ID   HAT2_ASHGO              Reviewed;         423 AA.
AC   Q75C99;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Histone acetyltransferase type B subunit 2;
GN   Name=HAT2; OrderedLocusNames=ACR017W;
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.
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: Regulatory subunit of the histone acetylase B (HAT-B)
CC       complex. The complex acetylates 'Lys-12' of histone H4 which is
CC       required for telomeric silencing. {ECO:0000250|UniProtKB:P39984}.
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.
CC       {ECO:0000250|UniProtKB:P39984}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016816; AAS51244.1; -; Genomic_DNA.
DR   RefSeq; NP_983420.1; NM_208773.1.
DR   AlphaFoldDB; Q75C99; -.
DR   SMR; Q75C99; -.
DR   STRING; 33169.AAS51244; -.
DR   PRIDE; Q75C99; -.
DR   EnsemblFungi; AAS51244; AAS51244; AGOS_ACR017W.
DR   GeneID; 4619545; -.
DR   KEGG; ago:AGOS_ACR017W; -.
DR   eggNOG; KOG0264; Eukaryota.
DR   HOGENOM; CLU_020445_3_1_1; -.
DR   InParanoid; Q75C99; -.
DR   OMA; PHEEGCL; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0033698; C:Rpd3L complex; IBA:GO_Central.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; IBA:GO_Central.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR022052; Histone-bd_RBBP4_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF12265; CAF1C_H4-bd; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW   WD repeat.
FT   CHAIN           1..423
FT                   /note="Histone acetyltransferase type B subunit 2"
FT                   /id="PRO_0000227732"
FT   REPEAT          138..174
FT                   /note="WD 1"
FT   REPEAT          175..224
FT                   /note="WD 2"
FT   REPEAT          228..268
FT                   /note="WD 3"
FT   REPEAT          271..311
FT                   /note="WD 4"
FT   REPEAT          315..355
FT                   /note="WD 5"
FT   REPEAT          372..412
FT                   /note="WD 6"
FT   REGION          357..361
FT                   /note="Interaction with the histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:P39984"
FT   SITE            288
FT                   /note="Important for interaction with HAT1"
FT                   /evidence="ECO:0000250|UniProtKB:P39984"
SQ   SEQUENCE   423 AA;  46854 MW;  56AA85D269F99CF5 CRC64;
     MTTKLKGLKE LGNTSDPLRT VSYQVRTKMS DYEDDNTDVQ SLTVEEEYEL WNSNVPVMYE
     FVSETKLTWP SLTIQWLPSD GQSPEQSLIF GTHTAGEEVN YLKVATINLP AGIAGLDQGD
     EEDEANDHSS FAIANKFPHI EEVIRARYMP ANSNIIATIN GKGTISIFDR TLEESKAQVS
     TLAFHKENGY GLAFNPHISG ELLSGSDDTT VALWDIEAAK KPKSILTSHD DIVNDVKWHE
     FESNVFGTVS EDKTLQVHDK RVRLEPVKKL PTASPFNTLS FSKHSRNLLA AAGVDSQIYL
     YDMRDMSSPL HVMSGHQDSV TTVEFSPHTD GIICSSGSDR RAIIWDLTQI GAEQSQDDAD
     DGAPELMMMH AGHRSPVNEF SFNPQIPWLL ASTEEDNVIQ AWKVSMKLVN ASPPAISDPS
     LLV