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Q4P3S3

- ESA1_USTMA

UniProt

Q4P3S3 - ESA1_USTMA

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Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)
Status
Reviewed - Annotation score: 4 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, 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].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei426 – 4261Important for catalytic activityBy similarity
Active sitei460 – 4601Proton donor/acceptorBy similarity
Binding sitei464 – 4641Acetyl-CoABy similarity

GO - Molecular functioni

  1. H4 histone acetyltransferase activity Source: EnsemblFungi

GO - Biological processi

  1. chromatin silencing at rDNA Source: EnsemblFungi
  2. DNA repair Source: EnsemblFungi
  3. DNA-templated transcription, elongation Source: EnsemblFungi
  4. positive regulation of transcription elongation from RNA polymerase II promoter Source: EnsemblFungi
  5. regulation of cell cycle Source: EnsemblFungi
  6. regulation of transcription by chromatin organization Source: EnsemblFungi
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:2.3.1.48By similarity)
Gene namesi
Name:ESA1
ORF Names:UM05240
OrganismiUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)
Taxonomic identifieri237631 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago
ProteomesiUP000000561: Unassembled WGS sequence

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. Piccolo NuA4 histone acetyltransferase complex Source: EnsemblFungi
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 565565Histone acetyltransferase ESA1PRO_0000051560Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei384 – 3841N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

Autoacetylation at Lys-384 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

STRINGi5270.UM05240.1.

Structurei

3D structure databases

ProteinModelPortaliQ4P3S3.
SMRiQ4P3S3. Positions 284-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini284 – 553270MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni425 – 4295Acetyl-CoA bindingBy similarity
Regioni434 – 4407Acetyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi367 – 38822ESA1-RPD3 motifBy 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.By similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
InParanoidiQ4P3S3.
KOiK11304.
OMAiEVEWPAP.
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.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4P3S3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPRTQKSTS GTPGGSGTPG PDEGPQISPG GTYGLEDVVV GCKAFVQKPD
60 70 80 90 100
VVTGEMEERK AEILSIREKP KPRLTKKQQA ELADKPAPTL EETLEYYVHY
110 120 130 140 150
CEFNKRLDEW VSGTRLITSR ELEWPKKEVT SDKTKRKVIR AGSGATTPST
160 170 180 190 200
PLTPTGKGYR GAGASNLLKK AAAQAAKNVQ GESGLETPQK RKADSGDTST
210 220 230 240 250
AQSIRADSID ADADGEDDEN GAVVAMEMLG GNDQQEKDDV ATESNGGLTA
260 270 280 290 300
SLNANQGQET FSKKQEIEKL RTSGSMTQSV SEVARVKNLN KIQMGKSEVE
310 320 330 340 350
TWYFSPYPLE YAHIDTLYIC EMCLSYFPSP FTLKRHRSKC TLLHPPGNEI
360 370 380 390 400
YRHEDISFFE IDGRLQRTWC RNLCLLSKCF LDHKTLYYDV DPFLYYCMVK
410 420 430 440 450
RDDLGCHLLG YFSKEKDSAE NYNVACILTL PQHQRAGYGK LLIEFSYELT
460 470 480 490 500
KIEGKLGSPE KPLSDLGLLS YRAYWAEIIV ELLLKTEDEI SIEEIAQKTA
510 520 530 540 550
FTHADILHTC MALNMLKQYQ GKHMIVLSDL IISKYTAKRP RKRINPQKLH
560
WTAKNWHRSQ LNFGW
Length:565
Mass (Da):63,408
Last modified:July 19, 2005 - v1
Checksum:iC35F30CBD96EB754
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACP01000190 Genomic DNA. Translation: EAK82853.1.
RefSeqiXP_761387.1. XM_756294.1.

Genome annotation databases

EnsemblFungiiUM05240T0; UM05240P0; UM05240.
GeneIDi3633352.
KEGGiuma:UM05240.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACP01000190 Genomic DNA. Translation: EAK82853.1 .
RefSeqi XP_761387.1. XM_756294.1.

3D structure databases

ProteinModelPortali Q4P3S3.
SMRi Q4P3S3. Positions 284-551.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5270.UM05240.1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii UM05240T0 ; UM05240P0 ; UM05240 .
GeneIDi 3633352.
KEGGi uma:UM05240.1.

Phylogenomic databases

eggNOGi COG5027.
HOGENOMi HOG000182457.
InParanoidi Q4P3S3.
KOi K11304.
OMAi EVEWPAP.
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.
IPR015880. Znf_C2H2-like.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEi PS51726. MYST_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis."
    Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.
    , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.
    Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 521 / FGSC 9021.

Entry informationi

Entry nameiESA1_USTMA
AccessioniPrimary (citable) accession number: Q4P3S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2005
Last modified: October 29, 2014
This is version 72 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3