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Q9HLA5 (KAE1B_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 93. 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:
Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein

Including the following 2 domains:

  1. tRNA N6-adenosine threonylcarbamoyltransferase
    EC=2.6.99.4
    Alternative name(s):
    N6-L-threonylcarbamoyladenine synthase
    Short name=t(6)A synthase
    t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1
    tRNA threonylcarbamoyladenosine biosynthesis protein Kae1
  2. Serine/threonine-protein kinase Bud32
    EC=2.7.11.1
Gene names
Ordered Locus Names:Ta0324
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function By similarity. HAMAP-Rule MF_01447

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. HAMAP-Rule MF_01447

L-threonylcarbamoyladenylate + adenine37 in tRNA = AMP + N(6)-L-threonylcarbamoyladenine37 in tRNA. HAMAP-Rule MF_01447

Cofactor

Binds 1 Fe2+ ion per subunit By similarity. HAMAP-Rule MF_01447

Subunit structure

Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01447.

Sequence similarities

In the N-terminal section; belongs to the KAE1 / TsaD family.

In the C-terminal section; belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 529529Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein HAMAP-Rule MF_01447
PRO_0000303661

Regions

Domain329 – 529201Protein kinase
Nucleotide binding335 – 3428ATP By similarity
Region1 – 324324Kae1 HAMAP-Rule MF_01447
Region128 – 1325Threonylcarbamoyl-AMP binding By similarity

Sites

Active site4471Proton acceptor; for kinase activity By similarity
Metal binding1071Iron By similarity
Metal binding1111Iron By similarity
Metal binding1281Iron By similarity
Metal binding2851Iron By similarity
Binding site1601Threonylcarbamoyl-AMP By similarity
Binding site1731Threonylcarbamoyl-AMP; via amide nitrogen By similarity
Binding site1771Threonylcarbamoyl-AMP By similarity
Binding site2571Threonylcarbamoyl-AMP By similarity
Binding site3551ATP By similarity

Secondary structure

.................................................... 529
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HLA5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9C878F334EE056D3

FASTA52958,202
        10         20         30         40         50         60 
MIVLGLEGTA HTISCGIIDE SRILAMESSM YRPKTGGIRP LDAAVHHSEV IDTVISRALE 

        70         80         90        100        110        120 
KAKISIHDID LIGFSMGPGL APSLRVTATA ARTISVLTGK PIIGVNHPLG HIEIGRRVTG 

       130        140        150        160        170        180 
AIDPVMLYVS GGNTQVIAHV NGRYRVLGET LDIGIGNMID KFAREAGIPF PGGPEIEKLA 

       190        200        210        220        230        240 
MKGTKLLDLP YSVKGMDTAF SGILTAALQY LKTGQAIEDI SYSIQETAFA MLVEVLERAL 

       250        260        270        280        290        300 
YVSGKDEILM AGGVALNRRL RDMVTNMARE AGIRSYLTDR EYCMDNGIMI AQAALLMYKS 

       310        320        330        340        350        360 
GVRMSVEETA VNPRFRIDEV DAPWITDASR KDYGKAGAES RIEEVSFHGR PAIRKVRISK 

       370        380        390        400        410        420 
SYRNSDLDKK IRYERMRNEF TILRKLKEAG VNSPVVYDFD PFSMSITMQK IPGRMMSAEL 

       430        440        450        460        470        480 
NEGRTDFLNE LGIMIAKMHR AGIAHGDLTV NNIIVNDSVF IIDPSMGKVN AEIEDMAVDI 

       490        500        510        520 
YALEDSIKGL GLDSGSVIGQ MLKSYRNNFN LADDVLETVS AIRRRHRYV 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
[2]"Atomic structure of the KEOPS complex: an ancient protein kinase-containing molecular machine."
Mao D.Y., Neculai D., Downey M., Orlicky S., Haffani Y.Z., Ceccarelli D.F., Ho J.S., Szilard R.K., Zhang W., Ho C.S., Wan L., Fares C., Rumpel S., Kurinov I., Arrowsmith C.H., Durocher D., Sicheri F.
Mol. Cell 32:259-275(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 1-329.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445064 Genomic DNA. Translation: CAC11469.1.
RefSeqNP_393804.1. NC_002578.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ENOX-ray3.02A/B1-329[»]
ProteinModelPortalQ9HLA5.
SMRQ9HLA5. Positions 1-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta0324.

Proteomic databases

PRIDEQ9HLA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC11469; CAC11469; CAC11469.
GeneID1455944.
KEGGtac:Ta0324.

Phylogenomic databases

eggNOGCOG0533.
HOGENOMHOG000109569.
KOK15904.
OMARDNAGMI.

Family and domain databases

HAMAPMF_01447. Kae1_Bud32_arch.
InterProIPR022495. Bud32.
IPR000905. Gcp-like_dom.
IPR022449. Kae1.
IPR017861. KAE1/YgjD.
IPR011009. Kinase-like_dom.
IPR018934. RIO-like_kinase.
IPR009220. tRNA_threonyl_synthase/kinase.
[Graphical view]
PfamPF00814. Peptidase_M22. 1 hit.
PF01163. RIO1. 1 hit.
[Graphical view]
PIRSFPIRSF036401. Gcp_STYKS. 1 hit.
PRINTSPR00789. OSIALOPTASE.
SUPFAMSSF56112. SSF56112. 1 hit.
TIGRFAMsTIGR03724. arch_bud32. 1 hit.
TIGR03722. arch_KAE1. 1 hit.
TIGR00329. gcp_kae1. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9HLA5.

Entry information

Entry nameKAE1B_THEAC
AccessionPrimary (citable) accession number: Q9HLA5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 93 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references