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Q6FPH9 (ESA1_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. 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
Ordered Locus Names:CAGL0J03696g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces

Protein attributes

Sequence length446 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-263 is required for proper function By similarity.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

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 – 446446Histone acetyltransferase ESA1
PRO_0000051554

Regions

Region313 – 3197Acetyl-CoA binding By similarity
Motif246 – 26722ESA1-RPD3 motif By similarity
Compositional bias94 – 1018Poly-Lys

Sites

Active site2631 By similarity
Active site3051Nucleophile By similarity
Binding site3081Acetyl-CoA By similarity
Binding site3431Acetyl-CoA By similarity

Amino acid modifications

Modified residue2631N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FPH9 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 8E5A7B01F9D4CD94

FASTA44652,552
        10         20         30         40         50         60 
MAGAEVEEEA GIPKKIESTE EVLIKCQCWV RKDEEERLAE ILSINARVSP SKFYVHYVNF 

        70         80         90        100        110        120 
NKRLDEWVTG DRINLDKEVI FPRPKRQLEE DTNKKQKKKK KFPQKAAVVE SDAKSSEMGE 

       130        140        150        160        170        180 
GSDVMDLDNL NVRGLKDEEI SREDEIKKLR TSGSMIQNPH EVAHVRNLSK IIMGKFEIEP 

       190        200        210        220        230        240 
WYFSPYPIEL TDLDVVYIDD FTLQYFGSRK QYERYRKKCT LRHPPGNEIY RDDYVSFFEI 

       250        260        270        280        290        300 
DGRKQRTWCR NLCLLSKLFL DHKTLYYDVD PFLFYCMTRR DEMGHHFVGY FSKEKESADG 

       310        320        330        340        350        360 
YNVACILTLP QYQRMGYGRL LIEFSYELSK KEGKVGSPEK PLSDLGLLSY RAYWSDVLIT 

       370        380        390        400        410        420 
LLVEHGKEVT IDEISSMTSM TTTDILHTLK TLNILRYYKG QHIIFLNDDI LERYNQLKTK 

       430        440 
KRRHIDAEKL LWKPPVFTAS QLRFAW 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR380956 Genomic DNA. Translation: CAG60814.1.
RefSeqXP_447865.1. XM_447865.1.

3D structure databases

ProteinModelPortalQ6FPH9.
SMRQ6FPH9. Positions 7-90, 163-435.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2889685.
KEGGcgr:CAGL0J03696g.

Phylogenomic databases

HOGENOMHOG000182457.
KOK11304.
OMASQLRFAW.
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. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Entry information

Entry nameESA1_CANGA
AccessionPrimary (citable) accession number: Q6FPH9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 69 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