ID   LCSQ_PURLI              Reviewed;         596 AA.
AC   A0A179GC70;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Nucleotidyltransferase lcsQ {ECO:0000303|PubMed:27416025};
DE            EC=2.7.7.- {ECO:0000305|PubMed:27416025};
DE   AltName: Full=Leucinostatins biosynthesis cluster protein Q {ECO:0000303|PubMed:27416025};
DE   Flags: Precursor;
GN   Name=lcsQ {ECO:0000303|PubMed:27416025}; ORFNames=VFPBJ_11787, VFPFJ_08910;
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: Nucleotidyltransferase; part of the gene cluster that
CC       mediates the biosynthesis of the lipopeptide antibiotics leucinostatins
CC       that show extensive biological activities, including antimalarial,
CC       antiviral, antibacterial, antifungal, and antitumor activities, as well
CC       as phytotoxic (PubMed:27416025). The function of lcsQ within the
CC       leucinostatins biosynthesis has not been identified yet (Probable).
CC       {ECO:0000269|PubMed:27416025, ECO:0000305|PubMed:27416025}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
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 tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. {ECO:0000305}.
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DR   EMBL; LSBH01000009; OAQ74993.1; -; Genomic_DNA.
DR   EMBL; LSBI01000008; OAQ83107.1; -; Genomic_DNA.
DR   RefSeq; XP_018175735.1; XM_018325983.1.
DR   AlphaFoldDB; A0A179GC70; -.
DR   STRING; 33203.A0A179GC70; -.
DR   EnsemblFungi; OAQ74993; OAQ74993; VFPBJ_11787.
DR   EnsemblFungi; OAQ83107; OAQ83107; VFPFJ_08910.
DR   GeneID; 28891032; -.
DR   KEGG; plj:VFPFJ_08910; -.
DR   OrthoDB; 730946at2759; -.
DR   Proteomes; UP000078240; Unassembled WGS sequence.
DR   Proteomes; UP000078340; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd05398; NT_ClassII-CCAase; 1.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; Reference proteome; RNA-binding; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..596
FT                   /note="Nucleotidyltransferase lcsQ"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000446613"
FT   REGION          475..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  66953 MW;  F5DF83B6617B3654 CRC64;
     MLLRLSPSRM ALKRKLDSFL RNVHSQSAPP AAMAHARTVR LSAREEQLRA LLLDVCRSID
     AAGDVTQPII LRWAGGWVRD KLLGIESHDI DVAINAMTGV HFAQRMCDFC TLPDAIKRHG
     IGPRDVGNLH NVARNPDKSK HLETAMVKIF GLDLDFVNLR RETYADDSRN PAMEFGSAEE
     DALRRDATIN ALFFNLHTGC VEDFTGGLPD MAARMIRTPL DPLQTFTDDP LRVLRLVRFA
     SRLQFYIDPA TQRVMDHPTV LQALRVKISR ERVGVELEKM LKGTCPPQVE VHFWAQPTRR
     ALELLDELHL YHAIFTDPAR EPTERPDLRR WHVAYECLGW LLGNRSPGSI GTLLAQSEEA
     VYVAWNLAAV SPWMPVEEPP GVKKKANALP PVAVIAREGF RAPNKLTDVM AASHRHRKEI
     LQLKEAVCHG EPWTRQRDRC GMAIRRWDSQ GGFWTLQVLS TLLVDAMEQV DSWPIVAHPG
     KPSQPADVPE TPLSSGASKS KNLDPSIAKR DDFITGWQKF LDHVVELNVY NAPTMKRLLD
     GRALAQALGV KPGKWTGKAL DVCMAWQLRN PDETDPSKAI EEVRMRRDEL GIPLDG