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Q4IEV4

- ESA1_GIBZE

UniProt

Q4IEV4 - ESA1_GIBZE

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Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)
Status
Reviewed - Annotation score: 4 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
Sitei358 – 3581Important for catalytic activityBy similarity
Active sitei392 – 3921Proton donor/acceptorBy similarity
Binding sitei396 – 3961Acetyl-CoABy similarity

GO - Molecular functioni

  1. H4 histone acetyltransferase activity Source: EnsemblFungi

GO - Biological processi

  1. chromatin silencing at rDNA Source: EnsemblFungi
  2. DNA repair Source: EnsemblFungi
  3. DNA-templated transcription, elongation Source: EnsemblFungi
  4. positive regulation of transcription elongation from RNA polymerase II promoter Source: EnsemblFungi
  5. regulation of cell cycle Source: EnsemblFungi
  6. regulation of transcription by chromatin organization Source: EnsemblFungi
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:FGSG_04254
OrganismiGibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)
Taxonomic identifieri229533 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium
ProteomesiUP000009057: Chromosome 2

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. Piccolo NuA4 histone acetyltransferase complex Source: EnsemblFungi
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Histone acetyltransferase ESA1PRO_0000051557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei316 – 3161N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

Autoacetylation at Lys-316 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

STRINGi5518.FG04254.1.

Structurei

3D structure databases

ProteinModelPortaliQ4IEV4.
SMRiQ4IEV4. Positions 216-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini216 – 490275MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni357 – 3615Acetyl-CoA bindingBy similarity
Regioni366 – 3727Acetyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi299 – 32022ESA1-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

eggNOGiCOG5027.
InParanoidiQ4IEV4.
KOiK11304.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 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.

Q4IEV4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGGTPGGEP TVGSGEPRLK SLATPETIKT GCIAWVEKEG QPRRAEILSI
60 70 80 90 100
KTTKSGKQFY CNFDNFNKRL DEWVPVIRLD FTREVEWPNP EKEKPKDPKA
110 120 130 140 150
KKAPTVQSKK TQPSKKSQKR PSKREQSTTS EANTPHPWTD FVENQNRQKS
160 170 180 190 200
ASIGPDGDSQ ARASVDGGET PGGGDEMEVD ERETEVKREP AEFSREVEIE
210 220 230 240 250
KLRTSGSMTQ NPTEVSRIRN ISKVQFGRFD LYPWYFSPYP EIFSQEDVIF
260 270 280 290 300
ICEFCLSYYG DLKAFTRHRK KCTLQHPPGN ELYRNEEISF FEIDGRRQRT
310 320 330 340 350
WCRNLCLLSK MFLDHKTLYY DVDPFLFYVM TVRTEKGCHM VGYFSKEKES
360 370 380 390 400
ADGYNVACIL TMPQYQRKGY GRLLIQFSYE LSRIEGKLGS PEKPLSDLGL
410 420 430 440 450
LSYRQYWSEN ILEFLMGYNE RDEKVTIEAI STALAMTTQD VEHTLQALRM
460 470 480 490 500
QVYHKSDHKI VIPEKLIEQR EKTKLKRKRT VDPTKIQWKP PVFTASSRTW

GW
Length:502
Mass (Da):58,095
Last modified:August 16, 2005 - v1
Checksum:i61DCF761F2C3CD43
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231664 Genomic DNA. Translation: ESU08867.1.
RefSeqiXP_384430.1. XM_384430.1.

Genome annotation databases

EnsemblFungiiFGSG_04254T0; FGSG_04254P0; FGSG_04254.
GeneIDi2786341.
KEGGifgr:FG04254.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231664 Genomic DNA. Translation: ESU08867.1 .
RefSeqi XP_384430.1. XM_384430.1.

3D structure databases

ProteinModelPortali Q4IEV4.
SMRi Q4IEV4. Positions 216-491.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5518.FG04254.1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii FGSG_04254T0 ; FGSG_04254P0 ; FGSG_04254 .
GeneIDi 2786341.
KEGGi fgr:FG04254.1.

Phylogenomic databases

eggNOGi COG5027.
InParanoidi Q4IEV4.
KOi K11304.
OrthoDBi EOG7RFTRR.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEi PS51726. MYST_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.
  2. "Comparative genomics reveals mobile pathogenicity chromosomes in Fusarium."
    Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., Antoniw J., Baker S.E.
    , Bluhm B.H., Breakspear A., Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., Rep M.
    Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.

Entry informationi

Entry nameiESA1_GIBZE
AccessioniPrimary (citable) accession number: Q4IEV4
Secondary accession number(s): V6R4L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: August 16, 2005
Last modified: October 29, 2014
This is version 68 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