ID A0A9P6IDV7_9PEZI Unreviewed; 1266 AA.
AC A0A9P6IDV7;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE SubName: Full=Histone deacetylase hos3 {ECO:0000313|EMBL:KAF9881738.1};
GN ORFNames=CkaCkLH20_00884 {ECO:0000313|EMBL:KAF9881738.1};
OS Colletotrichum karsti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum boninense species complex.
OX NCBI_TaxID=1095194 {ECO:0000313|EMBL:KAF9881738.1, ECO:0000313|Proteomes:UP000781932};
RN [1] {ECO:0000313|EMBL:KAF9881738.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CkLH20 {ECO:0000313|EMBL:KAF9881738.1};
RA He L.;
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF9881738.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CkLH20 {ECO:0000313|EMBL:KAF9881738.1};
RA Li H.;
RT "Whole genome sequencing of Colletotrichum sp.";
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF9881738.1}.
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DR EMBL; JAATWM020000002; KAF9881738.1; -; Genomic_DNA.
DR RefSeq; XP_038751199.1; XM_038883604.1.
DR AlphaFoldDB; A0A9P6IDV7; -.
DR GeneID; 62156678; -.
DR OrthoDB; 5232919at2759; -.
DR Proteomes; UP000781932; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:TreeGrafter.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProtKB-ARBA.
DR CDD; cd09998; HDAC_Hos3; 1.
DR FunFam; 3.40.800.20:FF:000011; Histone deacetylase HOS3; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR053244; HDAC_HD_type_1.
DR InterPro; IPR000286; HDACs.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR47558; HISTONE DEACETYLASE HOS3; 1.
DR PANTHER; PTHR47558:SF1; HISTONE DEACETYLASE HOS3; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000781932}.
FT DOMAIN 249..578
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..13
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..758
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..833
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..934
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..945
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..999
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1030
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1077
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1186
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1209
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1266 AA; 136743 MW; F4E10B4C8DAAA935 CRC64;
MNTPTDADKE LSHSLKQLSL STGSPASNSP RTPSALSPLR PAVNRASPGP VPSPRMPSRS
PSFARELSRS RSSTPTLQQR SATPTLQRKT STSSLHSVSG PSSRTPSRAP SRRTSLAHAS
SPVAKSPLRT SPPEYIKPPP TANTIARDYF KTELATHHSP LSTLGTETVV ILHDACYGHR
FSRPKTSKGA LSTIVERPER IKAGVLGVAM AYVRLGERHC DGSYPIHPSL NPTTIPNIPF
RIYKTERRLP ITSQAVTNVH GTKWMEELKM MCDVAEAKLS MGGKELQRPE MNRGADGPPA
KFHEGDLYLC SESLEAFEGA LGAVCEAVDR VFTSGPRRAF VAVRPPGHHC SASYPSGFCW
VNNVHVGIMH AILNHGLTHA AIIDFDLHHG DGSQAIAWAH NSRGVNMAKN AAAWKKASIG
YFSLHDINSY PCEMGDEEKV KNASLCIDNA HGQNMWNVHL GSWDSEQEFW DLYESKYSII
LEKTRSYLKT QSARVRALNL PPKAAIFFSA GFDASEWETK GMQRHNVNVP TEFYARIAQD
VVKLAAEEGL SVDGRVISVL EGGYSDRALY SGIFSHLSGL SGDQTVSEPT RGRPSLGYEM
GQRIGAIQEG QPIPEKDPSA PSLHPYNPSW WASSELDELE VAMGNRPASP RMIRQVTPGN
YSTPTAASIG KAVDPTRLRR MASGHGVAYS RPPTPPPPDV HWTVAAHELS RLLIPSDRQV
DSCKPEDLNA EATKARRDRQ SILNPDLVPP PPPAPAPVER PTSRMSLRER KPVTYAEEDD
KQSKNRRRTV AGAPALSADK ATARGIPSDA NGAAKRPGRR LSAASSVVST ASTMPYETNG
VASRPDTSMT IRPETSMTMR PDTSMTMRPE TSMTIRPESS MSVRTQAGPS LNVKKTRAPA
AKKEVPKKEA PKTTRTVKKP AVPAKTTPPQ AGQPSQPPKP KPSPAAGPED DMDKLTAGMK
KIKINLITKT QKEERAKAAQ AAQAAPKAAT PPVVEQAPAE QPPVEQPIVE QPIVEQPPIE
QPSIEQPQSP AFQEPKPSTP APTEEVVMTT PPPIVTPPQE DPVVTPPKSE PITTPPMEPE
DLNYMSSPDP LAPTPQVPKS ITEPMLSIAR PDPLQIELPA SSPVVTPAVE TPPGQDVFIN
YQPEGPAPIT MTPTEPLKWL PPNENTPVKP SPGKSPAKSP TKVSPPKKSP TKPSPAKLSP
PRASSSRAPV AKMKRANLPV FTSTSAIPFA QPKKNGSPKP KAEPVVKAEP AESAKSAREI
PETPQK
//
