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Reviewed, UniProtKB/Swiss-Prot A9IRH6 (SYT_BORPD)

Last modified November 3, 2009. Version 17. 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: Bpet2834
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length650 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 By similarity.

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 – 650650Threonyl-tRNA synthetase HAMAP MF_00184
PRO_1000098545

Regions

Region247 – 538292Catalytic HAMAP MF_00184

Sites

Metal binding3381Zinc; catalytic By similarity
Metal binding3891Zinc; catalytic By similarity
Metal binding5151Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A9IRH6-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 0ACABD26091B19A7

FASTA65073,361
        10         20         30         40         50         60 
MVQITLPDGS QRQFPGPVTV AEVAQSIGTG LAKAALGGRV TEPGGEPRLV DTSYRLEHDA 

        70         80         90        100        110        120 
QLAIVTAKDA DGLDMIRHST AHLLAYAVKE LFPDAQVTIG PVIDNGFYYD FSYKRPFTPE 

       130        140        150        160        170        180 
DLAAIEKKMT ELARKDETVT REEWTRDDAV AYFKSIGEDY KAEIIASIPA NETLSLYREG 

       190        200        210        220        230        240 
NFVDLCRGPH VPSTGKLKVF KLMKVAGAYW RGDSNNEMLQ RIYGTAWATK DDQDAYLHML 

       250        260        270        280        290        300 
EEAERRDHRK IGRDLDLFHF QDEAPGLIFW HPKGWALWQQ VEQYMRAVYN DNGYQEVKAP 

       310        320        330        340        350        360 
QILDLSLWKK TGHWDNYREN MFTTESENRV YGLKPMNCPG HVQIFNAGLH SYRELPLRYG 

       370        380        390        400        410        420 
EFGQCHRNEP SGSLHGMMRV RGFTQDDGHI FCTEDQLQDE CADFTALLQK VYRDFGFHEV 

       430        440        450        460        470        480 
LYKVATRPEK RIGSDDIWDK AETALMESLR RTGCEFEISP GEGAFYGPKI EYTLKDAIGR 

       490        500        510        520        530        540 
HWQCGTVQVD FSMPVRLGAE YVDAQDQRRA PVMLHRAILG SLERFIGMLI ENHAGAMPPW 

       550        560        570        580        590        600 
LAPVQAVVCC ISEPSADYAA QITQTLKKQG FRVQSDLRGE KITRKIREHS LQKVPYILVV 

       610        620        630        640        650 
GDKEKQNGTV AVRGLGGLDL GVIALEDFAA RLAEDVAARR DVVQPESSAN 

« Hide

References

[1]"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae."
Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. expand/collapse author list , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.
BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM902716 Genomic DNA. Translation: CAP43176.1.
RefSeqYP_001631444.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5817395.
GenomeReviewsGene locus Bpet2834 in contig AM902716_GR.
KEGGbpt:Bpet2834.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMANTKIAIG.

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_BORPD
AccessionPrimary (citable) accession number: A9IRH6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: November 3, 2009
This is version 17 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