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Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Sitei334Important for catalytic activityBy similarity1
Active sitei368Proton donor/acceptorBy similarity1
Binding sitei372Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri225 – 250C2HC MYST-type; degeneratePROSITE-ProRule annotationAdd BLAST26

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, Chromatin regulator, Transferase
Biological processTranscription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase ESA1 (EC:2.3.1.48By similarity)
Gene namesi
Name:ESA1
Ordered Locus Names:DEHA2C12628g
OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic identifieri284592 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
Proteomesi
  • UP000000599 Componenti: Chromosome C

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000515561 – 521Histone acetyltransferase ESA1Add BLAST521

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei292N6-acetyllysine; by autocatalysisBy similarity1

Post-translational modificationi

Autoacetylation at Lys-292 is required for proper function.By similarity

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex.By similarity

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini192 – 509MYST-type HATPROSITE-ProRule annotationAdd BLAST318

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni333 – 337Acetyl-CoA bindingBy similarity5
Regioni342 – 348Acetyl-CoA bindingBy similarity7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi275 – 296ESA1-RPD3 motifBy similarityAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi101 – 129Lys-richAdd BLAST29

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri225 – 250C2HC MYST-type; degeneratePROSITE-ProRule annotationAdd BLAST26

Phylogenomic databases

HOGENOMiHOG000182457.
InParanoidiQ6BU95.
KOiK11304.
OMAiRAYWSDT.
OrthoDBiEOG093709DG.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiView protein in InterPro
IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
IPR025995. Tudor-knot.
PfamiView protein in Pfam
PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
SMARTiView protein in SMART
SM00298. CHROMO. 1 hit.
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 2 hits.
PROSITEiView protein in PROSITE
PS51726. MYST_HAT. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6BU95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVGEDKSGT ATPQHNTSIR ITDDEERSDE KKFTDDDIIT GCKLYVSKDG
60 70 80 90 100
EYRLAEILQD HMKKGKKVFY VHYQEFNKRL DEWISADRID FTRALISPQV
110 120 130 140 150
KVDKKDDKKE GKSKTSKKSK SKNGKTGSKS VTSTPQPNED TAPGTPRNDD
160 170 180 190 200
EMDLDNLNVQ GLKRPGEEVS REDEIKKLRT SGSMTQNHSE VARVRNLSSV
210 220 230 240 250
ILGEHIIEPW YFSPYPIELT EEDEIYICDF TLAYFGSLKQ FERFRTKCSM
260 270 280 290 300
KHPPGNEIYR DSKVSFWEID GRKQRTWCRN LCLLSKLFLD HKTLYYDVDP
310 320 330 340 350
FLFYIMTVKS SQGHHVVGYF SKEKESADGY NVACILTLPC YQKMGFGKLL
360 370 380 390 400
IQFSYMLSNV ENKVGSPEKP LSDLGLLSYR AFWTDTLVKL LVERNNPHLF
410 420 430 440 450
KKNNPQLLTE ASSKDSSVSP PPGGRQSANI QNGNTPSSDI TIDEISSITC
460 470 480 490 500
MTTTDILHTL TALQILRYYK GQHIIVITDH VMAMYDKLVK KIKDKKKHEL
510 520
DPSKLSWTPP AFTANQLRFG W
Length:521
Mass (Da):59,628
Last modified:December 16, 2008 - v2
Checksum:i0F7475FDB336E216
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382135 Genomic DNA. Translation: CAG86300.2.
RefSeqiXP_458224.2. XM_458224.1.

Genome annotation databases

EnsemblFungiiCAG86300; CAG86300; DEHA2C12628g.
GeneIDi2900534.
KEGGidha:DEHA2C12628g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382135 Genomic DNA. Translation: CAG86300.2.
RefSeqiXP_458224.2. XM_458224.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG86300; CAG86300; DEHA2C12628g.
GeneIDi2900534.
KEGGidha:DEHA2C12628g.

Phylogenomic databases

HOGENOMiHOG000182457.
InParanoidiQ6BU95.
KOiK11304.
OMAiRAYWSDT.
OrthoDBiEOG093709DG.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiView protein in InterPro
IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
IPR025995. Tudor-knot.
PfamiView protein in Pfam
PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
SMARTiView protein in SMART
SM00298. CHROMO. 1 hit.
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 2 hits.
PROSITEiView protein in PROSITE
PS51726. MYST_HAT. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiESA1_DEBHA
AccessioniPrimary (citable) accession number: Q6BU95
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 16, 2008
Last modified: February 15, 2017
This is version 83 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.