ID   HAT2_NEUCR              Reviewed;         446 AA.
AC   Q7S7N3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Histone acetyltransferase type B subunit 2;
GN   Name=hat-2; ORFNames=NCU06679;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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 hat-1 and
CC       hat-2. 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; CM002240; EAA31758.2; -; Genomic_DNA.
DR   RefSeq; XP_960994.2; XM_955901.3.
DR   AlphaFoldDB; Q7S7N3; -.
DR   SMR; Q7S7N3; -.
DR   STRING; 5141.EFNCRP00000006678; -.
DR   EnsemblFungi; EAA31758; EAA31758; NCU06679.
DR   GeneID; 3877141; -.
DR   KEGG; ncr:NCU06679; -.
DR   VEuPathDB; FungiDB:NCU06679; -.
DR   HOGENOM; CLU_020445_3_2_1; -.
DR   InParanoid; Q7S7N3; -.
DR   OMA; PHEEGCL; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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   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; 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..446
FT                   /note="Histone acetyltransferase type B subunit 2"
FT                   /id="PRO_0000227742"
FT   REPEAT          138..178
FT                   /note="WD 1"
FT   REPEAT          189..229
FT                   /note="WD 2"
FT   REPEAT          231..270
FT                   /note="WD 3"
FT   REPEAT          286..326
FT                   /note="WD 4"
FT   REPEAT          330..370
FT                   /note="WD 5"
FT   REPEAT          387..427
FT                   /note="WD 6"
FT   REGION          372..376
FT                   /note="Interaction with the histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:P39984"
FT   REGION          427..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  50400 MW;  CBCF5435B80CF239 CRC64;
     MARDEIVDDV DVNMEEDDAE AEQRLINEEY KIWKKNSPFL YDMMLSTALE WPTLTTQWFP
     DVKNPKDKSH TVHRLLLGTH TAEGKPNYLQ IAEVEIPKMV ELNPRDYDEE RGEIGGYGSK
     ASSGEPLCIR FKITQKIDHP GEVNKARYQP QNPDIIATLA VDGRVLIFDR TKHSITPSGT
     PSPQLELIGH KEEGFGLNWN PHEEGCLVTG SEDKTVLLWD LKTYEGTSKQ LKYSRKYTHH
     SHIVNDVQHH PLVKSWIGTV SDDLTLQIID VRRPETDKAA IVARNGHSDA INALAFNPRV
     ETIIATASAD KTIGIWDMRN MKSKVHTLEG HQDAVTSLEW HPTESAILGS GSYDRRLLFW
     DISRVGDEQT QDDAEDGPPE LLFMHGGHTN HLADFSWNRN DPWLVCSAAE DNLLQIWKVA
     NSIVSKEPAD MSTPELDDPK PKQSSH