HAT2_CANGA
ID HAT2_CANGA Reviewed; 419 AA.
AC Q6FXI8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Histone acetyltransferase type B subunit 2;
GN Name=HAT2; OrderedLocusNames=CAGL0B03575g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Regulatory subunit of the histone acetylase B (HAT-B)
CC complex. The complex acetylates Lys-12 of histone H4 which is required
CC 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; CR380948; CAG58027.1; -; Genomic_DNA.
DR RefSeq; XP_445127.1; XM_445127.1.
DR AlphaFoldDB; Q6FXI8; -.
DR SMR; Q6FXI8; -.
DR STRING; 5478.XP_445127.1; -.
DR EnsemblFungi; CAG58027; CAG58027; CAGL0B03575g.
DR GeneID; 2886650; -.
DR KEGG; cgr:CAGL0B03575g; -.
DR CGD; CAL0127754; CAGL0B03575g.
DR VEuPathDB; FungiDB:CAGL0B03575g; -.
DR eggNOG; KOG0264; Eukaryota.
DR HOGENOM; CLU_020445_3_1_1; -.
DR InParanoid; Q6FXI8; -.
DR OMA; PITDFNW; -.
DR Proteomes; UP000002428; Chromosome B.
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:0004402; F:histone acetyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
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; 3.
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..419
FT /note="Histone acetyltransferase type B subunit 2"
FT /id="PRO_0000227736"
FT REPEAT 131..171
FT /note="WD 1"
FT REPEAT 177..217
FT /note="WD 2"
FT REPEAT 225..265
FT /note="WD 3"
FT REPEAT 267..307
FT /note="WD 4"
FT REPEAT 311..351
FT /note="WD 5"
FT REPEAT 368..408
FT /note="WD 6"
FT REGION 353..357
FT /note="Interaction with the histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:P39984"
FT SITE 284
FT /note="Important for interaction with HAT1"
FT /evidence="ECO:0000250|UniProtKB:P39984"
SQ SEQUENCE 419 AA; 47022 MW; 370A115B385B0283 CRC64;
MSVQLDPSAL QKMAEVAAAA EQQSNEPMTV DEEYELWKSN VPMLYDFVSE TRLTWPTLTV
EWLPQKNLVA ARTRQQLILG THTSGEEQNY LKIGAVDLPV EVTENSKKDR EIDEEDEDMV
LSNVKIVKKF PHDGEITRAR YMPQDDNIIA TINGEGKIFI YDRSKNGVEA LLSTLEYHTE
NGYGLAFNAN EKYSLLSGSD DSNIALWDIS NFEKNIKPTI TFEDAHTDII NDVKWHSSEA
HIFGSVSEDS TMKLFDKRSS QIIHNINTKK PYNTLAFSPF SSNLFAAAGT DNLVYLYDIR
DVSNPLYAMT GHEDAVTAIE FDPNNDGILY SSGSDRRTIV WDLQEIGAEQ TQDEIEDGPP
EVLMIHAGHK TSINDIAVNP NINWLVASAE EDNIVQIWKC SSNIPRIGGE PEVDLSILD
