Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B9E5W0 (SYT_CLOK1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:CKR_2834
OrganismClostridium kluyveri (strain NBRC 12016) [Complete proteome] [HAMAP]
Taxonomic identifier583346 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

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-Rule MF_00184

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00184

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00184

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

threonine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 637637Threonine--tRNA ligase HAMAP-Rule MF_00184
PRO_1000199538

Regions

Region242 – 532291Catalytic HAMAP-Rule MF_00184

Sites

Metal binding3331Zinc; catalytic By similarity
Metal binding3841Zinc; catalytic By similarity
Metal binding5091Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
B9E5W0 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 4BD227D00D952C0E

FASTA63773,463
        10         20         30         40         50         60 
MIKISLKNGK EIEVEKGLKV IDIAAKLSIS LSKKALGAVV DGKVVELNYK INKDCKVEIL 

        70         80         90        100        110        120 
TFEDEEGKKI LRHTASHILA QAIKRLYPEV KLAIGPAIDS GFYYDVDAEF SFTPELLEKI 

       130        140        150        160        170        180 
EGKMNEIIKE NIKLERFELP REEAIKFMEE KNEPYKVELI KDLPEDSIIS FYKQGDFVDL 

       190        200        210        220        230        240 
CAGPHVPSTG RAKAVKLLSI AGAYWRGNEN NKMLQRIYGT VFEKKSDLQD YLKLMEEAKK 

       250        260        270        280        290        300 
RDHRKLGKEL DLFSIHEEGP GFPFFHPKGM VIRNTLQNFW REMHYKADYS EIMTPIILNE 

       310        320        330        340        350        360 
ELWHRSGHWD HYKENMYFTK IDDGNYAIKP MNCPGSILVY KNDIRSYRDL PKRYAEMGVV 

       370        380        390        400        410        420 
HRHEKSGALH GLMRVRCFTQ DDAHIFVTKD DIADEIIKVI DLIDNFYKIF GFEYFVELST 

       430        440        450        460        470        480 
RPEDSMGSDE DWEAATEGLK NALKMVGLDY KINEGDGAFY GPKIDFHLKD CIGRTWQCGT 

       490        500        510        520        530        540 
VQLDFQMPEK FDLNYIGADG EKHRPVMIHR VVFGSIERFI GILIEHYAGA FPAWIAPVQV 

       550        560        570        580        590        600 
QVMNITDAQA DYVAEVAKTL KENNIRVECD IRNEKIGYKI REAQMHKVPY MIILGDKEMK 

       610        620        630 
DKNISVRSRK EGDIGAMSLE DFILKLKEEI DKKISHV 

« Hide

References

[1]"Complete genome sequence of Clostridium kluyveri and comparative genomics of Clostridia species."
Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A., Yukawa H.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 12016.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009049 Genomic DNA. Translation: BAH07885.1.
RefSeqYP_002473299.1. NC_011837.1.

3D structure databases

ProteinModelPortalB9E5W0.
SMRB9E5W0. Positions 241-633.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING583346.CKR_2834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH07885; BAH07885; CKR_2834.
GeneID7275302.
KEGGckr:CKR_2834.
PATRIC19475913. VBICloKlu118830_3199.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0441.
HOGENOMHOG000003879.
KOK01868.
OrthoDBEOG61KBFJ.
ProtClustDBPRK00413.

Enzyme and pathway databases

BioCycCKLU583346:GJNQ-2883-MONOMER.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPMF_00184. Thr_tRNA_synth.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
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. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsTIGR00418. thrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYT_CLOK1
AccessionPrimary (citable) accession number: B9E5W0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries