ID A0A167XD98_9HYPO Unreviewed; 354 AA.
AC A0A167XD98;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase {ECO:0000256|PIRNR:PIRNR037755};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR037755};
GN ORFNames=AAL_07447 {ECO:0000313|EMBL:KZZ89939.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ89939.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ89939.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ89939.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(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:KZZ89939.1}.
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DR EMBL; AZGY01000023; KZZ89939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167XD98; -.
DR STRING; 1081109.A0A167XD98; -.
DR OrthoDB; 5471626at2759; -.
DR Proteomes; UP000078544; 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:UP000078544};
KW Transferase {ECO:0000256|PIRNR:PIRNR037755}.
FT DOMAIN 154..257
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 40260 MW; 3C672D95C193B7C0 CRC64;
MTATSGDVPG GLDSGTSIAA DKMAALKIDD DHVNAEVPAH RSHDPARNSK RTDPFQFGSR
FLGEGDDVFE FNAWDHVETD DAYKEYAERQ FEMQRQSPVS DFDKGRFNGN PAKWWDQFYK
NNTANFFKNR KWLQQEFPVL AEVTKEDAGP KTLLEIGAGA GNTAFPILAN NRNPELKIHA
CDFSRNAVEV MRGHEMYDTD FIQADVWDVS AGDLPPGLSE ASVDVAIMVF VFSALSPREW
VQAVGNVYRV LKPGGVVCFR DYGRGDLAQV RFRKGRYLEE NFYIRGDGTR VYFFDQDELA
AIWRNCTSPG DIEPREKPLG FEIDNLGVDR RLIVNRAEKL KMYRCWLQGR FRKL
//
