Reviewed, UniProtKB/Swiss-Prot Q4WYU4 (BUD32_ASPFU)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase bud32
    EC=2.7.11.1

Gene names

Name:	bud32
ORF Names:	AFUA_3G14290

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Component of the EKC/KEOPS complex which promotes both telomere uncapping and telomere elongation By similarity. The complex is required for efficient recruitment of transcriptional coactivators. Important for bud site selection By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Component of the EKC/KEOPS complex By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Telomere By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosomal protein Cytoplasm Nucleus Telomere
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 277	277	Serine/threonine-protein kinase bud32		PRO_0000278906
Regions
	Domain	20 – 277	258	Protein kinase
	Nucleotide binding	26 – 34	9	ATP By similarity
Sites
	Active site	172	1	Proton acceptor By similarity
	Binding site	49	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4WYU4-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: EDA5381E429544A8	FASTA	277	30,938
	10 20 30 40 50 60 MASTDPYTPP PLPSPFTNTT PPPQLLTQGA EAHLYKTVFL SPSAPAALKV RPSKPYRHPI 70 80 90 100 110 120 LDRRLTRQRI LQEARCLVKL VREGVNVPAV LALDWEGQSG EKGFGGAWLM MEWIEGMVVR 130 140 150 160 170 180 VVLERWEKYM KRNQAGLGAE EFEKEEARVR DLMKRIGHAV GALHKAGVIH GDLTTSNLIL 190 200 210 220 230 240 RPPTRAEQQP AADETNPSME GDVVLIDFGL ASQSLQDEDR AVDLYVLERA FGSTHPRTEP 250 260 270 LFTEVLSGYK ESYKGASSAL KRLEEVRMRG RKRSMIG

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAHF01000002 Genomic DNA. Translation: EAL92159.1.
RefSeq	XP_754197.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3511826.
KEGG	afm:AFUA_3G14290.
Phylogenomic databases
HOGENOM	Q4WYU4.
OMA	Q4WYU4. VVYFVDY.
Enzyme and pathway databases
BRENDA	2.7.11.1. 18841.
Family and domain databases
InterPro	IPR002575. APH_trans. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR008266. Tyr_pkinase_AS. [Graphical view]
Pfam	PF01636. APH. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BUD32_ASPFU

Accession

Primary (citable) accession number: Q4WYU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	July 5, 2005
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)