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Protein

EKC/KEOPS complex subunit BUD32

Gene

BUD32

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) 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.6 Publications

Miscellaneous

Present with 3020 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43ATPPROSITE-ProRule annotation1
Active sitei161Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi22 – 30ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • positive regulation of transcription by RNA polymerase II Source: SGD
  • protein phosphorylation Source: SGD
  • telomere maintenance Source: SGD
  • telomere maintenance via recombination Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
  • tRNA processing Source: UniProtKB-KW
  • tRNA threonylcarbamoyladenosine metabolic process Source: SGD

Keywordsi

Molecular functionActivator, Hydrolase, Kinase, Serine/threonine-protein kinase, Transferase
Biological processTranscription, Transcription regulation, tRNA processing
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30931-MONOMER
BRENDAi2.7.11.1 984

Names & Taxonomyi

Protein namesi
Recommended name:
EKC/KEOPS complex subunit BUD32 (EC:3.6.-.-By similarity)
Alternative name(s):
Atypical serine/threonine protein kinase BUD32 (EC:2.7.11.11 Publication)
Bud site selection protein 32
Low-dye-binding protein 14
piD261
Gene namesi
Name:BUD32
Synonyms:LDB14
Ordered Locus Names:YGR262C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR262C
SGDiS000003494 BUD32

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi187S → A: Reduced kinase activity. 1 Publication1
Mutagenesisi189S → A: Reduced kinase activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4515

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000881891 – 261EKC/KEOPS complex subunit BUD32Add BLAST261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei187Phosphoserine; by autocatalysis1 Publication1
Modified residuei189Phosphoserine; by autocatalysis1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53323
PaxDbiP53323
PRIDEiP53323

PTM databases

iPTMnetiP53323

Interactioni

Subunit structurei

Component of the EKC/KEOPS complex composed of at least BUD32, CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi33513, 126 interactors
DIPiDIP-5008N
IntActiP53323, 68 interactors
MINTiP53323
STRINGi4932.YGR262C

Structurei

Secondary structure

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 13Combined sources9
Beta strandi20 – 24Combined sources5
Beta strandi29 – 35Combined sources7
Beta strandi37 – 39Combined sources3
Beta strandi49 – 53Combined sources5
Helixi73 – 84Combined sources12
Beta strandi94 – 98Combined sources5
Turni99 – 102Combined sources4
Beta strandi103 – 107Combined sources5
Helixi114 – 116Combined sources3
Beta strandi118 – 121Combined sources4
Helixi122 – 129Combined sources8
Helixi136 – 154Combined sources19
Beta strandi166 – 172Combined sources7
Beta strandi175 – 180Combined sources6
Helixi192 – 207Combined sources16
Helixi214 – 230Combined sources17
Helixi233 – 253Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WW5X-ray2.00A1-261[»]
4WW7X-ray1.67A1-261[»]
4WW9X-ray1.95A1-261[»]
4WWAX-ray2.95A1-261[»]
ProteinModelPortaliP53323
SMRiP53323
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 261Protein kinasePROSITE-ProRule annotationAdd BLAST246

Domaini

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).By similarity1 Publication

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000012914
HOGENOMiHOG000226425
InParanoidiP53323
KOiK08851
OMAiHKLYMEY
OrthoDBiEOG092C484K

Family and domain databases

InterProiView protein in InterPro
IPR022495 Bud32
IPR011009 Kinase-like_dom_sf
IPR010440 LipoPS_kinase
IPR000719 Prot_kinase_dom
IPR008266 Tyr_kinase_AS
PfamiView protein in Pfam
PF06293 Kdo, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
TIGRFAMsiTIGR03724 arch_bud32, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit

Sequencei

Sequence statusi: Complete.

P53323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQEFIDKVS SYLTPDVDIA PISQGAEAIV FTTTTHPYLP RAKDSHQKYI
60 70 80 90 100
IKYRPPKRYR HPQIDQALTK HRTLNESRLL AKLYLIPGLC VPQLIACDPY
110 120 130 140 150
NGFIWLEFLG EDLPGGHGFS NLKNFLWMHD QDPYSDLVAT TLRKVGRQIG
160 170 180 190 200
LLHWNDYCHG DLTSSNIVLV RDGARWTPHL IDFGLGSVSN LVEDKGVDLY
210 220 230 240 250
VLERAILSTH SKHAEKYNAW IMEGFEEVYR EQGAKGAKKL KEVTKRFEEV
260
RLRGRKRSML G
Length:261
Mass (Da):29,936
Last modified:October 1, 1996 - v1
Checksum:iD12E97BAE21B3385
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07777 Genomic DNA Translation: CAA69084.1
Z73047 Genomic DNA Translation: CAA97291.1
AY558547 Genomic DNA Translation: AAS56873.1
BK006941 Genomic DNA Translation: DAA08352.1
PIRiS64595
RefSeqiNP_011778.1, NM_001181391.1

Genome annotation databases

EnsemblFungiiYGR262C; YGR262C; YGR262C
GeneIDi853178
KEGGisce:YGR262C

Similar proteinsi

Entry informationi

Entry nameiBUD32_YEAST
AccessioniPrimary (citable) accession number: P53323
Secondary accession number(s): D6VV41
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 171 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health