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Q2UMQ5 (ESA1_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 ESA1

EC=2.3.1.48
Gene names
Name:esa1
ORF Names:AO090001000664
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Subunit structure

Component of the NuA4 histone acetyltransferase complex By similarity.

Subcellular location

Nucleus By similarity.

Domain

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.

Post-translational modification

Autoacetylation at Lys-318 is required for proper function By similarity.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Contains 1 chromo domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionActivator
Chromatin regulator
Transferase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processregulation 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_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 506506Histone acetyltransferase ESA1
PRO_0000234078

Regions

Domain39 – 9557Chromo
Region368 – 3747Acetyl-CoA binding By similarity
Motif301 – 32222ESA1-RPD3 motif

Sites

Active site3181 By similarity
Active site3601Nucleophile By similarity
Binding site3631Acetyl-CoA By similarity
Binding site3981Acetyl-CoA By similarity

Amino acid modifications

Modified residue3181N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2UMQ5 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: B7FE46EDE0DA5846

FASTA50658,335
        10         20         30         40         50         60 
MGVRDSHGEA TATPDPVEKG FATLNTIRIG VKAMVQKDGE LRKAEILSIR QRKDGPSFYV 

        70         80         90        100        110        120 
HYVDFNKRLD EWIDSTRIDL SHEVEWPQPE KPEKKKAGPG NKAPSKNAQK RARAGSREVS 

       130        140        150        160        170        180 
ATPDLLTGKN TNIGKAQRPS KAGGKENRDE TPANLSVLDS EAISADVTPK PEMEDVDMIG 

       190        200        210        220        230        240 
VSFTDTKEEH EQGKMSREEE IERLRTSGSM TQNPTEIHRV RNLNRLQMGK FDIEPWYFSP 

       250        260        270        280        290        300 
YPASFSDVDM VYIDEFCLSY FDNKRAFERH RSKCTLVHPP GNEIYRDDRI SFFEVDGRRQ 

       310        320        330        340        350        360 
RTWCRNLCLL SKLFLDHKTL YYDVDPFLFY CMATRDETGC HLVGYFSKEK DSAEGYNLAC 

       370        380        390        400        410        420 
ILTLPQYQRL GYGRLLIAFS YELSKREGKL GSPEKPLSDL GLLSYRQYWR ETLVELLIEP 

       430        440        450        460        470        480 
GRESMSENEL AVLTSMTEKD VHETLVVFNM LRYHKGNWVI VLTDQVVEQH NKRLEKEKIK 

       490        500 
GSRKIDPARL QWKPPVFTAS SRTWNW 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007154 Genomic DNA. Translation: BAE57160.1.
RefSeqXP_001819162.1. XM_001819110.2.

3D structure databases

ProteinModelPortalQ2UMQ5.
SMRQ2UMQ5. Positions 219-495.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00000594.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00000606; CADAORAP00000594; CADAORAG00000606.
GeneID5991133.
KEGGaor:AOR_1_1198164.

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000182457.
KOK11304.
OMADVTPFMY.
OrthoDBEOG7RFTRR.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 2 hits.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Entry information

Entry nameESA1_ASPOR
AccessionPrimary (citable) accession number: Q2UMQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 60 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