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Protein

Histone acetyltransferase esa1

Gene

esa1

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

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 activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei362 – 3621Important for catalytic activityBy similarity
Active sitei396 – 3961Proton donor/acceptorBy similarity
Binding sitei400 – 4001Acetyl-CoABy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase esa1 (EC:2.3.1.48By similarity)
Gene namesi
Name:esa1
ORF Names:AN10956
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome IV

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Histone acetyltransferase esa1PRO_0000413170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei320 – 3201N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex.By similarity

Protein-protein interaction databases

STRINGi162425.CADANIAP00000591.

Structurei

3D structure databases

ProteinModelPortaliC8VBH4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini220 – 496277MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni361 – 3655Acetyl-CoA bindingBy similarity
Regioni370 – 3767Acetyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi303 – 32422ESA1-RPD3 motifBy similarityAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated

Phylogenomic databases

HOGENOMiHOG000182457.
InParanoidiC8VBH4.
KOiK12860.
OMAiDVTPFMY.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR021786. DUF3351.
IPR002717. HAT_MYST-type.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11831. Myb_Cef. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C8VBH4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVRDSHGEA AGTPDPVEKG IATLNTIRIG VKAMVHKDGA LRKAEILSIK
60 70 80 90 100
QRKDGLAFYV HYVDFNKRLD EWVASSRLDL SQEVEWPQPE KPEKKKSGPA
110 120 130 140 150
KAPSKNKRVR AGSRDVSATP DTLTGKNTNV GKAQRPSKAG GKENRGDETP
160 170 180 190 200
ADLSMLASEA VSADGTPKAV SEDIDMMDAS FTDAKEIKEE ERALGLMSRE
210 220 230 240 250
EEIEKLRTSG SMTQNPTEVH RVRNLDRLQM GKYDIEPWYF SPYPASFSDA
260 270 280 290 300
EVVYIDEFCL SYFDNKRAFE RHRTKCTLTH PPGNEIYRDD NISFFEVDGR
310 320 330 340 350
RQRTWCRNLC LLSKLFLDHK TLYYDVDPFL FYCMCTRDET GCHLVGYFSK
360 370 380 390 400
EKESGEGYNL ACILTLPQYQ RRGYGRLLIS FSYELSKREG KVGSPEKPLS
410 420 430 440 450
DLGLLGYRQY WRETLVEILL DSGRETVSEN ELAMLTSMTE KDVHETLVTF
460 470 480 490 500
KMLRYNKGQW IIVLTDEVIE ERNKRLEKEK IKGSRKIDPA RLQWKPPVFT

ASSRTWNW
Length:508
Mass (Da):58,152
Last modified:November 3, 2009 - v1
Checksum:i148B5CA949A47101
GO

Sequence cautioni

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.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000129 Genomic DNA. Translation: EAA62075.1. Sequence problems.
BN001304 Genomic DNA. Translation: CBF79494.1.
RefSeqiXP_680764.1. XM_675672.1.

Genome annotation databases

EnsemblFungiiCADANIAT00000591; CADANIAP00000591; CADANIAG00000591.
GeneIDi2869457.
KEGGiani:AN7495.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000129 Genomic DNA. Translation: EAA62075.1. Sequence problems.
BN001304 Genomic DNA. Translation: CBF79494.1.
RefSeqiXP_680764.1. XM_675672.1.

3D structure databases

ProteinModelPortaliC8VBH4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00000591.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00000591; CADANIAP00000591; CADANIAG00000591.
GeneIDi2869457.
KEGGiani:AN7495.2.

Phylogenomic databases

HOGENOMiHOG000182457.
InParanoidiC8VBH4.
KOiK12860.
OMAiDVTPFMY.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR021786. DUF3351.
IPR002717. HAT_MYST-type.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11831. Myb_Cef. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

Entry informationi

Entry nameiESA1_EMENI
AccessioniPrimary (citable) accession number: C8VBH4
Secondary accession number(s): Q5AW35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: November 3, 2009
Last modified: June 24, 2015
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.