ID   TCPN_CLAP2              Reviewed;         281 AA.
AC   M1W079;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=N-methyltransferase tcpN {ECO:0000303|PubMed:27390873};
DE            EC=2.1.1.- {ECO:0000305|PubMed:27390873};
DE   AltName: Full=Thioclapurine biosynthesis protein N {ECO:0000303|PubMed:27390873};
GN   Name=tcpN {ECO:0000303|PubMed:27390873}; ORFNames=CPUR_02672;
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1;
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=27390873; DOI=10.1371/journal.pone.0158945;
RA   Dopstadt J., Neubauer L., Tudzynski P., Humpf H.U.;
RT   "The epipolythiodiketopiperazine gene cluster in Claviceps purpurea:
RT   dysfunctional cytochrome P450 enzyme prevents formation of the previously
RT   unknown clapurines.";
RL   PLoS ONE 11:E0158945-E0158945(2016).
CC   -!- FUNCTION: N-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of an unusual class of epipolythiodioxopiperazines
CC       (ETPs) lacking the reactive thiol group important for toxicity
CC       (PubMed:27390873). Firstly, L-tyrosine is prenylated by tcpD, before
CC       undergoing condensation with L-glycine in a reaction catalyzed by the
CC       NRPS tcpP leading to the diketopiperazine (DKP) backbone
CC       (PubMed:27390873). Afterwards the alpha-carbon of tyrosine is oxidized
CC       by the cytochrome P450 tcpC to form a hydroxyl group (PubMed:27390873).
CC       However, in contrast other ETP biosynthesis pathways studied so far,
CC       tcpC is not able to bishydroxylate the DKP at both alpha-carbon
CC       positions, but hydroxylates the alpha-carbon of the tyrosine part and
CC       the nitrogen of the glycine part (PubMed:27390873). The next steps
CC       involve an alpha,beta-elimination reaction catalyzed by tcpI, a
CC       methylation by the methyltransferase tcpN the action of the four enzyme
CC       cascade tcpG/K/J/I (PubMed:27390873). Due to a dysfunctional cytochrome
CC       P450 monooxygenase tcpC, the pathway leads to the biosynthesis of
CC       probable non-toxic metabolites lacking the reactive thiol group
CC       (PubMed:27390873). {ECO:0000269|PubMed:27390873}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:27390873}.
CC   -!- INDUCTION: Expression is positively regulated by the thioclapurine
CC       cluster-specific transcription factor tcpZ (PubMed:27390873).
CC       {ECO:0000269|PubMed:27390873}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC       methyltransferase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAGA01000011; CCE28981.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1W079; -.
DR   SMR; M1W079; -.
DR   EnsemblFungi; CCE28981; CCE28981; CPUR_02672.
DR   VEuPathDB; FungiDB:CPUR_02672; -.
DR   eggNOG; ENOG502SIG3; Eukaryota.
DR   HOGENOM; CLU_010595_9_3_1; -.
DR   OrthoDB; 1242994at2759; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..281
FT                   /note="N-methyltransferase tcpN"
FT                   /id="PRO_0000437731"
SQ   SEQUENCE   281 AA;  31255 MW;  06A9AB2A5D01CC62 CRC64;
     MESVVDGSSQ SRHQSENDRL NIQHALIKSI MGGKLLMAPV NLERPDLRIL DSGTAQANWL
     LDLAALVPTT AQLTGTDIAP EQFPPPSQRP PNMTLQKQSI FDPWNEAMLG SFDVVHQRFV
     LAACQSDEHG QRAVADLLAL TKPGGWIELH EGNMLAIQEG EAHSAMMRFR DIAVAAWVSI
     GQVPDPGPRL TDWMRDAGVV DMHEEVQTIG LGAAARNQQE AEWSTELCLN MLRTIRRMTA
     GKGADAPSEQ EFDTLEVALR EELQEVGNQW YYYLAYGRRR T