ID A0A4S2MZE0_9PEZI Unreviewed; 1587 AA.
AC A0A4S2MZE0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=Histone deacetylase interacting domain-containing protein {ECO:0000259|SMART:SM00761};
GN ORFNames=EX30DRAFT_330663 {ECO:0000313|EMBL:TGZ81993.1};
OS Ascodesmis nigricans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Ascodesmidaceae; Ascodesmis.
OX NCBI_TaxID=341454 {ECO:0000313|EMBL:TGZ81993.1, ECO:0000313|Proteomes:UP000298138};
RN [1] {ECO:0000313|EMBL:TGZ81993.1, ECO:0000313|Proteomes:UP000298138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 389.68 {ECO:0000313|EMBL:TGZ81993.1,
RC ECO:0000313|Proteomes:UP000298138};
RG DOE Joint Genome Institute;
RA Lutkenhaus R., Traeger S., Breuer J., Kuo A., Lipzen A., Pangilinan J.,
RA Dilworth D., Sandor L., Poggeler S., Barry K., Grigoriev I.V.,
RA Nowrousian M.;
RT "Comparative genomics and transcriptomics to analyze fruiting body
RT development in filamentous ascomycetes.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00810}.
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DR EMBL; ML220117; TGZ81993.1; -; Genomic_DNA.
DR FunCoup; A0A4S2MZE0; 1078.
DR STRING; 341454.A0A4S2MZE0; -.
DR InParanoid; A0A4S2MZE0; -.
DR OrthoDB; 10265969at2759; -.
DR Proteomes; UP000298138; Unassembled WGS sequence.
DR GO; GO:0070822; C:Sin3-type 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 Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00810}; Reference proteome {ECO:0000313|Proteomes:UP000298138};
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 761..862
FT /note="Histone deacetylase interacting"
FT /evidence="ECO:0000259|SMART:SM00761"
FT REGION 1..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1549..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..52
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..95
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..135
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..177
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..213
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..256
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..268
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..466
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..582
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..645
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1079
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1587 AA; 175858 MW; 582A235C23C8ED4A CRC64;
MTTGAKDGWH PAPPAPSEQP SQQPQSATAG PQGPSALSGH QQSPSHSQLS QGAYRAGQPP
PPSAPVQLPP PREMSGASSY FSSPSHPHNP ASHPHTLPQL PGISSTAHSS YSLPGISTSS
ASTYGPQSSG GQQLPSGPPP SQQAGAQRDQ PPPSQSQSTR APGPPQQQTP QRPGMPNTSP
PVPPPTAMHG SPSLSNQQQQ QPAGLAAQQS QGGDPAQVAQ TLMLQRAAQE QQRQQQQQQA
HQLHSLSGLQ QGPPQSMGGG PGGAGAVGAP GQVPGAQGPA NGPNGPILND ALSYLDQVKF
QFADHSDVYN KFLDIMKDFK SQTIDTPGVI ERVSTLFSGH PSLIQGFNTF LPPGYRIECS
TDLGDTKITV TTPNGIHTAP SGDAVSIAGN QGMPLPQPGL PTAPAPGQPS RYYEQQPQPQ
RWGHAEGVYG PYGQVQTPGQ QEAMEIARQQ QMAQAQAQAV QQQRIQTNGT GPKVGPQGPG
TPGAGERGKG PVEFNHAITY VNKIKNRFAQ QPEIYKNFLE ILQTYQRESK PIQEVYSQVT
MLFHEAPDLL EDFKQFLPES AAQARAAAAA KAAQEETQNA GPQGPGAGGP SATRLPAVGT
FPPPPTVSKK GTAKRQQQAT PHVEMKADQQ QRPSAAKRTK VTHHKPTVEQ QIESVQPSLT
PFNPEPLGPP PLPSATNEEL SFFDRVKKFI GNKQTYNEFL KLLNLFSQGL IDKPILIEKV
HNFIGGNAEL MKWFKQFMQW DNKEETVENV PKLMNKVRLS VCRALGPSYR LLPRQEAQKP
CSGRDEMCWE VLNDNWASHP TWASEDSGFV AHKKNQYEEI LHRIEEERHD YDFNIEANLR
TIQLLEPIAQ RIAGMSQEEK NSFKLPPGLG GQSTTIYQRI IKKVYDREKG QEVIDHLHNH
PAQTVPIVLK RLKQKDEEWK SAQREWQKVW RDQTVRAFWR SLDHQGIAIK TTDKKAISHK
ALVAEIQAKF KEQTAKRLSP STPPPAYQFR YLFQDHEIIF DAIRLLLTGL DHNSSYSMGD
REKIEGFVKS FIPLFFSLDG AKAHAQGKRH EDDGDDSVME DAPSPRSATG AAATAGTSAR
RPHHRLDTQD LLRDVLKRHK KGSRKDKEGS IYSRGSRDSS QEIHDSHGDV EMTSPASDSR
LSKDESVWIS RPHKFDSTNS PLSPSMDIED TQLPRKRTVY TLFCNATLYS FFRLLQLLCS
RLGDVKAQEE QVRHDINIRK QQKVADLLNI SGQKVTDIFH DTSDNAQYYP QILDMCERFI
EGDLDSQTFE EHLRNVVIHA GWKLYTVDRL VNAILKFVHQ IVPSDAKERN QEKEKNADMV
LRFQKDRMRT EIGGSSGEKG EFQELMVYRK AVEGILGPDE TVYRLDWHED ESALTVRLLP
RENPTVSSDS LDKQQKWEYY IQSYMLTSPT EGIPYSRLTR TVLPRNLPSS TASPAYYHTT
STTNPPSPAT GPSDSADASG TKDDVGRRVS ELHVSENMQV RICVNTFRMF FHPHTEDYMI
RRPLPRIRGT QGRKKKFAEV LNGLGWRRDA DDAEVEKVRK SWERWVNGEE EGIEEQTAKA
DVDMKEGEAQ AEGKTVKDAD GDEVMEG
//
