ID S3C7P9_OPHP1 Unreviewed; 517 AA. AC S3C7P9; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-APR-2021, entry version 36. DE RecName: Full=Histone acetyltransferase type B catalytic subunit {ECO:0000256|ARBA:ARBA00021268, ECO:0000256|PIRNR:PIRNR038084}; DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|PIRNR:PIRNR038084}; GN ORFNames=F503_04424 {ECO:0000313|EMBL:EPE08837.1}; OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma. OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE08837.1, ECO:0000313|Proteomes:UP000016923}; RN [1] {ECO:0000313|EMBL:EPE08837.1, ECO:0000313|Proteomes:UP000016923} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE08837.1, RC ECO:0000313|Proteomes:UP000016923}; RX PubMed=23725015; DOI=10.1186/1471-2164-14-373; RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R., RA Robertson G., Birol I., Bohlmann J., Breuil C.; RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and RT a comparison with the bark beetle-associated pine pathogen Grosmannia RT clavigera."; RL BMC Genomics 14:373-373(2013). CC -!- FUNCTION: Catalytic component of the histone acetylase B (HAT-B) CC complex. Has intrinsic substrate specificity that modifies lysine in CC recognition sequence GXGKXG. Involved in DNA double-strand break CC repair. {ECO:0000256|PIRNR:PIRNR038084}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000256|ARBA:ARBA00000780, CC ECO:0000256|PIRNR:PIRNR038084}; 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:0000256|PIRNR:PIRNR038084}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR038084}. CC Nucleus {ECO:0000256|PIRNR:PIRNR038084}. CC -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000256|ARBA:ARBA00010543, CC ECO:0000256|PIRNR:PIRNR038084}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KE148148; EPE08837.1; -; Genomic_DNA. DR STRING; 61273.S3C7P9; -. DR EnsemblFungi; EPE08837; EPE08837; F503_04424. DR eggNOG; KOG2696; Eukaryota. DR HOGENOM; CLU_036024_2_1_1; -. DR OrthoDB; 708105at2759; -. DR Proteomes; UP000016923; Unassembled WGS sequence. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC. 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:UniProtKB-UniRule. DR GO; GO:0006348; P:chromatin silencing at telomere; IEA:UniProtKB-UniRule. DR Gene3D; 3.90.360.10; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR019467; Hat1_N. DR InterPro; IPR037113; Hat1_N_sf. DR InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su. DR PANTHER; PTHR12046; PTHR12046; 1. DR Pfam; PF10394; Hat1_N; 1. DR PIRSF; PIRSF038084; HAT-B_cat; 1. DR SUPFAM; SSF55729; SSF55729; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, KW ECO:0000256|PIRNR:PIRNR038084}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR038084}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW Nucleus {ECO:0000256|PIRNR:PIRNR038084}; KW Reference proteome {ECO:0000313|Proteomes:UP000016923}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038084}. FT DOMAIN 8..165 FT /note="Hat1_N" FT /evidence="ECO:0000259|Pfam:PF10394" FT REGION 381..414 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 486..517 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 454..474 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 298 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR038084-1" FT SITE 181 FT /note="Interaction with histone H4 N-terminus" FT /evidence="ECO:0000256|PIRSR:PIRSR038084-3" SQ SEQUENCE 517 AA; 58045 MW; B86FFD5BD7F0A356 CRC64; MEHSYDEWVS NANEAVEISL VQPAPSGLRS IASFNPKFTY SIFGNEETIF GYQDLKISLR YHASDMRPNL HVSSSKKMKV VGENEPVDIP AILKDFLPPV AFQKASEFED AVKQTPAADY TPPGERIKEF YSSDGRYEIW KGTLSDPAVK QLVSRVQIMV PFFIEGGTFI GSDDSESADR WTIFFLYRTR QSSGSADRYE HEFAGYSTVY RFLLPLGAAT PPRTVANGES AAETAELQLP ASDSGEPEFS LATLPCRSRI SQFIILPPFQ GKGNAGRLYS TIFDEYLAEP QTTEITVEDP NEAFDDLRDI ADLKFLSRLP AFTKTVSINK TVQIPRTGPS PNNIVDASAL DTLRYQAKIA PRQFNRAVEM YLMQKLAPAV RPTLEGDEDE EEEEEDERAA ARTAANGKGK APAMPALATK EQQHEYRLWR MFVKQRLYRH NKEILGQLDR SQRIEKLEET LRSVELEYAR ILSMFESRTK LATVEEAQST ATKRKLTTEA GAEVAQNGSK KARIEDA //