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Reviewed, UniProtKB/Swiss-Prot A1V3R3 (SYT_BURMS)

Last modified June 16, 2009. Version 18. 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:
    Threonyl-tRNA synthetase
    EC=6.1.1.3
Alternative name(s):
    Threonine--tRNA ligase
      Short name=ThrRS
Gene names
Name: thrS
Ordered Locus Names: BMASAVP1_A1539
OrganismBurkholderia mallei (strain SAVP1) [Complete proteome] [HAMAP]
Taxonomic identifier320388 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length635 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP MF_00184

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm. HAMAP MF_00184

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processthreonyl-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

threonine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 635635Threonyl-tRNA synthetase HAMAP MF_00184
PRO_1000020354

Regions

Region242 – 533292Catalytic HAMAP MF_00184

Sites

Metal binding3331Zinc; catalytic By similarity
Metal binding3841Zinc; catalytic By similarity
Metal binding5101Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A1V3R3-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 6AA2BEB8B94C0344

FASTA63572,265
        10         20         30         40         50         60 
MVSIRLPDGS VRQYEHPVTV AEVAASIGPG LAKAALGGKL DGELVDTSAL IDRDASLAIV 

        70         80         90        100        110        120 
TDKDADGLDI IRHSTAHLLA YAVKELHPDA QVTIGPVIDN GFYYDFSYHR PFTPEDLEAI 

       130        140        150        160        170        180 
EKRMQELAKR DEPVTRRVVS RDEAVSYFRS IGEKYKAEII ESIPASDEIK LYSHGSFTDL 

       190        200        210        220        230        240 
CRGPHVPSTG KLKVFKLMKV AGAYWRGDSK NEQLQRIYGT AWTRKEDQDA YLHMLEEAEK 

       250        260        270        280        290        300 
RDHRKLGKQL DLFHIQEEAP GMVFWHPKGW TLWQQVEQYM RRRLDAAGYL EIKTPMIMDR 

       310        320        330        340        350        360 
SLWEASGHWQ NYRENMFTTE SEKRDYAIKP MNCPGHVQVF KHGLRSYRDL PLRYAEFGSC 

       370        380        390        400        410        420 
HRNEASGALH GLMRVRGFVQ DDAHIFCTED QINSEAIAFN KLAMSVYEDF GFDRIDIKLS 

       430        440        450        460        470        480 
LRPEQRMGSD ETWDHAEEGL RNALKACGLE WEELPGEGAF YGPKIEYHIK DALGRSWQCG 

       490        500        510        520        530        540 
TLQLDMMLPE RLGAEYVAED NSRRRPVMLH RAIVGSMERF LGILIEHHAG AMPVWLAPAH 

       550        560        570        580        590        600 
AVVLNIAESQ AEYARTVAQS LQKQGLRVSA DLRNEKISYK IREHTLEKVP YLLVVGDKER 

       610        620        630 
EAQTVAVRAR GGVDLGVMPV EAFVERLRED IQAFK 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000526 Genomic DNA. Translation: ABM52129.1.
RefSeqYP_992866.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4681248.
GenomeReviewsGene locus BMASAVP1_A1539 in contig CP000526_GR.
KEGGbmv:BMASAVP1_A1539.
TIGRBMASAVP1_A1539.

Phylogenomic databases

OMAA1V3R3. QDEAPGM.

Family and domain databases

HAMAPMF_00184.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR012675. b-grasp_ferredoxin-like.
IPR004095. TGS.
IPR002320. Thr-tRNA-synth_IIa.
IPR018158. Thr-tRNA-synth_IIa_cons-reg.
IPR012947. tRNA_SAD.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
TIGRFAMsTIGR00418. thrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYT_BURMS
AccessionPrimary (citable) accession number: A1V3R3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: June 16, 2009
This is version 18 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