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Q5AAJ8 (RT109_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase RTT109

EC=2.3.1.48
Gene names
Name:RTT109
ORF Names:CaO19.7491
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G2/M phase of the cell cycle and is involved in transcription DNA repair process. Required for efficient pathogenesis in mice suggesting that efficient DNA repair is required for pathogenesis. Plays an important role in the regulation of white-opaque genotoxin induced-switching. Ref.2 Ref.3 Ref.4

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Subcellular location

Nucleus By similarity.

Disruption phenotype

Leads to a decreased pathogenicity in mice and increased susceptibility to killing by macrophages in vitro. Ref.3

Sequence similarities

Belongs to the RTT109 family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
Virulence
   Cellular componentNucleus
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

filamentous growth

Inferred from mutant phenotype Ref.3. Source: CGD

filamentous growth of a population of unicellular organisms

Inferred from mutant phenotype Ref.3. Source: CGD

histone H3-K56 acetylation

Inferred from mutant phenotype Ref.2. Source: CGD

histone acetylation

Inferred from mutant phenotype Ref.3. Source: CGD

negative regulation of filamentous growth of a population of unicellular organisms

Inferred from mutant phenotype Ref.3. Source: CGD

pathogenesis

Inferred from mutant phenotype Ref.3. Source: CGD

phenotypic switching

Inferred from mutant phenotype Ref.4. Source: CGD

regulation of phenotypic switching

Inferred from mutant phenotype Ref.4. Source: CGD

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionH3 histone acetyltransferase activity

Inferred from mutant phenotype Ref.3. Source: CGD

histone acetyltransferase activity (H3-K56 specific)

Inferred from mutant phenotype Ref.2. Source: CGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Histone acetyltransferase RTT109
PRO_0000420188

Sequences

Sequence LengthMass (Da)Tools
Q5AAJ8 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: DABD3DCD9A24DDF4

FASTA35941,735
        10         20         30         40         50         60 
MLPPDILQNG EFETIYFQTN PTYIKSPIHI PKSTIGKPDT VKIRHFFALL HQDLVVLGLE 

        70         80         90        100        110        120 
VFVYLQIYSD FVEKYVYVSK CDTVGLEKST IKIGKVIGPV LQYIINYNGY KIKMKNLDEK 

       130        140        150        160        170        180 
SKDLSDPSTL VRLQRLRDKL PDIYPNLPYY NDIPPKEECI EYRTLPKTQN LRLCVFTKPA 

       190        200        210        220        230        240 
KEYLFPNSAK NPYKNLLNGQ SLLRWWISII DSITKGWNNH KLMIPGADKY ATRKFIEKYS 

       250        260        270        280        290        300 
DWSEGHIFKK DGLAVQAIPL FPDDPKGRFL ELVIVECRYG KMTVSRFYQE LAYRQEFLLG 

       310        320        330        340        350 
DCVSLIGCCK ENLEVTYHDD SVSTVTISEY KEFMNSLKSV DFSDRVEVSN FVSNYRKSK 

« Hide

References

« Hide 'large scale' references
[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[2]"Modulation of histone H3 lysine 56 acetylation as an antifungal therapeutic strategy."
Wurtele H., Tsao S., Lepine G., Mullick A., Tremblay J., Drogaris P., Lee E.H., Thibault P., Verreault A., Raymond M.
Nat. Med. 16:774-780(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"Histone acetyltransferase Rtt109 is required for Candida albicans pathogenesis."
Lopes da Rosa J., Boyartchuk V.L., Zhu L.J., Kaufman P.D.
Proc. Natl. Acad. Sci. U.S.A. 107:1594-1599(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]"Regulation of white and opaque cell-type formation in Candida albicans by Rtt109 and Hst3."
Stevenson J.S., Liu H.
Mol. Microbiol. 81:1078-1091(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000039 Genomic DNA. Translation: EAK99733.1.
RefSeqXP_718648.1. XM_713555.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0005733.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3639678.
KEGGcal:CaO19.7491.

Organism-specific databases

CGDCAL0005733. orf19.7491.

Phylogenomic databases

eggNOGCOG5087.
KOK11309.
OrthoDBEOG79PJZ1.

Family and domain databases

InterProIPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR016849. Histone_H3-K56_AcTrfase_yeast.
[Graphical view]
PfamPF08214. KAT11. 1 hit.
[Graphical view]
PIRSFPIRSF027124. Histone_acetylase_Rtt109. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRT109_CANAL
AccessionPrimary (citable) accession number: Q5AAJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: April 26, 2005
Last modified: April 16, 2014
This is version 51 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

Candida albicans

Candida albicans: entries and gene names