Reviewed, UniProtKB/Swiss-Prot Q6BU95 (ESA1_DEBHA)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase ESA1
    EC=2.3.1.48

Gene names

Name:	ESA1
Ordered Locus Names:	DEHA2C12628g

Organism

Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

4959 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	521 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.

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 – 521	521	Histone acetyltransferase ESA1		PRO_0000051556
Regions
	Motif	275 – 296	22	ESA1-RPD3 motif By similarity
	Compositional bias	101 – 129	29	Lys-rich
Sites
	Active site	334	1	By similarity
	Binding site	337	1	Coenzyme A By similarity
	Binding site	372	1	Coenzyme A By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BU95-1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 0F7475FDB336E216	FASTA	521	59,628
	10 20 30 40 50 60 MSVGEDKSGT ATPQHNTSIR ITDDEERSDE KKFTDDDIIT GCKLYVSKDG EYRLAEILQD 70 80 90 100 110 120 HMKKGKKVFY VHYQEFNKRL DEWISADRID FTRALISPQV KVDKKDDKKE GKSKTSKKSK 130 140 150 160 170 180 SKNGKTGSKS VTSTPQPNED TAPGTPRNDD EMDLDNLNVQ GLKRPGEEVS REDEIKKLRT 190 200 210 220 230 240 SGSMTQNHSE VARVRNLSSV ILGEHIIEPW YFSPYPIELT EEDEIYICDF TLAYFGSLKQ 250 260 270 280 290 300 FERFRTKCSM KHPPGNEIYR DSKVSFWEID GRKQRTWCRN LCLLSKLFLD HKTLYYDVDP 310 320 330 340 350 360 FLFYIMTVKS SQGHHVVGYF SKEKESADGY NVACILTLPC YQKMGFGKLL IQFSYMLSNV 370 380 390 400 410 420 ENKVGSPEKP LSDLGLLSYR AFWTDTLVKL LVERNNPHLF KKNNPQLLTE ASSKDSSVSP 430 440 450 460 470 480 PPGGRQSANI QNGNTPSSDI TIDEISSITC MTTTDILHTL TALQILRYYK GQHIIVITDH 490 500 510 520 VMAMYDKLVK KIKDKKKHEL DPSKLSWTPP AFTANQLRFG W

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382135 Genomic DNA. Translation: CAG86300.2.
RefSeq	XP_458224.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6BU95.
Genome annotation databases
GeneID	2900534.
GenomeReviews	Gene locus DEHA2C12628g in contig CR382135_GR.
KEGG	dha:DEHA0C13585g.
Phylogenomic databases
HOGENOM	Q6BU95.
OMA	VLCECDD.
Enzyme and pathway databases
BRENDA	2.3.1.48. 74267.
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]
ProtoNet	Search...

Entry information

Entry name

ESA1_DEBHA

Accession

Primary (citable) accession number: Q6BU95

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 16, 2008
Last modified:	November 3, 2009
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)