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Database: UniProt
Entry: A0A139HHR3_9PEZI
LinkDB: A0A139HHR3_9PEZI
Original site: A0A139HHR3_9PEZI 
ID   A0A139HHR3_9PEZI        Unreviewed;      1343 AA.
AC   A0A139HHR3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Fork-head domain-containing protein {ECO:0000259|PROSITE:PS50039};
GN   ORFNames=AC578_2563 {ECO:0000313|EMBL:KXT01942.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT01942.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT01942.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT01942.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) 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:KXT01942.1}.
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DR   EMBL; LFZN01000048; KXT01942.1; -; Genomic_DNA.
DR   STRING; 321146.A0A139HHR3; -.
DR   OrthoDB; 5385885at2759; -.
DR   Proteomes; UP000070133; 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   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   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:UP000070133}.
FT   DOMAIN          836..911
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        836..911
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          910..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1294..1343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..79
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..727
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..965
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1084..1104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1136..1156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1159..1186
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1190..1220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1230..1260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1310..1334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1343 AA;  144022 MW;  B07246347C4916FD CRC64;
     MNPMTPLSIR PRRVQSMGQQ VAGYSGATST FSPLLSSVQE AAAAYQPPPP FPFASSVANV
     PAAPSFLPPP PPPTHPWPHY TSTRPAGPSR ERNAPSSWVI SRKMESAGSI APAAPAQSAS
     ESHIMTGTGL EGVKEHDAEN SNHHMSHATL PSPFNTTPNS GQWPGIGIDT PVQSTIDHGV
     ESSIRNTAAF GLDNMPKPGA DPVQVNGNMA DPPVPLHPHM NGDDFAAFGY PADTVSSLEE
     PETTLSAAAE EPTPEVHNAF AMLQFPDSYC YVHTPYLMLG RDLKFEAYVK AQRKQERRAA
     KREAKRKKAQ RHAAEFLANY EQEPSMPSVY DDQLASDDEP ADDGNLVGHP MPSLLSNYSQ
     QGGVVSFVGE DDQDMIMAQY QHRKKKLNSS SNHSIAPQSL HDLAEGDALH TEGYTGREYP
     DADPSEWAQL SVHPQNPDAI GSISKEHLLL KYNPDLGRWV ADVHGQNGIW IEEKHHQKGA
     RDIILNHGAE IFIGEIGFFF CLPSNVVAQL QQQEMGQDDD DDEVLESVEV DSNVGTSPAA
     RRISDTVDSV PSDDEDDVAL AERSQKTKAK KSKEPKKPLG KIKLSLGKKA RPPAEEAAGS
     GTGKGKGKGK GKGKGKDKSS AKSTAKAKAQ DGATKEDAKA EEQSQSAGEP QAKTEASPTA
     GPADPSGERA AKPPRPEPKL DPTSAFANAA PGQLPEKRKG PGRPPKNGLL SKRDDAAVKR
     KLREYDRIGQ RPPALPILLE MVRSEQRAKD AAAKAQAKGE PLPDAPVPTI EASGAPHPAV
     PGPSQPVGVA QTPLQGSGSP NDVPAQRQMP PTLPRRARSP SPIKPEHEFT EEQLKKPTMT
     YIYIIDEILT NIEGGQADLQ TIYDKIQKRW PFFKYRVNSV GWQSSVRHNL LQSDRFVEAG
     KSGKGKYWTI DHNYPLSDKK RKPTPPPRPQ MPYQYGPYGQ QPMNGQMAYN PNGQAGPSNY
     ASPYTASGPN PPPQPGPMRQ NSNGHYQQQG PHANGPPRPP LQQAQYNPLV LAIVAFRIQY
     LSQFAPEQVN TMTEAFDELT AEVENFLKAS IAAPSGAEAK FDVNSEPCKT LLTIFDAHKD
     DWMTPTVQTP QPADSSTPAP TQVAAPGAQT AAPAQPANNI ASANAGAGQP QGAPPMPVTQ
     HGQQGVGQNG SQNMAPNGPG AAPAPPRPQA PPQPQSQYPP HPPYMQAAPA GITGTSTSVA
     PNQNGISASA KTQNAATAPP PPQYTHGLPT PQHVAASSAM PSTINPPPAS MATNSMPERT
     TDRTQESHAA VDSKVEWSPM PQAIAEQERQ PLKTACQGTW TPIEEPRPTS AGVKRSREDE
     AEDMETKRVK SGTEGVGEQK PPE
//
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