Reviewed, UniProtKB/Swiss-Prot Q6FPH9 (ESA1_CANGA)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase ESA1
    EC=2.3.1.48

Gene names

Name:	ESA1
Ordered Locus Names:	CAGL0J03696g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	446 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
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 – 446	446	Histone acetyltransferase ESA1		PRO_0000051554
Regions
	Motif	246 – 267	22	ESA1-RPD3 motif By similarity
	Compositional bias	94 – 101	8	Poly-Lys
Sites
	Active site	305	1	By similarity
	Binding site	308	1	Coenzyme A By similarity
	Binding site	343	1	Coenzyme A By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FPH9-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 8E5A7B01F9D4CD94	FASTA	446	52,552
	10 20 30 40 50 60 MAGAEVEEEA GIPKKIESTE EVLIKCQCWV RKDEEERLAE ILSINARVSP SKFYVHYVNF 70 80 90 100 110 120 NKRLDEWVTG DRINLDKEVI FPRPKRQLEE DTNKKQKKKK KFPQKAAVVE SDAKSSEMGE 130 140 150 160 170 180 GSDVMDLDNL NVRGLKDEEI SREDEIKKLR TSGSMIQNPH EVAHVRNLSK IIMGKFEIEP 190 200 210 220 230 240 WYFSPYPIEL TDLDVVYIDD FTLQYFGSRK QYERYRKKCT LRHPPGNEIY RDDYVSFFEI 250 260 270 280 290 300 DGRKQRTWCR NLCLLSKLFL DHKTLYYDVD PFLFYCMTRR DEMGHHFVGY FSKEKESADG 310 320 330 340 350 360 YNVACILTLP QYQRMGYGRL LIEFSYELSK KEGKVGSPEK PLSDLGLLSY RAYWSDVLIT 370 380 390 400 410 420 LLVEHGKEVT IDEISSMTSM TTTDILHTLK TLNILRYYKG QHIIFLNDDI LERYNQLKTK 430 440 KRRHIDAEKL LWKPPVFTAS QLRFAW

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 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380956 Genomic DNA. Translation: CAG60814.1.
RefSeq	XP_447865.1.
3D structure databases
SMR	Q6FPH9. Positions 7-90, 163-435.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FPH9.
Genome annotation databases
GeneID	2889685.
GenomeReviews	Gene locus CAGL0J03696g in contig CR380956_GR.
KEGG	cgr:CAGL0J03696g.
Phylogenomic databases
eggNOG	fuNOG04749.
HOGENOM	HBG631736.
OMA	ILRYYKG.
OrthoDB	EOG9GF4XV.
PhylomeDB	Q6FPH9.
Enzyme and pathway databases
BRENDA	2.3.1.48. 189220.
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_CANGA

Accession

Primary (citable) accession number: Q6FPH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)