ID A0A1Q2YFG8_9ASCO Unreviewed; 1158 AA.
AC A0A1Q2YFG8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pre-rRNA-processing protein FHL1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PMKS-001705 {ECO:0000313|EMBL:GAV28235.1};
OS Pichia membranifaciens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4926 {ECO:0000313|EMBL:GAV28235.1, ECO:0000313|Proteomes:UP000186136};
RN [1] {ECO:0000313|EMBL:GAV28235.1, ECO:0000313|Proteomes:UP000186136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS47-1 {ECO:0000313|EMBL:GAV28235.1,
RC ECO:0000313|Proteomes:UP000186136};
RA Konishi M., Ishida M., Arakawa T., Kato Y., Horiuchi J.;
RT "Whole genome shotgun sequence of Pichia membranifaciens KS47-1.";
RL Submitted (AUG-2016) 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:GAV28235.1}.
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DR EMBL; BDGI01000062; GAV28235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2YFG8; -.
DR Proteomes; UP000186136; 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: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 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:UP000186136}.
FT DOMAIN 221..279
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 463..551
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 463..551
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1158 AA; 126094 MW; 2288D6AC31D1C43E CRC64;
MSSLARTAPA SESLHGASPA DSTTAATSST GATNATTGHM FQTAPSTAVS ASAAAYSADT
ASAGPDPTAM KVQHSLELAP PQTQDSNTYG YASSSDLNVQ GKNTVFNGLN IEHFEMEELQ
KINNDGVALH PSTNMEINHI LSEFPEGADT LDDRSKSSKT EEETETVHLQ VSPNESLIKT
KQQINTVDKQ KDETIVDPQK IQAYAMLDFD SFTFYVQTMQ ILLGRMVEGD SLTDALDIHL
GNQKAISRRH AKIFYNFGNQ RFELSVLGRN GAFVDGNFVE KGVTVPLSDG TKIQIGETEF
AFVLPNKEKE AVPVSVPPND QIENLDSLVA NFDEIKKDIQ SDKLLISKDP HVLDMVLDPD
VQKLRELEIE KEIGKVLARE HPEHQNGAHL ENAINGELSQ TNMKKKSTSN LKSGKSSDPS
KDNDALQDPS KAESKAKTKP KRQPKAKKKV YTIDEIPEQY RTKPNLPYSI LITDCLRQKG
TEKGMSLSEI YKGIQELYPY YFYCPDGWQS SVRHNLSLNK SFRKISKEGK GWLWGINEEV
VAEKDRARQK QLENAKAKGK SSSTSTSSPK SIQPSRQLQA NLHIHNPTNV GSKNIVANDS
NNKSTDSLQY ANPSSQNINS SSSASFVHTS ANNKTSEQPA VKAENTSNNT SNNNHSNMSA
NTKKALAYLQ KELISLTKSR KMYDRATSTE ILTKALAMTI SQVDQAAKNF AIKGFPLVIL
IDKNPGHVTK ILTAALNAAT LQVCKQKGLT PHLPPKTPIP PASIPHNKVN ANIDSSARAD
GSKGTPESTN KTIPKAEPGT TNEFSKSPNV PILHIKKEGT ETRDPIFHKA TPKTQSVQSP
LVTNNSQFID EASLSLTPIS GTGTGVNGST ATENNNLLTS QHIDAATPPL QTVNKQATGP
VVYQISKAGI KPSFKPAVKP ISGASVKSFG PSHPAIHQTS IKPIKPVRLG GISGTGIIKP
QFYAKGKVPA TENIRNAAAE GISEEEEIKR SIAKFGRPTA KPAVAMNDSE KKADMEVKEE
IPETEINPIA SNQDSQKSTH YVIENSTLEP SVPSTDKQIE TANKEVKEET KEASISEDKK
ITTLPSKKTK EDGEGDDELD DELHMMLADL EKDEDHDEPE SKKRTIGEVR EHAKGEGEAK
NEMEVEGGDE KRVKTDSN
//
