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Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
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, 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
Sitei423 – 4231Important for catalytic activityBy similarity
Active sitei457 – 4571Proton donor/acceptorBy similarity
Binding sitei461 – 4611Acetyl-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
Ordered Locus Names:CNB03160
OrganismiCryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Taxonomic identifieri214684 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex
ProteomesiUP000002149 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiFungiDB:CNB03160.

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 – 564564Histone acetyltransferase ESA1PRO_0000051555Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei381 – 3811N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

Autoacetylation at Lys-381 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

STRINGi214684.XP_568893.1.

Structurei

3D structure databases

ProteinModelPortaliP0CP02.
SMRiP0CP02. Positions 281-553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini281 – 552272MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni422 – 4265Acetyl-CoA bindingBy similarity
Regioni431 – 4377Acetyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi364 – 38522ESA1-RPD3 motifBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi65 – 8521Pro-richAdd
BLAST
Compositional biasi121 – 19979Lys-richAdd
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

InParanoidiP0CP02.
KOiK11304.
OMAiGCIAMVE.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
IPR025995. Tudor-knot.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CP02-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPSAPSTPH GRGSGSEPGT PAPSVAAGGS YTIDDVVPGV KIYVIKPLSN
60 70 80 90 100
GQAEQRRAEI LSTRPKPKPS AFAPPPPPNA PSPDPRDDTE YYVHYVEFNK
110 120 130 140 150
RLDEWVGGSR LVLSKEMEWP KSKDEPKKKD RPAKAQPSKA PSRATGSPIP
160 170 180 190 200
SDSLLKKAAN KAAMAAGKAT PGKAMPSSKL GKASKIGKAG KFPQKRKAKT
210 220 230 240 250
EADTEAEEES NEDNDALGEE EDMDEDGDVT LITSDGAIDP SREVVAAPSN
260 270 280 290 300
PRAAPQVFSK KQEIEKLRTS GSMTQSHSEI SRVKNLNKLQ IGKHEVETWY
310 320 330 340 350
FSPYPIEYAH LPVLYICEFC LLYYPSATQL RRHRAKCTLL HPPGNEIYRH
360 370 380 390 400
EGISFFEIDG RKQRTWCRNL CLISKCFLDH KTLYYDVDPF LYYCMTVKDD
410 420 430 440 450
YGCHLIGYFS KEKESAEGYN VACILTLPQH QRKGYGRLLI EFSYELSKVE
460 470 480 490 500
GKLGSPEKPL SDLGLLGYRA YWQEKIVELL LDSDYEISLD EIAQKTSITH
510 520 530 540 550
GDIMHTCQAL QMIKYYKNSH IIHLTDAVIE QHKKTKAKPR RAINPAYLKW
560
KPPVFSRAQL AFGF
Length:564
Mass (Da):63,050
Last modified:June 28, 2011 - v1
Checksum:i76BE79DB995BF692
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017342 Genomic DNA. Translation: AAW41586.1.
RefSeqiXP_568893.1. XM_568893.1.
UniGeneiFne.2644.

Genome annotation databases

EnsemblFungiiAAW41586; AAW41586; CNB03160.
GeneIDi3255895.
KEGGicne:CNB03160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017342 Genomic DNA. Translation: AAW41586.1.
RefSeqiXP_568893.1. XM_568893.1.
UniGeneiFne.2644.

3D structure databases

ProteinModelPortaliP0CP02.
SMRiP0CP02. Positions 281-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi214684.XP_568893.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAW41586; AAW41586; CNB03160.
GeneIDi3255895.
KEGGicne:CNB03160.

Organism-specific databases

EuPathDBiFungiDB:CNB03160.

Phylogenomic databases

InParanoidiP0CP02.
KOiK11304.
OMAiGCIAMVE.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
IPR025995. Tudor-knot.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans."
    Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S.
    , Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.
    Science 307:1321-1324(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JEC21 / ATCC MYA-565.

Entry informationi

Entry nameiESA1_CRYNJ
AccessioniPrimary (citable) accession number: P0CP02
Secondary accession number(s): Q55XW1, Q5KM33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 24, 2015
This is version 24 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.