ID   BUD32_PYRAB             Reviewed;         220 AA.
AC   Q9UYB9;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=KEOPS complex subunit Bud32;
DE            EC=3.6.-.- {ECO:0000305|PubMed:23945934};
DE   AltName: Full=Atypical serine/threonine protein kinase Bud32;
DE            EC=2.7.11.1 {ECO:0000305|PubMed:23945934};
GN   Name=bud32; OrderedLocusNames=PAB1047, PYRAB15890;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
RN   [3]
RP   FUNCTION IN T(6)A TRNA MODIFICATION, AND SUBUNIT.
RX   PubMed=23258706; DOI=10.1093/nar/gks1287;
RA   Perrochia L., Crozat E., Hecker A., Zhang W., Bareille J., Collinet B.,
RA   van Tilbeurgh H., Forterre P., Basta T.;
RT   "In vitro biosynthesis of a universal t6A tRNA modification in Archaea and
RT   Eukarya.";
RL   Nucleic Acids Res. 41:1953-1964(2013).
RN   [4]
RP   FUNCTION IN THE KEOPS COMPLEX, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS
RP   OF ASP-127.
RX   PubMed=23945934; DOI=10.1093/nar/gkt720;
RA   Perrochia L., Guetta D., Hecker A., Forterre P., Basta T.;
RT   "Functional assignment of KEOPS/EKC complex subunits in the biosynthesis of
RT   the universal t6A tRNA modification.";
RL   Nucleic Acids Res. 41:9484-9499(2013).
CC   -!- FUNCTION: Component of the 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 KEOPS complex and likely plays a
CC       supporting role to the catalytic subunit Kae1.
CC       {ECO:0000269|PubMed:23258706, ECO:0000269|PubMed:23945934}.
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:0000305|PubMed:23945934};
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:0000305|PubMed:23945934};
CC   -!- SUBUNIT: Component of the KEOPS complex that consists of Kae1, Bud32,
CC       Cgi121 and Pcc1; the whole complex dimerizes.
CC       {ECO:0000269|PubMed:23258706, ECO:0000269|PubMed:23945934}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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 KEOPS complex, the catalytic subunit Kae1 switches the
CC       activity of Bud32 from kinase into ATPase (PubMed:23945934).
CC       {ECO:0000250|UniProtKB:P53323, ECO:0000305|PubMed:23945934}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ248288; CAB50493.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE71048.1; -; Genomic_DNA.
DR   PIR; G75006; G75006.
DR   RefSeq; WP_010868707.1; NC_000868.1.
DR   AlphaFoldDB; Q9UYB9; -.
DR   SMR; Q9UYB9; -.
DR   STRING; 272844.PAB1047; -.
DR   GeneID; 1495877; -.
DR   KEGG; pab:PAB1047; -.
DR   PATRIC; fig|272844.11.peg.1695; -.
DR   eggNOG; arCOG01185; Archaea.
DR   HOGENOM; CLU_063953_2_0_2; -.
DR   OrthoDB; 31344at2157; -.
DR   PhylomeDB; Q9UYB9; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000408; C:EKC/KEOPS complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
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:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:UniProtKB.
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; PF01163; RIO1; 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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Hydrolase; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase; tRNA processing.
FT   CHAIN           1..220
FT                   /note="KEOPS complex subunit Bud32"
FT                   /id="PRO_0000430322"
FT   DOMAIN          1..220
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        127
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         27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MUTAGEN         127
FT                   /note="D->R: Completely abolishes ATPase activity of the
FT                   KEOPS complex and completely impairs the tRNA modification
FT                   activity of the complex."
FT                   /evidence="ECO:0000269|PubMed:23945934"
SQ   SEQUENCE   220 AA;  26343 MW;  A37A9382419FEF75 CRC64;
     MKLIKQGAEA KIYLAEFSEL YFDYPIKVIV KERIKKRYRI PEIDLKLRKE RTIREARILR
     RAKEFGVNVP YVFEVDTKNM IIVMEYIEGE RLKELLEKLP MEERLKVCRE VGRQIGKLHE
     AGIVHGDLTT SNMILREGKV YFIDFGLAEF DDTIEAQGVD LHLLKRAMES THYKWFERGF
     EEVLKGYIEI RGEDKGREIR EKIREIELRG RYRERSWITQ
//