ID B2ASN1_PODAN Unreviewed; 513 AA. AC B2ASN1; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 08-JUN-2016, entry version 49. DE RecName: Full=Histone acetyltransferase {ECO:0000256|RuleBase:RU361211}; DE EC=2.3.1.48 {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; OC Sordariomycetes; Sordariomycetidae; Sordariales; Lasiosphaeriaceae; OC Podospora. 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., RA Porcel B.M., Couloux A., Aury J.-M., Segurens B., Poulain J., RA Anthouard V., Grossetete S., Khalili H., Coppin E., RA Dequard-Chablat M., Picard M., Contamine V., Arnaise S., Bourdais A., RA Berteaux-Lecellier V., Gautheret D., de Vries R.P., Battaglia E., RA Coutinho P.M., Danchin E.G.J., Henrissat B., El Khoury R., RA 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 RT 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: Acetyl-CoA + [histone] = CoA + acetyl- CC [histone]. {ECO:0000256|RuleBase:RU361211}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}. CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. CC {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 ProteinModelPortal; B2ASN1; -. DR SMR; B2ASN1; 227-502. DR STRING; 515849.XP_001906733.1; -. DR EnsemblFungi; CAP67404; CAP67404; PODANS_1_24050. DR GeneID; 6190909; -. DR KEGG; pan:PODANSg3766; -. DR eggNOG; KOG2747; Eukaryota. DR eggNOG; COG5027; LUCA. DR KO; K11304; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR016197; Chromodomain-like. DR InterPro; IPR002717; HAT_MYST-type. DR InterPro; IPR025995; Tudor-knot. DR Pfam; PF01853; MOZ_SAS; 1. DR Pfam; PF11717; Tudor-knot; 1. DR SUPFAM; SSF54160; SSF54160; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51726; MYST_HAT; 1. PE 3: Inferred from homology; KW Nucleus {ECO:0000256|RuleBase:RU361211}. FT DOMAIN 227 501 MYST-type HAT (histone FT acetyltransferase). {ECO:0000259|PROSITE: FT PS51726}. FT ACT_SITE 403 403 Proton donor/acceptor. FT {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 //