ID   HAT1_USTMA              Reviewed;         448 AA.
AC   Q4PBE6;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE            EC=2.3.1.48;
GN   Name=HAT1; ORFNames=UM02567;
OS   Ustilago maydis (Smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=5270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   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.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
CC   -!- FUNCTION: Catalytic component of the histone acetylase B (HAT-B)
CC       complex. Acetylates 'Lys-12' of histone H4 which is required for
CC       telomeric silencing. Has intrinsic substrate specificity that
CC       modifies lysine in recognition sequence GXGKXG. Involved in DNA
CC       double-strand break repair (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
CC   -!- SUBUNIT: Component of the HAT-B complex composed of at least HAT1
CC       and HAT2. The HAT-B complex binds to histone H4 tail (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the HAT1 family.
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DR   EMBL; AACP01000086; EAK83737.1; -; Genomic_DNA.
DR   RefSeq; XP_758714.1; -.
DR   GeneID; 3630647; -.
DR   KEGG; uma:UM02567.1; -.
DR   OMA; Q4PBE6; AETIYGY.
DR   BRENDA; 2.3.1.48; 2320.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR019467; Hat1_N.
DR   InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su.
DR   Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
DR   Pfam; PF10394; Hat1_N; 1.
DR   PIRSF; PIRSF038084; HAT-B_cat; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Chromatin regulator; Complete proteome; Cytoplasm;
KW   DNA damage; DNA repair; Nucleus; Transferase.
FT   CHAIN         1    448       Histone acetyltransferase type B
FT                                catalytic subunit.
FT                                /FTId=PRO_0000227727.
SQ   SEQUENCE   448 AA;  51083 MW;  4BBAE5DC8D52776A CRC64;
     MKDSWSSNST TSTAIRLVGS PYGTDSPFQP TFTYPIYGEA ETIYGYEGLA IKLSVASGSL
     VPLLEVTYRA KNEATTAEID DVEGKIKEFL APDFLSTSSP SAMEEFETVV KADKEFRPLG
     DKVHSYTRGK VDKGKAKSST ASLASSTLSA SDPNARVFEI YRSTWHTPGF REYHRRMQLF
     TLLFIEGASY IQEDETNWEF FTLYEKVSRD DKQTWHFMGY TSLYKFWCWP DSSRIRLSQF
     VILPPFQKQG HGGALYTTVY DQIRERANVT ELTVEDPSED FDRLRDGNDL RRLLAPGGFA
     DSAKAQNKLH APLDKEWIES QRLQHKLAPR QWSRVLEMVQ LMNLDTTDHE QVKQYRLQVK
     ARIYRQNKDI LMQLEKQQQR SKLQETFEGV VEEYGDMVGV DVEDLLDDGP SGTGALYGAD
     EEEDQEQGQG DRHYSNGNGP PRKMARLA
//