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Q7S9B6 (ESA1_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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 esa-1

EC=2.3.1.48
Alternative name(s):
Histone acetyltransferase hat-4
Gene names
Name:esa-1
Synonyms:hat-4
ORF Names:NCU05218
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

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-320 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 – 506506Histone acetyltransferase esa-1
PRO_0000051559

Regions

Region370 – 3767Acetyl-CoA binding By similarity
Motif303 – 32422ESA1-RPD3 motif By similarity
Compositional bias90 – 12132Lys-rich

Sites

Active site3201 By similarity
Active site3621Nucleophile By similarity
Binding site3651Acetyl-CoA By similarity
Binding site4001Acetyl-CoA By similarity

Amino acid modifications

Modified residue3201N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7S9B6 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 53A62414D139674A

FASTA50658,807
        10         20         30         40         50         60 
MSPPGGDATV GSDEKRQKGK ATPDTIKMGC IAMVMKEGQL RRAEILSIKD TKSGRQFYCN 

        70         80         90        100        110        120 
FDNFNKRLDE WVPAARIDFE QDVEWPNPDK DKQKDAKTKK NNSTVSKKQP SKKNNQKKAS 

       130        140        150        160        170        180 
KREQSVASDG QTPHPWTEFV ESQPGKNNRQ RGKTEDGTDV NASLEVGGDK GVKRKADEID 

       190        200        210        220        230        240 
MDEDEIPAAK KQRQPSFSRE QEIEKLRTSG SMTQNPTEIS RIRNISKVEF GRYVLFPWYF 

       250        260        270        280        290        300 
SPYPQIFDQE DCIYICEFCL SYYGELKSFV RHRQKCTLHH PPGNEIYRDD YVSFFEIDGR 

       310        320        330        340        350        360 
RQRTWCRNLC LLSKMFLDHK TLYYDVDPFL FYVMTTRDDR GCHIIGYFSK EKESTDGYNV 

       370        380        390        400        410        420 
ACILTLPQYQ RKGYGRLLIQ FSYELSKIEG KLGSPEKPLS DLGLLSYRQY WSENIIDILL 

       430        440        450        460        470        480 
GYNERKEACT IENIAVALAM TTQDVEHTLQ ALKMQVYHKG EHKIVVPEKL IKQREKSKAK 

       490        500 
QKRLIDPERI QWKPPVFTAL NRTWGW 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM002239 Genomic DNA. Translation: EAA32981.1.
RefSeqXP_962217.1. XM_957124.1.

3D structure databases

ProteinModelPortalQ7S9B6.
SMRQ7S9B6. Positions 220-495.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU05218.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000004956; EFNCRP00000004952; EFNCRG00000004950.
GeneID3878365.
KEGGncr:NCU05218.

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. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Entry information

Entry nameESA1_NEUCR
AccessionPrimary (citable) accession number: Q7S9B6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 15, 2003
Last modified: April 16, 2014
This is version 72 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