Reviewed, UniProtKB/Swiss-Prot Q7S9B6 (ESA1_NEUCR)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase esa-1
    EC=2.3.1.48
Alternative name(s):
    Histone acetyltransferase hat-4

Gene names

Name:	esa-1
Synonyms:	hat-4
ORF Names:	NCU05218

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	506 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, 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 – 506	506	Histone acetyltransferase esa-1		PRO_0000051559
Regions
	Motif	303 – 324	22	ESA1-RPD3 motif By similarity
	Compositional bias	90 – 121	32	Lys-rich
Sites
	Active site	362	1	By similarity
	Binding site	365	1	Coenzyme A By similarity
	Binding site	400	1	Coenzyme A By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7S9B6-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 53A62414D139674A	FASTA	506	58,807
	10 20 30 40 50 60 MSPPGGDATV GSDEKRQKGK ATPDTIKMGC IAMVMKEGQL RRAEILSIKD TKSGRQFYCN 70 80 90 100 110 120 FDNFNKRLDE WVPAARIDFE QDVEWPNPDK DKQKDAKTKK NNSTVSKKQP SKKNNQKKAS 130 140 150 160 170 180 KREQSVASDG QTPHPWTEFV ESQPGKNNRQ RGKTEDGTDV NASLEVGGDK GVKRKADEID 190 200 210 220 230 240 MDEDEIPAAK KQRQPSFSRE QEIEKLRTSG SMTQNPTEIS RIRNISKVEF GRYVLFPWYF 250 260 270 280 290 300 SPYPQIFDQE DCIYICEFCL SYYGELKSFV RHRQKCTLHH PPGNEIYRDD YVSFFEIDGR 310 320 330 340 350 360 RQRTWCRNLC LLSKMFLDHK TLYYDVDPFL FYVMTTRDDR GCHIIGYFSK EKESTDGYNV 370 380 390 400 410 420 ACILTLPQYQ RKGYGRLLIQ FSYELSKIEG KLGSPEKPLS DLGLLSYRQY WSENIIDILL 430 440 450 460 470 480 GYNERKEACT IENIAVALAM TTQDVEHTLQ ALKMQVYHKG EHKIVVPEKL IKQREKSKAK 490 500 QKRLIDPERI QWKPPVFTAL NRTWGW

References

[1]

"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AABX02000019 Genomic DNA. Translation: EAA32981.1.
RefSeq	XP_962217.1.
3D structure databases
HSSP	HSSP built from PDB template 1FY7 based on UniProtKB Q08649.
ModBase	Search...
Genome annotation databases
GeneID	3878365.
KEGG	ncr:NCU05218.
NMPDR	fig|5141.1.peg.2508.
Enzyme and pathway databases
BRENDA	2.3.1.48. 266.
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_NEUCR

Accession

Primary (citable) accession number: Q7S9B6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 15, 2003
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)