Q5A7Q2 (ESA1_CANAL) 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:	CaO19.5416, CaO19.12871

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	541 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	histone H4 acetylation Inferred by curator. Source: CGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuA4 histone acetyltransferase complex Inferred from physical interaction. Source: CGD
Molecular function	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 – 541	541	Histone acetyltransferase ESA1		PRO_0000051553
Regions
	Region	346 – 352	7	Acetyl-CoA binding By similarity
	Motif	279 – 300	22	ESA1-RPD3 motif By similarity
Sites
	Active site	338	1	Nucleophile By similarity
	Binding site	341	1	Acetyl-CoA By similarity
	Binding site	376	1	Acetyl-CoA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5A7Q2 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 699B10696D755DE9	FASTA	541	61,922
	10 20 30 40 50 60 MAVAEIKKEK GSSLSPEPSS PIQILSTEPD ANTDIKQEKF TPKDILPGCK VHVSKDGEFR 70 80 90 100 110 120 LAEILQEHIK KGRKVFYVHY QDFNKRLDEW IELDRIDFTR SLILPEIKAD TKENKSKKKS 130 140 150 160 170 180 KSKGQTKLSK NNTTANSTTG TPQPSDGQPI MGDDEMDLEN LNVQGLKRPG EEFSREDEIK 190 200 210 220 230 240 KLRTSGSMTQ NHSEVARVRN LSTIILGEHI IEPWYFSPYP IELTEEDEIY ICDFTLSYFG 250 260 270 280 290 300 SKKQFERFRS KCSMKHPPGN EIYRDSKVSF WEIDGRKQRT WCRNLCLLSK LFLDHKTLYY 310 320 330 340 350 360 DVDPFLFYIM TIKSDQGHHV VGYFSKEKES ADGYNVACIL TLPCYQKRGF GKLLIQFSYM 370 380 390 400 410 420 LTKVERKVGS PEKPLSDLGL LSYRAYWTDT LVKLLVERNS PALFRKNNSQ LEYDEAENGK 430 440 450 460 470 480 DSSATPTPGP GSNASQSSIL ASAAASRSGL NSSPIFSNEI TIEDISSITC MTTTDILHTL 490 500 510 520 530 540 TTLQMLRYYK GQHIIVLTDQ IMELYEKLVK KVKEKKKHEL NPKLLHWTPP SFTANQLRFG W

References

[1]

"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACQ01000051 Genomic DNA. Translation: EAK98737.1. AACQ01000050 Genomic DNA. Translation: EAK98837.1.
RefSeq	XP_717694.1. XM_712601.1. XP_717788.1. XM_712695.1.
3D structure databases
ProteinModelPortal	Q5A7Q2.
SMR	Q5A7Q2. Positions 196-530.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5A7Q2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3640518. 3640628.
KEGG	cal:CaO19.12871. cal:CaO19.5416.
Organism-specific databases
CGD	CAL0005186. orf19.5416.
Phylogenomic databases
PhylomeDB	Q5A7Q2.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000953. Chromo_domain/shadow. IPR016197. Chromodomain-like. IPR002717. MOZ_SAS. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
KO	K11304.
Pfam	PF01853. MOZ_SAS. 1 hit. [Graphical view]
SMART	SM00298. CHROMO. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF54160. Chromodomain-like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ESA1_CANAL

Accession

Primary (citable) accession number: Q5A7Q2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program