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P36174 (KAE1B_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:rrnAC2490
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 – 548548Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein HAMAP-Rule MF_01447
PRO_0000096977

Regions

Domain349 – 548200Protein kinase
Nucleotide binding355 – 3628ATP By similarity
Region1 – 338338Kae1 HAMAP-Rule MF_01447
Region143 – 1475Threonylcarbamoyl-AMP binding By similarity

Sites

Active site4601Proton acceptor; for kinase activity By similarity
Metal binding1221Iron By similarity
Metal binding1261Iron By similarity
Metal binding2991Iron By similarity
Binding site1751Threonylcarbamoyl-AMP By similarity
Binding site1881Threonylcarbamoyl-AMP; via amide nitrogen By similarity
Binding site1921Threonylcarbamoyl-AMP By similarity
Binding site2711Threonylcarbamoyl-AMP By similarity
Binding site3711ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P36174 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: A708A918A7FEB672

FASTA54859,796
        10         20         30         40         50         60 
MRILGIEGTA WAASASVFET PDPARVTDDD HVFIETDAYA PDSGGIHPRE AAEHMGEAIP 

        70         80         90        100        110        120 
TVVETAIEHT HGRAGRDGDD SAPIDAVAFA RGPGLGPCLR IVATAARAVA QRFDVPLVGV 

       130        140        150        160        170        180 
NHMVAHLEVG RHRSGFDSPV CLNASGANAH ILGYRNGRYR VLGETMDTGV GNAIDKFTRH 

       190        200        210        220        230        240 
IGWSHPGGPK VEQHARDGEY HELPYVVKGM DFSFSGIMSA AKQAVDDGVP VENVCRGMEE 

       250        260        270        280        290        300 
TIFAMLTEVS ERALSLTGAD ELVLGGGVGQ NARLQRMLGE MCEQREAEFY APENRFLRDN 

       310        320        330        340        350        360 
AGMIAMLGAK MYAAGDTIAI EDSRIDSNFR PDEVAVTWRG PEESVDSYRM GGDEVQGAEA 

       370        380        390        400        410        420 
TVHFDGDRVI KVRVPRSYRH PTLDERLRTE RTRQEARLTS EARRNGVPTP LVRDVDPQES 

       430        440        450        460        470        480 
RIVFQRVGDT DLREGLSEGR VADVGRWLAR IHDAGFVHGD PTTRNVRVGG RDEQADRTTL 

       490        500        510        520        530        540 
IDFGLGYYTQ EAEDHAMDLH VLAQSLAGTA DDPETLLSAA EDAYRTESDH ADAVFASLDD 


IEGRGRYQ 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[2]"Nucleotide sequence of the genes for ribosomal proteins HS15 and HSH from Haloarcula marismortui: an archaeon-specific gene cluster."
Arndt E., Steffens C.
FEBS Lett. 314:211-214(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-226.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY596297 Genomic DNA. Translation: AAV47295.1.
X70117 Genomic DNA. Translation: CAA49709.1.
PIRS27037.
RefSeqYP_137001.1. NC_006396.1.

3D structure databases

ProteinModelPortalP36174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC2490.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV47295; AAV47295; rrnAC2490.
GeneID3129623.
KEGGhma:rrnAC2490.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0533.
HOGENOMHOG000109569.
KOK15904.
OMARDNAGMI.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-2250-MONOMER.

Family and domain databases

HAMAPMF_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.
[Graphical view]
PfamPF00814. Peptidase_M22. 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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAE1B_HALMA
AccessionPrimary (citable) accession number: P36174
Secondary accession number(s): Q5UZK8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 4, 2005
Last modified: June 11, 2014
This is version 98 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