HAT2_USTMA
ID HAT2_USTMA Reviewed; 433 AA.
AC Q4P553; A0A0D1CIB0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Histone acetyltransferase type B subunit 2;
GN Name=HAT2; ORFNames=UMAG_11999;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003156; KIS66698.1; -; Genomic_DNA.
DR RefSeq; XP_011391769.1; XM_011393467.1.
DR AlphaFoldDB; Q4P553; -.
DR SMR; Q4P553; -.
DR STRING; 5270.UM04760P0; -.
DR EnsemblFungi; KIS66698; KIS66698; UMAG_11999.
DR GeneID; 23567792; -.
DR KEGG; uma:UMAG_11999; -.
DR VEuPathDB; FungiDB:UMAG_11999; -.
DR eggNOG; KOG0264; Eukaryota.
DR HOGENOM; CLU_020445_3_1_1; -.
DR InParanoid; Q4P553; -.
DR OrthoDB; 831322at2759; -.
DR Proteomes; UP000000561; Chromosome 17.
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; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
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..433
FT /note="Histone acetyltransferase type B subunit 2"
FT /id="PRO_0000227744"
FT REPEAT 134..174
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 187..227
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 237..277
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 282..322
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 326..366
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 383..433
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REGION 368..372
FT /note="Interaction with the histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:P39984"
SQ SEQUENCE 433 AA; 48169 MW; 545821C55F77933A CRC64;
MDASDFVEDE AAIAQQKLSN EEYKIWKKNS PFLYDLVVTH ALEWPSLTCQ WLPDKESPAG
QSYTQHRLLL GTHTSGQDQN YLQFAQVQLP TTGADGASNS AESRLDLKQY DEDKGEIGSY
SATTARLSIV QKINHDGEIN RARYCPQNCD LIATRSVTGK TYIFDRTKHS NTPSADGVCR
PDIILEGQHK EGYGLSWSPL KQGHILAASE DTTVCHWDIN NYTKPNNTLQ PSATYTGHTA
IVEDVAWHNH HESLFGSVGD DRQLLIWDIR EPASAPKYRV EAHTGEVNAL AFSPENENIL
VTGSSDKSVG VWDLRNLKVK LHSLESHTDE ILSVCWSPHH ATVLASASAD RRVNLWDLSK
IGQEQTPDDA EDGPPELIFV HGGHTSRPTD LAWSPHMEWA LTSAAEDNIV MVWRPSKAVI
DTGNEELTPD DLE
