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Database: UniProt
Entry: A0A1V6PGH9_PENDC
LinkDB: A0A1V6PGH9_PENDC
Original site: A0A1V6PGH9_PENDC 
ID   A0A1V6PGH9_PENDC        Unreviewed;      1193 AA.
AC   A0A1V6PGH9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Fork-head domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENDEC_c005G02364 {ECO:0000313|EMBL:OQD76109.1};
OS   Penicillium decumbens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD76109.1, ECO:0000313|Proteomes:UP000191522};
RN   [1] {ECO:0000313|Proteomes:UP000191522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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:OQD76109.1}.
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DR   EMBL; MDYL01000005; OQD76109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6PGH9; -.
DR   STRING; 69771.A0A1V6PGH9; -.
DR   OMA; HYKSDKV; -.
DR   OrthoDB; 5385885at2759; -.
DR   Proteomes; UP000191522; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IEA:InterPro.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR045178; Fhl1/FHA1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR21712:SF29; PRE-RRNA-PROCESSING PROTEIN FHL1; 1.
DR   PANTHER; PTHR21712; UNCHARACTERIZED; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00089};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00089}; Reference proteome {ECO:0000313|Proteomes:UP000191522}.
FT   DOMAIN          442..475
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          763..851
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        763..851
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..978
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          995..1127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..579
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..606
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..708
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..909
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..972
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1004..1077
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1112
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1193 AA;  127539 MW;  86E6A11150DB75EB CRC64;
     MSSQTMTAPA VGHRPPDPGH DTPMYDYGCP KNDGSPTNEP RSDSAVRDMH NSAPTTSKGL
     PATPVGIKSE PSEDQDFPMS ENQKESNTQS AAGALLAQLL GNQSAPNSAS ATDQSTGQQC
     DQKNGSFDEL NNHLMAQPAE LSTSIDPSQQ QDPASISRKM SNGGKPAVDV LATAEMNPQE
     GNSTAHRGSD AMDFLSDSLN HKSSMDQPSL LPPFDFATIP KNAFEALQQN ELLTAAYLSQ
     GADLSALGYR GGAASIAGSE PQIQAFAKLE FDDGHFYVNT YSFILGRDVR AARAAHHREV
     QYRQTMRSSR AKSSSGGNTS QTPNRMKREE SGAIMGSVVS DRGGIMGFDP DVPPNLPANV
     ELSRRSSKSS YDGSAAPFHA NPAQLESTTD YNALAMQSLQ EGTGEAKPVD TLALLPSPDS
     CPTIPIHPPS TIDGIAAGHR GISRRHVRIS YNFDRNLFEM EVMGRNGAFI GADWLSPGQI
     RPLHSGDYIQ IGGVRIRFLL PDVPIGDTGA DRMEAKPTEE KEEQKSIDVD ADADADADAD
     ADADADADAD ADADADADAD ADADADADAD ADADADAEHE IDDIDRLCSE SADGKDSKRI
     KNKDGSKLVP SIEAGGDGQQ PARRRGPGRP PKDGIMSKRE RAELAREQKM AAKREANGGV
     TPPPLANTKP KAGKTVSVSK EPSLPESPTS SKPAEKRKYT KRKKGDSTPM DYPLPSTEGG
     QFTAEQRPEE YVKPPPVKKR KPSRSPSPNY PPESAYTPED LAKPPYNYAV LIFDALTEAV
     TPMTLKQIYR ALKLKYPYFR FKCETEGWTS SVRHNLNGNG HLFMHAERDG KGWSWQLRPG
     ASVEKEKKRR PSPPPPPPQQ SAPPPQYMSP MTHSYAPPAG APALMPNQHQ QFQFPTMPTN
     FSASSAPPQQ HSSPYPPPAP ITSASTAAPT AAPAPAPAAA PAPAPAPTPT PAPVSAPAPI
     PTPAPAPVPA AASFPIPSTI RNSLPAAFAQ TIPSTYTSPY ATNPAPQAPQ PAQSQTPRPG
     QGPPAQHQSP YAPQKPPSSQ PPHVNPPHQA FPPPAGPSYP PPQHQQPAQP QQHPHPPQHV
     SQPHQQQQQQ PRPPPQAPQP HSQPPPPVQQ NSAPSGPSES SSFTERANKA IDDFEAVLME
     DYEDKNYIRE VLRSARARVL GNATESSFPG GEPKDEAVIM DVLRNLVGSL KDE
//
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