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Q6CKE9

- ESA1_KLULA

UniProt

Q6CKE9 - ESA1_KLULA

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Protein

Histone acetyltransferase ESA1

Gene
ESA1, KLLA0F11209g
Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
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, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. 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 sitei256 – 2561 By similarity
Active sitei298 – 2981Nucleophile By similarity
Binding sitei301 – 3011Acetyl-CoA By similarity
Binding sitei336 – 3361Acetyl-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:KLLA0F11209g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598: Chromosome F

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 – 439439Histone acetyltransferase ESA1PRO_0000051558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei256 – 2561N6-acetyllysine; by autocatalysis By similarity

Post-translational modificationi

Autoacetylation at Lys-256 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

STRINGi28985.Q6CKE9.

Structurei

3D structure databases

ProteinModelPortaliQ6CKE9.
SMRiQ6CKE9. Positions 16-88, 156-428.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni306 – 3127Acetyl-CoA binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi239 – 26022ESA1-RPD3 motif By 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.

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.

Phylogenomic databases

eggNOGiCOG5027.
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.

Q6CKE9-1 [UniParc]FASTAAdd to Basket

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MSHGEEKEPG IPQKVDSIDE IFVGCKSWVL KDGQDRLAEI LSINSRRDPP    50
KFYVHYEDFN KRLDEWITAD RLQIDKEVIF PRPKELEEKK DSKKKKQQQN 100
KSATPQAASA TPDGGDVMDL DNLNVQGIPN EDISREDEIK KLRTSGSMTQ 150
NQNEVARVRN LNKVIMGKYE IEPWYFSPYP IELTDEDVVY IDDFSLQYFG 200
SKKQYERYRK KCTLRHPPGN EIYRDDYVSF FEIDGRKQRT WCRNLCLLSK 250
LFLDHKTLYY DVDPFLFYCM TRRDELGHHI VGYFSKEKES ADAYNVACIL 300
TLPQYQRMGY GRLLIEFSYE LSKKEGKVGS PEKPLSDLGL LSYRAYWADT 350
LIKLLVEHGQ EITIDEVSSI SSMTTTDILH TAKALEILRF YRGQHVLYLN 400
SDVMKRYKKL KNNKRRSIDP QKLIWTPPVF TASQLRFAW 439
Length:439
Mass (Da):51,474
Last modified:August 16, 2004 - v1
Checksum:i20E81CA743A33F81
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR382126 Genomic DNA. Translation: CAG98298.1.
RefSeqiXP_455590.1. XM_455590.1.

Genome annotation databases

GeneIDi2895129.
KEGGikla:KLLA0F11209g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR382126 Genomic DNA. Translation: CAG98298.1 .
RefSeqi XP_455590.1. XM_455590.1.

3D structure databases

ProteinModelPortali Q6CKE9.
SMRi Q6CKE9. Positions 16-88, 156-428.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 28985.Q6CKE9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2895129.
KEGGi kla:KLLA0F11209g.

Phylogenomic databases

eggNOGi COG5027.
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_KLULA
AccessioniPrimary (citable) accession number: Q6CKE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: August 16, 2004
Last modified: April 16, 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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