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Q5A7Q2 (ESA1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histone acetyltransferase ESA1
EC=2.3.1.48
Gene names
Name:ESA1
ORF Names:CaO19.12871, CaO19.5416
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida ›

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Protein existenceInferred 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, 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 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-296 is required for proper function By similarity.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 541541Histone acetyltransferase ESA1
PRO_0000051553

Regions

Region346 – 3527Acetyl-CoA binding By similarity
Motif279 – 30022ESA1-RPD3 motif By similarity

Sites

Active site2961 By similarity
Active site3381Nucleophile By similarity
Binding site3411Acetyl-CoA By similarity
Binding site3761Acetyl-CoA By similarity

Amino acid modifications

Modified residue2961N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5A7Q2 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 699B10696D755DE9

FASTA54161,922
        10         20         30         40         50         60 
MAVAEIKKEK GSSLSPEPSS PIQILSTEPD ANTDIKQEKF TPKDILPGCK VHVSKDGEFR 

        70         80         90        100        110        120 
LAEILQEHIK KGRKVFYVHY QDFNKRLDEW IELDRIDFTR SLILPEIKAD TKENKSKKKS 

       130        140        150        160        170        180 
KSKGQTKLSK NNTTANSTTG TPQPSDGQPI MGDDEMDLEN LNVQGLKRPG EEFSREDEIK 

       190        200        210        220        230        240 
KLRTSGSMTQ NHSEVARVRN LSTIILGEHI IEPWYFSPYP IELTEEDEIY ICDFTLSYFG 

       250        260        270        280        290        300 
SKKQFERFRS KCSMKHPPGN EIYRDSKVSF WEIDGRKQRT WCRNLCLLSK LFLDHKTLYY 

       310        320        330        340        350        360 
DVDPFLFYIM TIKSDQGHHV VGYFSKEKES ADGYNVACIL TLPCYQKRGF GKLLIQFSYM 

       370        380        390        400        410        420 
LTKVERKVGS PEKPLSDLGL LSYRAYWTDT LVKLLVERNS PALFRKNNSQ LEYDEAENGK 

       430        440        450        460        470        480 
DSSATPTPGP GSNASQSSIL ASAAASRSGL NSSPIFSNEI TIEDISSITC MTTTDILHTL 

       490        500        510        520        530        540 
TTLQMLRYYK GQHIIVLTDQ IMELYEKLVK KVKEKKKHEL NPKLLHWTPP SFTANQLRFG 


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References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACQ01000051 Genomic DNA. Translation: EAK98737.1.
AACQ01000050 Genomic DNA. Translation: EAK98837.1.
RefSeqXP_717694.1. XM_712601.1.
XP_717788.1. XM_712695.1.

3D structure databases

ProteinModelPortalQ5A7Q2.
SMRQ5A7Q2. Positions 196-530.
ModBaseSearch...

Protein-protein interaction databases

STRING5476.CAL0005186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3640518.
3640628.
KEGGcal:CaO19.12871.
cal:CaO19.5416.

Organism-specific databases

CGDCAL0005186. orf19.5416.

Phylogenomic databases

eggNOGCOG5027.
KOK11304.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF54160. Chromodomain-like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameESA1_CANAL
AccessionPrimary (citable) accession number: Q5A7Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: April 26, 2005
Last modified: May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families

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