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Q2UMQ5

- ESA1_ASPOR

UniProt

Q2UMQ5 - ESA1_ASPOR

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Protein

Histone acetyltransferase ESA1

Gene
esa1, AO090001000664
Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - 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].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei318 – 3181 By similarity
Active sitei360 – 3601Nucleophile By similarity
Binding sitei363 – 3631Acetyl-CoA By similarity
Binding sitei398 – 3981Acetyl-CoA By 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:2.3.1.48)
Gene namesi
Name:esa1
ORF Names:AO090001000664
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: 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 – 506506Histone acetyltransferase ESA1PRO_0000234078Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei318 – 3181N6-acetyllysine; by autocatalysis By similarity

Post-translational modificationi

Autoacetylation at Lys-318 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

STRINGi5062.CADAORAP00000594.

Structurei

3D structure databases

ProteinModelPortaliQ2UMQ5.
SMRiQ2UMQ5. Positions 219-495.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 9557ChromoAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 3747Acetyl-CoA binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi301 – 32222ESA1-RPD3 motifAdd
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.

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.
Contains 1 chromo domain.

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
KOiK11304.
OMAiDVTPFMY.
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.

Sequencei

Sequence statusi: Complete.

Q2UMQ5-1 [UniParc]FASTAAdd to Basket

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MGVRDSHGEA TATPDPVEKG FATLNTIRIG VKAMVQKDGE LRKAEILSIR    50
QRKDGPSFYV HYVDFNKRLD EWIDSTRIDL SHEVEWPQPE KPEKKKAGPG 100
NKAPSKNAQK RARAGSREVS ATPDLLTGKN TNIGKAQRPS KAGGKENRDE 150
TPANLSVLDS EAISADVTPK PEMEDVDMIG VSFTDTKEEH EQGKMSREEE 200
IERLRTSGSM TQNPTEIHRV RNLNRLQMGK FDIEPWYFSP YPASFSDVDM 250
VYIDEFCLSY FDNKRAFERH RSKCTLVHPP GNEIYRDDRI SFFEVDGRRQ 300
RTWCRNLCLL SKLFLDHKTL YYDVDPFLFY CMATRDETGC HLVGYFSKEK 350
DSAEGYNLAC ILTLPQYQRL GYGRLLIAFS YELSKREGKL GSPEKPLSDL 400
GLLSYRQYWR ETLVELLIEP GRESMSENEL AVLTSMTEKD VHETLVVFNM 450
LRYHKGNWVI VLTDQVVEQH NKRLEKEKIK GSRKIDPARL QWKPPVFTAS 500
SRTWNW 506
Length:506
Mass (Da):58,335
Last modified:January 24, 2006 - v1
Checksum:iB7FE46EDE0DA5846
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP007154 Genomic DNA. Translation: BAE57160.1.
RefSeqiXP_001819162.1. XM_001819110.2.

Genome annotation databases

EnsemblFungiiCADAORAT00000606; CADAORAP00000594; CADAORAG00000606.
GeneIDi5991133.
KEGGiaor:AOR_1_1198164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP007154 Genomic DNA. Translation: BAE57160.1 .
RefSeqi XP_001819162.1. XM_001819110.2.

3D structure databases

ProteinModelPortali Q2UMQ5.
SMRi Q2UMQ5. Positions 219-495.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5062.CADAORAP00000594.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAORAT00000606 ; CADAORAP00000594 ; CADAORAG00000606 .
GeneIDi 5991133.
KEGGi aor:AOR_1_1198164.

Phylogenomic databases

eggNOGi COG5027.
HOGENOMi HOG000182457.
KOi K11304.
OMAi DVTPFMY.
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. 2 hits.
SSF55729. SSF55729. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiESA1_ASPOR
AccessioniPrimary (citable) accession number: Q2UMQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 60 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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