Reviewed, UniProtKB/Swiss-Prot Q4IEV4 (ESA1_GIBZE)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase ESA1
    EC=2.3.1.48

Gene names

Name:	ESA1
ORF Names:	FG04254

Organism

Gibberella zeae (Wheat head blight fungus) (Fusarium graminearum)

Taxonomic identifier

5518 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Gibberella

Protein attributes

Sequence length	502 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, 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.
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
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 – 502	502	Histone acetyltransferase ESA1		PRO_0000051557
Regions
	Motif	299 – 320	22	ESA1-RPD3 motif By similarity
Sites
	Active site	358	1	By similarity
	Binding site	361	1	Coenzyme A By similarity
	Binding site	396	1	Coenzyme A By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4IEV4-1 [UniParc]. Last modified August 16, 2005. Version 1. Checksum: 61DCF761F2C3CD43	FASTA	502	58,095
	10 20 30 40 50 60 MAGGTPGGEP TVGSGEPRLK SLATPETIKT GCIAWVEKEG QPRRAEILSI KTTKSGKQFY 70 80 90 100 110 120 CNFDNFNKRL DEWVPVIRLD FTREVEWPNP EKEKPKDPKA KKAPTVQSKK TQPSKKSQKR 130 140 150 160 170 180 PSKREQSTTS EANTPHPWTD FVENQNRQKS ASIGPDGDSQ ARASVDGGET PGGGDEMEVD 190 200 210 220 230 240 ERETEVKREP AEFSREVEIE KLRTSGSMTQ NPTEVSRIRN ISKVQFGRFD LYPWYFSPYP 250 260 270 280 290 300 EIFSQEDVIF ICEFCLSYYG DLKAFTRHRK KCTLQHPPGN ELYRNEEISF FEIDGRRQRT 310 320 330 340 350 360 WCRNLCLLSK MFLDHKTLYY DVDPFLFYVM TVRTEKGCHM VGYFSKEKES ADGYNVACIL 370 380 390 400 410 420 TMPQYQRKGY GRLLIQFSYE LSRIEGKLGS PEKPLSDLGL LSYRQYWSEN ILEFLMGYNE 430 440 450 460 470 480 RDEKVTIEAI STALAMTTQD VEHTLQALRM QVYHKSDHKI VIPEKLIEQR EKTKLKRKRT 490 500 VDPTKIQWKP PVFTASSRTW GW

References

[1]

"The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization." Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S. , Goswami R.S., Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C. Science 317:1400-1402(2007) [PubMed: 17823352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PH-1 / FGSC 9075 / NRRL 31084.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACM01000185 Genomic DNA. Translation: EAA73580.1.
RefSeq	XP_384430.1.
3D structure databases
SMR	Q4IEV4. Positions 13-92, 216-491.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4IEV4.
Genome annotation databases
GeneID	2786341.
KEGG	fgr:FG04254.1.
Phylogenomic databases
eggNOG	fuNOG04749.
PhylomeDB	Q4IEV4.
Enzyme and pathway databases
BRENDA	2.3.1.48. 74326.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000953. Chromodomain. IPR002717. MOZ_SAS. IPR011991. WHTH_trsnscrt_rep_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]
ProtoNet	Search...

Entry information

Entry name

ESA1_GIBZE

Accession

Primary (citable) accession number: Q4IEV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	August 16, 2005
Last modified:	February 9, 2010
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)