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Database: UniProt
Entry: A0A0J1ASJ0_9TREE
LinkDB: A0A0J1ASJ0_9TREE
Original site: A0A0J1ASJ0_9TREE 
ID   A0A0J1ASJ0_9TREE        Unreviewed;       681 AA.
AC   A0A0J1ASJ0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Fork-head domain-containing protein {ECO:0000259|PROSITE:PS50039};
GN   ORFNames=CC85DRAFT_331712 {ECO:0000313|EMBL:KLT38314.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT38314.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT38314.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT38314.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR   EMBL; KQ087324; KLT38314.1; -; Genomic_DNA.
DR   RefSeq; XP_018274805.1; XM_018427086.1.
DR   AlphaFoldDB; A0A0J1ASJ0; -.
DR   STRING; 879819.A0A0J1ASJ0; -.
DR   GeneID; 28987689; -.
DR   OrthoDB; 5385885at2759; -.
DR   Proteomes; UP000053611; 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:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProt.
DR   CDD; cd00059; FH_FOX; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR030456; TF_fork_head_CS_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11829:SF343; FORK HEAD DOMAIN TRANSCRIPTION FACTOR SLP1-RELATED; 1.
DR   PANTHER; PTHR11829; FORKHEAD BOX PROTEIN; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00089}; Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053611}.
FT   DOMAIN          414..511
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        414..511
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..568
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  73206 MW;  EBA92824A8E2AB4B CRC64;
     MLDEAPITPA RRPRGGRPMA DLRANSREDD DGNVPTSDEI VSSSPLQPAF EPKMVLRNGA
     SVDLISWLRT HFHHQPPPHT PVTSVMNLNH VQRLLQERFP RVPDQAELKR AVLAAFPHSQ
     WEEPLHDSAP EPPIMRGLAW NGKDVAEDDD DTPGRTRPVH RRPRLETNGV STSRSPTNSP
     LLSPDSSSTR RAMPDTPARS VLDEFAEIVT RTPGVKERSL EPIALPLPTA APTVPKTQAR
     YWKKRPASQS PEQGRTRRES TPDALQELLE AAEAIEGSPL TTSKTERGGH KRRRTIAGGS
     TTQDFAAGLS FAANRGRSVR GTASPQIAGL SLLNPKDQDD EEPISPLASE ESHASRLIAI
     GQGRWGARGG SSSTSQLSQV SEVAAPAGPS KGAGRKVNEL PTSTQGQFPG YDCKPPYPYH
     EMIRHAIEHA PDRKLQLAQI YSSIAERFPF FKTLDEKKTA GWQNSIRHNL SLKKMFVRVN
     KADGTDEGGK GGWWTVQPGV PDEGRPGRKA KAKRAKAEAE SGPPSGTSTA AGTPAPPGVK
     IAPSPAPSVA TLPGPTPRPT PSPAVTRPSL PKPELHGRYI APGPAPQPQP PLQSKTASTK
     VSPNQSQSQP QPKRIAPDQQ TPTHSAKAPL SQSQSQSQSQ SQTQPPSKGQ APNGTATHTL
     FPRAPSTSTA PGDPFVDEKS S
//
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