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Database: UniProt
Entry: A0A9D5D840_9LILI
LinkDB: A0A9D5D840_9LILI
Original site: A0A9D5D840_9LILI 
ID   A0A9D5D840_9LILI        Unreviewed;      1466 AA.
AC   A0A9D5D840;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   18-JUN-2025, entry version 10.
DE   RecName: Full=Histone deacetylase interacting domain-containing protein {ECO:0000259|SMART:SM00761};
GN   ORFNames=J5N97_004166 {ECO:0000313|EMBL:KAJ0985810.1};
OS   Dioscorea zingiberensis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae;
OC   Dioscorea.
OX   NCBI_TaxID=325984 {ECO:0000313|EMBL:KAJ0985810.1, ECO:0000313|Proteomes:UP001085076};
RN   [1] {ECO:0000313|EMBL:KAJ0985810.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Dzin_1.0 {ECO:0000313|EMBL:KAJ0985810.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAJ0985810.1};
RA   Li Z., Yang C.;
RL   Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAJ0985810.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Dzin_1.0 {ECO:0000313|EMBL:KAJ0985810.1};
RX   PubMed=36204203;
RA   Li Y., Tan C., Li Z., Guo J., Li S., Chen X., Wang C., Dai X., Yang H.,
RA   Song W., Hou L., Xu J., Tong Z., Xu A., Yuan X., Wang W., Yang Q., Chen L.,
RA   Sun Z., Wang K., Pan B., Chen J., Bao Y., Liu F., Qi X., Gang D.R., Wen J.,
RA   Li J.;
RT   "The genome of Dioscorea zingiberensis sheds light on the biosynthesis,
RT   origin and evolution of the medicinally important diosgenin saponins.";
RL   Hortic Res 9:0-0(2022).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00810}.
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:KAJ0985810.1}.
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DR   EMBL; JAGGNH010000001; KAJ0985810.1; -; Genomic_DNA.
DR   OrthoDB; 10265969at2759; -.
DR   Proteomes; UP001085076; Miscellaneous, Linkage group lg01.
DR   GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:TreeGrafter.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR   FunFam; 1.20.1160.11:FF:000001; Paired amphipathic helix protein Sin3; 1.
DR   FunFam; 1.20.1160.11:FF:000002; Paired amphipathic helix protein SIN3; 1.
DR   FunFam; 1.20.1160.11:FF:000003; Paired amphipathic helix SIN3-like protein; 1.
DR   Gene3D; 1.20.1160.11; Paired amphipathic helix; 3.
DR   InterPro; IPR013194; HDAC_interact_dom.
DR   InterPro; IPR003822; PAH.
DR   InterPro; IPR036600; PAH_sf.
DR   InterPro; IPR039774; Sin3-like.
DR   InterPro; IPR031693; Sin3_C.
DR   PANTHER; PTHR12346:SF0; SIN3A, ISOFORM G; 1.
DR   PANTHER; PTHR12346; SIN3B-RELATED; 1.
DR   Pfam; PF02671; PAH; 3.
DR   Pfam; PF08295; Sin3_corepress; 1.
DR   Pfam; PF16879; Sin3a_C; 1.
DR   SMART; SM00761; HDAC_interact; 1.
DR   SUPFAM; SSF47762; PAH2 domain; 3.
DR   PROSITE; PS51477; PAH; 3.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00810}; Reference proteome {ECO:0000313|Proteomes:UP001085076};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          493..593
FT                   /note="Histone deacetylase interacting"
FT                   /evidence="ECO:0000259|SMART:SM00761"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          842..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          946..994
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          562..589
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        9..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        948..963
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1049
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1057..1066
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1084..1095
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1466 AA;  166240 MW;  FBE0AF27D060411B CRC64;
     MKKGREDSYS SSQIKRPNSS TSGQTHMANS AAVSNSSKLT THDALAYLKA VKDIFHDTKE
     KYDEFLEVMK DFKSQRIDTS GVIARVKELF KGHRDLILGF NTFLPKGYEI KLPAEEKKPV
     EFQEAITFVN KIKNRFQNEE HVYKSFLDIL NMYRRENKSI TDVYEEVAAL FRDHPDLLDE
     FTHFLPDTSA TGAQHNVTAT RPMFRWDGRP SIVPGLKLTS PGQRERTYNS HTERDLTVDR
     PDLEHDRQRR RAEREKDRKE DRDKREHERD EKDLEHDSRD LDTMQRRRKP SRIGNDAAPE
     QLHQGGEGAE NFATYSISTS SYDDKNALKS VYPQEVSYFD KVKEKLHPDG YQEFLKCIDI
     YSKEIISKTE LKNLLCDVLE KYPDLMDGLD EIFANPGSID GFLTGVINKK SLWNEGHMTR
     PVKGEERDRD REYERDDKDK ERERERERDR ERERLDKSVP FVSKDVGSQR STLAANKEKY
     NLSKPISELD LSNCQRCTPS YRLLPKNYPT PPASHRTELG ASVLNDVWVS VTSGSEDYSF
     KHMRKNQYEE SLFRCEDDRF ELDMLLESVN AATKRVEELL EKMQDNTIKM ESPIRLEDHF
     TPLNLRCIER LYGDHGLDVM DVLRKNASLA LPVILTRLKQ KQEEWSRCRS DFNKVWAEIY
     AKNYHKSLDH RSFYFKQQDT KSLSTKALLA EIKEINEKKR KEDDVLLAIA AGNRRPIIPN
     VEFEYTDPDI HEDLYHIIKY SCGEVCASTD QLDKVLRIWT AFLEPLFGVL PRPQGAEDAV
     DVVRTKSRAI KSNLVSVREN NGSPSAVVAG NTKQLNPIMN GDDGNLQEQG SLYKARLANG
     DTPVNRNGFH DADRSAGRSD NPCSTPLHAK VQTTPVADEI SGITIQTAAA EQLVDNNSLA
     SRGEQTQCRA NLENTSGSTN AKSGHAGAER VLETCANNEV LPLEGGENSR QVVSANGGSA
     TESTKVRRYH DPSTSQNNLK VEREEGELSP NGDFEEDNFV VFENSAVDAV PKGKNSPSSR
     QYQTKPGEVA CSSVAAGDND ADADDEGDES AQRSTEDSEN ASEAGEDVSG SESGDGEECS
     REDHEEEDDD ADHDDPDGKA ESEGEAEGMV DAHDADEGTS LPFPERFLHT SKPLAKHVHE
     ALHDKEDKCS RIFYGNDSFY VLFRLHQTLY ERILSAKINS STAERKWRTT KETSPPDLYA
     KFMGALYNLL DGSADNTKFE DDCRAIIGTQ SYVLFTLDKL IYKVVKQLQA VASDDMDNKL
     LQLYAYEKSR RPGRFMDVVY HENARVLLHD ESIYRFECTS SPTRLSIQLM EYGQEKAEVT
     AVSIDPNFTA YLYNDFLSSD PDKKKRRAVF LGRNKRKFGT DEYSAYSTAM DGVRVVNGLE
     CKISCNSSKV SYVLDTEDLL VRFVKKRRYS YGGVPTSKRI LPLEWDETST LTLHNVVEIT
     TLQNPSCTYE AASCLGSLAS SDIDDV
//
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