ID   HAT2_ASPOR              Reviewed;         436 AA.
AC   Q2UA71;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Histone acetyltransferase type B subunit 2;
GN   Name=hat2; ORFNames=AO090102000516;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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}.
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DR   EMBL; AP007162; BAE61544.1; -; Genomic_DNA.
DR   RefSeq; XP_001822677.1; XM_001822625.2.
DR   AlphaFoldDB; Q2UA71; -.
DR   SMR; Q2UA71; -.
DR   STRING; 510516.Q2UA71; -.
DR   EnsemblFungi; BAE61544; BAE61544; AO090102000516.
DR   GeneID; 5994722; -.
DR   KEGG; aor:AO090102000516; -.
DR   VEuPathDB; FungiDB:AO090102000516; -.
DR   HOGENOM; CLU_020445_3_1_1; -.
DR   OMA; PHEEGCL; -.
DR   Proteomes; UP000006564; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
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; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
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..436
FT                   /note="Histone acetyltransferase type B subunit 2"
FT                   /id="PRO_0000227734"
FT   REPEAT          136..176
FT                   /note="WD 1"
FT   REPEAT          187..227
FT                   /note="WD 2"
FT   REPEAT          237..277
FT                   /note="WD 3"
FT   REPEAT          284..324
FT                   /note="WD 4"
FT   REPEAT          328..368
FT                   /note="WD 5"
FT   REPEAT          385..425
FT                   /note="WD 6"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..374
FT                   /note="Interaction with the histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:P39984"
FT   COMPBIAS        1..21
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  48983 MW;  7AD4493166876F66 CRC64;
     MEPYDDGFIE EQEEQEEERT EEKVINEEYK TWKKNAPFLY DMILSTALEW PTLTTQWLPD
     KQEVPDKPYS THRLLLGTHT SSDAQNYLQI AHVQLPNPSA PNPDDYDEER GEIGGYGGSS
     KKAPMEIKFN IVQKIDHKGE VNKARYQPQN PNVIATMCTD GRVMIWDRSK HPSLPTGTVN
     PQMELLGHTK EGFGLSWSPH TAGHLVTGSE DKTVRLWDLT TYTKGNKALK PSRTYTHHSS
     IVNDVQYHPL HSSLIGTVSD DITLQILDIR EAETTRAAAS AEGQHRDAIN AIAFNPAAET
     VLATGSADKS IGLWDLRNLK TKLHTLECHT DSVTSLSWHP FEESVLASAS YDRKIMFWDL
     SRSGEEQTPD DAQDGPPELL FMHGGHTNRI SDFSWNLNDP WVLCSAAEDN LLQVWKVADA
     IVGKDLEDVP TEELEA