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Protein

Histone acetyltransferase esa1

Gene

esa1

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 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
Sitei337 – 3371Important for catalytic activityBy similarity
Active sitei371 – 3711Proton donor/acceptorBy similarity
Binding sitei375 – 3751Acetyl-CoABy similarity

GO - Molecular functioni

  1. histone acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
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:AFUA_2G05530
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 2

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Histone acetyltransferase esa1PRO_0000051552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei295 – 2951N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

Autoacetylation at Lys-295 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

STRINGi5085.CADAFUAP00003874.

Structurei

3D structure databases

ProteinModelPortaliQ4WHG1.
SMRiQ4WHG1. Positions 9-67, 196-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini195 – 471277MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni336 – 3405Acetyl-CoA bindingBy similarity
Regioni345 – 3517Acetyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi278 – 29922ESA1-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.
HOGENOMiHOG000182457.
InParanoidiQ4WHG1.
KOiK11304.
OMAiEVEWPAP.
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. 2 hits.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4WHG1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLLMFALLQ DGELRKAEIL SIRQRKDGPS FYVHYVDFNK RLDEWIDASR
60 70 80 90 100
LDLSHEVEWP QPEKPEKKKT GVGNKAPSKN AQKRARADSR DVSATPDLLT
110 120 130 140 150
GKNVNVGKAQ RPSKAGGKEN RDGTPLSMPI VTAEAISTDG TPKAESDDVE
160 170 180 190 200
MVDVSFTDGK SIKEEERALG LMSREEEIER LRTSGSMTQN PTEIHRVRNL
210 220 230 240 250
NRLQMGKYDI EPWYFSPYPA SFSDADIIYI DEFCLSYFDD KRAFERHRTK
260 270 280 290 300
CTLVHPPGNE IYRDDYISFF EVDGRRQRTW CRNLCLLSKL FLDHKTLYYD
310 320 330 340 350
VDPFLFYCMC TRDETGCHLV GYFSKEKDSA EGYNLACILT LPQYQRRGFG
360 370 380 390 400
RLLISFSYEL SKREGKLGSP EKPLSDLGLL GYRQYWRETL VEILMEPGRE
410 420 430 440 450
TVSENELALL TSMTEKDVHE TLVVLNMLRY YKGNWVIVLT DYVVEQHKKR
460 470 480
LEKEKLKGAR KIDPARLQWK PPVFTASSRT WNW
Length:483
Mass (Da):55,969
Last modified:July 5, 2005 - v1
Checksum:i8EBF3CDAE55CE6F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000008 Genomic DNA. Translation: EAL87644.1.
RefSeqiXP_749682.1. XM_744589.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00003874; CADAFUAP00003874; CADAFUAG00003874.
GeneIDi3506677.
KEGGiafm:AFUA_2G05530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000008 Genomic DNA. Translation: EAL87644.1.
RefSeqiXP_749682.1. XM_744589.1.

3D structure databases

ProteinModelPortaliQ4WHG1.
SMRiQ4WHG1. Positions 9-67, 196-472.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5085.CADAFUAP00003874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00003874; CADAFUAP00003874; CADAFUAG00003874.
GeneIDi3506677.
KEGGiafm:AFUA_2G05530.

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
InParanoidiQ4WHG1.
KOiK11304.
OMAiEVEWPAP.
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. 2 hits.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiESA1_ASPFU
AccessioniPrimary (citable) accession number: Q4WHG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2005
Last modified: January 7, 2015
This is version 72 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.