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UniProtKB/Swiss-Prot entry Q7S9B6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ESA1_NEUCR
Primary accession number Q7S9B6
Secondary accession numbers None
Integrated into Swiss-Prot on December 20, 2005
Sequence was last modified on December 15, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 35)
Name and origin of the protein
Protein name Histone acetyltransferase esa-1
Synonyms EC 2.3.1.48
Histone acetyltransferase hat-4
Gene name
Name: esa-1
Synonyms: hat-4
ORFNames: NCU05218
From
Neurospora crassa [TaxID: 5141] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
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: 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.
  • SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AABX02000019; EAA32981.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_962217.1; -.
3D structure databases
HSSP Q08649; 1FY7. [HSSP ENTRY / PDB]
ModBase Q7S9B6.
Ontologies
GO
GO:0004402; Molecular function: histone acetyltransferase activity (inferred from electronic annotation from EC).
GO:0016568; Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016181; Acyl_CoA_acyltransferase.
IPR000953; Chromodomain.
IPR002717; MOZ_SAS.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF01853; MOZ_SAS; 1.
Pfam graphical view of domain structure.
SMART SM00298; CHROMO; 1.
SMART graphical view of domain structure.
BLOCKS Q7S9B6.
ProtoNet Q7S9B6.
Genome annotation databases
GeneID 3878365; -.
KEGG ncr:NCU05218; -.
NMPDR fig|5141.1.peg.2508; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Activator; Chromatin regulator; Complete proteome; Nucleus; Transcription; Transcription regulation; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   506  506     Histone acetyltransferase esa-1. PRO_0000051559
MOTIF   303   324  22     ESA1-RPD3 motif (By similarity). 
COMPBIAS   90   121  32     Lys-rich. 
ACT_SITE   362   362        By similarity. 
BINDING   365   365        Coenzyme A (By similarity). 
BINDING   400   400        Coenzyme A (By similarity). 
Sequence information
Length: 506 AA [This is the length of the unprocessed precursor] Molecular weight: 58807 Da [This is the MW of the unprocessed precursor] CRC64: 53A62414D139674A [This is a checksum on the sequence]
        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 

Q7S9B6 in FASTA format

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