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UniProtKB/Swiss-Prot entry Q4IEV4


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

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Entry information
Entry name ESA1_GIBZE
Primary accession number Q4IEV4
Secondary accession numbers None
Integrated into Swiss-Prot on December 20, 2005
Sequence was last modified on August 16, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 27)
Name and origin of the protein
Protein name Histone acetyltransferase ESA1
Synonym EC 2.3.1.48
Gene name
Name: ESA1
ORFNames: FG04254
From
Gibberella zeae (Fusarium graminearum) [TaxID: 5518] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae; Gibberella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PH-1 / NRRL 31084;
DOI=10.1126/science.1143708; PubMed=17823352 [NCBI, ExPASy, EBI, Israel, Japan]
Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
"The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization.";
Science 317:1400-1402(2007).
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
AACM01000185; EAA73580.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_384430.1; -.
3D structure databases
ModBase Q4IEV4.
Ontologies
GO
GO:0000785; Cellular component: chromatin (inferred from electronic annotation from InterPro).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from InterPro).
GO:0003682; Molecular function: chromatin binding (inferred from electronic annotation from InterPro).
GO:0004402; Molecular function: histone acetyltransferase activity (inferred from electronic annotation from EC).
GO:0006333; Biological process: chromatin assembly or disassembly (inferred from electronic annotation from InterPro).
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.
Genome annotation databases
GeneID 2786341; -.
KEGG fgr:FG04254.1; -.
Other
ProtoNet Q4IEV4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Activator; Chromatin regulator; Nucleus; Transcription; Transcription regulation; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   502  502     Histone acetyltransferase ESA1. PRO_0000051557
MOTIF   299   320  22     ESA1-RPD3 motif (By similarity). 
ACT_SITE   358   358        By similarity. 
BINDING   361   361        Coenzyme A (By similarity). 
BINDING   396   396        Coenzyme A (By similarity). 
Sequence information
Length: 502 AA [This is the length of the unprocessed precursor] Molecular weight: 58095 Da [This is the MW of the unprocessed precursor] CRC64: 61DCF761F2C3CD43 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGGTPGGEP TVGSGEPRLK SLATPETIKT GCIAWVEKEG QPRRAEILSI KTTKSGKQFY 

        70         80         90        100        110        120 
CNFDNFNKRL DEWVPVIRLD FTREVEWPNP EKEKPKDPKA KKAPTVQSKK TQPSKKSQKR 

       130        140        150        160        170        180 
PSKREQSTTS EANTPHPWTD FVENQNRQKS ASIGPDGDSQ ARASVDGGET PGGGDEMEVD 

       190        200        210        220        230        240 
ERETEVKREP AEFSREVEIE KLRTSGSMTQ NPTEVSRIRN ISKVQFGRFD LYPWYFSPYP 

       250        260        270        280        290        300 
EIFSQEDVIF ICEFCLSYYG DLKAFTRHRK KCTLQHPPGN ELYRNEEISF FEIDGRRQRT 

       310        320        330        340        350        360 
WCRNLCLLSK MFLDHKTLYY DVDPFLFYVM TVRTEKGCHM VGYFSKEKES ADGYNVACIL 

       370        380        390        400        410        420 
TMPQYQRKGY GRLLIQFSYE LSRIEGKLGS PEKPLSDLGL LSYRQYWSEN ILEFLMGYNE 

       430        440        450        460        470        480 
RDEKVTIEAI STALAMTTQD VEHTLQALRM QVYHKSDHKI VIPEKLIEQR EKTKLKRKRT 

       490        500 
VDPTKIQWKP PVFTASSRTW GW 

Q4IEV4 in FASTA format

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