ID K5W011_PHACS Unreviewed; 789 AA.
AC K5W011;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Histone deacetylase domain-containing protein {ECO:0000259|Pfam:PF00850};
GN ORFNames=PHACADRAFT_164149 {ECO:0000313|EMBL:EKM52219.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM52219.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM52219.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM52219.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
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DR EMBL; JH930475; EKM52219.1; -; Genomic_DNA.
DR RefSeq; XP_007398576.1; XM_007398514.1.
DR AlphaFoldDB; K5W011; -.
DR STRING; 650164.K5W011; -.
DR GeneID; 18909276; -.
DR KEGG; pco:PHACADRAFT_164149; -.
DR HOGENOM; CLU_355683_0_0_1; -.
DR InParanoid; K5W011; -.
DR OrthoDB; 10780at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
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:UP000008370}.
FT DOMAIN 100..382
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 475..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..542
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 85344 MW; A14D5562E7EDDAE0 CRC64;
MPEGPGRQPT IFFQELHEKH KNYAKKEELE SPQRVRAVEY GTAAILARLE LANPNYPSPL
KIVRSMAELR NIADNVAARI MFGMKDEDEP GRENYAERLW QWCKDCALPS GKFEPDLYIC
SQSYVAFAGA LATTCEAVDA VAAAHTAPSG SDSTRAFVAV RPPGHHSRPD NPAGMGFLNY
VVLGAIHAYT AHGYSHIIIL DIDLHHGDGT QTMVQQINDS VHRAQDGQSG PIVYFGSMHD
VNVYPCRDAS KDMPDARLSS HGEGGQWIKN VIMEPHATEA DFWTAYETRY KTLLTDATAF
LQQTSASSNK VIVFISCGFS ASQYEYGGVA GNCRVPPAFF YRFTRDACAL ADTHAQGRLV
SILEGGYSDR ALLSGTMAHV AGLIDDEPKI ESAWWNEPNL IELEKVAVRK KGRRHYLDKL
PTWVQRAHQV VQHLHAPLPE QLPESSVLNL PPFVPYPPPP PKQTAQSRWG LFPASTSASA
PVASGSTAPL SPSSVTSSGE PRVSDRLEEK RKYLASLRLW LPGGDSDEEG EDEDEVDEMD
ESHKETDDLP VIRGRGRGRP RGRGSRGGRG RGVRGGPGSR GGRGSRGGRG SRGGRGRGRG
RGGGGVHTEA IVHSPEEEDS GSPTPLSAER VGPAITAGPL ANVSPEAGPS NGKRPPEPAS
APADEQHKRL RQDSTQSDAT AVQGAGPVSA VAALRRSLDD FAGRVDTHAD TLPAELVRAV
RGARGCVAKL ERFADDVRLV DETVDLLREL SDAAFVACGT IEDKQLAKGL RFGLVDLEGA
VEEFRRNGK
//
