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Database: UniProt
Entry: A0A1A6A9B9_9TREE
LinkDB: A0A1A6A9B9_9TREE
Original site: A0A1A6A9B9_9TREE 
ID   A0A1A6A9B9_9TREE        Unreviewed;      1759 AA.
AC   A0A1A6A9B9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Pre-rRNA-processing protein fhl1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=I303_02662 {ECO:0000313|EMBL:OBR86652.1};
OS   Kwoniella dejecticola CBS 10117.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296121 {ECO:0000313|EMBL:OBR86652.1, ECO:0000313|Proteomes:UP000078595};
RN   [1] {ECO:0000313|EMBL:OBR86652.1, ECO:0000313|Proteomes:UP000078595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10117 {ECO:0000313|EMBL:OBR86652.1,
RC   ECO:0000313|Proteomes:UP000078595};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus dejecticola CBS10117.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR   EMBL; KI894029; OBR86652.1; -; Genomic_DNA.
DR   RefSeq; XP_018264494.1; XM_018406000.1.
DR   STRING; 1296121.A0A1A6A9B9; -.
DR   GeneID; 28966361; -.
DR   VEuPathDB; FungiDB:I303_02662; -.
DR   OrthoDB; 5385885at2759; -.
DR   Proteomes; UP000078595; 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; 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:SF29; PRE-RRNA-PROCESSING PROTEIN FHL1; 1.
DR   PANTHER; PTHR21712; UNCHARACTERIZED; 1.
DR   Pfam; PF00498; FHA; 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; 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:UP000078595}.
FT   DOMAIN          411..456
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          1157..1254
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        1157..1254
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          65..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1239..1278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1423..1514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1571..1759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..221
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..408
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..591
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..789
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..823
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..916
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        993..1013
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1106
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1240..1278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1433..1465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1578..1626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1670..1692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1705..1745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1759 AA;  182572 MW;  64B9AAB5079C98DF CRC64;
     MSEQYVLNNN AYQLDDQYNY AGATVGAGPS NPTTTATAMF SPGDGGDFSG PAPMSTPMPM
     PMRSMGQDVF SSAAGPSNSN MNSTGQGQGQ GLGQGPNQWY PPIPSLASLP VDKSKTDPKP
     AYYKLQFGDE VTGFSYYVRT LAVMIGRNVD RHGSALPPPS ITAPSVPINP PLDPNQPSPP
     LIASVEDIMM PQIALAEFPT PPLPPAHTSF SVPPQSPPHP SSAPLSTTFL NDGFAVPPRA
     QSEGMIDHAG PPDLSFLQDE DYPDIDMGGF GVLEELAEAV RAESIKAASM ERSVEPDSRM
     SQSLSIPPNG SQEGGLSDFM VKLEEGVKAE SAELDFIGTG DRQIPIVIDE PSGSAGPQAM
     EVDHSQSQSQ RQVMNDISAM DMDLSQVKLE HLDDLPPPPP PPPPKSSAPV EHVDVDLGPL
     KSVSRNHAKI EYKADLGHFC LEIFGRNGAW VDDRYFVKGS IVPLAQGSQI QIATRIFSFV
     LPPSPVSSPT YTHYALDGVT PEIAEDLPYP YNLPPSEVGY HEFYGEPGPG PSSAASMAAR
     APPAFNAFAA ADGYGLGIEG VGENSWVGWG SDDDDGGDSE EDEEELDESG EEWEPSPPKS
     VKPKKTKMKS KASKGGLVPG EEESELSSVA SEGEDTKKKP KKQTLPATAP TTTSHVIRPK
     PIAPAPAPSQ IVPPPIAASI TAPGQLPTTI APADMILPPA DVKAAESRKS SVADNPKANK
     DAEGKLTSPK KVKKKKDKDK EKEKEKEMDK AQDKGKAQDK DKDETQGKDK NKPEDKAGNT
     KDNEPKTGDV VVDKNTIQAT DNATKVNETK DKSAADGAKG DDPKKKKKKK KPKPDEDTVK
     VEAVDTTAIN GDGKEKDKDA AAATPKKAKK SKNAEVDKTA GAAEDIKPEI SEKKKKKKKP
     KADADADGKA ADGKADSAKQ LDTPAVPAEP PTLAAALPPP ATVGTAASAA QPMPTLAAAM
     GPTSTPKPPN AVSAASHQPA AQPPPAPITQ RPGQQLAPVQ PGQPGQPTHV QAGQSIPVRP
     PMPGVRPPSQ LQLPNGQHVR PPIPGQPQTP PNYPPGQVPH PQHQPVGPGQ PHPSQIARPP
     PFGHPMQPQN RSTPPAAPPS PVPLPPFYCT ELNETPGQPG HIIVNVPIPP SGAGPRPPPG
     PLLGLDGNVF IGPPPLKPTQ TFATIIHRSL QCLPRGRGTL GEVCNWVAGE WEWFRLNVDS
     GWQNSIRHNL SLNKAFLKVP RIPEDDPESK GSVWIIDPEE GPLFEEKQKK DAQKSASKDK
     NAESRREKER IRAEERAKKQ REAAIEAARN PPQMIQRTIP VAPRPIPRPV PVAQPAAPPA
     PPAPVSANAK GILQPKAKIV VVMQPITAAM RARSVISTTD ANGNLLPFVC DGTTLVLDQS
     TFGHLTSDIM DKLTLLGAAG AVDVLSAWVI NKNKQQATKA AQAKAGTGAT AGVKNGMTAN
     TTGSAKPGVS SATSTSATTS AARPLAATPT AAATANKPSA PAAATPGAPA KPVVGAKPAV
     NSATGKPIPG PAPPGTSLTK VIGMIAAVAN AKGDVNTVGP NASALLRYIR VVGVDIDLRV
     AERIWATGVV PPLPQKKAPT KSNASGTNAA NGNATTAKAA TPAHTTNPSA KPGSASNAVS
     ASKVPSPAGP TPSPASATSA LKPPAPTVSA APAINKSPAP APASAPLSQA EAAVPNTNKA
     SVGASPTATA VSTGVKRKLE DGDDNVSALS STKGTGTGSS ASNPIVIGGS AGASGSNTIL
     GASGEQQENK KPRLETSGA
//
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