MET1_DOTSN
ID MET1_DOTSN Reviewed; 433 AA.
AC M2YKT1;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Hps1-dma1 cluster O-methyltransferase {ECO:0000303|PubMed:31053329};
DE EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020};
GN ORFNames=DOTSEDRAFT_139328;
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990;
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [3]
RP FUNCTION, AND PATHWAY.
RX PubMed=31053329; DOI=10.1016/j.funbio.2019.02.006;
RA Ozturk I.K., Dupont P.Y., Chettri P., McDougal R., Boehl O.J., Cox R.J.,
RA Bradshaw R.E.;
RT "Evolutionary relics dominate the small number of secondary metabolism
RT genes in the hemibiotrophic fungus Dothistroma septosporum.";
RL Fungal Biol. 123:397-407(2019).
CC -!- FUNCTION: O-methyltransferase; part of the hps1-dma1 gene cluster that
CC probably mediates the biosynthesis a derivative of cyclopiazonic acid
CC (CPA) (Probable). The hybrid polyketide synthase-nonribosomal peptide
CC synthetase (PKS-NRPS) nps1 might incorporates acetyl-CoA, malonyl-CoA,
CC and tryptophan (Trp) and utilizes a C-terminal redox-incompetent
CC reductase domain to make and release the tryptophan tetramic acid,
CC cyclo-acetoacetyl-L-tryptophan (c-AATrp), as the first intermediate in
CC the pathway (By similarity). In addition, the cluster also includes the
CC tryptophan dimethylallyltransferase dma1, the FAD-dependent
CC oxidoreductase toxD, the cytochrome P450 monooxygenase cyp3.1 and the
CC methyltransferase DOTSEDRAFT_139328; the latter 2 being not present in
CC all CPA-producing fungi but involved in additional modifications that
CC occur in biosynthesis the of a range of CPA and CPA-like products
CC (Probable). Further studies are required to clarify whether the CPA-
CC like hps1-dma1 cluster is functional or a non-functional relic
CC reflecting evolution of D.septosporum (Probable).
CC {ECO:0000250|UniProtKB:B6F209, ECO:0000305|PubMed:31053329}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:31053329}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000305}.
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DR EMBL; KB446545; EME39475.1; -; Genomic_DNA.
DR AlphaFoldDB; M2YKT1; -.
DR SMR; M2YKT1; -.
DR STRING; 675120.M2YKT1; -.
DR EnsemblFungi; EME39475; EME39475; DOTSEDRAFT_139328.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_1_4_1; -.
DR OMA; ASFMCEA; -.
DR OrthoDB; 817726at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..433
FT /note="Hps1-dma1 cluster O-methyltransferase"
FT /id="PRO_0000447731"
FT REGION 36..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 285
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 433 AA; 48521 MW; 31FDF08F2A035875 CRC64;
MGGSDHTKTS SQSTLRSLSD EISSLTDVVA GFLESNGHPE RSLNSTDSVR LSDAPEDVEA
ARRRLVTALH EMTLLTMSPF EAVRDILLEV SSLPALHAIS HFEIIDHVPL DGEISYAELA
RKINVPQRRL TRMLRAAMSR SIFQEPRPGY IAHNSLSAAM VHSKWLRYHA ASTMENFLPA
APKFVEQIER FGDRETRCTS PAGIAFNTET DCIQYLLSQP KHQQVLVNLM KHTGEISGMG
PQHLTEHYDW PKASDQIIVD VGGASGSVSR AIACGVPSVR FVVQDRADAV RQGESETPSE
LKDRFTFQEY DFFQTQPVKN ADVYFLRWIL HDWPDEDAVT ILRQVALAMG PTSKMLIAER
LVLLPGEGDP WDQKIATSMD MFMMAFNGSE RTLEHFQSLI ENTGEAIEIS RVIRRPNGVQ
YSLIEVARKD SER