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Q64VP2 (SYT_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:BF1687
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length646 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 – 646646Threonine--tRNA ligase HAMAP MF_00184
PRO_0000100936

Regions

Region242 – 541300Catalytic HAMAP MF_00184

Sites

Metal binding3371Zinc; catalytic By similarity
Metal binding3881Zinc; catalytic By similarity
Metal binding5181Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64VP2 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 22C3B3A70B4B73EC

FASTA64674,406
        10         20         30         40         50         60 
MIKITFPDGS VREYNEGVNG LQIAESISSR LAQDVLACGV NGEIYDLGRP INEDASVVLY 

        70         80         90        100        110        120 
KWEDEQGKHA FWHTSAHLLA EALQELYPGI QFGIGPAIEN GFYYDVDPGE AVIKEADLPA 

       130        140        150        160        170        180 
IEAKMAELVA KKEAVVRRDI AKGDALKMFG DRGETYKCEL ISELEDGHIT TYTQGDFTDL 

       190        200        210        220        230        240 
CRGPHLMTTA PIKAIKLTSV AGAYWRGHED RKMLTRIYGI TFPKKKMLDE YLALMEEAKK 

       250        260        270        280        290        300 
RDHRKIGKEM QLFMFSDTVG KGLPMWLPKG TALRLRLQDF LRRIQTRYDY QEVITPPIGN 

       310        320        330        340        350        360 
KLLYVTSGHY AKYGKDAFQP IHTPEEGEEY FLKPMNCPHH CEIYKNFPRS YKDLPLRIAE 

       370        380        390        400        410        420 
FGTVCRYEQS GELHGLTRVR SFTQDDAHIF CRPDQVKGEF LRVMDIISIV FRSMDFDNFE 

       430        440        450        460        470        480 
AQISLRDKVN REKYIGSDEN WEKAEQAIIE ACEEKGLKAK IEYGEAAFYG PKLDFMVKDA 

       490        500        510        520        530        540 
IGRRWQLGTI QVDYNLPERF ELEYMGSDNQ KHRPVMIHRA PFGSMERFVA VLIEHTAGKF 

       550        560        570        580        590        600 
PLWLTPEQVV ILPISEKFNE YAEKVKTYLK MKEIRAIVDD RNEKIGRKIR DNEMKRIPYM 

       610        620        630        640 
LIVGEKEAEN GEVSVRRQGE GDKGTMKFEE FGEILNEEVQ NMINKW 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD48434.1.
RefSeqYP_098968.1. NC_006347.1.

3D structure databases

ProteinModelPortalQ64VP2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3081309.
GenomeReviewsGene locus BF1687 in contig AP006841_GR.
KEGGbfr:BF1687.
PATRIC21049043. VBIBacFra17906_1639.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG352811.
OMAGRKWQLG.
PhylomeDBQ64VP2.
ProtClustDBPRK00413.

Enzyme and pathway databases

BioCycBFRA295405:BF1687-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_BACFR
AccessionPrimary (citable) accession number: Q64VP2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 52 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