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Q3SK34 (SYT_THIDA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. 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:
Threonine--tRNA ligase

EC=6.1.1.3
Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS
Gene names
Name:thrS
Ordered Locus Names:Tbd_1007
OrganismThiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP]
Taxonomic identifier292415 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
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. HAMAP MF_00184

Subunit structure

Homodimer By similarity. HAMAP MF_00184

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

threonine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 637637Threonine--tRNA ligase HAMAP MF_00184
PRO_1000020547

Regions

Region244 – 535292Catalytic HAMAP MF_00184

Sites

Metal binding3351Zinc; catalytic By similarity
Metal binding3861Zinc; catalytic By similarity
Metal binding5121Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SK34 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 38B90F70D31E6CB3

FASTA63772,180
        10         20         30         40         50         60 
MVTVTLPDGS VRPFEGPVTV AEVASSIGAG LAKAALAGKV DGKLVDTSYV IDADAQLAIV 

        70         80         90        100        110        120 
TAKDAEALDL IRHDAAHVMA QAVQELYPGT QVTIGPAIED GFYYDFAREQ PFTPEDLEKI 

       130        140        150        160        170        180 
EKRMDEIVKR DLPIRREVWS RDEAMKVFGD LGETYKVQII DEVIPKGEEL SIYRQGEWFD 

       190        200        210        220        230        240 
VCRGPHLPST GKLPRAFKLM KLAGAYWRGD SKNAMLQRIY GTAWAKKEDL EAYLHRLEEA 

       250        260        270        280        290        300 
EKRDHRRLAK QLDLLHMQDE APGMVFWHPK GWIVWQQIEQ YMREKFVEYG YQEVRTPAVM 

       310        320        330        340        350        360 
DRSMWEKSGH WENYRDNMFT TASENRDYAV KPMNCPGHVQ IFNSGLHSYR DLPLRLAEFG 

       370        380        390        400        410        420 
SCHRNEPSGA LHGIMRVRGF TQDDAHIFCM EEQVEQEVAD FIVMLQKVYA DFGFNDVLVK 

       430        440        450        460        470        480 
LSTRPDKRVG SDESWDKAES ALAAALEKNG LSFDLQPGEG AFYGPKIEFT LKDTLGRLWQ 

       490        500        510        520        530        540 
CGTIQLDFNL PVRLGAEFVA EDNTRKIPVM LHRAILGSME RFIGILIEHH AGNFPLWLAP 

       550        560        570        580        590        600 
VQVMVMNISE RQAAYAEAVA EALRRAGIRA ALDLSNNKIN YKIREHSLQK LPYQLVVGDK 

       610        620        630 
EMEARVVAVR ARGNQDMGQL GLDDLIARLR AEVLARQ 

« Hide

References

[1]"The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
J. Bacteriol. 188:1473-1488(2006) [PubMed: 16452431] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25259.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000116 Genomic DNA. Translation: AAZ96960.1.
RefSeqYP_314765.1. NC_007404.1.

3D structure databases

ProteinModelPortalQ3SK34.
SMRQ3SK34. Positions 243-636.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3SK34.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3671231.
GenomeReviewsGene locus Tbd_1007 in contig CP000116_GR.
KEGGtbd:Tbd_1007.
NMPDRfig|292415.3.peg.737.
PATRIC23968163. VBIThiDen82923_0992.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0441.
HOGENOMHBG352811.
OMAVGSDALW.
PhylomeDBQ3SK34.

Enzyme and pathway databases

BioCycTDEN292415:TBD_1007-MONOMER.

Family and domain databases

HAMAPMF_00184. Thr_tRNA_synth.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_ferredoxin-type.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-synth_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KOK01868.
PfamPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF81271. TGS-like. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR00418. ThrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYT_THIDA
AccessionPrimary (citable) accession number: Q3SK34
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 11, 2005
Last modified: January 25, 2012
This is version 56 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