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O67583 (SYT_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. 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:aq_1667
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length638 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
Reference 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 – 638638Threonine--tRNA ligase HAMAP MF_00184
PRO_0000100933

Regions

Region243 – 536294Catalytic HAMAP MF_00184

Sites

Metal binding3361Zinc; catalytic By similarity
Metal binding3871Zinc; catalytic By similarity
Metal binding5131Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
O67583 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 5ECBA8227C047955

FASTA63874,097
        10         20         30         40         50         60 
MEKIKVKIKG KEYEVEKGTP LGKIFELAGI KDALGGVING KIIDLQTPVR ESGEIKPVYR 

        70         80         90        100        110        120 
GSKESLEIMR HSLAHIMAQA LKELYGAKKV HLGVGPTTEE GFYYDVEVEG HKITEEDLPK 

       130        140        150        160        170        180 
IEQKMKEIIE RDYPILRREL SREEAIKLFD KLKEKYKIDI IKEIPEEEVI SVYEQGDFID 

       190        200        210        220        230        240 
LCKGPHLPST GKAGAFKLTS ISGAYWKGRS DQPQLTRIYG IAYWSDKEVK ERLKFYEEVK 

       250        260        270        280        290        300 
KRDHRRLGKE LEFFTIDDNV GAGLILWLPR GAIYRKVLED YLREEHLKRG YQLVYTPHVG 

       310        320        330        340        350        360 
KSKLWETSGH LECYKQNMFP SMKIDEEEYY VKPMNCPFHI AIYKSRTRSY KELPLKLFEL 

       370        380        390        400        410        420 
GTVYRYELSG VLHGLLRVRG FTQDDAHIVC TPEQVNDVIR ETLDFALSTL KDFGFNEFKI 

       430        440        450        460        470        480 
YLSTRPEYSI GSDEQWEVSQ NALKKAIEDL GYEYEIDEGG GAFYGPKIDV KIRDAIGRMW 

       490        500        510        520        530        540 
QLSTIQFDFN LPERFDMTYV GPDNKKHRPY MIHRALLGSI ERFTGILLEH YAGLLPIWLS 

       550        560        570        580        590        600 
PTQVMIIPIA DRHHEYAKKV YEFLKENGIR AEMDLREERM NAKIRDAELK KIPVILVVGD 

       610        620        630 
REAQNNTVSV RTKKEGNLGS MELNKFLDWI KEKIKNKE 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07549.1.
PIRF70444.
RefSeqNP_214149.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67583.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193299.
GenomeReviewsGene locus aq_1667 in contig AE000657_GR.
KEGGaae:aq_1667.
NMPDRfig|224324.1.peg.1164.
PATRIC20960356. VBIAquAeo85532_1290.

Phylogenomic databases

HOGENOMHBG352811.
OMARTAMEDY.
PhylomeDBO67583.
ProtClustDBPRK00413.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1667-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.
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.
KOK01868.
PfamPF03129. HGTP_anticodon. 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.
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_AQUAE
AccessionPrimary (citable) accession number: O67583
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 83 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