ID BUD32_DICDI Reviewed; 252 AA.
AC Q54W07;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
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:Q96S44};
GN Name=bud32; ORFNames=DDB_G0279977;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 osgep (By similarity).
CC {ECO:0000250|UniProtKB:Q96S44}.
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:Q96S44};
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:Q96S44};
CC -!- SUBUNIT: Component of the EKC/KEOPS complex; the whole complex
CC dimerizes. {ECO:0000250|UniProtKB:Q96S44}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96S44}.
CC -!- MISCELLANEOUS: This protein is considered an atypical serine/threonine
CC kinase, because it lacks the conventional structural elements necessary
CC for the substrate recognition as well as a lysine residue that in all
CC other serine/threonine kinases participates in the catalytic event.
CC Bud32 has protein kinase activity in vitro, but in the context of the
CC EKC/KEOPS complex, the catalytic subunit osgep switches the activity of
CC 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; AAFI02000035; EAL67460.1; -; Genomic_DNA.
DR RefSeq; XP_641443.1; XM_636351.1.
DR AlphaFoldDB; Q54W07; -.
DR SMR; Q54W07; -.
DR STRING; 44689.Q54W07; -.
DR PaxDb; 44689-DDB0216402; -.
DR EnsemblProtists; EAL67460; EAL67460; DDB_G0279977.
DR GeneID; 8622328; -.
DR KEGG; ddi:DDB_G0279977; -.
DR dictyBase; DDB_G0279977; bud32.
DR eggNOG; KOG3087; Eukaryota.
DR HOGENOM; CLU_063953_0_0_1; -.
DR InParanoid; Q54W07; -.
DR OMA; HKLYMEY; -.
DR PhylomeDB; Q54W07; -.
DR PRO; PR:Q54W07; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000408; C:EKC/KEOPS complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; ISS:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0070525; P:tRNA threonylcarbamoyladenosine metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR022495; Bud32.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR NCBIfam; TIGR03724; arch_bud32; 1.
DR PANTHER; PTHR12209:SF0; EKC_KEOPS COMPLEX SUBUNIT TP53RK; 1.
DR PANTHER; PTHR12209; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; tRNA processing.
FT CHAIN 1..252
FT /note="EKC/KEOPS complex subunit bud32"
FT /id="PRO_0000362004"
FT DOMAIN 35..252
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 41..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 252 AA; 28577 MW; DA5D216BB813DEB3 CRC64;
MDANECSNSE NSATTTIPKS ASPSTTISTK VVKLDEIGIL ISQGAEAKTY ETDLYGLKCI
VKERFSKAYR HPILDQKISS KRILQEVRSL NKCKKKGIQV PSLYLVDIGN NRIYMEFIKG
ETVKHYLYKN QESTQHQNQI ESIMKELGNQ IGIIHEMNVI HGDLTTSNML LRESTNELVF
IDFGLSYTSN SVEDKAVDLY VLERAFISTH PNSEQLFQTI LSNYELTSSN SKIVIQKLNQ
VRLRGRKKTC FG
//
