Reviewed, UniProtKB/Swiss-Prot Q6CKE9 (ESA1_KLULA)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase ESA1
    EC=2.3.1.48

Gene names

Name:	ESA1
Ordered Locus Names:	KLLA0F11209g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	439 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, 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 + 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, DNA-dependent 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 – 439	439	Histone acetyltransferase ESA1		PRO_0000051558
Regions
	Motif	239 – 260	22	ESA1-RPD3 motif By similarity
Sites
	Active site	298	1	By similarity
	Binding site	301	1	Coenzyme A By similarity
	Binding site	336	1	Coenzyme A By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CKE9-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 20E81CA743A33F81	FASTA	439	51,474
	10 20 30 40 50 60 MSHGEEKEPG IPQKVDSIDE IFVGCKSWVL KDGQDRLAEI LSINSRRDPP KFYVHYEDFN 70 80 90 100 110 120 KRLDEWITAD RLQIDKEVIF PRPKELEEKK DSKKKKQQQN KSATPQAASA TPDGGDVMDL 130 140 150 160 170 180 DNLNVQGIPN EDISREDEIK KLRTSGSMTQ NQNEVARVRN LNKVIMGKYE IEPWYFSPYP 190 200 210 220 230 240 IELTDEDVVY IDDFSLQYFG SKKQYERYRK KCTLRHPPGN EIYRDDYVSF FEIDGRKQRT 250 260 270 280 290 300 WCRNLCLLSK LFLDHKTLYY DVDPFLFYCM TRRDELGHHI VGYFSKEKES ADAYNVACIL 310 320 330 340 350 360 TLPQYQRMGY GRLLIEFSYE LSKKEGKVGS PEKPLSDLGL LSYRAYWADT LIKLLVEHGQ 370 380 390 400 410 420 EITIDEVSSI SSMTTTDILH TAKALEILRF YRGQHVLYLN SDVMKRYKKL KNNKRRSIDP 430 QKLIWTPPVF TASQLRFAW

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 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382126 Genomic DNA. Translation: CAG98298.1.
RefSeq	XP_455590.1.
3D structure databases
SMR	Q6CKE9. Positions 156-428.
ModBase	Search...
Genome annotation databases
GeneID	2895129.
KEGG	kla:KLLA0F11209g.
Phylogenomic databases
HOGENOM	Q6CKE9.
OMA	Q6CKE9. VLCECDD.
Enzyme and pathway databases
BRENDA	2.3.1.48. 74088.
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_KLULA

Accession

Primary (citable) accession number: Q6CKE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	August 16, 2004
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)