ID B2AAV8_PODAN Unreviewed; 783 AA. AC B2AAV8; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111}; DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111}; GN ORFNames=PODANS_1_5330 {ECO:0000313|EMBL:CAP60220.1}; 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:CAP60220.1}; RN [1] {ECO:0000313|EMBL:CAP60220.1, ECO:0000313|Proteomes:UP000001197} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383 RC {ECO:0000313|Proteomes:UP000001197}, and S mat+ RC {ECO:0000313|EMBL:CAP60220.1}; 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:CAP60220.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP60220.1}; RA Genoscope - CEA; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000001197} RP GENOME REANNOTATION. RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383 RC {ECO:0000313|Proteomes:UP000001197}; RX PubMed=24558260; DOI=10.1534/genetics.113.159988; RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A., RA Couloux A., Wincker P., Debuchy R., Silar P.; RT "Maintaining two mating types: Structure of the mating type locus and its RT role in heterokaryosis in Podospora anserina."; RL Genetics 197:421-432(2014). RN [4] {ECO:0000313|EMBL:CDP22861.1} RP NUCLEOTIDE SEQUENCE. RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E., RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.; RT "Maintaining two mating types: Structure of the mating type locus and its RT role in heterokaryosis in Podospora anserina."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1 CC subfamily. {ECO:0000256|ARBA:ARBA00006457}. 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; CU633438; CAP60220.1; -; Genomic_DNA. DR EMBL; FO904936; CDP22861.1; -; Genomic_DNA. DR RefSeq; XP_001912738.1; XM_001912703.1. DR AlphaFoldDB; B2AAV8; -. DR STRING; 515849.B2AAV8; -. DR GeneID; 6196758; -. DR KEGG; pan:PODANSg09787; -. DR VEuPathDB; FungiDB:PODANS_1_5330; -. DR eggNOG; KOG1342; Eukaryota. DR HOGENOM; CLU_007727_0_1_1; -. DR OrthoDB; 1327607at2759; -. DR Proteomes; UP000001197; Chromosome 1. DR GO; GO:1902494; C:catalytic complex; IEA:UniProt. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt. DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC. DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt. DR CDD; cd10004; RPD3-like; 1. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR003084; His_deacetylse_1. DR InterPro; IPR023801; His_deacetylse_dom. DR InterPro; IPR037138; His_deacetylse_dom_sf. DR InterPro; IPR023696; Ureohydrolase_dom_sf. DR PANTHER; PTHR10625:SF13; HISTONE DEACETYLASE HDAC1; 1. DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PRINTS; PR01270; HDASUPER. DR PRINTS; PR01271; HISDACETLASE. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. PE 3: Inferred from homology; KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853}; KW Reference proteome {ECO:0000313|Proteomes:UP000001197}. FT DOMAIN 196..484 FT /note="Histone deacetylase" FT /evidence="ECO:0000259|Pfam:PF00850" FT REGION 545..603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 616..635 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 666..783 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 574..594 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 617..633 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 697..721 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 722..750 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 767..783 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 783 AA; 87632 MW; 90085EF360F56F60 CRC64; MDPLTSALSN LREPRRRRGI GELPSSLVAA AHGLSAEHQL FPHTQNGGAD FDSPTFLLSH GSERTYIKYE DDTRINLLNW PSHPGRAKLD WDSSRDPDPG FEPIPFCPPL LSPIRFLPSS REHEHHELDE LCETKETPPQ HTFSSIRFAT MSNSNSTDPA GVERTRPLFE VVKNDKKRVA YFYDSDIGNY AYVTGHPMKP HRIRLAHSLV MNYNVYKFLE IYRAKPAVTS EMTQFHTDEY IEFLQKVTPD NMDSFMREQG KYNVGDDCPV FDGLFEFCGI SAGGSMEGAA RLNREKCDIA INWAGGLHHA KKSEASGFCY VNDIVLAILE LLRFKKRVLY IDIDVHHGDG VEEAFYTTDR VMTVSFHKYG EYFPGTGELR DIGIGTGKHY AVNFPLRDGI DDVAYETIFE PVITNVMQYY QPEAVVLQCG GDSLSGDRLG CFNLSMRGHA NCVNFVRGFN LPTLVLGGGG YTMRNVARTW AYETGRLVGV EMDRVLPFNE YYEYYGPDYE LDVRNSNMEN ANSYEYLEKI KIQVIENLKR TAPVPSVQMQ DVPRQSMGVS DDQDDEMDDL DEDENKDVRM TQRQWEKRVE RQDEYEDSDD EDMAAANGVF KLNGRTRQET NFRDTKEDDT MEVDSGVATP AEQPVEITEN DDTMIDEALA EIAAEAEAEA QVKEPAATET APEAPTAAVD GDGDVDMGEV TESKAAETVI KTEDVEEPVP AKQDDSQSTA VVSPKKTTEV AAQPSRTSKS PEPAVAADKQ TESVPEASEV VPPTTTQDNT TNS //