTAEGLD YLVVATTRPE 

       250        260        270        280        290        300 
TMLGDTGVAV NPEDPRYKDL IGKQVLLPLV NRLIPIVGDD HADMEKGTGC VKITPGHDFN 

       310        320        330        340        350        360 
DNEVGKRHAL PQINILDKDA AILATAEVYD TKGEVCNAYD TGLPSEFAGM DRFVARKAIV 

       370        380        390        400        410        420 
AKFDELGLLV EVKDHDLVAP YGDRSGVIIE PLLTDQWYVR VEKLAGPAVD AVKDGQIEFV 

       430        440        450        460        470        480 
PKQYENMYFS WMNNIQDWCI SRQLWWGHRI PAWYDENEKV YVGRTEEEVR ANNDIAADMK 

       490        500        510        520        530        540 
LRQDDDVLDT WFSSALWTFS TLGWPKDTED LKTFHPTDVL VTGFDIIFFW VARMIMMTMH 

       550        560        570        580        590        600 
FNKDENGKAQ IPFKKIYMTG LIRDENGDKM SKSKGNVVDP LDMIDGISLE DLLQKRTGNM 

       610        620        630        640        650        660 
MQPKLAKKIE KLTRKEYPEG IEAHGTDALR FTLTSVATTG RDISWDMKRL EGYRNFTNKL 

       670        680        690        700        710        720 
WNASRYVMMN TEEFDCGQSS PEGKAGDMEL SLADRWIIGQ FEQTVKTVHE AFDTYRFDLA 

       730        740        750        760        770        780 
SQALYEFTWN QFCDWYLELT KPVLFKENEA QQRGTRHTLV NVLEALLRLM HPIMPFITET 

       790        800        810        820        830        840 
IWQRVQPLSD FSKNGDSIMV QAFPQFDESK CDQQAIDDLE WVKQFIIAIR NIRGEMDISP 

       850        860        870        880        890        900 
SKELPVLLKN VNDNDQRRLD ENEQFLSSLA KLESITVLAD DEQGPASASA VVGDLSVLIP 

       910        920        930        940        950        960 
MAGLIDKEAE LARLDKAIEK LEKEAGRVRG KLGNENFVSK APAAVIEKEQ AKLADAESTL 

       970 
AKILEQKIQI AAL

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References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed: 16043709] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000083 Genomic DNA. Translation: AAZ27693.1.
RefSeqYP_267488.1. NC_003910.7.

3D structure databases

ProteinModelPortalQ488M6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ488M6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3521952.
GenomeReviewsGene locus CPS_0738 in contig CP000083_GR.
KEGGcps:CPS_0738.
NMPDRfig|167879.3.peg.512.
PATRIC21464789. VBIColPsy94388_0652.
TIGRCPS_0738.

Phylogenomic databases

eggNOGCOG0525.
HOGENOMHBG577712.
OMATDQWYVS.

Enzyme and pathway databases

BioCycCPSY167879:CPS_0738-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.
IPR011321. Val-tRNA_synth_Ia_C.
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. 3 hits.
G3DSA:1.10.287.380. Val-tRNA_synth_Ia_C. 1 hit.
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_COLP3
AccessionPrimary (citable) accession number: Q488M6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 46 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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