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

Q8PZ92 (KAE1B_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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=2.3.1.-
    Alternative name(s):
    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:MM_0602
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length547 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

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 caution

The sequence AAM30298.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 547547Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein HAMAP-Rule MF_01447
PRO_0000303656

Regions

Domain340 – 547208Protein kinase
Nucleotide binding355 – 3639ATP By similarity
Region1 – 329329Kae1 HAMAP-Rule MF_01447
Region134 – 1385Threonylcarbamoyl-AMP binding By similarity

Sites

Active site4641Proton acceptor; for kinase activity By similarity
Metal binding1131Iron By similarity
Metal binding1171Iron By similarity
Metal binding1341Iron By similarity
Metal binding2901Iron By similarity
Binding site1661Threonylcarbamoyl-AMP By similarity
Binding site1791Threonylcarbamoyl-AMP; via amide nitrogen By similarity
Binding site1831Threonylcarbamoyl-AMP By similarity
Binding site2621Threonylcarbamoyl-AMP By similarity
Binding site3771ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8PZ92 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: C1480C5A413E3593

FASTA54760,533
        10         20         30         40         50         60 
MKKTFILGIE GTAWNLSAAI VTETEIIAEV TETYKPEKGG IHPREAAQHH AKYAAGVIKK 

        70         80         90        100        110        120 
LLAEAKQNGI EPSDLDGIAF SQGPGLGPCL RTVATAARML GLSLGIPLIG VNHCIAHIEI 

       130        140        150        160        170        180 
GIWKTPAKDP VVLYVSGANS QVISYMEGRY RVFGETLDIG LGNALDKFAR GAGLPHPGGP 

       190        200        210        220        230        240 
KIEAYAKEAK RYIPLPYVIK GMDLSFSGLS TAASEALRKA SLEDVCYSYQ ETAFAMVVEV 

       250        260        270        280        290        300 
AERALAHTGK KEVLLAGGVG ANTRLREMLN EMCEARGAKF YVPEKRFMGD NGTMIAYTGL 

       310        320        330        340        350        360 
LMYKSGNTIS LEDSRVNPSF RTDDVKVTWI KEEEMKKVPE ISPETFFRMP PGEILDNGAE 

       370        380        390        400        410        420 
AVVYLQEGPE GKRALVKERV PKAYRHKEID ERIRRERNRT EARLMSEARR AGVPTPIIYD 

       430        440        450        460        470        480 
VEEFKLKMQF IEGVPIKYLI TPPLSEKVGE LVGKLHSSGI VHGDLTTSNL LLAGERLYLI 

       490        500        510        520        530        540 
DFGLAYFDKS LEARGVDVHV LFQTFESTHR NYEALVKAFE KGYASTFIDS EDVLRRVEEI 


KKRARYA 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM30298.1. Different initiation.
RefSeqNP_632626.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8PZ92.
SMRQ8PZ92. Positions 5-330.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192952.MM_0602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM30298; AAM30298; MM_0602.
GeneID1478944.
KEGGmma:MM_0602.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0533.
HOGENOMHOG000109569.
KOK15904.
OMARDNAGMI.
ProtClustDBPRK09605.

Enzyme and pathway databases

BioCycMMAZ192952:GCK2-618-MONOMER.

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.
IPR018934. RIO-like_kinase.
IPR009220. tRNA_threonyl_synthase/kinase.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PANTHERPTHR11735:SF6. PTHR11735:SF6. 1 hit.
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.
PROSITEPS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAE1B_METMA
AccessionPrimary (citable) accession number: Q8PZ92
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 85 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