ID S8CAS1_DACHA Unreviewed; 1084 AA.
AC S8CAS1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Fork-head domain-containing protein {ECO:0000259|PROSITE:PS50039};
GN ORFNames=H072_1144 {ECO:0000313|EMBL:EPS44812.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS44812.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS44812.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS44812.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EPS44812.1}.
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DR EMBL; AQGS01000032; EPS44812.1; -; Genomic_DNA.
DR RefSeq; XP_011107136.1; XM_011108834.1.
DR AlphaFoldDB; S8CAS1; -.
DR STRING; 1284197.S8CAS1; -.
DR eggNOG; KOG2294; Eukaryota.
DR HOGENOM; CLU_299342_0_0_1; -.
DR OMA; DICEWIS; -.
DR OrthoDB; 5385885at2759; -.
DR Proteomes; UP000015100; 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 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; IPR045178; Fhl1/FHA1.
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; PTHR21712:SF29; PRE-RRNA-PROCESSING PROTEIN FHL1; 1.
DR PANTHER; PTHR21712; UNCHARACTERIZED; 1.
DR Pfam; PF00250; Forkhead; 1.
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};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT DOMAIN 565..659
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 565..659
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..411
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..961
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..995
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1084 AA; 117798 MW; 58A1549157DC6B8B CRC64;
MADSEPNRQQ GGRVAIPEQI MTPCPSPDEA VRFAGEEKTP QNEVANIQSA PATDNPVVAR
VDGASMTADI PAINDNHHPD RNATNKLATS PAASASTLNT DDNPVVIKDD EEAAAQTLKN
EEEDDDDDDD YDSGTQPQQT PEEAVVVAAT EPPAPLVCDS QKTPLDPEFL QSLDQPLELS
NLDLQLAENE DPTGIVSTAD LIQTVTGGAW YPTNPESGIT PRIEAFAKLE FHYGQDFYLS
SVNIVLGRQD KEPSLFNGKR KKRRQENHYG DSVLVPDEIK VPLFPPPDID VASISRRHLR
IQYDYELSTW KLTALCDTGF RLTRSGKDKF FSIGKMITLE NSDHIRFGNL AFTWFLPDQD
ESEQQMVDDD VTMEDGIERK LLDAMNAGDL SSDLDSDNDS DDGDDEDEGS DLDSREQSHD
NGTPTPRSSK FNGDDDSSLM PPPPVKRGRG RPPKNGISVR EQKLLKRQAQ EEFLANGGNV
ANLDMSKYGN LPVDKLFAKE GEKMAQQIEK EARKRAKAEE KEAKIREKQA AKDLKPPKIP
KERKRKRTKS PPAREEDYTP EQLAKPSLPY TVMIYDAIQN SEKKALTLPE IYRSLETTYP
YFKVRAETTG WQSSVRHNLR GSGEGGGSSL FERGERSGKG YIWKIAKGAN IDKERKKRKP
VTGSPHTTQA SMQAAPQPQM TIPSGGSWSQ SAQTSQFGHP AQFAQQYQSH QTVQTFAQTT
YQAKAPTAPT VQIPKAATTH SIVTTTTSDH STIKRAVAQP AVPPPPAWNP AQAKPQITQA
SVPNGGVPAR IPQQTRAPVA PQVQPPARQH QVNVATLQQA RAAAPVTASS APIPGSAVPA
ARPPAAIAIQ PSPATKPAVS SEVDSKARDL LDNPTFLKIM KEHLQKYPGH NINSPEVRKA
LWAEFKKTTG AKAPLLKTGI AKPPVPKAPP VVQKPSLPSA LPQRAALQPN PQPPPNAVPV
TTPVKSAPIS IPKLPVGLPN QPSMPQTPTT PQPGQIKPST PHQTTTSEQP TSAQQRVGDL
LKGMTMDAQK KAKILQFLKN AKEKKAAEAM GASKTTPISG IKRPAEAAPT NGPVAKRTAI
EGQQ
//
