ID A0A150V2C7_9PEZI Unreviewed; 380 AA.
AC A0A150V2C7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase {ECO:0000256|PIRNR:PIRNR037755};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR037755};
GN ORFNames=M433DRAFT_69321 {ECO:0000313|EMBL:KYG44495.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG44495.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG44495.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG44495.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase.
CC {ECO:0000256|PIRNR:PIRNR037755}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC {ECO:0000256|ARBA:ARBA00009725, ECO:0000256|PIRNR:PIRNR037755}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYG44495.1}.
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DR EMBL; JPDO01000225; KYG44495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V2C7; -.
DR STRING; 766039.A0A150V2C7; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:UniProt.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR GO; GO:0001510; P:RNA methylation; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR026113; METTL2/6/8-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22809:SF11; METHYLTRANSFERASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR22809; METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR PIRSF; PIRSF037755; Mettl2_prd; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|PIRNR:PIRNR037755};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Transferase {ECO:0000256|PIRNR:PIRNR037755}.
FT DOMAIN 154..260
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 380 AA; 44131 MW; E3126FCE543DDF28 CRC64;
MRAYVTIAPE PTPPPTPPFP SAEQDAYGVP ALYQPLRQAH TKSRVDNPQK RRDPFQFGTR
YLEEGDDIFA HNAWDHVEVD PQYNDFIQQQ TVFQRENAVT DFDKKRFNER PEKWWDKFYS
NNRANFFKDR KWLVQEFPIL GEVTKENYGA CTVLEVGAGA GNTAFPLLTM NRNPDLRVHA
CDYSKKAIEV MRNAKEYVQQ GEPATLRADV WDAASDDLPP GLQEGKVDLI LMIFIFSALS
PRQWEQAVRN IYRLLKPGGE VLFRDYGRGD LAQVRFKKGR YLEDNFYVRG DGTRVYFFEE
NELRNIWTGQ AFGKRTSSTV DEGPAFEIVN LAVDRRMLVN RQRKLKMYRC WMQGRFRKSS
ETPELKRIET DGEAQTAISP
//
