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Q750F5

- HAT1_ASHGO

UniProt

Q750F5 - HAT1_ASHGO

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Protein

Histone acetyltransferase type B catalytic subunit

Gene

HAT1

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.By similarity

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei173 – 1731Interaction with histone H4 N-terminusBy similarity
Active sitei254 – 2541Proton donor/acceptorBy similarity

GO - Molecular functioni

  1. histone acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. chromatin silencing at telomere Source: InterPro
  2. DNA repair Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase type B catalytic subunit (EC:2.3.1.48By similarity)
Gene namesi
Name:HAT1
Ordered Locus Names:AGL001W
OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Taxonomic identifieri284811 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
ProteomesiUP000000591: Chromosome VII

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. histone acetyltransferase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Histone acetyltransferase type B catalytic subunitPRO_0000227716Add
BLAST

Interactioni

Subunit structurei

Component of the HAT-B complex composed of at least HAT1 and HAT2. The HAT-B complex binds to histone H4 tail (By similarity).By similarity

Protein-protein interaction databases

STRINGi33169.AGOS_AGL001W.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 1953Interaction with histone H4 N-terminusBy similarity
Regioni219 – 2213Acetyl-CoA bindingBy similarity
Regioni226 – 2327Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Belongs to the HAT1 family.Curated

Phylogenomic databases

eggNOGiNOG326277.
HOGENOMiHOG000074728.
InParanoidiQ750F5.
KOiK11303.
OrthoDBiEOG7HTHSD.

Family and domain databases

Gene3Di1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]
PANTHERiPTHR12046. PTHR12046. 1 hit.
PfamiPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.

Sequencei

Sequence statusi: Complete.

Q750F5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEELKPELW TTSSNSALKL SLVNDENAVQ FSPIFTYPIF GQAEQLFGYQ
60 70 80 90 100
DLNILLAFDS VTFKPFLNIK YTKKLERGLD DVEGSILKFL PEGDVILKDE
110 120 130 140 150
VEWVDAFNGE REKFALPNSE SKVAEYTSGG ESFAIFKVHL SDPNIRQLHR
160 170 180 190 200
RMQIFTLLFI EAASYIDEDD SAWDIFMTFN TSTRQCIGYT TTYKHWRYIN
210 220 230 240 250
GQEFDSSEKT TKRAKISQFI IFPPYQSKSH GSHLYSAAID VWSKEEKISE
260 270 280 290 300
VTVEDPNEAF DDLRDRCDFM RLSGSGLSSS IPEDVPIPRT WLTEQARKYK
310 320 330 340 350
LSLVQFTRLV EMILLYDNSP NFEIQVKARL YQKNHEVLTG MDSDTRKAKL
360 370 380 390
QEAFTSLKED YARILQKVPN RRRVLPSDEE NAGESKRHKK E
Length:391
Mass (Da):45,208
Last modified:January 9, 2013 - v2
Checksum:iFC2A69642885E61D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016820 Genomic DNA. Translation: AAS54489.2.
RefSeqiNP_986665.2. NM_211727.2.

Genome annotation databases

GeneIDi4622964.
KEGGiago:AGOS_AGL001W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016820 Genomic DNA. Translation: AAS54489.2 .
RefSeqi NP_986665.2. NM_211727.2.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 33169.AGOS_AGL001W.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 4622964.
KEGGi ago:AGOS_AGL001W.

Phylogenomic databases

eggNOGi NOG326277.
HOGENOMi HOG000074728.
InParanoidi Q750F5.
KOi K11303.
OrthoDBi EOG7HTHSD.

Family and domain databases

Gene3Di 1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view ]
PANTHERi PTHR12046. PTHR12046. 1 hit.
Pfami PF10394. Hat1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF038084. HAT-B_cat. 1 hit.
SUPFAMi SSF55729. SSF55729. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
    Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
    Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
  2. "Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
    Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
    G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 312.
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Entry informationi

Entry nameiHAT1_ASHGO
AccessioniPrimary (citable) accession number: Q750F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 9, 2013
Last modified: October 29, 2014
This is version 71 of the entry and version 2 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