(data stored in ACNUC7421 zone)

SWISSPROT: HAT1_ASHGO

ID   HAT1_ASHGO              Reviewed;         391 AA.
AC   Q750F5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q12341};
GN   Name=HAT1; OrderedLocusNames=AGL001W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 312.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Catalytic component of the histone acetylase B (HAT-B)
CC       complex. Acetylates 'Lys-12' of histone H4 which is required for
CC       telomeric silencing. Has intrinsic substrate specificity that modifies
CC       lysine in recognition sequence GXGKXG. Involved in DNA double-strand
CC       break repair. {ECO:0000250|UniProtKB:Q12341}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000250|UniProtKB:Q12341};
CC   -!- SUBUNIT: Component of the HAT-B complex composed of at least HAT1 and
CC       HAT2. The HAT-B complex binds to histone H4 tail (By similarity).
CC       {ECO:0000250|UniProtKB:Q12341}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
DR   EMBL; AE016820; AAS54489.2; -; Genomic_DNA.
DR   RefSeq; NP_986665.2; NM_211727.2.
DR   SMR; Q750F5; -.
DR   STRING; 33169.AAS54489; -.
DR   EnsemblFungi; AAS54489; AAS54489; AGOS_AGL001W.
DR   GeneID; 4622964; -.
DR   KEGG; ago:AGOS_AGL001W; -.
DR   HOGENOM; HOG000074728; -.
DR   InParanoid; Q750F5; -.
DR   KO; K11303; -.
DR   OMA; YEYYAYP; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0010485; F:H4 histone acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR   Gene3D; 3.90.360.10; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR019467; Hat1_N.
DR   InterPro; IPR037113; Hat1_N_sf.
DR   InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su.
DR   PANTHER; PTHR12046; PTHR12046; 1.
DR   Pfam; PF10394; Hat1_N; 1.
DR   PIRSF; PIRSF038084; HAT-B_cat; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750F5.
DR   SWISS-2DPAGE; Q750F5.
KW   Acyltransferase; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW   Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..391
FT                   /note="Histone acetyltransferase type B catalytic subunit"
FT                   /id="PRO_0000227716"
FT   REGION          193..195
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   REGION          219..221
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   REGION          226..232
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   ACT_SITE        254
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q12341"
FT   SITE            173
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
SQ   SEQUENCE   391 AA;  45208 MW;  FC2A69642885E61D CRC64;
     MAEELKPELW TTSSNSALKL SLVNDENAVQ FSPIFTYPIF GQAEQLFGYQ DLNILLAFDS
     VTFKPFLNIK YTKKLERGLD DVEGSILKFL PEGDVILKDE VEWVDAFNGE REKFALPNSE
     SKVAEYTSGG ESFAIFKVHL SDPNIRQLHR RMQIFTLLFI EAASYIDEDD SAWDIFMTFN
     TSTRQCIGYT TTYKHWRYIN GQEFDSSEKT TKRAKISQFI IFPPYQSKSH GSHLYSAAID
     VWSKEEKISE VTVEDPNEAF DDLRDRCDFM RLSGSGLSSS IPEDVPIPRT WLTEQARKYK
     LSLVQFTRLV EMILLYDNSP NFEIQVKARL YQKNHEVLTG MDSDTRKAKL QEAFTSLKED
     YARILQKVPN RRRVLPSDEE NAGESKRHKK E
//

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