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Q7S9B6

- ESA1_NEUCR

UniProt

Q7S9B6 - ESA1_NEUCR

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Protein

Histone acetyltransferase esa-1

Gene

esa-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
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, 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].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei362 – 3621Important for catalytic activityBy similarity
Active sitei396 – 3961Proton donor/acceptorBy similarity
Binding sitei400 – 4001Acetyl-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 esa-1 (EC:2.3.1.48By similarity)
Alternative name(s):
Histone acetyltransferase hat-4
Gene namesi
Name:esa-1
Synonyms:hat-4
ORF Names:NCU05218
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 4, Linkage Group IV

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 – 506506Histone acetyltransferase esa-1PRO_0000051559Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei320 – 3201N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

Autoacetylation at Lys-320 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

STRINGi5141.NCU05218.1.

Structurei

3D structure databases

ProteinModelPortaliQ7S9B6.
SMRiQ7S9B6. Positions 220-495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini220 – 494275MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni361 – 3655Acetyl-CoA bindingBy similarity
Regioni370 – 3767Acetyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi303 – 32422ESA1-RPD3 motifBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi90 – 12132Lys-richAdd
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.
InParanoidiQ7S9B6.
KOiK11304.
OMAiDVTPFMY.
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.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7S9B6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPPGGDATV GSDEKRQKGK ATPDTIKMGC IAMVMKEGQL RRAEILSIKD
60 70 80 90 100
TKSGRQFYCN FDNFNKRLDE WVPAARIDFE QDVEWPNPDK DKQKDAKTKK
110 120 130 140 150
NNSTVSKKQP SKKNNQKKAS KREQSVASDG QTPHPWTEFV ESQPGKNNRQ
160 170 180 190 200
RGKTEDGTDV NASLEVGGDK GVKRKADEID MDEDEIPAAK KQRQPSFSRE
210 220 230 240 250
QEIEKLRTSG SMTQNPTEIS RIRNISKVEF GRYVLFPWYF SPYPQIFDQE
260 270 280 290 300
DCIYICEFCL SYYGELKSFV RHRQKCTLHH PPGNEIYRDD YVSFFEIDGR
310 320 330 340 350
RQRTWCRNLC LLSKMFLDHK TLYYDVDPFL FYVMTTRDDR GCHIIGYFSK
360 370 380 390 400
EKESTDGYNV ACILTLPQYQ RKGYGRLLIQ FSYELSKIEG KLGSPEKPLS
410 420 430 440 450
DLGLLSYRQY WSENIIDILL GYNERKEACT IENIAVALAM TTQDVEHTLQ
460 470 480 490 500
ALKMQVYHKG EHKIVVPEKL IKQREKSKAK QKRLIDPERI QWKPPVFTAL

NRTWGW
Length:506
Mass (Da):58,807
Last modified:December 15, 2003 - v1
Checksum:i53A62414D139674A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CM002239 Genomic DNA. Translation: EAA32981.1.
RefSeqiXP_962217.1. XM_957124.1.

Genome annotation databases

EnsemblFungiiEFNCRT00000004956; EFNCRP00000004952; EFNCRG00000004950.
GeneIDi3878365.
KEGGincr:NCU05218.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CM002239 Genomic DNA. Translation: EAA32981.1 .
RefSeqi XP_962217.1. XM_957124.1.

3D structure databases

ProteinModelPortali Q7S9B6.
SMRi Q7S9B6. Positions 220-495.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5141.NCU05218.1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFNCRT00000004956 ; EFNCRP00000004952 ; EFNCRG00000004950 .
GeneIDi 3878365.
KEGGi ncr:NCU05218.

Phylogenomic databases

eggNOGi COG5027.
HOGENOMi HOG000182457.
InParanoidi Q7S9B6.
KOi K11304.
OMAi DVTPFMY.
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.
PROSITEi PS51726. MYST_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiESA1_NEUCR
AccessioniPrimary (citable) accession number: Q7S9B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 15, 2003
Last modified: October 29, 2014
This is version 74 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