Q75BY2 (ESA1_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase ESA1
EC=2.3.1.48

Gene names

Name:	ESA1
Ordered Locus Names:	ACR138W

Organism

Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

284811 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Inferred 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, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. 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.
Sequence similarities	Belongs to the MYST (SAS/MOZ) family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Activator Chromatin regulator Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 520	520	Histone acetyltransferase ESA1		PRO_0000051551
Regions
	Region	387 – 393	7	Acetyl-CoA binding By similarity
	Motif	320 – 341	22	ESA1-RPD3 motif By similarity
	Compositional bias	174 – 181	8	Poly-Lys
Sites
	Active site	379	1	Nucleophile By similarity
	Binding site	382	1	Acetyl-CoA By similarity
	Binding site	417	1	Acetyl-CoA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q75BY2 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 96666EDCD090024B	FASTA	520	60,846
	10 20 30 40 50 60 METHRRSDPR FPPGPSMEPQ PGQTAVLKLR MVVLHNPVYT FRAWMDFTAA ANYVEHEIFV 70 80 90 100 110 120 KHHQQAGVLE LGQTIRRGCW LLGSTMAQEE EKDAGISKYI STTDEIIIGC KCWVEKDGEQ 130 140 150 160 170 180 RLAEILSINN RRQPPKFYVH YEDFNKRLDE WILASRINIE REVTFPKPRD PDEKKKKKQK 190 200 210 220 230 240 KSATPQATDG ETLESADIMD LENLNVQGLR DEGISRDDEI KKLRTSGSMT QNPHEVSRVR 250 260 270 280 290 300 NLSKIIMGKH EIEPWYFSPY PIELTDEDVV YIDDFSLQYF GSKKQYARYR QKCTLRHPPG 310 320 330 340 350 360 NEIYRDDYVS FFEIDGRKQR TWCRNLCLLS KLFLDHKTLY YDVDPFLFYC MTQRDELGHH 370 380 390 400 410 420 LVGYFSKEKE SADGYNVACI LTLPQYQRMG YGRLLIEFSY ELSKKENKVG SPEKPLSDLG 430 440 450 460 470 480 LLSYRAYWSD TLIKLLVENG TEITIDEISS MTSLTTTDIL HTAKALNILR YYKGQHILYL 490 500 510 520 NEDVLLRYEK LIAKKRRSID PEKLIWKPPI FTASQLRFAW

References

[1]

"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016816 Genomic DNA. Translation: AAS51364.1.
RefSeq	NP_983540.2. NM_208893.2.
3D structure databases
ProteinModelPortal	Q75BY2.
SMR	Q75BY2. Positions 102-173, 237-509.
ModBase	Search...
Protein-protein interaction databases
STRING	Q75BY2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4619672.
GenomeReviews	Gene locus ACR138W in contig AE016816_GR.
KEGG	ago:AGOS_ACR138W.
NMPDR	fig|33169.1.peg.1185.
Organism-specific databases
AGD	ACR138W.
Phylogenomic databases
eggNOG	fuNOG04749.
HOGENOM	HBG631736.
OMA	EEDEKGH.
OrthoDB	EOG4R7ZKC.
PhylomeDB	Q75BY2.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000953. Chromo_domain/shadow. IPR016197. Chromodomain-like. IPR002717. MOZ_SAS. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
KO	K11304.
Pfam	PF01853. MOZ_SAS. 1 hit. [Graphical view]
SMART	SM00298. CHROMO. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF54160. Chromodomain-like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ESA1_ASHGO

Accession

Primary (citable) accession number: Q75BY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program