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EKC/KEOPS complex subunit BUD32 (EC 3.6.-.-) (Atypical serine/threonine protein kinase BUD32) (EC 2.7.11.1) (Bud site selection protein 32) (Low-dye-binding protein 14) (piD261)

 BUD32_YEAST             Reviewed;         261 AA.
P53323; D6VV41;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 166.
RecName: Full=EKC/KEOPS complex subunit BUD32;
EC=3.6.-.-;
AltName: Full=Atypical serine/threonine protein kinase BUD32;
EC=2.7.11.1;
AltName: Full=Bud site selection protein 32;
AltName: Full=Low-dye-binding protein 14;
AltName: Full=piD261;
Name=BUD32; Synonyms=LDB14; OrderedLocusNames=YGR262C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9090059;
DOI=10.1002/(SICI)1097-0061(19970315)13:3<287::AID-YEA75>3.0.CO;2-5;
Clemente M.L., Sartori G., Cardazzo B., Carignani G.;
"Analysis of an 11.6 kb region from the right arm of chromosome VII of
Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals
the presence of three new genes.";
Yeast 13:287-290(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
INVOLVEMENT IN BUDDING.
PubMed=11452010; DOI=10.1091/mbc.12.7.2147;
Ni L., Snyder M.;
"A genomic study of the bipolar bud site selection pattern in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 12:2147-2170(2001).
[6]
PHOSPHORYLATION AT SER-187 AND SER-189, AND MUTAGENESIS OF SER-187 AND
SER-189.
PubMed=12023889; DOI=10.1042/BJ20011376;
Facchin S., Lopreiato R., Stocchetto S., Arrigoni G., Cesaro L.,
Marin O., Carignani G., Pinna L.A.;
"Structure-function analysis of yeast piD261/Bud32, an atypical
protein kinase essential for normal cell life.";
Biochem. J. 364:457-463(2002).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
IDENTIFICATION IN THE EKC/KEOPS COMPLEX, FUNCTION OF THE EKC/KEOPS
COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16874308; DOI=10.1038/sj.emboj.7601235;
Kisseleva-Romanova E., Lopreiato R., Baudin-Baillieu A.,
Rousselle J.-C., Ilan L., Hofmann K., Namane A., Mann C., Libri D.;
"Yeast homolog of a cancer-testis antigen defines a new transcription
complex.";
EMBO J. 25:3576-3585(2006).
[10]
FUNCTION, AND IDENTIFICATION IN THE EKC/KEOPS COMPLEX.
PubMed=16564010; DOI=10.1016/j.cell.2005.12.044;
Downey M., Houlsworth R., Maringele L., Rollie A., Brehme M.,
Galicia S., Guillard S., Partington M., Zubko M.K., Krogan N.J.,
Emili A., Greenblatt J.F., Harrington L., Lydall D., Durocher D.;
"A genome-wide screen identifies the evolutionarily conserved KEOPS
complex as a telomere regulator.";
Cell 124:1155-1168(2006).
[11]
FUNCTION IN T(6)A37 FORMATION.
PubMed=21183954; DOI=10.1038/emboj.2010.343;
Srinivasan M., Mehta P., Yu Y., Prugar E., Koonin E.V., Karzai A.W.,
Sternglanz R.;
"The highly conserved KEOPS/EKC complex is essential for a universal
tRNA modification, t6A.";
EMBO J. 30:873-881(2011).
[12]
FUNCTION IN T(6)A37 FORMATION.
PubMed=21459853; DOI=10.1093/nar/gkr178;
Daugeron M.C., Lenstra T.L., Frizzarin M., El Yacoubi B., Liu X.,
Baudin-Baillieu A., Lijnzaad P., Decourty L., Saveanu C., Jacquier A.,
Holstege F.C., de Crecy-Lagard V., van Tilbeurgh H., Libri D.;
"Gcn4 misregulation reveals a direct role for the evolutionary
conserved EKC/KEOPS in the t6A modification of tRNAs.";
Nucleic Acids Res. 39:6148-6160(2011).
[13]
FUNCTION IN T(6)A TRNA MODIFICATION.
PubMed=23258706; DOI=10.1093/nar/gks1287;
Perrochia L., Crozat E., Hecker A., Zhang W., Bareille J.,
Collinet B., van Tilbeurgh H., Forterre P., Basta T.;
"In vitro biosynthesis of a universal t6A tRNA modification in Archaea
and Eukarya.";
Nucleic Acids Res. 41:1953-1964(2013).
[14]
FUNCTION IN THE EKC/KEOPS COMPLEX.
PubMed=23620299; DOI=10.1093/nar/gkt322;
Wan L.C., Mao D.Y., Neculai D., Strecker J., Chiovitti D., Kurinov I.,
Poda G., Thevakumaran N., Yuan F., Szilard R.K., Lissina E.,
Nislow C., Caudy A.A., Durocher D., Sicheri F.;
"Reconstitution and characterization of eukaryotic N6-
threonylcarbamoylation of tRNA using a minimal enzyme system.";
Nucleic Acids Res. 41:6332-6346(2013).
-!- FUNCTION: Component of the EKC/KEOPS complex that is required for
the formation of a threonylcarbamoyl group on adenosine at
position 37 (t(6)A37) in tRNAs that read codons beginning with
adenine. The complex is probably involved in the transfer of the
threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the
N6 group of A37. BUD32 has ATPase activity in the context of the
EKC/KEOPS complex and likely plays a supporting role to the
catalytic subunit KAE1. The EKC/KEOPS complex also promotes both
telomere uncapping and telomere elongation. The complex is
required for efficient recruitment of transcriptional
coactivators. Important for bud site selection.
{ECO:0000269|PubMed:16564010, ECO:0000269|PubMed:16874308,
ECO:0000269|PubMed:21183954, ECO:0000269|PubMed:21459853,
ECO:0000269|PubMed:23258706, ECO:0000269|PubMed:23620299}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least
BUD32, CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
{ECO:0000269|PubMed:16564010, ECO:0000269|PubMed:16874308}.
-!- INTERACTION:
Q03705:CGI121; NbExp=9; IntAct=EBI-3809, EBI-912262;
P46984:GON7; NbExp=6; IntAct=EBI-3809, EBI-26178;
Q03835:GRX3; NbExp=3; IntAct=EBI-3809, EBI-22178;
P32642:GRX4; NbExp=11; IntAct=EBI-3809, EBI-22211;
P36132:KAE1; NbExp=21; IntAct=EBI-3809, EBI-26411;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}. Chromosome, telomere
{ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 3020 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: This protein is considered an atypical
serine/threonine kinase, because it lacks the conventional
structural elements necessary for the substrate recognition as
well as a lysine residue that in all other serine/threonine
kinases participates in the catalytic event (PubMed:12023889).
BUD32 has protein kinase activity in vitro, but in the context of
the EKC/KEOPS complex, the catalytic subunit KAE1 switches the
activity of BUD32 from kinase into ATPase (By similarity).
{ECO:0000250, ECO:0000305|PubMed:12023889}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; Y07777; CAA69084.1; -; Genomic_DNA.
EMBL; Z73047; CAA97291.1; -; Genomic_DNA.
EMBL; AY558547; AAS56873.1; -; Genomic_DNA.
EMBL; BK006941; DAA08352.1; -; Genomic_DNA.
PIR; S64595; S64595.
RefSeq; NP_011778.1; NM_001181391.1.
PDB; 4WW5; X-ray; 2.00 A; A=1-261.
PDB; 4WW7; X-ray; 1.67 A; A=1-261.
PDB; 4WW9; X-ray; 1.95 A; A=1-261.
PDB; 4WWA; X-ray; 2.95 A; A=1-261.
PDBsum; 4WW5; -.
PDBsum; 4WW7; -.
PDBsum; 4WW9; -.
PDBsum; 4WWA; -.
ProteinModelPortal; P53323; -.
SMR; P53323; -.
BioGrid; 33513; 124.
DIP; DIP-5008N; -.
IntAct; P53323; 68.
MINT; MINT-571543; -.
STRING; 4932.YGR262C; -.
ChEMBL; CHEMBL4515; -.
iPTMnet; P53323; -.
MaxQB; P53323; -.
PRIDE; P53323; -.
DNASU; 853178; -.
EnsemblFungi; YGR262C; YGR262C; YGR262C.
GeneID; 853178; -.
KEGG; sce:YGR262C; -.
EuPathDB; FungiDB:YGR262C; -.
SGD; S000003494; BUD32.
GeneTree; ENSGT00390000012914; -.
HOGENOM; HOG000226425; -.
InParanoid; P53323; -.
KO; K08851; -.
OMA; HKLYMEY; -.
OrthoDB; EOG092C484K; -.
BioCyc; YEAST:G3O-30931-MONOMER; -.
BRENDA; 2.7.11.1; 984.
PRO; PR:P53323; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0000408; C:EKC/KEOPS complex; IDA:SGD.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IPI:SGD.
GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
GO; GO:0000723; P:telomere maintenance; IMP:SGD.
GO; GO:0000722; P:telomere maintenance via recombination; IMP:SGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006400; P:tRNA modification; TAS:Reactome.
GO; GO:0070525; P:tRNA threonylcarbamoyladenosine metabolic process; IMP:SGD.
InterPro; IPR022495; Bud32.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR010440; LipoPS_kinase.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008266; Tyr_kinase_AS.
Pfam; PF06293; Kdo; 1.
SUPFAM; SSF56112; SSF56112; 1.
TIGRFAMs; TIGR03724; arch_bud32; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
3D-structure; Activator; ATP-binding; Chromosome; Complete proteome;
Cytoplasm; Hydrolase; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Telomere; Transcription; Transcription regulation; Transferase;
tRNA processing.
CHAIN 1 261 EKC/KEOPS complex subunit BUD32.
/FTId=PRO_0000088189.
DOMAIN 16 261 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 22 30 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 161 161 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 43 43 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 187 187 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:12023889}.
MOD_RES 189 189 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:12023889}.
MUTAGEN 187 187 S->A: Reduced kinase activity.
{ECO:0000269|PubMed:12023889}.
MUTAGEN 189 189 S->A: Reduced kinase activity.
{ECO:0000269|PubMed:12023889}.
HELIX 5 13 {ECO:0000244|PDB:4WW7}.
STRAND 20 24 {ECO:0000244|PDB:4WW7}.
STRAND 29 35 {ECO:0000244|PDB:4WW7}.
STRAND 37 39 {ECO:0000244|PDB:4WW7}.
STRAND 49 53 {ECO:0000244|PDB:4WW7}.
HELIX 73 84 {ECO:0000244|PDB:4WW7}.
STRAND 94 98 {ECO:0000244|PDB:4WW7}.
TURN 99 102 {ECO:0000244|PDB:4WW7}.
STRAND 103 107 {ECO:0000244|PDB:4WW7}.
HELIX 114 116 {ECO:0000244|PDB:4WW7}.
STRAND 118 121 {ECO:0000244|PDB:4WWA}.
HELIX 122 129 {ECO:0000244|PDB:4WW7}.
HELIX 136 154 {ECO:0000244|PDB:4WW7}.
STRAND 166 172 {ECO:0000244|PDB:4WW7}.
STRAND 175 180 {ECO:0000244|PDB:4WW7}.
HELIX 192 207 {ECO:0000244|PDB:4WW7}.
HELIX 214 230 {ECO:0000244|PDB:4WW7}.
HELIX 233 253 {ECO:0000244|PDB:4WW7}.
SEQUENCE 261 AA; 29936 MW; D12E97BAE21B3385 CRC64;
MTQEFIDKVS SYLTPDVDIA PISQGAEAIV FTTTTHPYLP RAKDSHQKYI IKYRPPKRYR
HPQIDQALTK HRTLNESRLL AKLYLIPGLC VPQLIACDPY NGFIWLEFLG EDLPGGHGFS
NLKNFLWMHD QDPYSDLVAT TLRKVGRQIG LLHWNDYCHG DLTSSNIVLV RDGARWTPHL
IDFGLGSVSN LVEDKGVDLY VLERAILSTH SKHAEKYNAW IMEGFEEVYR EQGAKGAKKL
KEVTKRFEEV RLRGRKRSML G


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