MFL3_PHOSM
ID MFL3_PHOSM Reviewed; 1232 AA.
AC A0A3G1DJJ7;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=Squalestatin S1 biosynthesis transcriptional activator L3 {ECO:0000303|PubMed:27056201};
GN Name=L3 {ECO:0000303|PubMed:27056201};
OS Phoma sp. (strain ATCC 20986 / MF5453).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Phoma.
OX NCBI_TaxID=1828523;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=27056201; DOI=10.1039/c6cc02130a;
RA Bonsch B., Belt V., Bartel C., Duensing N., Koziol M., Lazarus C.M.,
RA Bailey A.M., Simpson T.J., Cox R.J.;
RT "Identification of genes encoding squalestatin S1 biosynthesis and in vitro
RT production of new squalestatin analogues.";
RL Chem. Commun. (Camb.) 52:6777-6780(2016).
CC -!- FUNCTION: Transcription factor that likely regulates the expression of
CC the gene cluster that mediates the biosynthesis of squalestatin S1
CC (SQS1, also known as zaragozic acid A), a lead compound for the
CC treatment of hyper-cholesterolemia by targeting squalene synthase (SS).
CC {ECO:0000305|PubMed:27056201}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:27056201}.
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DR EMBL; KU946987; AMY15054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G1DJJ7; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 4: Predicted;
KW DNA-binding; Metal-binding; Nucleus; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..1232
FT /note="Squalestatin S1 biosynthesis transcriptional
FT activator L3"
FT /id="PRO_0000447829"
FT DNA_BIND 763..790
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 33..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1232 AA; 136132 MW; DF6FFD83CDCD443B CRC64;
MSLSIPGLEY CRFRQTSRAL RRILSFSTTT SPCFADRSTE GMSKRREHPP LPGKQQDIWP
PSLSGMEQPV PSFKSFIRKT PPPTGSPGEK PLPPLPTLHR ESVDTTPSAA INTSPTRTPS
VPFWKAPANW DDSSTPVQEH QAPPVFSPRN YALLLPEASP GGLDSNEPTQ WPFDVAATHH
PRLNSIDEQV DQVSLSSACH LSAASASRSS SPRPDDDPST LSSNSNNDRL VINTTKLYST
SSESSASHNM SPVSPSEVMF SPSNVSTKQK VFGIELPGGP GTTIEDWSSR TPSNPRSETP
KSGLSMQGKK LQRLNRPIST IDPHPSDPDI SAKAQHLDAS LDYHSVLAGV YHEEHAHDAR
PTAARQKNKV PPSTRINPGK QRSGNREMVP RPLSWRKDSN SSFPNSALVD IEEDPKRVPN
SRKRYRKMTN WVPFHQPMHM HKGVSQRVEE TGSNNGSRYP KRKGKDSPES GGVHGKEADG
KSLMPHVRDF ATHVKNGIVS TSHAANRSIT SSPSQPSTAS TPPRAEQHTR LIRLGGGFAL
VRQSPAVTPP SHSSSRLDIS LPLQAPVSRS YGQIPDIEVE PVSRRPSSLY SQQSEAPVAP
GISVNKRNLR ISPSLSPQTR SNTSSPPTSP LAHEVSFPRT PPPPARSPNR PPYRPQKGAE
VVEDERVDSA NEDKSHKKSL HVGIMDMARD ARHAWKKHHQ DAKHEKLKQS IRVLGPTDPG
VAAAGVLVHL TPKAFIHHSS LLNTRTMRTL TIPAAVVKRK QACNSCRHRK RKCDAERPVC
GLCRRWGIAC EYNVPAAERG NPATGTAQPL QAPTRVPVLP GINVDAREAF PDAQTIGLDL
DFTSAESGFG YPALQSISQS RNAPNDQDPI ASFQLPNHDL LVEMVTLFFD NLYHLFPCFH
RKEFMKQLEE GTIQKESTLI LFSMCCLAAR VHPDAAVKKR QQEWYEQAKF SYQLTQRDPY
PALRTIQAAL LLIAHASTAG DFSSSWLFLG KVWRQAVALG INRMDTRNAA SMGIKPQHWN
SGHEQVYGLD KKEGRNAVEK EEYRRTLWLL LVMDRNHAWP TGWPNALPIS HFKVDLPIAD
SLFQEMTPEV QDAPSSNVPF VRNFSCLLGS LSSVTNPAVN VFQYICVAYV LLGQVSEVVH
TLQDEVDTLE YLQACEELDS QIVKLRLSLP RKATSILEAS PEDRGHVVWL QVMLNSCAML
LYYRCVKDES PKDDATNTFL HAVTAAQNVA QV
