ID   LCSF_PURLI              Reviewed;         552 AA.
AC   A0A179H0U5;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Transcription factor lcsF {ECO:0000303|PubMed:27416025};
DE   AltName: Full=Leucinostatins biosynthesis cluster protein F {ECO:0000303|PubMed:27416025};
GN   Name=lcsF {ECO:0000303|PubMed:27416025}; ORFNames=VFPBJ_02531;
OS   Purpureocillium lilacinum (Paecilomyces lilacinus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX   NCBI_TaxID=33203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP   FUNCTION.
RC   STRAIN=PLBJ-1;
RX   PubMed=27416025; DOI=10.1371/journal.ppat.1005685;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
CC   -!- FUNCTION: Transcription factor that regulates the expression of the
CC       gene cluster that mediates the biosynthesis of the lipopeptide
CC       antibiotics leucinostatins that show extensive biological activities,
CC       including antimalarial, antiviral, antibacterial, antifungal, and
CC       antitumor activities, as well as phytotoxic (PubMed:27416025). All 20
CC       genes in the cluster are up-regulated to some extent by lcsF, with the
CC       exception of lcsL and lcsP, which are down-regulated (PubMed:27416025).
CC       {ECO:0000269|PubMed:27416025}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; LSBH01000002; OAQ83764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A179H0U5; -.
DR   SMR; A0A179H0U5; -.
DR   EnsemblFungi; OAQ83764; OAQ83764; VFPBJ_02531.
DR   Proteomes; UP000078240; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   InterPro; IPR046347; bZIP_sf.
DR   SUPFAM; SSF57959; SSF57959; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN           1..552
FT                   /note="Transcription factor lcsF"
FT                   /id="PRO_0000446607"
FT   DOMAIN          31..76
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          31..55
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          56..63
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          169..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..198
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  60064 MW;  A3E572A2C05E79F0 CRC64;
     MAPASSNPGP YSLPDKDEVQ LSAEDDWTRV KDRKEKKRIQ NRVAQRSYRS RMKARLGELQ
     SRLQAHEEQK AKEEAERCDP SPPSPPSSSA TGLHLHTTPP SGNNAGANDT EPSSINSASP
     PTPPDVVGDL DPSQHAKAID QFSHQMDMAG NDDSQWFLDS TSLLQHGDTS SYIQPSVPTP
     PVSLSQCPPM PAYMPEGPRN PNDGPASLSQ SILQDCLRFQ IQLLAKINNP SEATSTTHKE
     EGSAAKSPGA LQQSHWSSCA TNPAAAAQNM MPSTNMARGN SFSVLPADFH NLDDMMELTS
     TGDLPNATWR PSQQFSGPET TPRSHNAENP TQQQSPINDD TPSTTQHGAV PDCYNAFVAK
     SSAQASSLGM EERLEAAIEG LEALGFTSVD SFAEAYYSSS FDESSHLAAE QSMSRKRRLP
     RMLSQILDSA QSWDPWDRRG LNEEVLRTAE SLLVAEGKSM DEKSLEASIS GLMQATEGSS
     KPTPPQQNVT GMKRVLQNEL PNLWPVMMAL AGGNRASRQR DRSNMVLAAI LILHCSSKMT
     KQKLLEFLDV CL