ID   A0A319EBD7_ASPSB        Unreviewed;       835 AA.
AC   A0A319EBD7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=N-methyltransferase {ECO:0000313|EMBL:PYI06740.1};
GN   ORFNames=BO78DRAFT_444977 {ECO:0000313|EMBL:PYI06740.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI06740.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI06740.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI06740.1,
RC   ECO:0000313|Proteomes:UP000248423};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00037882}.
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DR   EMBL; KZ826347; PYI06740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319EBD7; -.
DR   STRING; 1448318.A0A319EBD7; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR024775; DinB-like.
DR   InterPro; IPR019257; MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR017805; SAM_MeTrfase_EasF-type_put.
DR   InterPro; IPR005532; SUMF_dom.
DR   InterPro; IPR042095; SUMF_sf.
DR   NCBIfam; TIGR03439; methyl_EasF; 1.
DR   PANTHER; PTHR43397; ERGOTHIONEINE BIOSYNTHESIS PROTEIN 1; 1.
DR   PANTHER; PTHR43397:SF1; ERGOTHIONEINE BIOSYNTHESIS PROTEIN 1; 1.
DR   Pfam; PF12867; DinB_2; 1.
DR   Pfam; PF03781; FGE-sulfatase; 1.
DR   Pfam; PF10017; Methyltransf_33; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:PYI06740.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PYI06740.1}.
FT   DOMAIN          28..330
FT                   /note="Histidine-specific methyltransferase SAM-dependent"
FT                   /evidence="ECO:0000259|Pfam:PF10017"
FT   DOMAIN          370..493
FT                   /note="DinB-like"
FT                   /evidence="ECO:0000259|Pfam:PF12867"
FT   DOMAIN          554..833
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
FT   REGION          685..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..701
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   835 AA;  94740 MW;  4102F11C390D4FB1 CRC64;
     MSPSYPLAKG VDIVDIRQND VEFSLVNDIQ RGIDPPAGTS RSMPTMLLYD AQGLKLFEDI
     TYLEEYYLTN AEIEVLRTHA KRIVERIPDN AQLLELGSGN LRKVEILLQE FEAASKTVDY
     YALDLSLSEL ERTFSEVSLD QYHYVEFHGL HGTYDDALTW LENPENRQLP TVIMSMGSSI
     GNFDRPAAAK FLSQYSRLLG PSDLMMLGLD SCTDPDKVYR AYNDSKGITR QFYENGLTHA
     NAVLGYEAFN PSEWDVVTDY DTVEGRHQAF YVPNREVTIN GVLLSKGEKL IFEEAFKYDA
     KQCDQLWHEA GFIEDAEFGN DSGDYLIHVL SSAALSFPTS PSQYAARPIP GFEEFQSLWT
     AWDIVTKAMV PREELLSKPI KLRNALVFYL GHIPTFLADV HLTRALGGKP THPKSYRLIF
     ERGIDPDVDD PKKCHSHSEI PDEWPALGDI LDYQARVRSR VRSIFQKHNV AEDRTLGEAL
     WIGFEHEAMH LETFLYMLIQ SDRTISPPAV PKPDFEKLFQ DARKEERPNE WFSIPEQTLS
     IGLDDNGHTV PRASFGWDNE KPERTITVKA FEAQARPITN GEYAKYLQAN QLPQKPESWV
     LVKPETYPSS SGTNQGSRRT NDFMANFAIR TVFGSVPLEL AQDWPVIASY DELAKYAKWV
     DCRIPTFEEA KSIYAHAARL RETSHGMNGH SETNGVNGNG YIKTNPMRPR TPDHQPVQHP
     SPETLPVFVD LDDCNVGFKH WHPTPVIQNG DRLAGHGELG GVWEWTSTEL GPHDGFEAMQ
     IYPGYTSDFF DGKHNIILGG SWATHPRIAG RTTFVNWYQR NYPYPWAGAR LVRDV
//