ID W6ZBJ6_COCMI Unreviewed; 320 AA.
AC W6ZBJ6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=S-adenosyl-L-methionine-dependent methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=COCMIDRAFT_97145 {ECO:0000313|EMBL:EUC44824.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC44824.1};
RN [1] {ECO:0000313|EMBL:EUC44824.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC44824.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KI963996; EUC44824.1; -; Genomic_DNA.
DR RefSeq; XP_007688638.1; XM_007690448.1.
DR AlphaFoldDB; W6ZBJ6; -.
DR GeneID; 19128997; -.
DR KEGG; bor:COCMIDRAFT_97145; -.
DR eggNOG; ENOG502QS1V; Eukaryota.
DR HOGENOM; CLU_056435_7_0_1; -.
DR OrthoDB; 36423at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR008854; TPMT.
DR PANTHER; PTHR10259; THIOPURINE S-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10259:SF11; THIOPURINE S-METHYLTRANSFERASE; 1.
DR Pfam; PF05724; TPMT; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51585; SAM_MT_TPMT; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 320 AA; 35393 MW; 32FCBE979C393332 CRC64;
MATQNQDRLR TLFSSASDSD HSNRWDDLWR EATFLPWDRG HANPALIDVL SERSRPISSP
DPNPSLGAPP PNSESAGYVS LPGPLREDGK RRRALVPGCG KGYDVALFAA YGYDAYGLEV
SSHAAEAARK YLADPGKGPL EGEYAIKDEK IGRGAMKVVC GDFFDDAWLK DVDGWDGDAG
FDIIYDNTFL CALPPSLRPK WASRMTELLR QSSSNNTGTG GVLICLEFPT HKPVKSGGPP
WSLPPLVHTE LLKQPGRGIL YDDQGVVTKT EREETDNALV KIAHFTPRRT HEIGVIQGLV
RDCVSMWRHK ADCPEEQRWH
//
