ID B2ASN1_PODAN Unreviewed; 513 AA. AC B2ASN1; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 24-JAN-2024, entry version 84. 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 -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)- CC (2E)-butenoyl-L-lysyl-[protein]; 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] = CoA + H(+) + CC N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180, CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780, CC ChEBI:CHEBI:144968; 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=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, CC Rhea:RHEA-COMP:11338, 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:ARBA00024456}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; CC Evidence={ECO:0000256|ARBA:ARBA00024456}; 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|RuleBase:RU361211}; 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; 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:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA. DR GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:RHEA. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR CDD; cd04301; NAT_SF; 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; 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 Activator {ECO:0000256|ARBA:ARBA00023159}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204}; KW Nucleus {ECO:0000256|RuleBase:RU361211}; 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 //