ID A0A0A2LLP2_PENIT Unreviewed; 390 AA.
AC A0A0A2LLP2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase {ECO:0000256|PIRNR:PIRNR037755};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR037755};
GN ORFNames=PITC_092750 {ECO:0000313|EMBL:KGO77315.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO77315.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO77315.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO77315.1,
RC ECO:0000313|Proteomes:UP000030104};
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:KGO77315.1}.
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DR EMBL; JQGA01000203; KGO77315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2LLP2; -.
DR STRING; 40296.A0A0A2LLP2; -.
DR HOGENOM; CLU_029724_1_1_1; -.
DR OMA; PAKYWDI; -.
DR OrthoDB; 5471626at2759; -.
DR PhylomeDB; A0A0A2LLP2; -.
DR Proteomes; UP000030104; 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:KGO77315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Transferase {ECO:0000256|PIRNR:PIRNR037755, ECO:0000313|EMBL:KGO77315.1}.
FT DOMAIN 136..245
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..327
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"
FT COMPBIAS 308..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 44521 MW; A7E15FDFA44E6D29 CRC64;
MTVEPNIQEV TQNVEPPQVA PHRSHDPTNN LKRTDPFQFG SRYLEKGDDV FEFNAWDHVE
PDDEFKAFAE TQYARQRETR VSDFDRNRFN TNPAKWWDIF YKNNTANFFK DRKWLRQEFP
ILAEVTQKDA GPQVVLEVGA GAGNTAFPLL ANNENEHLKV HACDFSKYAV KVMRESELYN
EKYMSADVWD AAAVPDENGD SLPPGLTEGS VDVVILIFIF SALAPNQWDQ AIRNIYRLLK
PGGRVLFRDY GRGDLAQVRF KKGRYMAENF YIRGDGTRVY FFEQDQLVDM WGTWSAENGL
QIPIGDENPE DASEKKTDEP SAKAKQLAKD NGAFEVVNMG ADRRLIVNRG TKQKMYRCWM
QGNFLKRGGA EAKAEAKSEA KAEAVTESTQ
//
