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Q4P3S3 (ESA1_USTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. 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:UM05240
OrganismUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome]
Taxonomic identifier237631 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

Protein attributes

Sequence length565 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, 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-384 is required for proper function By similarity.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 565565Histone acetyltransferase ESA1
PRO_0000051560

Regions

Region434 – 4407Acetyl-CoA binding By similarity
Motif367 – 38822ESA1-RPD3 motif By similarity

Sites

Active site3841 By similarity
Active site4261Nucleophile By similarity
Binding site4291Acetyl-CoA By similarity
Binding site4641Acetyl-CoA By similarity

Amino acid modifications

Modified residue3841N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4P3S3 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: C35F30CBD96EB754

FASTA56563,408
        10         20         30         40         50         60 
MAPRTQKSTS GTPGGSGTPG PDEGPQISPG GTYGLEDVVV GCKAFVQKPD VVTGEMEERK 

        70         80         90        100        110        120 
AEILSIREKP KPRLTKKQQA ELADKPAPTL EETLEYYVHY CEFNKRLDEW VSGTRLITSR 

       130        140        150        160        170        180 
ELEWPKKEVT SDKTKRKVIR AGSGATTPST PLTPTGKGYR GAGASNLLKK AAAQAAKNVQ 

       190        200        210        220        230        240 
GESGLETPQK RKADSGDTST AQSIRADSID ADADGEDDEN GAVVAMEMLG GNDQQEKDDV 

       250        260        270        280        290        300 
ATESNGGLTA SLNANQGQET FSKKQEIEKL RTSGSMTQSV SEVARVKNLN KIQMGKSEVE 

       310        320        330        340        350        360 
TWYFSPYPLE YAHIDTLYIC EMCLSYFPSP FTLKRHRSKC TLLHPPGNEI YRHEDISFFE 

       370        380        390        400        410        420 
IDGRLQRTWC RNLCLLSKCF LDHKTLYYDV DPFLYYCMVK RDDLGCHLLG YFSKEKDSAE 

       430        440        450        460        470        480 
NYNVACILTL PQHQRAGYGK LLIEFSYELT KIEGKLGSPE KPLSDLGLLS YRAYWAEIIV 

       490        500        510        520        530        540 
ELLLKTEDEI SIEEIAQKTA FTHADILHTC MALNMLKQYQ GKHMIVLSDL IISKYTAKRP 

       550        560 
RKRINPQKLH WTAKNWHRSQ LNFGW 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACP01000190 Genomic DNA. Translation: EAK82853.1.
RefSeqXP_761387.1. XM_756294.1.

3D structure databases

ProteinModelPortalQ4P3S3.
SMRQ4P3S3. Positions 284-551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5270.UM05240.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiUM05240T0; UM05240P0; UM05240.
GeneID3633352.
KEGGuma:UM05240.1.

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000182457.
KOK11304.
OMAEVEWPAP.
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.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Entry information

Entry nameESA1_USTMA
AccessionPrimary (citable) accession number: Q4P3S3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 70 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