ID A0A1B7P3L8_9EURO Unreviewed; 1764 AA.
AC A0A1B7P3L8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Histone deacetylase interacting domain-containing protein {ECO:0000259|SMART:SM00761};
GN ORFNames=ACJ72_02013 {ECO:0000313|EMBL:OAX83626.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX83626.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX83626.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX83626.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:OAX83626.1}.
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DR EMBL; LGUA01000153; OAX83626.1; -; Genomic_DNA.
DR STRING; 1658172.A0A1B7P3L8; -.
DR OrthoDB; 199155at2759; -.
DR Proteomes; UP000091918; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:InterPro.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 1.20.1160.11; Paired amphipathic helix; 3.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR013194; HDAC_interact_dom.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR039774; Sin3-like.
DR InterPro; IPR031693; Sin3_C.
DR InterPro; IPR026893; Tyr/Ser_Pase_IphP-type.
DR InterPro; IPR016130; Tyr_Pase_AS.
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 Pfam; PF13350; Y_phosphatase3; 2.
DR SMART; SM00761; HDAC_interact; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF47762; PAH2 domain; 3.
DR PROSITE; PS51477; PAH; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00810}; Reference proteome {ECO:0000313|Proteomes:UP000091918}.
FT DOMAIN 864..965
FT /note="Histone deacetylase interacting"
FT /evidence="ECO:0000259|SMART:SM00761"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1764 AA; 196530 MW; 1DA9C524AE44AF76 CRC64;
MNPSNKDTWH PGGGGSQPHP GVDQMNQPPP ARPLGSYGEL LSPVCPLLAR PYHPVNQSSG
HTLPTLSDIT QGAGAPPASH QPPPRYGQHQ PPSHPPNHPL PGIGQSMQHS PPQTSLNRER
ERDSRERDRE RERERELDRQ RELAREDEMI QREREYRERE RDRDIMDRYN REQSHHPVQS
HAGPIPIHQP VASKGHNPLG GPNGLLSNLG ANAAPNPSQG PMPSSNAPGG LFGNQMQQHP
DGPPRTYLHQ GQPSQQSMHG FNGTAPPQIP GSVAALAQGQ QPILNDALSY LDQVKVRFVE
QPDVYNRFLD IMKDFKSQAI DTPGVIQRVS TLFNGHPALI QGFNTFLPPG YRIECGTEDN
PDAIRVTTPS GTNTISMQSA ARPSLEATGD SVPQGGPGPA AGSDYYDQPR PGWQQPPNQG
QQQQQQQQQQ QQQQQQPQQM SRMNMGPNGP YSPKGHLMSS AMYGGNQGAQ NQPQESAYEY
PGQQDQQAQG NAAAIAHQQE QRGVSQLQNA VSAATAGSGR ASVMNLGSMQ AQGQNQPINN
LAGLGSGVLQ GVQGDMSKRG PVEFNHAISY VNKIKNRFAD SPDTYKQFLE ILQTYQRESK
PIQDVYAQVT VLFNSAPDLL EDFKQFLPES AAQAKAQAAA ARQAAEEATP LSNIRGEPGY
SSSSALLQAQ NRDVKMPPLG QFNVKEPAKD IKKRRGQPPA QGTGSAGLGA PSNVAAESAS
IASNQANRAP GAQSGAAGKR AKLSHKPTTQ AEAPPAVSPT LVPALPEPIS PTFSLTPSHE
EYAFFDRVKK FIGNKQTFGE FLKLCNLYSA DLIDRNILIN RAASFIGGNQ EIMSWFKRFM
HVEPKDEIIE PKAKPESGIV NLSHCRALGP SYRLLPKRER QKPCSGRDDM CQSVLNDEWA
SHPTWASEDS GFVAHRKNQY EDSLHRIEED RHDYDHHIEA CIRTIQLMEP LVQQIATMSE
AERANFKLPP GLEARAKQFT GESSRRYMIE SVAKKLSTRC LHGHALFFLL FLPDLSRSVK
NGRLVKVLQR EWDKVWREQM QKGFWRSLDH QAIIMKGSDK KLFVAKHIQH EIQAKLEELR
NIRKSGYQVP NYQFDFAFDD SEVLVDATHL LLCHIDHNSG GFGADPNKVI NFLKDFIPVF
FGMDREGFKT YLNEVYDTTS ASEEADDESL PPEDDREWQK LDLLRDVLER RNEKTPRIDR
DISVRSGSRA STPGVGSLVP STPIPDPTEP FDVAELKWME HPSQGNFNQQ REIPLNESYK
KKVHHLYCNL NIYCFFRTFE IFYSRLLRIK LHEKEAHESV RRAMASKAAY DLGMIDKSPS
DLLYDTDPKS NLYHQIVRMC EEVIKGNIDM SHMEETLRRF YLKTGWQLYN LDKILSGISR
YAGGIFNSDP KDKSSDIINI FFKERDKDTT THNQEIQYRK QIEKLIKEGD IYRVTFPDDA
SKSDRHRLTE ELRLASVIDL RSTTEHTMAA NRRISTKFNE AEEQTTPSSS QPQAITNDEH
LLKLPGVRRF MISLAGWNLE KLLLWRLSWF NLIKAISLLA SGYRQAATKL VVEQAMVPRG
LKGLAHDTLT ASQDEIKELF GYLGDPTAYP TLIHCTQGKD RTGLVIILLL LLVGSPGSDV
RMMKKENGEE GEDYCISTVE GGLCKVIDTA PGVPSDADAD ADADSGTATT GIATGTRKNA
GKIPLSAITS DYRMSEDELL PELEERLAEM QVMGLPEEYA KCPVGFTEDV VRFLEEDYGG
IRGYLKAVGV EDQVVERVRG LLTA
//
