ID A0A1B7Y744_COLHI Unreviewed; 1140 AA.
AC A0A1B7Y744;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 08-OCT-2025, entry version 38.
DE SubName: Full=Forkhead domain-containing protein {ECO:0000313|EMBL:OBR07861.1};
GN ORFNames=CH63R_09382 {ECO:0000313|EMBL:OBR07861.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:OBR07861.1, ECO:0000313|Proteomes:UP000092177};
RN [1] {ECO:0000313|Proteomes:UP000092177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA Thon M.R., O'Connell R.J.;
RT "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT structure and association of transposable elements with secondary
RT metabolite gene clusters.";
RL BMC Genomics 18:667-667(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:OBR07861.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LTAN01000006; OBR07861.1; -; Genomic_DNA.
DR RefSeq; XP_018156379.1; XM_018304356.1.
DR AlphaFoldDB; A0A1B7Y744; -.
DR GeneID; 28868463; -.
DR KEGG; chig:CH63R_09382; -.
DR VEuPathDB; FungiDB:CH63R_09382; -.
DR OrthoDB; 5402974at2759; -.
DR Proteomes; UP000092177; Chromosome 6.
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; IPR017956; AT_hook_DNA-bd_motif.
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; PRE-RRNA-PROCESSING PROTEIN FHL1; 1.
DR PANTHER; PTHR21712:SF29; PRE-RRNA-PROCESSING PROTEIN FHL1; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00384; AT_hook; 2.
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:UP000092177}.
FT DOMAIN 322..373
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 695..757
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 695..757
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..48
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..458
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..491
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..515
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..535
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..631
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..838
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..861
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..933
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..949
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 121638 MW; 6228BA4455B64587 CRC64;
MTSSNAGQNG LAPVPTTPPP KNKTTPTPGR PDPDDHNTTT NATTATATSS HQQPPRADAL
AAHPQSNPDT SGKRQSTPGA ADTDMTDAHA NTAPSATMSH PASAAHNMDA DPFASSFPHT
PMPNMDHAYM MMALAHMAGN QMSNQMSPPP TVTPAQVTLP STIGNGNDPL VASTHNLAAA
TQGLESFARI EFADSVFQMT TYAVIIGRDQ KALMQAKRDE KYRKKAEEYE RDGLPPPEPF
NQRKFSKSYV SEEGGMLGPE SDSEGDGRPA KRRKTTSTGS SQKPEEDEAD ENFISNRQYV
SHTPGAAAVD LASLRPSPHH VPFIGIHSPG PDIAKKTKAI SREHLKIQFN KEQGVFEAIP
LHKNGFFIDD VHHKDGVAVL RSGDQLQIKD VDFRFVINGV PEGRTGAEEY LEEDKLKKKQ
TGGKEMSFEF EASHGNGLDD TSDSSLSSPA PSDAGLSDLD MDIDEAEEDA EVEAEQAEAE
AEEAEEAEAE AAEAAAEAAE VAEAAEVAEA AAALEAEAEA DADADDDADA DADAEGELHQ
EYGEEVEDIQ PTTEVKSEEQ EMAHLLMGAG APLGYPNKKR GPGRPPKNGF MSKREQRLLK
KAQQEMAKKT LPQPPPGEPP IKRKVGRPRK HPLPEEGGDR PEKRKYKPRK PKGEDGAEGS
DAERRAKEKK EKKVRPKSPP LELKIEDYTE EQLQKPNKNY GVLIDETLTA AGPDGLTLKQ
IYKRITQRYP WFYFHTETKG WESSVRHNLI GNEAFKKDDT TGLWSRVPGV ELDAGKKRKA
SSPDRSVSAG YGHYSHPAYT QYAQQPGHMP PGYQHLPHNY HAQAYAGQQA QAQAQAAART
THYSPPGATP TPGQPAPPPV ASQPVAPATL PGYGAAAAIA RPQGVAGQPS TYSSPYASRP
PPIHPAVKSE DSAGTASTSA PPTTQPAPAA IPGAQPPQIP AAAPQQARPT PTPPAQAEPR
PVIQPRLLSA VNGLKNGLIG NLKNAKNPKA EAIVMSALNR CLGLKNAATE NQTMEDICMK
GIQKLLDGFS TRSNTPGSGG TPTPTGPGNV FDPKVFNALV GFKNVSSNAL KVRIGESKAE
AVTLSAIDRV LGLADASIVP PPAEASTSAS PQAGFDGIES HLMNSVKQLL LGLNQKLHGT
//
