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
//