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Q6CXB9 (BUD32_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase BUD32

EC=2.7.11.1
Gene names
Name:BUD32
Ordered Locus Names:KLLA0A09625g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Protein existenceInferred 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. Chromosometelomere By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263Serine/threonine-protein kinase BUD32
PRO_0000278916

Regions

Domain16 – 263248Protein kinase
Nucleotide binding22 – 309ATP By similarity

Sites

Active site1631Proton acceptor By similarity
Binding site541ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6CXB9 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 0772C5015D2A3782

FASTA26329,818
        10         20         30         40         50         60 
MSAEIIASIA DVLTDNIPLT PISQGAEAVV FTSPVHPYLP KNRTDGDDKL YILKYRPEKK 

        70         80         90        100        110        120 
YRHPVIDKTL TKHRTLGESR LLAKLRLIDG LNVPKLIGCD PYHGCIWLEF LGEDLPNGHG 

       130        140        150        160        170        180 
FSNLKNFLWM NASDPYSDLV RDTMINVGKQ IGLMHWNDYC HGDLTTSNIV LVRAGEDWQP 

       190        200        210        220        230        240 
YLIDFGLGSI STLVEDKGVD LYVLERAIIS THSSFANRYN LWVLEGFKSV FESHGKAGLG 

       250        260 
KYKDLIRRFE EVRLRGRKRS MIG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382121 Genomic DNA. Translation: CAH03008.1.
RefSeqXP_451420.1. XM_451420.1.

3D structure databases

ProteinModelPortalQ6CXB9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6CXB9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2896318.
GenomeReviewsGene locus KLLA0A09625g in contig CR382121_GR.
KEGGkla:KLLA0A09625g.

Phylogenomic databases

eggNOGfuNOG08130.
HOGENOMHBG574115.
OMAMLLKPPL.
OrthoDBEOG4R7ZKZ.

Family and domain databases

InterProIPR022495. Kinase-assoc_endopept-1.
IPR011009. Kinase-like_dom.
IPR010440. LipoPS_kinase.
IPR000719. Prot_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
KOK08851.
PfamPF06293. Kdo. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
TIGRFAMsTIGR03724. Arch_bud32. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBUD32_KLULA
AccessionPrimary (citable) accession number: Q6CXB9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: August 16, 2004
Last modified: December 14, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families