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C8VBH4 (ESA1_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase esa1

EC=2.3.1.48
Gene names
Name:esa1
ORF Names:AN10956
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Post-translational modification

Autoacetylation at Lys-320 is required for proper function By similarity.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Sequence caution

The sequence EAA62075.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene AN7495 has been split into 2 genes: AN10944 and AN10956.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508Histone acetyltransferase esa1
PRO_0000413170

Regions

Region370 – 3767Acetyl-CoA binding By similarity
Motif303 – 32422ESA1-RPD3 motif By similarity

Sites

Active site3201 By similarity
Active site3621Nucleophile By similarity
Binding site3651Acetyl-CoA By similarity
Binding site4001Acetyl-CoA By similarity

Amino acid modifications

Modified residue3201N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
C8VBH4 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: 148B5CA949A47101

FASTA50858,152
        10         20         30         40         50         60 
MGVRDSHGEA AGTPDPVEKG IATLNTIRIG VKAMVHKDGA LRKAEILSIK QRKDGLAFYV 

        70         80         90        100        110        120 
HYVDFNKRLD EWVASSRLDL SQEVEWPQPE KPEKKKSGPA KAPSKNKRVR AGSRDVSATP 

       130        140        150        160        170        180 
DTLTGKNTNV GKAQRPSKAG GKENRGDETP ADLSMLASEA VSADGTPKAV SEDIDMMDAS 

       190        200        210        220        230        240 
FTDAKEIKEE ERALGLMSRE EEIEKLRTSG SMTQNPTEVH RVRNLDRLQM GKYDIEPWYF 

       250        260        270        280        290        300 
SPYPASFSDA EVVYIDEFCL SYFDNKRAFE RHRTKCTLTH PPGNEIYRDD NISFFEVDGR 

       310        320        330        340        350        360 
RQRTWCRNLC LLSKLFLDHK TLYYDVDPFL FYCMCTRDET GCHLVGYFSK EKESGEGYNL 

       370        380        390        400        410        420 
ACILTLPQYQ RRGYGRLLIS FSYELSKREG KVGSPEKPLS DLGLLGYRQY WRETLVEILL 

       430        440        450        460        470        480 
DSGRETVSEN ELAMLTSMTE KDVHETLVTF KMLRYNKGQW IIVLTDEVIE ERNKRLEKEK 

       490        500 
IKGSRKIDPA RLQWKPPVFT ASSRTWNW 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000129 Genomic DNA. Translation: EAA62075.1. Sequence problems.
BN001304 Genomic DNA. Translation: CBF79494.1.
RefSeqXP_680764.1. XM_675672.1.

3D structure databases

ProteinModelPortalC8VBH4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00000591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00000591; CADANIAP00000591; CADANIAG00000591.
GeneID2869457.
KEGGani:AN7495.2.

Phylogenomic databases

HOGENOMHOG000182457.
KOK12860.
OMADVTPFMY.
OrthoDBEOG7RFTRR.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR021786. DUF3351.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11831. Myb_Cef. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Entry information

Entry nameESA1_EMENI
AccessionPrimary (citable) accession number: C8VBH4
Secondary accession number(s): Q5AW35
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: November 3, 2009
Last modified: June 11, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families