Reviewed, UniProtKB/Swiss-Prot Q2UMQ5 (ESA1_ASPOR)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase ESA1
    EC=2.3.1.48

Gene names

Name:	esa1
ORF Names:	AO090001000664

Organism

Aspergillus oryzae [Complete proteome]

Taxonomic identifier

5062 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	506 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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, 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 + acetylhistone.
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. Contains 1 chromo domain.

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	chromatin assembly or disassembly Inferred from electronic annotation. Source: InterPro chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chromatin binding Inferred from electronic annotation. Source: InterPro 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 – 506	506	Histone acetyltransferase ESA1		PRO_0000234078
Regions
	Domain	39 – 95	57	Chromo
	Motif	301 – 322	22	ESA1-RPD3 motif
Sites
	Active site	360	1	By similarity
	Binding site	363	1	Coenzyme A By similarity
	Binding site	398	1	Coenzyme A By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2UMQ5-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: B7FE46EDE0DA5846	FASTA	506	58,335
	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

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP007154 Genomic DNA. Translation: BAE57160.1.
RefSeq	XP_001819162.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5991133.
GenomeReviews	Gene locus esa1 in contig AP007154_GR.
KEGG	aor:AO090001000664.
Enzyme and pathway databases
BRENDA	2.3.1.48. 2240.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000953. Chromodomain. IPR002717. MOZ_SAS. IPR011991. Wing_hlx_DNA_bd. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF01853. MOZ_SAS. 1 hit. [Graphical view]
SMART	SM00298. CHROMO. 1 hit. [Graphical view]
PROSITE	PS00598. CHROMO_1. False negative. PS50013. CHROMO_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ESA1_ASPOR

Accession

Primary (citable) accession number: Q2UMQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	January 24, 2006
Last modified:	September 22, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)