ID A0A0A2IM41_PENEN Unreviewed; 385 AA.
AC A0A0A2IM41;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase {ECO:0000256|PIRNR:PIRNR037755};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR037755};
GN ORFNames=PEX2_036870 {ECO:0000313|EMBL:KGO50516.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO50516.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO50516.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO50516.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO50516.1}.
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DR EMBL; JQFZ01000331; KGO50516.1; -; Genomic_DNA.
DR RefSeq; XP_016593723.1; XM_016740962.1.
DR AlphaFoldDB; A0A0A2IM41; -.
DR STRING; 27334.A0A0A2IM41; -.
DR GeneID; 27676381; -.
DR HOGENOM; CLU_029724_1_1_1; -.
DR OrthoDB; 5471626at2759; -.
DR Proteomes; UP000030143; 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 ECO:0000313|EMBL:KGO50516.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Transferase {ECO:0000256|PIRNR:PIRNR037755, ECO:0000313|EMBL:KGO50516.1}.
FT DOMAIN 136..245
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 385 AA; 44002 MW; 14F3986A732BF164 CRC64;
MTIDPSIQEV TQNVEPPQVA PHRSHDPTNN LKRTDPFQFG SRFLEKGDDV FEFNAWDHVE
PDDEFKAFAE TQYARQRETR VSDFDRNRFN TNPAKWWDIF YKNNTANFFK DRKWLRQEFP
ILAEVTQKDA GPQVVLEVGA GAGNTAFPLL ANNENEHLKI HACDFSKYAV KVMRESELYN
EKYMSADVWD AAGVPDENGD SLPPGLTEGS VDVVILIFIF SALAPNQWDH AIRNIYRLLK
PGGRVLFRDY GRGDLAQVRF KKGRYMAENF YIRGDGTRVY FFEQDQLVDM WGTWSAENGL
QIPIGDEEPT EEASEKKTDE PSAEAKQLAK DNGAFDVLNM GADRRLIVNR GTKQKMYRCW
MQGNFLKRGG AQTEANDAVV AESTQ
//
