ID A0A1S8BJP6_9PEZI Unreviewed; 1237 AA.
AC A0A1S8BJP6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Histone deacetylase HOS3 {ECO:0000313|EMBL:OMP87696.1};
GN ORFNames=BK809_0007783 {ECO:0000313|EMBL:OMP87696.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP87696.1, ECO:0000313|Proteomes:UP000190776};
RN [1] {ECO:0000313|EMBL:OMP87696.1, ECO:0000313|Proteomes:UP000190776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F98.1 {ECO:0000313|EMBL:OMP87696.1,
RC ECO:0000313|Proteomes:UP000190776};
RA Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT in grapevine trunk diseases.";
RL Submitted (JAN-2017) 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:OMP87696.1}.
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DR EMBL; MSZU01000076; OMP87696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8BJP6; -.
DR STRING; 420778.A0A1S8BJP6; -.
DR OrthoDB; 10780at2759; -.
DR Proteomes; UP000190776; Unassembled WGS sequence.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR CDD; cd09998; HDAC_Hos3; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
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:UP000190776}.
FT DOMAIN 266..601
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1237 AA; 134180 MW; 80E0451F1F4DBBD2 CRC64;
MENDSASSDT AADPSTATAE PAPRSLQIPP TVDPDAQPAK PANRLTINTA ARPSLPPSPA
MDSPHRRSSS YYNRIPKSPT PGAPLPSPLN RSASSLGVRP ASPALSRRSS IVSLQGAAAE
STHTPRKSVS RRTSGNLRSS SSAALASPRS VPVDEPAPLT AQKVASDYFA KELEYHKNEE
LSTQTVVILH DACYGHRFSR PKTTKSALSM IVERPERIHA GILGISTAYV RFAERHAGGP
HAPHPKRDPP KELPFTIRRT SRTLDITSPI VTNVHGTKWM AELQTMCNTT AEKLASNGKE
LARIDESGQP EKEKFHEGDL YLSPESLNAF QGALGGVCDG IDAVFAGTRD KPRNAFVCVR
PPGHHCSADF PSGFCWLNNV HVGIEYAAQT HGLTHAAIID FDLHHGDGSQ AIAWERNTEV
ANMPAKQPKN APTQKRTQIG YFSLHDINSY PCEYGEMDKV QAASLCIENA HGQTVWNVHL
QPWKTEEEFW KLYETRYLIL LEKARVFLRT NSQRLRASPN QSQPKAAIFI SAGFDASEWE
GQGMQRHKVN VPTDFYARFT QDIVKLSQEE NLGVDGRVIS VLEGGYSDRA LASGVLSHLS
GLCEGQKVPA TKKEPAALNS LGNGMMIDRA ALQQAYENGE QTLRYNVEWW HEANLTALET
MVYPPPPPAP KKQQRGQQGN FATPTQSFTA KVVDPEKFIR NASGHLVPIR ELPRPPTPPP
PDVNWIVAAH ELCKLLVPND RQTKSYKPED LAEPRSKKEK VLPPEVPVNP TGGRQLRERK
PKITDYSEPP SDDEKLQPRS TLDADRRRTM GDYPAGEDND LPELPQFQRR QSLVSEMGSV
AGERPSSRAS TVASRQPPAN GVQVKKTRAP KPTKPDATVK QPPRPIASRA SSYSQHNKAP
AATKSTKAKT DSSGDDVDQL TSGIKRITLK MPTKEEHDAR QAATAAAEKD TKKPAAPKTT
KKAPAARSTK TVAASRRAAT KETRETKEMK EAKEAQEAKE AQEAKDANGA KDAKESKPTP
PPSEHTEDAM SIVSYTSTSN QSEPVAAVSE STLAVPGGLE PQHGRALSRA SIENMAERIK
NSFPPSLASP SELSEGSTPQ GLLETAGPVH VPEVTPRPDS PPPPPPATMP QFIQYEPAEG
EHGATATAEP DAGVAQQTTA LQWLPPNSDP EAGGRSQGPP PSPGRKQKQA LPVFTSNSFI
PFGPPASSKA GADSVVTERQ ETAEDVRNMP DVPEAKE
//
