Q4P3S3 (ESA1_USTMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase ESA1
EC=2.3.1.48

Gene names

Name:	ESA1
ORF Names:	UM05240

Organism

Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome]

Taxonomic identifier

237631 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago › Ustilago maydis

Protein attributes

Sequence length	565 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, 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.
Post-translational modification	Autoacetylation at Lys-384 is required for proper function By similarity.
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
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: EnsemblFungi DNA-dependent transcription, elongation Inferred from electronic annotation. Source: EnsemblFungi chromatin silencing at rDNA Inferred from electronic annotation. Source: EnsemblFungi histone H4 acetylation Inferred from electronic annotation. Source: GOC positive regulation of transcription elongation from RNA polymerase II promoter Inferred from electronic annotation. Source: EnsemblFungi regulation of cell cycle Inferred from electronic annotation. Source: EnsemblFungi regulation of transcription by chromatin organization Inferred from electronic annotation. Source: EnsemblFungi
Cellular_component	Piccolo NuA4 histone acetyltransferase complex Inferred from electronic annotation. Source: EnsemblFungi
Molecular_function	H4 histone acetyltransferase activity Inferred from electronic annotation. Source: EnsemblFungi zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 565	565	Histone acetyltransferase ESA1		PRO_0000051560
Regions
	Region	434 – 440	7	Acetyl-CoA binding By similarity
	Motif	367 – 388	22	ESA1-RPD3 motif By similarity
Sites
	Active site	384	1	By similarity
	Active site	426	1	Nucleophile By similarity
	Binding site	429	1	Acetyl-CoA By similarity
	Binding site	464	1	Acetyl-CoA By similarity
Amino acid modifications
	Modified residue	384	1	N6-acetyllysine; by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4P3S3 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: C35F30CBD96EB754	FASTA	565	63,408
	10 20 30 40 50 60 MAPRTQKSTS GTPGGSGTPG PDEGPQISPG GTYGLEDVVV GCKAFVQKPD VVTGEMEERK 70 80 90 100 110 120 AEILSIREKP KPRLTKKQQA ELADKPAPTL EETLEYYVHY CEFNKRLDEW VSGTRLITSR 130 140 150 160 170 180 ELEWPKKEVT SDKTKRKVIR AGSGATTPST PLTPTGKGYR GAGASNLLKK AAAQAAKNVQ 190 200 210 220 230 240 GESGLETPQK RKADSGDTST AQSIRADSID ADADGEDDEN GAVVAMEMLG GNDQQEKDDV 250 260 270 280 290 300 ATESNGGLTA SLNANQGQET FSKKQEIEKL RTSGSMTQSV SEVARVKNLN KIQMGKSEVE 310 320 330 340 350 360 TWYFSPYPLE YAHIDTLYIC EMCLSYFPSP FTLKRHRSKC TLLHPPGNEI YRHEDISFFE 370 380 390 400 410 420 IDGRLQRTWC RNLCLLSKCF LDHKTLYYDV DPFLYYCMVK RDDLGCHLLG YFSKEKDSAE 430 440 450 460 470 480 NYNVACILTL PQHQRAGYGK LLIEFSYELT KIEGKLGSPE KPLSDLGLLS YRAYWAEIIV 490 500 510 520 530 540 ELLLKTEDEI SIEEIAQKTA FTHADILHTC MALNMLKQYQ GKHMIVLSDL IISKYTAKRP 550 560 RKRINPQKLH WTAKNWHRSQ LNFGW

References

[1]

"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W. Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521 / FGSC 9021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACP01000190 Genomic DNA. Translation: EAK82853.1.
RefSeq	XP_761387.1. XM_756294.1.
3D structure databases
ProteinModelPortal	Q4P3S3.
SMR	Q4P3S3. Positions 284-551.
ModBase	Search...
Protein-protein interaction databases
STRING	5270.UM05240.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	UM05240T0; UM05240P0; UM05240.
GeneID	3633352.
KEGG	uma:UM05240.1.
Phylogenomic databases
eggNOG	COG5027.
HOGENOM	HOG000182457.
KO	K11304.
OMA	CMCTRDE.
OrthoDB	EOG4R7ZKC.
Family and domain databases
Gene3D	3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000953. Chromo_domain/shadow. IPR016197. Chromodomain-like. IPR002717. MOZ_SAS. IPR025995. Tudor-knot. IPR015880. Znf_C2H2-like. [Graphical view]
Pfam	PF01853. MOZ_SAS. 1 hit. PF11717. Tudor-knot. 1 hit. [Graphical view]
SMART	SM00298. CHROMO. 1 hit. SM00355. ZnF_C2H2. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF54160. Chromodomain-like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ESA1_USTMA

Accession

Primary (citable) accession number: Q4P3S3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 19, 2005
Last modified:	April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program