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Q58530 (KAE1B_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:MJ1130
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length535 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 By similarity. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In vitro, exhibits low ATPase activity, but does not bind DNA and does not have endonuclease activity. Ref.3

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

Enzyme regulation

Activity provided by the Kae1 region seems to be regulated via phosphorylation by the protein kinase Bud32, which is itself activated by Cgi121. Ref.3

Subunit structure

Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes. Ref.3

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 – 535535Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein HAMAP-Rule MF_01447
PRO_0000096979

Regions

Domain333 – 535203Protein kinase
Nucleotide binding339 – 3479ATP By similarity
Region1 – 323323Kae1 HAMAP-Rule MF_01447
Region127 – 1315Threonylcarbamoyl-AMP binding Probable

Sites

Active site4511Proton acceptor; for kinase activity By similarity
Metal binding1061Iron Probable
Metal binding1101Iron Probable
Metal binding1271Iron Probable
Metal binding2841Iron Probable
Binding site1591Threonylcarbamoyl-AMP Probable
Binding site1721Threonylcarbamoyl-AMP; via amide nitrogen By similarity
Binding site1761Threonylcarbamoyl-AMP Probable
Binding site2561Threonylcarbamoyl-AMP Probable
Binding site3601ATP By similarity

Secondary structure

........................................................................ 535
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q58530 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: B18EEFACE8E5A99F

FASTA53560,570
        10         20         30         40         50         60 
MICLGLEGTA EKTGVGIVTS DGEVLFNKTI MYKPPKQGIN PREAADHHAE TFPKLIKEAF 

        70         80         90        100        110        120 
EVVDKNEIDL IAFSQGPGLG PSLRVTATVA RTLSLTLKKP IIGVNHCIAH IEIGKLTTEA 

       130        140        150        160        170        180 
EDPLTLYVSG GNTQVIAYVS KKYRVFGETL DIAVGNCLDQ FARYVNLPHP GGPYIEELAR 

       190        200        210        220        230        240 
KGKKLVDLPY TVKGMDIAFS GLLTAAMRAY DAGERLEDIC YSLQEYAFSM LTEITERALA 

       250        260        270        280        290        300 
HTNKGEVMLV GGVAANNRLR EMLKAMCEGQ NVDFYVPPKE FCGDNGAMIA WLGLLMHKNG 

       310        320        330        340        350        360 
RWMSLDETKI IPNYRTDMVE VNWIKEIKGK KRKIPEHLIG KGAEADIKRD SYLDFDVIIK 

       370        380        390        400        410        420 
ERVKKGYRDE RLDENIRKSR TAREARYLAL VKDFGIPAPY IFDVDLDNKR IMMSYINGKL 

       430        440        450        460        470        480 
AKDVIEDNLD IAYKIGEIVG KLHKNDVIHN DLTTSNFIFD KDLYIIDFGL GKISNLDEDK 

       490        500        510        520        530 
AVDLIVFKKA VLSTHHEKFD EIWERFLEGY KSVYDRWEII LELMKDVERR ARYVE 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii."
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. expand/collapse author list , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]"Structure of the archaeal Kae1/Bud32 fusion protein MJ1130: a model for the eukaryotic EKC/KEOPS subcomplex."
Hecker A., Lopreiato R., Graille M., Collinet B., Forterre P., Libri D., van Tilbeurgh H.
EMBO J. 27:2340-2351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH AN ATP ANALOG.
[3]"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 (2.67 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM AND CGI121, FUNCTION, SUBUNIT, ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB99132.1.
RefSeqNP_248122.1. NC_000909.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VWBX-ray3.05A/B1-535[»]
3EN9X-ray2.67A/B1-535[»]
3ENHX-ray3.60A/B1-535[»]
ProteinModelPortalQ58530.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ1130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB99132; AAB99132; MJ_1130.
GeneID1452026.
KEGGmja:MJ_1130.

Phylogenomic databases

eggNOGCOG0533.
KOK15904.
OMARDNAGMI.
PhylomeDBQ58530.

Family and domain databases

HAMAPMF_01446. Kae1_arch.
MF_01447. Kae1_Bud32_arch.
InterProIPR022495. Bud32.
IPR000905. Gcp-like_dom.
IPR022449. Kae1.
IPR017861. KAE1/YgjD.
IPR011009. Kinase-like_dom.
IPR017860. Peptidase_M22_CS.
IPR000719. Prot_kinase_dom.
IPR009220. tRNA_threonyl_synthase/kinase.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PfamPF00814. Peptidase_M22. 1 hit.
PF00069. Pkinase. 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.
PROSITEPS01016. GLYCOPROTEASE. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ58530.

Entry information

Entry nameKAE1B_METJA
AccessionPrimary (citable) accession number: Q58530
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 113 of the entry and version 2 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names