ID A0A059IXM2_TRIIM Unreviewed; 1250 AA.
AC A0A059IXM2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Fork-head domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=H109_07864 {ECO:0000313|EMBL:KDB20168.1};
OS Trichophyton interdigitale (strain MR816).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB20168.1, ECO:0000313|Proteomes:UP000024533};
RN [1] {ECO:0000313|EMBL:KDB20168.1, ECO:0000313|Proteomes:UP000024533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR816 {ECO:0000313|EMBL:KDB20168.1,
RC ECO:0000313|Proteomes:UP000024533};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Trichophyton interdigitale MR816.";
RL Submitted (FEB-2014) 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:KDB20168.1}.
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DR EMBL; AOKY01000886; KDB20168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059IXM2; -.
DR STRING; 1215338.A0A059IXM2; -.
DR HOGENOM; CLU_008570_0_0_1; -.
DR OMA; HYKSDKV; -.
DR Proteomes; UP000024533; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Reference proteome {ECO:0000313|Proteomes:UP000024533}.
FT DOMAIN 498..531
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 802..890
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 802..890
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1003
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 134704 MW; C1C9FC188FE348E2 CRC64;
MSSSQAVAAS LMGPPPPDAV PERSRFDRLD DRHQQHPQHH REQSQRQTTP TPASTAAEEA
SAATLPAAAN TSEAKLSSDD APDRQSSPQS ESQKQAAAST LLAQLLSSQT TAAAAAPNTE
TSVTATTTTT TTTTTTTTTT STTDNNSNNT SPDHPVAAVN SDSNAWPNSS EQQQQQQEQH
QRPETAATPP ANATDASAVN DFHGLPKMGD LSAADALPAI DMQADPSMLG SLDNVDLKVS
DLNAHNFSDF TALATTPVNP RDAIDHNALL TSGAAYYDDS PTMNGGGPTP RIVGYPDFSN
STDVKGREGS ESVAGSEPRI QAFAKLEFDD GHFYVNTYSF ILGRDVRAAR AAFQREYQAK
QNNKAHSSSG HKTRTPSRVK REGSAYMGSV ISDKGGIMGF DPDIPQNGPP QMSWKSSNSS
ADQVARPLLH ISQGESQANS EPREMTDYNA LAMQSLQRGH HEPKRVDTLS LLPSPEACPT
IPIHPPMPAH GGSSHRAISR KHVKIAYNFH KNVFEMEVIG RNGAFMGADW LAPGQVRPLH
SGDFIQIGGV RVRFLLPDVP IGDTGADAAP SSPPEMGQGL PDQPENEVPE ASVERPTVEK
ESERSEADEP VKAKGKAQQQ QQQQRHDPKA TAAEPGQAKR RGPGRPPKDG IMSKRERAEI
AREQKLAAKR EANGVAAATA ASSPPAGITA GKKPAKAARE PASASTTAPA AGPSAISPEE
PSTAPVKVEK RKYTKRKKPD STPGETVMQS IEGGGAGIAA NMEIQQHTEP IRPPAPKKRK
PSKSPSPDYP PESFYTPKEL AKPPYNYAVL IFDALSESPT PMTLKQIYRA LKLKYPYFRF
KCETEGWTSS VRHNLNGNTH LFMHAERDGK GWSWKLIPGA SVDKEKKRRP SPPPVQDVSS
NSQQRFLPPN TPGAPYNAPP GQFNNNRRQY PPYQQPPPNA QFSPHQQQQQ QQQAPLQTPS
ATQPSQPVAA AKPPPLPPPP QPPAAIAVPP AHPPAPSLPP QLLKSLPPAL SVVNLTPYRS
PYILASPSFV PPQQRPPHQQ PIQPHPPPPT HPPIHHQQQQ PRPPPPQMQQ PHHPQPPPQQ
QQPPPNQYRF HNQILPPNHG QPHRPPQQSQ PPPPPQHAQA PPPPPLHNTP VTSAPASQPS
HLPPTTAPAP TQPNVSVPAP VPTPAQTPVQ KPGGMEPAFL ARANQAIDNF EAVLIEDYED
KDYIRNVLRS ARDRVLHNAK ESSFPGGETK DETVIIDALR GIIGSLGQDH
//
