LCSO_PURLI
ID LCSO_PURLI Reviewed; 593 AA.
AC A0A179HKZ8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=ABC1 family protein lscO {ECO:0000303|PubMed:27416025};
DE AltName: Full=Leucinostatins biosynthesis cluster protein O {ECO:0000303|PubMed:27416025};
GN Name=lcsO {ECO:0000303|PubMed:27416025}; ORFNames=VFPBJ_02529, VFPFJ_04701;
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, FUNCTION,
RP AND INDUCTION.
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: ABC1 family protein; part of the gene cluster that mediates
CC the biosynthesis of the lipopeptide antibiotics leucinostatins that
CC show extensive biological activities, including antimalarial,
CC antiviral, antibacterial, antifungal, and antitumor activities, as well
CC as phytotoxic (PubMed:27416025). The function of lcsO within the
CC leucinostatins biosynthesis has not been identified yet (Probable).
CC {ECO:0000269|PubMed:27416025, ECO:0000305|PubMed:27416025}.
CC -!- INDUCTION: Expression is positively regulated by the leucinostatins
CC biosynthesis cluster-specific transcription regulator lcsF.
CC {ECO:0000269|PubMed:27416025}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
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DR EMBL; LSBH01000002; OAQ83762.1; -; Genomic_DNA.
DR EMBL; LSBI01000004; OAQ90542.1; -; Genomic_DNA.
DR RefSeq; XP_018179261.1; XM_018321781.1.
DR AlphaFoldDB; A0A179HKZ8; -.
DR SMR; A0A179HKZ8; -.
DR STRING; 33203.A0A179HKZ8; -.
DR EnsemblFungi; OAQ83762; OAQ83762; VFPBJ_02529.
DR EnsemblFungi; OAQ90542; OAQ90542; VFPFJ_04701.
DR GeneID; 28886830; -.
DR KEGG; plj:VFPFJ_04701; -.
DR OrthoDB; 790106at2759; -.
DR Proteomes; UP000078240; Unassembled WGS sequence.
DR Proteomes; UP000078340; Unassembled WGS sequence.
DR CDD; cd13969; ADCK1-like; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR045307; ADCK1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..593
FT /note="ABC1 family protein lscO"
FT /id="PRO_0000446610"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 67402 MW; CDB9A9F5858E68F4 CRC64;
MDVAFPGMER HDEKNPPGDD GTKPTGGKKA RPAIKIKWYW KGLILLVELC IGDYLLDRYV
FGGVMLRTTI AYAVLARVGL DYKLHYGKDC WLARHPEEDL HHRNAQRVCT MLKWNGGLYL
KAGQAVAMQG SVLPEEYQRM FGEMFDDAPH SSWSDVEKVI KQDFGGRSIE DVFGVAPSDQ
QGDSQFVFER EPRASASIAQ VHYARLPDGR GLAVKVQRRE ISKQVSWDLW SMKLMTEYTA
WVTGLPMGGM GQFVADRVMQ ETDFEHEASN SEKMADLIAT DSSLRDRVYI PKVYREFTSK
RVLTTEWVDA VQLWDRDAIT GQVAPSRSAT SDKPGLGLRL DDVMRTVVEL FSAQMFSWGF
VHCDPHPGNI LVRQNPKRPD SAQVVLLDHG LYITMSDKLR RQYARFWKAL VTNDDASLQR
VSREWGMKSA DAWADASLMR PYKNPSSSDD ESGESWQRTK ETPEERKQRM IDEAAAYLGD
EGLFPRELLF LERNITIVQG NNRFLGSPVN RIKLIGSCAL KAIRDDGQGK ESIRERISTR
VALLSLDLAF WWSAMKQYFG YGEGLEQELK EAEDRQLRET KDAVAELFGI TVN