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TR03_CURCL
ID   TR03_CURCL              Reviewed;         996 AA.
AC   A0A348AXX6;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=KK-1 biosynthesis cluster protein TR03 {ECO:0000303|PubMed:29686660};
GN   Name=TR03 {ECO:0000303|PubMed:29686660}; ORFNames=TRAF135003;
OS   Curvularia clavata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX   NCBI_TaxID=95742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=BAUA-2787;
RX   PubMed=29686660; DOI=10.3389/fmicb.2018.00690;
RA   Yoshimi A., Yamaguchi S., Fujioka T., Kawai K., Gomi K., Machida M.,
RA   Abe K.;
RT   "Heterologous Production of a Novel Cyclic Peptide Compound, KK-1, in
RT   Aspergillus oryzae.";
RL   Front. Microbiol. 9:690-690(2018).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       KK-1, a novel cyclic decapeptide compound with potent antifungal
CC       activity (PubMed:29686660). The nonribosomal peptide synthetase (NRPS)
CC       catalyzes the elongation and cyclization of the decapeptide chain
CC       composed of 1 pipecolic acid residue (Pip), 1 alanine residue (Ala), 1
CC       aspartic acid residue (Asp), 1 isoleucine residue (Ile), 1 glycine
CC       residue (Gly), 1 tyrosine residue (Tyr) and 4 valine residues (Val)
CC       (PubMed:29686660). The Asp, Ile and 3 Val residues are N-methylated by
CC       the 5 methyltransferase domains from the NRPS (found in modules 3, 5,
CC       6, 7 and 9), whereas the Tyr residue is O-methylated, probably by the
CC       cluster encoded O-methyltransferase OMT (PubMed:29686660). The other
CC       tailoring enzymes from the cluster may be involved in further
CC       modifications leading to the synthesis of KK-1 (Probable).
CC       {ECO:0000269|PubMed:29686660, ECO:0000305|PubMed:29686660}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29686660}.
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DR   EMBL; LC371755; BBC83959.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A348AXX6; -.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
PE   4: Predicted;
KW   Antibiotic biosynthesis.
FT   CHAIN           1..996
FT                   /note="KK-1 biosynthesis cluster protein TR03"
FT                   /id="PRO_0000450435"
FT   REGION          307..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   996 AA;  110139 MW;  9AC610F22A5AAB8F CRC64;
     MALQERRAAV TSSDILSAHA ISSPALAAAA INFAASFHRD ARTCCSAHER SQLQKVYRDK
     ILANDKFTAN IAAAFLSVLG PNAGRNDAGA ERERWGDFDR LAQRGKNMRD RESQHLQHQS
     GIIAAWGPRC FEYYGWHVLP LPLLRQVHDL AVLIPSWDDA VELLNSRMLL RHELRVLHGN
     NKALRIGEHS AASKVQDSRS PVERTDIVAA LDWARANATS AAARQAVKEA AQGMNGTPIN
     TFGLKRDCYG MVVPSVGPYD PDGDDDNDED VVDVSPRPAK HIKLSAAEPL RLMFPGSLSH
     VQACQRHDTD GEKASTAPIR SNKLSQSKQP ELDTAAESLR TRHIHNERIN EPLDEVSDCS
     LSLQTIAVGG GSAQEETPDQ DVEHAHPEVE ITSAISSELR KVDERTDGIR IGRVIMRRSH
     CMVREQDNQT NEEGTGEVQS QRDRRARDLG KDMETDMDID SQLEEMLDIH ALEAQRNHEE
     MSDGEDVVAG VAGPGTPTHR AAEEGGCREK EAENAKTDEE QVQDKAALDQ AGNTNTNREV
     ENAAPKAHSQ EGALRASRTG TIVERTVELH STHSIHQRAS VNTTAPTVAR SSDSDDSDSL
     HSPTALQNLQ AYIDTRTHQL TQVLSQLNST PDVRHHAQLQ LDWLSPQRWA SVYVEPEHHM
     GATSSASSDS ADIWCLDWDT FHQYADSNHV FRRPVVIKQK FQDSGMYEVD RYVDMLWQRF
     PEQHIEVQNS ITGTSRLMSM AEYCSTALTV TEAGTSLSDN TTSVSNAVNL RCLARADEPL
     LTRLERFQLL STLASRVAGT IGRTEHSPPS NLESLLGFDA LSFADAFSSS HANLFGGSWV
     RCLDGLKIYA IAADLDAEDW RRFADEGYKW SPRGKGRLIA LEEDDVLFIP PGLRAIHASF
     TPEPCLMEGG MLWDECAIPE ILDELLWIAR HQAGTVQPLE FQLSSLIDAL EQWLNENNHI
     NQSSPSHTAA EERQTLKASI QSLRDCLSGR SAAFPS
 
 
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