BUD32_ENCCU
ID BUD32_ENCCU Reviewed; 197 AA.
AC Q8SVD9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=EKC/KEOPS complex subunit BUD32;
DE EC=3.6.-.- {ECO:0000250|UniProtKB:Q9UYB9};
DE AltName: Full=Atypical serine/threonine protein kinase BUD32;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53323};
GN Name=BUD32; OrderedLocusNames=ECU06_0400;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP PREDICTION OF FUNCTION.
RX PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA Barton G.J.;
RT "The complement of protein kinases of the microsporidium Encephalitozoon
RT cuniculi in relation to those of Saccharomyces cerevisiae and
RT Schizosaccharomyces pombe.";
RL BMC Genomics 8:309-309(2007).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC is probably involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase
CC activity in the context of the EKC/KEOPS complex and likely plays a
CC supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex
CC also promotes both telomere uncapping and telomere elongation. The
CC complex is required for efficient recruitment of transcriptional
CC coactivators. {ECO:0000250|UniProtKB:P53323}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P53323};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53323};
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least BUD32,
CC CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
CC {ECO:0000250|UniProtKB:P53323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53323}. Nucleus
CC {ECO:0000250|UniProtKB:P53323}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:P53323}.
CC -!- DOMAIN: This protein is considered an atypical serine/threonine kinase,
CC because it lacks the conventional structural elements necessary for the
CC substrate recognition as well as a lysine residue that in all other
CC serine/threonine kinases participates in the catalytic event (By
CC similarity). BUD32 has protein kinase activity in vitro, but in the
CC context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches
CC the activity of BUD32 from kinase into ATPase (By similarity).
CC {ECO:0000250|UniProtKB:P53323, ECO:0000250|UniProtKB:Q9UYB9}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL590446; CAD25400.1; -; Genomic_DNA.
DR RefSeq; NP_585796.1; NM_001041418.1.
DR AlphaFoldDB; Q8SVD9; -.
DR SMR; Q8SVD9; -.
DR STRING; 284813.Q8SVD9; -.
DR GeneID; 859219; -.
DR KEGG; ecu:ECU06_0400; -.
DR VEuPathDB; MicrosporidiaDB:ECU06_0400; -.
DR HOGENOM; CLU_063953_2_0_1; -.
DR InParanoid; Q8SVD9; -.
DR OMA; HKLYMEY; -.
DR OrthoDB; 1425238at2759; -.
DR Proteomes; UP000000819; Chromosome VI.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR022495; Bud32.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR12209; PTHR12209; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR03724; arch_bud32; 1.
PE 3: Inferred from homology;
KW Activator; ATP-binding; Chromosome; Cytoplasm; Hydrolase; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Telomere; Transcription;
KW Transcription regulation; Transferase; tRNA processing.
FT CHAIN 1..197
FT /note="EKC/KEOPS complex subunit BUD32"
FT /id="PRO_0000385501"
FT DOMAIN 1..197
FT /note="Protein kinase"
FT ACT_SITE 113
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 4..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 197 AA; 21847 MW; ADE3BAE0088019EF CRC64;
MGFHFQGAES IISADGETVV KKRARKAYRI EALDLKIING RTKREAKILR KLEALGIPAP
RLISTYGDTI VMEKVEGTVL KEMIDSSDNP GALFRDLGAL VSRLHIADII HGDLTTSNFI
HGSKIYAIDF GLSYISRKDE DKAVDLYVFE KAVGCAHDAK FLEDFYCGYM GEGSESVLKK
LGTVRLRGRK REAMAFG
