ID HAT1_GIBZE Reviewed; 478 AA. AC Q4I6A4; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Histone acetyltransferase type B catalytic subunit; DE EC=2.3.1.48; GN Name=HAT1; ORFNames=FG07254; OS Gibberella zeae (Fusarium graminearum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae; OC Gibberella. OX NCBI_TaxID=5518; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PH-1 / NRRL 31084; RX PubMed=17823352; DOI=10.1126/science.1143708; RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., RA Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., RA Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., RA Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J., RA Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., RA Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., RA Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., RA Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.; RT "The Fusarium graminearum genome reveals a link between localized RT polymorphism and pathogen specialization."; RL Science 317:1400-1402(2007). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACM01000303; EAA77852.1; -; Genomic_DNA. DR RefSeq; XP_387430.1; -. DR GeneID; 2788834; -. DR KEGG; fgr:FG07254.1; -. DR BRENDA; 2.3.1.48; 74326. 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; Cytoplasm; DNA damage; KW DNA repair; Nucleus; Transferase. FT CHAIN 1 478 Histone acetyltransferase type B FT catalytic subunit. FT /FTId=PRO_0000227724. SQ SEQUENCE 478 AA; 54501 MW; F84A44346A28CF0D CRC64; MEDTTQLLTF FKGLSDASTA IHISLVSPSE SGLQHVATFN PRHTYSIFGD DEKIFGYQDL KVNLRYRAND MRPHLNISYS KKSGTINELE PTDVAAILDE GNHLPKTRDF EESSKQLSDD WTPPGKLHTT FDSPEGQYEI WCGNLADPAV KQLNSRLQIF VPLFIEGGTY IGQDPDEDSA ELDLSDADRW TFFSLYQKRK VGDKTAYVFV GYSTIYRFYY FQPPTPPASP QSDEWELPNG NMDLGELPCR TRLSQFIILP PFQGKGNGAR LYKTIFEHYH KIPQTYEFTV EDPNEAFDDL RDICDLQFLR KMPEFNNLLV DTNIKIPKKG FLPKLIIGSS LLEEIRLRAK IAPRQFGRVL EMHLMSKLPV SVRPTMAIED QPAATKADQH EAKVWGLIVK QRLYRHNKEV LSQIEPAERV EKLDDTLHGV GLEYARILAA VDRSDKYEGQ TTASSKRKLD ADEITEDLSN KKARVEDA //