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Q5A7Q2

- ESA1_CANAL

UniProt

Q5A7Q2 - ESA1_CANAL

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Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, and histone H2A to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei338 – 3381Important for catalytic activityBy similarity
Active sitei372 – 3721Proton donor/acceptorBy similarity
Binding sitei376 – 3761Acetyl-CoABy similarity

GO - Molecular functioni

  1. H4 histone acetyltransferase activity Source: CGD

GO - Biological processi

  1. chromatin silencing Source: CGD
  2. filamentous growth of a population of unicellular organisms Source: CGD
  3. histone H4 acetylation Source: CGD
  4. regulation of transcription from RNA polymerase II promoter Source: CGD
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase ESA1 (EC:2.3.1.48By similarity)
Gene namesi
Name:ESA1
ORF Names:CaO19.12871, CaO19.5416
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000000559: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0005186. orf19.5416.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. NuA4 histone acetyltransferase complex Source: CGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 541541Histone acetyltransferase ESA1PRO_0000051553Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei296 – 2961N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

Autoacetylation at Lys-296 is required for proper function.By similarity

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex.By similarity

Protein-protein interaction databases

BioGridi1223612. 1 interaction.
STRINGi5476.CAL0005186.

Structurei

3D structure databases

ProteinModelPortaliQ5A7Q2.
SMRiQ5A7Q2. Positions 196-530.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini196 – 529334MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni337 – 3415Acetyl-CoA bindingBy similarity
Regioni346 – 3527Acetyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi279 – 30022ESA1-RPD3 motifBy similarityAdd
BLAST

Domaini

The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.By similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated

Phylogenomic databases

eggNOGiCOG5027.
InParanoidiQ5A7Q2.
KOiK11304.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 2 hits.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5A7Q2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVAEIKKEK GSSLSPEPSS PIQILSTEPD ANTDIKQEKF TPKDILPGCK
60 70 80 90 100
VHVSKDGEFR LAEILQEHIK KGRKVFYVHY QDFNKRLDEW IELDRIDFTR
110 120 130 140 150
SLILPEIKAD TKENKSKKKS KSKGQTKLSK NNTTANSTTG TPQPSDGQPI
160 170 180 190 200
MGDDEMDLEN LNVQGLKRPG EEFSREDEIK KLRTSGSMTQ NHSEVARVRN
210 220 230 240 250
LSTIILGEHI IEPWYFSPYP IELTEEDEIY ICDFTLSYFG SKKQFERFRS
260 270 280 290 300
KCSMKHPPGN EIYRDSKVSF WEIDGRKQRT WCRNLCLLSK LFLDHKTLYY
310 320 330 340 350
DVDPFLFYIM TIKSDQGHHV VGYFSKEKES ADGYNVACIL TLPCYQKRGF
360 370 380 390 400
GKLLIQFSYM LTKVERKVGS PEKPLSDLGL LSYRAYWTDT LVKLLVERNS
410 420 430 440 450
PALFRKNNSQ LEYDEAENGK DSSATPTPGP GSNASQSSIL ASAAASRSGL
460 470 480 490 500
NSSPIFSNEI TIEDISSITC MTTTDILHTL TTLQMLRYYK GQHIIVLTDQ
510 520 530 540
IMELYEKLVK KVKEKKKHEL NPKLLHWTPP SFTANQLRFG W
Length:541
Mass (Da):61,922
Last modified:April 26, 2005 - v1
Checksum:i699B10696D755DE9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000051 Genomic DNA. Translation: EAK98737.1.
AACQ01000050 Genomic DNA. Translation: EAK98837.1.
RefSeqiXP_717694.1. XM_712601.1.
XP_717788.1. XM_712695.1.

Genome annotation databases

GeneIDi3640518.
3640628.
KEGGical:CaO19.12871.
cal:CaO19.5416.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000051 Genomic DNA. Translation: EAK98737.1 .
AACQ01000050 Genomic DNA. Translation: EAK98837.1 .
RefSeqi XP_717694.1. XM_712601.1.
XP_717788.1. XM_712695.1.

3D structure databases

ProteinModelPortali Q5A7Q2.
SMRi Q5A7Q2. Positions 196-530.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1223612. 1 interaction.
STRINGi 5476.CAL0005186.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3640518.
3640628.
KEGGi cal:CaO19.12871.
cal:CaO19.5416.

Organism-specific databases

CGDi CAL0005186. orf19.5416.

Phylogenomic databases

eggNOGi COG5027.
InParanoidi Q5A7Q2.
KOi K11304.
OrthoDBi EOG7RFTRR.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 2 hits.
PROSITEi PS51726. MYST_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.

Entry informationi

Entry nameiESA1_CANAL
AccessioniPrimary (citable) accession number: Q5A7Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 66 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