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Database: UniProt
Entry: A0A319EUM1_9EURO
LinkDB: A0A319EUM1_9EURO
Original site: A0A319EUM1_9EURO 
ID   A0A319EUM1_9EURO        Unreviewed;       834 AA.
AC   A0A319EUM1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=N-methyltransferase {ECO:0000313|EMBL:PYH94932.1};
GN   ORFNames=BO71DRAFT_398530 {ECO:0000313|EMBL:PYH94932.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH94932.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH94932.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH94932.1,
RC   ECO:0000313|Proteomes:UP000247810};
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; KZ825863; PYH94932.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319EUM1; -.
DR   STRING; 1448320.A0A319EUM1; -.
DR   Proteomes; UP000247810; 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; IPR034660; DinB/YfiT-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.
DR   SUPFAM; SSF109854; DinB/YfiT-like putative metalloenzymes; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:PYH94932.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247810};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PYH94932.1}.
FT   DOMAIN          27..331
FT                   /note="Histidine-specific methyltransferase SAM-dependent"
FT                   /evidence="ECO:0000259|Pfam:PF10017"
FT   DOMAIN          370..492
FT                   /note="DinB-like"
FT                   /evidence="ECO:0000259|Pfam:PF12867"
FT   DOMAIN          554..832
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
FT   REGION          689..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   834 AA;  94418 MW;  B5181D37B21CB212 CRC64;
     MSPLCPVAKG VEIVDIRQND VAFSLVNDIQ RGIDPPPGTS RSMPTMLLYD AQGLKLFEDI
     TYLEEYYLTN AEIEVLQANA RRIVERIPDN AQLLELGSGN LRKVEILLRE FEAVGKNVDY
     YALDLSLSEL ERTFSEVSID QYHHVDLHGL HGTYDDALSW LNNPENRESP TVILSMGSSL
     GNFDRSSASK FLSQYSKILG PSDLMIIGLD SCVDSDKVYK AYNDSKGITR QFYENGLVHA
     NSVLGYEAFK PDEWNVETDY DIVEGRHQAF YVPTRDVTIN GILLPKGERL IFEEAFKYDA
     RQCEELWHEA GFIHDFEFTN ASGEYCVHLL SSAALSCPTS PSQYAAHVVP SFEDFQSLWT
     AWDIVTKAMV PHEDLLSKPI KLRNSLIFYL GHIPTFLDIH LTRALGSKPT HPKSYQLIFE
     RGIDPDVDDP EKCHKHSEIP DEWPAVQDIM DYQERVRGRV RSIFQKHNVA DNRCLSEALW
     IGFEHEAMHL ETFLYMLLQS ERTLSPPAVP RPDFEKLFRE AREDEKPNEW FVIPKQTLSI
     GLEDDGISTP SVSFGWDNEK PRRTATVEAF EAQARPITNG EYAKYLQANQ LPQKPESWVL
     VKSDAASNGV GQNGSHAPKN FLGNFAVRTV FGPVPLELAQ DWPVIASYDE LAKYAKWVDC
     RIPTFEEARS IYAYSDRLKE TSHSMLNGHS SSNGVNGNGF THPNPLKPRT PNHQPVQDPS
     SESMPVFVNL DDCNVGFKHW HPTPVIQNGD QLAGQGDMGG AWEWTSTTLA PHDEFEAMQI
     YPGYTSDFFD GKHNVILGGS WATHPRIAGR TTFVNWYQRN YPYPWAGARL VRDL
//
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