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Q5AAJ8

- RT109_CANAL

UniProt

Q5AAJ8 - RT109_CANAL

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Protein

Histone acetyltransferase RTT109

Gene

RTT109

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi

Functioni

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.3 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. H3 histone acetyltransferase activity Source: CGD
  2. histone acetyltransferase activity (H3-K56 specific) Source: CGD

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB-KW
  2. filamentous growth Source: CGD
  3. filamentous growth of a population of unicellular organisms Source: CGD
  4. histone acetylation Source: CGD
  5. histone H3-K56 acetylation Source: CGD
  6. negative regulation of filamentous growth of a population of unicellular organisms Source: CGD
  7. pathogenesis Source: CGD
  8. phenotypic switching Source: CGD
  9. regulation of phenotypic switching Source: CGD
  10. regulation of transcription, DNA-templated Source: UniProtKB-KW
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

DNA damage, Transcription, Transcription regulation, Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase RTT109 (EC:2.3.1.48)
Gene namesi
Name:RTT109
ORF Names:CaO19.7491
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000000559: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0005733. orf19.7491.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Leads to a decreased pathogenicity in mice and increased susceptibility to killing by macrophages in vitro.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Histone acetyltransferase RTT109PRO_0000420188Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5476.CAL0005733.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 359359Rtt109-type HATPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RTT109 family.Curated
Contains 1 Rtt109-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5087.
InParanoidiQ5AAJ8.
KOiK11309.
OrthoDBiEOG79PJZ1.

Family and domain databases

InterProiIPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR016849. Histone_H3-K56_AcTrfase_yeast.
[Graphical view]
PfamiPF08214. KAT11. 1 hit.
[Graphical view]
PIRSFiPIRSF027124. Histone_acetylase_Rtt109. 1 hit.
PROSITEiPS51728. RTT109_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5AAJ8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPPDILQNG EFETIYFQTN PTYIKSPIHI PKSTIGKPDT VKIRHFFALL
60 70 80 90 100
HQDLVVLGLE VFVYLQIYSD FVEKYVYVSK CDTVGLEKST IKIGKVIGPV
110 120 130 140 150
LQYIINYNGY KIKMKNLDEK SKDLSDPSTL VRLQRLRDKL PDIYPNLPYY
160 170 180 190 200
NDIPPKEECI EYRTLPKTQN LRLCVFTKPA KEYLFPNSAK NPYKNLLNGQ
210 220 230 240 250
SLLRWWISII DSITKGWNNH KLMIPGADKY ATRKFIEKYS DWSEGHIFKK
260 270 280 290 300
DGLAVQAIPL FPDDPKGRFL ELVIVECRYG KMTVSRFYQE LAYRQEFLLG
310 320 330 340 350
DCVSLIGCCK ENLEVTYHDD SVSTVTISEY KEFMNSLKSV DFSDRVEVSN

FVSNYRKSK
Length:359
Mass (Da):41,735
Last modified:April 26, 2005 - v1
Checksum:iDABD3DCD9A24DDF4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000039 Genomic DNA. Translation: EAK99733.1.
RefSeqiXP_718648.1. XM_713555.1.

Genome annotation databases

GeneIDi3639678.
KEGGical:CaO19.7491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000039 Genomic DNA. Translation: EAK99733.1 .
RefSeqi XP_718648.1. XM_713555.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5476.CAL0005733.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3639678.
KEGGi cal:CaO19.7491.

Organism-specific databases

CGDi CAL0005733. orf19.7491.

Phylogenomic databases

eggNOGi COG5087.
InParanoidi Q5AAJ8.
KOi K11309.
OrthoDBi EOG79PJZ1.

Family and domain databases

InterProi IPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR016849. Histone_H3-K56_AcTrfase_yeast.
[Graphical view ]
Pfami PF08214. KAT11. 1 hit.
[Graphical view ]
PIRSFi PIRSF027124. Histone_acetylase_Rtt109. 1 hit.
PROSITEi PS51728. RTT109_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiRT109_CANAL
AccessioniPrimary (citable) accession number: Q5AAJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3