BUD32_ENTBH
ID BUD32_ENTBH Reviewed; 203 AA.
AC B7XIB8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
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; ORFNames=EBI_24212;
OS Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterocytozoon.
OX NCBI_TaxID=481877;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348;
RX PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA Keeling P.J.;
RT "Patterns of genome evolution among the microsporidian parasites
RT Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT bieneusi.";
RL PLoS ONE 2:E1277-E1277(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348;
RX PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT Enterocytozoon bieneusi.";
RL PLoS Pathog. 5:E1000261-E1000261(2009).
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}.
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DR EMBL; ABGB01000018; EED44276.1; -; Genomic_DNA.
DR RefSeq; XP_002649746.1; XM_002649700.1.
DR AlphaFoldDB; B7XIB8; -.
DR SMR; B7XIB8; -.
DR STRING; 481877.B7XIB8; -.
DR EnsemblFungi; EED44276; EED44276; EBI_24212.
DR VEuPathDB; MicrosporidiaDB:EBI_24212; -.
DR HOGENOM; CLU_063953_2_0_1; -.
DR InParanoid; B7XIB8; -.
DR Proteomes; UP000001742; Unassembled WGS sequence.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR022495; Bud32.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR12209; PTHR12209; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR03724; arch_bud32; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 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..203
FT /note="EKC/KEOPS complex subunit BUD32"
FT /id="PRO_0000385502"
FT DOMAIN 1..203
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 4..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 203 AA; 23778 MW; EA4526B03F620F39 CRC64;
MILITSGAEA EIYESENMII KRRVKKNYRI DELDSMLNKT RTKREVNIIK KLNALNIPSP
MFYTTNKYDI VMEKIKGIPV KNILNNESLT SNQFLNKICA KTHKDILIEI GNIVYAMHNN
NIIHGDLTTL NFIYSDKIHI IDFGLSFYSN KDEDKAVDLY LFEKSLISVH NEEFVSYFYS
GYIVNETLNK KLLEIRKRGR KRE
