ID A0A2D3VLY9_9PEZI Unreviewed; 1285 AA.
AC A0A2D3VLY9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Fork-head domain-containing protein {ECO:0000259|PROSITE:PS50039};
GN ORFNames=RCC_08232 {ECO:0000313|EMBL:CZT22363.1};
OS Ramularia collo-cygni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT22363.1, ECO:0000313|Proteomes:UP000225277};
RN [1] {ECO:0000313|EMBL:CZT22363.1, ECO:0000313|Proteomes:UP000225277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URUG2 {ECO:0000313|EMBL:CZT22363.1,
RC ECO:0000313|Proteomes:UP000225277};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR EMBL; FJUY01000013; CZT22363.1; -; Genomic_DNA.
DR STRING; 112498.A0A2D3VLY9; -.
DR OrthoDB; 5385885at2759; -.
DR Proteomes; UP000225277; 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; 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:SF29; PRE-RRNA-PROCESSING PROTEIN FHL1; 1.
DR PANTHER; PTHR21712; UNCHARACTERIZED; 1.
DR Pfam; PF00250; Forkhead; 1.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 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:UP000225277}.
FT DOMAIN 743..818
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 743..818
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 26..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..423
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1285 AA; 138177 MW; CD5B21D21F50DAC2 CRC64;
MESENAPALA ALDNDHHNYT FEQELGGLTA MPTMSGLEDN PMLTQTPRRP SPDSNMHAAP
WXETPQLVTD HGVPSNLRDS HGQQEKELPQ VPAQPNPAIE GSTAILDRKP SDALVLSDDG
NDIHNGTMSA ILQDSQTQLS LGPEAPSTPS HMEPTTAAAS PEHITEEAFA MLKFNDSHCY
VRSTNLVIGR DMNFLAKYQQ QKKDEKKKRA RALQARRALD IYAREPSQPS LMGDDDPSGE
SLEGRPEPTG PLSVFSVFSE QGGPVAYNNP YSDDENEEHS RVRRRDRRNK SSSNTSVAPK
SLMAFAEGEN LQAENRYAAD GTLTDPRQWA QLPVHPPIPA DIKKISREHL LFHYDSXRGK
WLLDVIGNGA IFNGVSYMKD TTDLELNHND EIFIATLGMR FMLPESVVNE SEQEEEEEEE
EEQTSATKYA GHGSSTSPAR RLSELFSADD SSDDDDEPLA QVRASAKPPV PKLKLKFKKP
LPKDDLASEP EIVGGNGKGK GKGKAAKSKD KSEKAEKSEK SEKKPEKKSE KKPSKNESKA
ALREEPPPQP TEGSNTTDIT RKPSDAVREA GPSIATGAST EQSPPVVPHV IDPTSVLANL
APDQLPEKRK GPGRPPKNGL LSKRDESGVK RKTKEFERRG VPVPALETLI AMVRQEQKAK
DAANKAQARG EPVPDMPMPS IESSDMAQDG ERGRQQTPRE SHAIESGSPG ADRKLSPRLP
RPIPREASPI KPVTEFTEEE LKKPNMTYIY IIDEVLQNVE GGKADLQAIY DKIMKRWPFY
KYKVGSLGWQ SSVRHNLLSC DRFRDAGKSG KGKLWAINHD HPLDNKKRKP SPPPRPMQMP
MQNGQMPMQN MGQNQFGQPH YNGQYQQPGN GQQPYAGKPG SGPYYSPYTQ XGNYPPNGAH
GMSQXSNGAY PANAXQNPQP HVQQPPAPPN PFQPVIDAIL SFRTAWLASL SEDSELKPDE
LKAHEDAFAR GTNYFSTLYH GSGDATVTDA EISSVEPFMT LKSIFEEHKY LFEQKPAEAN
GPTGGAPGAS SGSQPVKQEL PAESNGPVSG MPPAANQAPM SHGGPAGTSN HPSPMPLQDA
TQTRPLAANG NSTQEHDTQM TSAADLTAAA NSITVSSTQL TPGTEIPTPS NVASNGAPAS
LPXPSVAMAN AGPSGVSMAP PASVVEPSVV DSDPAHASST AEASGGQSSA LPLVAQASMR
STDESQPGAG VSVVSPAAPM TAQQAAPKPT DTPIAVEARL PATPATGQTX ATIGEPSMSS
GGTKRSADDS EAGVEDGDSK RLKLS
//
