P0CP03 (ESA1_CRYNB) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 12.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Histone acetyltransferase ESA1 EC=2.3.1.48 | ||||
| Gene names |
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| Organism | Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans) [Complete proteome] | ||||
| Taxonomic identifier | 283643 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex › ![]() |
Protein attributes
| Sequence length | 564 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | 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 activity | Acetyl-CoA + [histone] = CoA + acetyl-[histone]. |
| Subunit structure | Component of the NuA4 histone acetyltransferase complex By similarity. |
| Subcellular location | Nucleus By similarity. |
| Domain | 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. |
| Post-translational modification | Autoacetylation at Lys-381 is required for proper function By similarity. |
| Sequence similarities | Belongs to the MYST (SAS/MOZ) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Molecular function | Activator Chromatin regulator Transferase |
| PTM | Acetylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | histone acetylation Inferred from electronic annotation. Source: GOC regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | histone acetyltransferase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 564 | 564 | Histone acetyltransferase ESA1 | PRO_0000410158 | |||||
Regions | |||||||||
| Region | 431 – 437 | 7 | Acetyl-CoA binding By similarity | ||||||
| Motif | 364 – 385 | 22 | ESA1-RPD3 motif By similarity | ||||||
| Compositional bias | 65 – 85 | 21 | Pro-rich | ||||||
| Compositional bias | 121 – 199 | 79 | Lys-rich | ||||||
Sites | |||||||||
| Active site | 381 | 1 | By similarity | ||||||
| Active site | 423 | 1 | Nucleophile By similarity | ||||||
| Binding site | 426 | 1 | Acetyl-CoA By similarity | ||||||
| Binding site | 461 | 1 | Acetyl-CoA By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 381 | 1 | N6-acetyllysine; by autocatalysis By similarity | ||||||
Sequences
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References
| [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. Hyman R.W.Science 307:1321-1324(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B-3501A. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AAEY01000009 Genomic DNA. Translation: EAL22621.1. |
| RefSeq | XP_777268.1. XM_772175.1. |
3D structure databases | |
| ProteinModelPortal | P0CP03. |
| SMR | P0CP03. Positions 281-553. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4934345. |
| KEGG | cnb:CNBB2530. |
Phylogenomic databases | |
| HOGENOM | HOG000182457. |
| KO | K11304. |
Family and domain databases | |
| Gene3D | 3.40.630.30. 1 hit. |
| InterPro | IPR016181. Acyl_CoA_acyltransferase. IPR000953. Chromo_domain/shadow. IPR016197. Chromodomain-like. IPR002717. MOZ_SAS. IPR025995. Tudor-knot. IPR015880. Znf_C2H2-like. [Graphical view] |
| Pfam | PF01853. MOZ_SAS. 1 hit. PF11717. Tudor-knot. 1 hit. [Graphical view] |
| SMART | SM00298. CHROMO. 1 hit. SM00355. ZnF_C2H2. 1 hit. [Graphical view] |
| SUPFAM | SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF54160. Chromodomain-like. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ESA1_CRYNB | ||||||||
| Accession | Primary (citable) accession number: P0CP03 Secondary accession number(s): Q55XW1, Q5KM33 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
