ID A0A1E4TH33_9ASCO Unreviewed; 616 AA.
AC A0A1E4TH33;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 02-APR-2025, entry version 31.
DE RecName: Full=FHA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CANCADRAFT_116276 {ECO:0000313|EMBL:ODV91071.1};
OS Tortispora caseinolytica NRRL Y-17796.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Trigonopsidomycetes; Trigonopsidales; Trigonopsidaceae; Tortispora.
OX NCBI_TaxID=767744 {ECO:0000313|EMBL:ODV91071.1, ECO:0000313|Proteomes:UP000095023};
RN [1] {ECO:0000313|Proteomes:UP000095023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17796 {ECO:0000313|Proteomes:UP000095023};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Jeffries T.W., Grigoriev I.V.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR EMBL; KV453842; ODV91071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4TH33; -.
DR OrthoDB; 5954824at2759; -.
DR Proteomes; UP000095023; 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 CDD; cd22701; FHA_FKH1-like; 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; IPR030456; TF_fork_head_CS_2.
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; SM00339; FH; 1.
DR SMART; SM00240; FHA; 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; 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:UP000095023}.
FT DOMAIN 84..146
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 279..368
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 279..368
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 67506 MW; AB4A92506F3163FF CRC64;
MADETRQEPP VSEPHKTEAL PEDGLDQTLP SLSSLSQFSN LPATTTTEEQ TSHPPEDSPN
ESRVSAYARL DFDTFTFYLQ TLELFLGRRS SKKLAHEDSQ DKVDVDLGPS KSISRRHARI
FFNFGHQRFE ITITGRNGAF VNGTYVELGV TVPLTHNTRV QIGQIPFTFV LPDMPDDAKP
ELYMDALDIE ENAIGKRKHR PSNADTEIVD EKKPRRKRSK AKTKSDQEIT SDKESKPEKE
PKADKDAKLD KKTKPKDEFA PYPYEELPED QIPPEYRERP NISLSQILIE VIRKYGNEKG
MSLSQIYRGI QESYPYFRYR PPGWQSSVRH NLSLNKVFTK ASKEAKNFLW GLDEQAVTEM
EEKRKRQAAQ AKVNQESKSQ NSRTHSQTVP AAPKLAANNS DQLSQLRALI SQMKQKQQGT
GSPSPAPTSN TASAAPITRM PTVSAGTACI DSASSARAAD ERTAADEHET PGDNKSATQT
PTPANITETQ SSVANQPPSS ATIPATTGEQ IPQITSTDAT KVASVPMTEG SPSVKPSTPA
PVAPSVSHAP PRATPQPATK GAAAAINPEV LNLLKEKLKA QLGDNISPQV LAEAIRKTIQ
QKKQAAGAMT ASQAKS
//
