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Q6FPH9

- ESA1_CANGA

UniProt

Q6FPH9 - ESA1_CANGA

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Protein
Histone acetyltransferase ESA1
Gene
ESA1, CAGL0J03696g
Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
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 sitei263 – 2631 By similarity
Active sitei305 – 3051Nucleophile By similarity
Binding sitei308 – 3081Acetyl-CoA By similarity
Binding sitei343 – 3431Acetyl-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
Ordered Locus Names:CAGL0J03696g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces
ProteomesiUP000002428: Chromosome J

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 – 446446Histone acetyltransferase ESA1
PRO_0000051554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei263 – 2631N6-acetyllysine; by autocatalysis By similarity

Post-translational modificationi

Autoacetylation at Lys-263 is required for proper function By similarity.

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ6FPH9.
SMRiQ6FPH9. Positions 7-90, 163-435.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni313 – 3197Acetyl-CoA binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi246 – 26722ESA1-RPD3 motif By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi94 – 1018Poly-Lys

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.

Phylogenomic databases

HOGENOMiHOG000182457.
KOiK11304.
OMAiSQLRFAW.
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.

Sequencei

Sequence statusi: Complete.

Q6FPH9-1 [UniParc]FASTAAdd to Basket

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MAGAEVEEEA GIPKKIESTE EVLIKCQCWV RKDEEERLAE ILSINARVSP    50
SKFYVHYVNF NKRLDEWVTG DRINLDKEVI FPRPKRQLEE DTNKKQKKKK 100
KFPQKAAVVE SDAKSSEMGE GSDVMDLDNL NVRGLKDEEI SREDEIKKLR 150
TSGSMIQNPH EVAHVRNLSK IIMGKFEIEP WYFSPYPIEL TDLDVVYIDD 200
FTLQYFGSRK QYERYRKKCT LRHPPGNEIY RDDYVSFFEI DGRKQRTWCR 250
NLCLLSKLFL DHKTLYYDVD PFLFYCMTRR DEMGHHFVGY FSKEKESADG 300
YNVACILTLP QYQRMGYGRL LIEFSYELSK KEGKVGSPEK PLSDLGLLSY 350
RAYWSDVLIT LLVEHGKEVT IDEISSMTSM TTTDILHTLK TLNILRYYKG 400
QHIIFLNDDI LERYNQLKTK KRRHIDAEKL LWKPPVFTAS QLRFAW 446
Length:446
Mass (Da):52,552
Last modified:July 19, 2004 - v1
Checksum:i8E5A7B01F9D4CD94
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR380956 Genomic DNA. Translation: CAG60814.1.
RefSeqiXP_447865.1. XM_447865.1.

Genome annotation databases

GeneIDi2889685.
KEGGicgr:CAGL0J03696g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR380956 Genomic DNA. Translation: CAG60814.1 .
RefSeqi XP_447865.1. XM_447865.1.

3D structure databases

ProteinModelPortali Q6FPH9.
SMRi Q6FPH9. Positions 7-90, 163-435.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2889685.
KEGGi cgr:CAGL0J03696g.

Phylogenomic databases

HOGENOMi HOG000182457.
KOi K11304.
OMAi SQLRFAW.
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.
ProtoNeti Search...

Entry informationi

Entry nameiESA1_CANGA
AccessioniPrimary (citable) accession number: Q6FPH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 69 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

Similar proteinsi