ID B2ASN1_PODAN Unreviewed; 513 AA. AC B2ASN1; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-NOV-2024, entry version 89. DE RecName: Full=Histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211}; DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211}; GN ORFNames=PODANS_1_24050 {ECO:0000313|EMBL:CAP67404.1}; OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) OS (Pleurage anserina). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora; OC Podospora anserina. OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP67404.1}; RN [1] {ECO:0000313|EMBL:CAP67404.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP67404.1}; RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77; RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M., RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V., RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M., RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D., RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B., RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H., RA Debuchy R., Wincker P., Weissenbach J., Silar P.; RT "The genome sequence of the model ascomycete fungus Podospora anserina."; RL Genome Biol. 9:R77.1-R77.22(2008). RN [2] {ECO:0000313|EMBL:CAP67404.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP67404.1}; RA Genoscope - CEA; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalytic component of the NuA4 histone acetyltransferase CC (HAT) complex which is involved in epigenetic transcriptional CC activation of selected genes principally by acetylation of nucleosomal CC histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 CC to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form CC H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. The NuA4 complex CC is involved in the DNA damage response and is required for chromosome CC segregation. The NuA4 complex plays a direct role in repair of DNA CC double-strand breaks (DSBs) through homologous recombination. CC Recruitment to promoters depends on H3K4me. Also acetylates non-histone CC proteins. In addition to protein acetyltransferase, can use different CC acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2- CC hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able CC to mediate protein 2-hydroxyisobutyrylation and crotonylation, CC respectively. {ECO:0000256|ARBA:ARBA00045805}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L- CC lysyl-[protein] + CoA + H(+); Xref=Rhea:RHEA:53908, Rhea:RHEA- CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, CC ChEBI:CHEBI:137954; Evidence={ECO:0000256|ARBA:ARBA00029286}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909; CC Evidence={ECO:0000256|ARBA:ARBA00029286}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2- CC hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+); CC Xref=Rhea:RHEA:24180, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:131780, ChEBI:CHEBI:144968; CC Evidence={ECO:0000256|ARBA:ARBA00029298}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181; CC Evidence={ECO:0000256|ARBA:ARBA00029298}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] CC + CoA + H(+); Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA- CC COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000256|ARBA:ARBA00024456}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; CC Evidence={ECO:0000256|ARBA:ARBA00024456}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] CC + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000256|RuleBase:RU361211}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] CC + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; CC Evidence={ECO:0000256|ARBA:ARBA00029280}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; CC Evidence={ECO:0000256|ARBA:ARBA00029280}; CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex. CC {ECO:0000256|ARBA:ARBA00011353}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}. CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. CC {ECO:0000256|ARBA:ARBA00010107, ECO:0000256|RuleBase:RU361211}. 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; CU633897; CAP67404.1; -; Genomic_DNA. DR RefSeq; XP_001906733.1; XM_001906698.1. DR AlphaFoldDB; B2ASN1; -. DR GeneID; 6190909; -. DR KEGG; pan:PODANSg3766; -. DR VEuPathDB; FungiDB:PODANS_1_24050; -. DR HOGENOM; CLU_011815_2_0_1; -. DR OrthoDB; 118560at2759; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IEA:TreeGrafter. DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA. DR GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:RHEA. DR GO; GO:0003712; F:transcription coregulator activity; IEA:TreeGrafter. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:TreeGrafter. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:TreeGrafter. DR CDD; cd04301; NAT_SF; 1. DR FunFam; 1.10.10.10:FF:000022; Histone acetyltransferase; 1. DR FunFam; 3.30.60.60:FF:000001; Histone acetyltransferase; 1. DR FunFam; 3.40.630.30:FF:000002; Histone acetyltransferase; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR002717; HAT_MYST-type. DR InterPro; IPR050603; MYST_HAT. DR InterPro; IPR025995; Tudor-knot. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR040706; Zf-MYST. DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10615:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1. DR Pfam; PF01853; MOZ_SAS; 1. DR Pfam; PF11717; Tudor-knot; 1. DR Pfam; PF17772; zf-MYST; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF54160; Chromo domain-like; 1. DR PROSITE; PS51726; MYST_HAT; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204}; KW Nucleus {ECO:0000256|RuleBase:RU361211}; KW Transcription {ECO:0000256|ARBA:ARBA00023015}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 227..501 FT /note="MYST-type HAT" FT /evidence="ECO:0000259|PROSITE:PS51726" FT REGION 92..200 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 92..112 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 150..165 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 403 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51" SQ SEQUENCE 513 AA; 59390 MW; E082CAA5C52D7478 CRC64; MSHGKRVSRQ QTLLCRDCSL FICVSHSWLA VLTSFDSAGC VAYVTKDGEP RRATILGIRE TKSGRQWYAN FDSFNKRLDE WVPQARINFD KEVEWPNPEK DKPKDPKSKK TTAATSKKSQ PSKKNQKRVS KREQSVASEG QTPHPWTEYV ENGQHKDKNQ ETEEKSMGSL EVGGTPGVLG PDEMEIDEDE TPAGAAKKDS LGPFSRQQEI EKLRTSGSMT QNPAEVSRIR NISQVEFGRY VLFPWYFSPY PEVFSQEESI FICEFCLSYY ADMKSFSRHR QKCTLQHPPG NEIYRDDFVS FFEIDGRRQR TWCRNLCLLS KMFLDHKTLY YDVDPFLFYV MTTRDERGCH LIGYFSKEKE STDGYNVACI LTLPQYQRKG YGRLLIQFSY ELSKIEGKLG SPEKPLSDLG LLSYRQYWSE NIIDLLLGFS ERDEKCTIET IAQHLAMTAT DVEHTLQALK MQVYHKGEHK IVLSDKLVEQ RAKSRAKQKR LIDPERIQWK PPVFTASSRT WGW //