ID   A0A1D9QFI4_SCLS1        Unreviewed;       778 AA.
AC   A0A1D9QFI4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN   ORFNames=sscle_11g083220 {ECO:0000313|EMBL:APA13552.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:APA13552.1, ECO:0000313|Proteomes:UP000177798};
RN   [1] {ECO:0000313|Proteomes:UP000177798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000177798};
RX   PubMed=28204478; DOI=10.1093/gbe/evx030;
RA   Derbyshire M., Denton-Giles M., Hegedus D., Seifbarghy S., Rollins J.,
RA   van Kan J., Seidl M.F., Faino L., Mbengue M., Navaud O., Raffaele S.,
RA   Hammond-Kosack K., Heard S., Oliver R.;
RT   "The complete genome sequence of the phytopathogenic fungus Sclerotinia
RT   sclerotiorum reveals insights into the genome architecture of broad host
RT   range pathogens.";
RL   Genome Biol. Evol. 9:593-618(2017).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events. {ECO:0000256|PIRNR:PIRNR037919}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037919};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR037919}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037919}.
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DR   EMBL; CP017824; APA13552.1; -; Genomic_DNA.
DR   RefSeq; XP_001591174.1; XM_001591124.1.
DR   AlphaFoldDB; A0A1D9QFI4; -.
DR   ESTHER; scls1-a7er46; Arb2_domain.
DR   GeneID; 5487188; -.
DR   KEGG; ssl:SS1G_07799; -.
DR   VEuPathDB; FungiDB:sscle_11g083220; -.
DR   OMA; FVSPACY; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000177798; Chromosome 11.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR019154; Arb2-like_domain.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR017321; Hist_deAcase_II_yeast.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF09757; Arb2; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037919};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037919};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037919};
KW   Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT   DOMAIN          108..433
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          486..745
FT                   /note="Arb2-like"
FT                   /evidence="ECO:0000259|Pfam:PF09757"
SQ   SEQUENCE   778 AA;  86463 MW;  00CD46E94AD14C76 CRC64;
     MDTLEPPLLQ PSSDLVMQLH DNLHGALING MLSNGNENGF VDPRVLISTE DAEIAYDNLE
     PDDEMDSSSS EDTKIIATPR KAYLPTGCCY DDRMKLHAIG DFSDNTPHPE DPRRIEAIMR
     AFKEAGLLYT GSPEDVDRIL KESPTKYMLR IPARVASKDE ICTVHYAGHF EWVESLSKKT
     SEDLRELNTI MDAGRKSLYV GLCTFEAALI SAGGAIETCK NVVEGHVKNA IAVIRPPGHH
     AEANESLGFC VFNNVPVAAK ICMLDYPKLC RKVLILDWDI HHGNGTQNMF YEDPNVLYIS
     LHVYENGNFY PGQPDDPDLP DGGIDKVGTG AGIGKNVNIG WPSQGMGDGE YMAAFQKIVM
     PIAQEFDPDL VIISAGFDAA AGDELGGCFV TPGCYSHMTH MLMSLAGGKV AVCLEGGYNL
     KAISRSALAV AKTLMGEPPI RQPIPPLNRV AAEVFEEVKY YQSPYWECMR SGVIDYKEAK
     FKGATRLDDI VRNYQSNVLS KNYQMVSLWV QRHQLARSFD HQVMVTPYIK SATRILLIVH
     DPPELLATPD PFTAKVELHN SYLVDPVTEY IAWAIENKIG VMDINIPLNT DTFPPATGGY
     NPRSGVFELE SQIQDLVGYI WDNFIQLYDS DNIILMGVGD SYLGIKQLLT IRDCRPRIAG
     VLAFITGSLR PVKSETDSTL SSWYKSNSEI YVADKHACWN DEESIRKVRK QRFGNVVRSE
     ETGLVKMLQR HQSSAKSWIL GKFEEKAKDD EVMTMEDEVS VADVDGAKKL TMGDMQLM
//

ID   A7ER46_SCLS1            Unreviewed;       778 AA.
AC   A7ER46;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN   ORFNames=SS1G_07799 {ECO:0000313|EMBL:EDN91938.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN91938.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events. {ECO:0000256|PIRNR:PIRNR037919}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037919};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR037919}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037919}.
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CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
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DR   EMBL; CH476630; EDN91938.1; -; Genomic_DNA.
DR   RefSeq; XP_001591174.1; XM_001591124.1.
DR   AlphaFoldDB; A7ER46; -.
DR   STRING; 665079.A7ER46; -.
DR   ESTHER; scls1-a7er46; Arb2_domain.
DR   GeneID; 5487188; -.
DR   KEGG; ssl:SS1G_07799; -.
DR   VEuPathDB; FungiDB:sscle_11g083220; -.
DR   InParanoid; A7ER46; -.
DR   OMA; FVSPACY; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR   GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR019154; Arb2-like_domain.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR017321; Hist_deAcase_II_yeast.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF09757; Arb2; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037919};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037919};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037919};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW   Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT   DOMAIN          108..433
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          486..745
FT                   /note="Arb2-like"
FT                   /evidence="ECO:0000259|Pfam:PF09757"
SQ   SEQUENCE   778 AA;  86463 MW;  00CD46E94AD14C76 CRC64;
     MDTLEPPLLQ PSSDLVMQLH DNLHGALING MLSNGNENGF VDPRVLISTE DAEIAYDNLE
     PDDEMDSSSS EDTKIIATPR KAYLPTGCCY DDRMKLHAIG DFSDNTPHPE DPRRIEAIMR
     AFKEAGLLYT GSPEDVDRIL KESPTKYMLR IPARVASKDE ICTVHYAGHF EWVESLSKKT
     SEDLRELNTI MDAGRKSLYV GLCTFEAALI SAGGAIETCK NVVEGHVKNA IAVIRPPGHH
     AEANESLGFC VFNNVPVAAK ICMLDYPKLC RKVLILDWDI HHGNGTQNMF YEDPNVLYIS
     LHVYENGNFY PGQPDDPDLP DGGIDKVGTG AGIGKNVNIG WPSQGMGDGE YMAAFQKIVM
     PIAQEFDPDL VIISAGFDAA AGDELGGCFV TPGCYSHMTH MLMSLAGGKV AVCLEGGYNL
     KAISRSALAV AKTLMGEPPI RQPIPPLNRV AAEVFEEVKY YQSPYWECMR SGVIDYKEAK
     FKGATRLDDI VRNYQSNVLS KNYQMVSLWV QRHQLARSFD HQVMVTPYIK SATRILLIVH
     DPPELLATPD PFTAKVELHN SYLVDPVTEY IAWAIENKIG VMDINIPLNT DTFPPATGGY
     NPRSGVFELE SQIQDLVGYI WDNFIQLYDS DNIILMGVGD SYLGIKQLLT IRDCRPRIAG
     VLAFITGSLR PVKSETDSTL SSWYKSNSEI YVADKHACWN DEESIRKVRK QRFGNVVRSE
     ETGLVKMLQR HQSSAKSWIL GKFEEKAKDD EVMTMEDEVS VADVDGAKKL TMGDMQLM
//