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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
 
 
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