ID HAT1_EMENI Reviewed; 496 AA. AC Q5AZR6; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Histone acetyltransferase type B catalytic subunit; DE EC=2.3.1.48; GN Name=hat1; ORFNames=AN6214; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC 4; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., RA Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., RA Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., RA Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., RA Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., RA Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., RA Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., RA Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., RA Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). 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; AACD01000105; EAA58000.1; -; Genomic_DNA. DR RefSeq; XP_663818.1; -. DR GeneID; 2870802; -. DR KEGG; ani:AN6214.2; -. DR BRENDA; 2.3.1.48; 3859. 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 1 496 Histone acetyltransferase type B FT catalytic subunit. FT /FTId=PRO_0000227722. SQ SEQUENCE 496 AA; 57779 MW; 92441200489692C4 CRC64; MSAEGEWSCD ANDAVQITIV HPDQQKPKTL SSFHPQFTYP IFGEEERIFG YKGLIIRLRF AAHNLRPHVH VSYDEKFTAV DDAEPVDIIG ALKEFLPEEA FSSLPEFESA VQEEDAKEFV PPGKLSHSYS IRGRNYEIWA ASLADPQVQL LLNRFQIMVS FYIEAGTPLS TDDPEWTLDR WTVYFVLTAA RYEKVEPPTP TASSYSIVGY ATTYRWWFYK RDRSENPMPR DGPFPPPELV RPGELPSRLR IAQFLILPPH QGTGHGVNLY NTIHKTCLDD PTIMELTVED PNESFDVLRD SADYHILRPE FLKHNIQINP DPWSDFSKKT KRVPTSSLLP LKTLNEIRTA YKIEPTQFAH IQEMFLLGQI PLKNRRKGGA NMARLLVKKY RDDDPNNRRY YWWRMLTKQR LYKRSRDVLI QLKMSERHKA LEDTVTNVED GYEQLFGFFN EREERLRAQQ EEAETSNNRD QRTKRKFTVE DEDDEDESAA AKRPKA //