ID A0A167XL36_9HYPO Unreviewed; 1442 AA.
AC A0A167XL36;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 18-JUN-2025, entry version 33.
DE SubName: Full=Histone deacetylase interacting {ECO:0000313|EMBL:KZZ90217.1};
GN ORFNames=AAL_07318 {ECO:0000313|EMBL:KZZ90217.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ90217.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ90217.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ90217.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ90217.1}.
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DR EMBL; AZGY01000022; KZZ90217.1; -; Genomic_DNA.
DR STRING; 1081109.A0A167XL36; -.
DR OrthoDB; 10265969at2759; -.
DR Proteomes; UP000078544; 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; 2.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00810}; Reference proteome {ECO:0000313|Proteomes:UP000078544};
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 685..786
FT /note="Histone deacetylase interacting"
FT /evidence="ECO:0000259|SMART:SM00761"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..114
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..985
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1048
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1442 AA; 161432 MW; 5E07C1BFF207B92F CRC64;
MNSQSIHGRN NGGAPFDRDR EIDDRHRAIQ QHEDLRRDQG REREREQAER YQTAGPGVPL
QSSAGSIPIH QPVASRIPGA IHSPGGLLAN HSGNPPPQAA PHGGPSGPIS FGGPLQHGSA
PAGGLQGSAA SQHQIYAPMG HSQGGPAVPQ PAPSSGPPGF APGPHTQQNQ DAQRGAKVAA
AAMVGVTPVS HQIPGGITQG QQPILNDALT YLDQVKVQFH DQPDVYNRFL DIMKDFKSQA
IDTPGVINRV SELFVGHPNL IQGFNTFLPP GYRIECGAGN DPNTIRVTTP MGTTVQSITG
RSQDGHGAPP SQPLFPERGG QWPPRSQHSV ESPEARFSTP VQNGANLFVQ AAAQNAAFEG
SGATQRNANQ GPISGANAPG ARQTPVPPSG PAVPNAAAGN QANMERRGPV EFNHAISYVN
KIKNRFQDKP EIYKQFLEIL QTYQREQKPI QDVYAQVTTL FNAAPDLLED FKQFLPESAG
QTKAATGRVE DVAPGAPSQA PTPAGGQKMP PLGSFAPPSS ATKDNKKRPR GEKQTSAPEV
VTPDVIATSK VVPGAINGSN SKRTKINHGK ATTDFTVIEP TLTPVMPEPY PPRPSATSNH
EEIAFFERVK KFLSNRQAMN EFLKLCNLFS QSIIDRNTLF HKGALFISAN PDLLTFWKNF
VGAETRDVVM DNQPAAPVEK LSLSNCRGYG PSYRLLPKRE RLKPCSGRDD FCNSVLNDQW
ASHPTWASED SGFVAHRKNQ FEEGLHRIEE ERHDYDFNIE ANLKCIHLLE PIAQQMLAMS
SAERESFHMP AALSGQSTSI FKRICKKIYG ERGIDVVNDM YSYPFEVVPV LLARMKQKDE
EWRFSQREWE KVWHSQTENM HLKSLDHMGI LVKSNDKRNL TAKHLVDAIK TKHEEQRRER
SLKGKAPRHQ LVWDFSNKGV VLELLRLMML YSLHNGQHST QEKERMLDFF ETFIPAFFDL
PEEMYQDKLP RMQPDSGEEE MDDIPAELTN GRNRRNGRKG DLLRGVLDPG RNGNKPRTKK
EDSAASGSKE TTPDITSANE DEMVDAPEEA AVPEVSNERW MPTIPKPVIV GGDDGLLDEG
GELKADGFFT RPWCNFFCNQ TIFVFFSIFQ TLYSRLLDVK ESKEMVSAAI ERLNKPRPAR
DIGFTENHMT FFRPSDEPDT FWNKTVDLIE EFITGETDDN RYQDVLRHYY LDNGWKLYTI
QDLLKTLCRL ALTCSSTDAK EKTPDLIHQY LNGYEKEETS YQTEISARKF AEKCVKDGDI
FVICWFPQKA EATVRWLQRD ETTFYMDEMQ MRERWQYYIS SFIRVEPTEG IPRSKLQKVV
LTRNLPSGDT DSDSDEIPKP LYYSEDLATS ICLKSSKMLW VPRTSERFVY DKSPKTQEER
ERRAKFTNAL NLHRESKLVE KMVHNPAWTK DMGPDEVQEQ NKTFRKWSDD GIAPPAGDVE
MD
//
