ID A0A0A2L3V7_PENIT Unreviewed; 242 AA.
AC A0A0A2L3V7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RNA methyltransferase {ECO:0000256|RuleBase:RU367087};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU367087};
GN ORFNames=PITC_035570 {ECO:0000313|EMBL:KGO73841.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73841.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO73841.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73841.1,
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 -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000256|ARBA:ARBA00008361, ECO:0000256|RuleBase:RU367087}.
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:KGO73841.1}.
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DR EMBL; JQGA01000771; KGO73841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L3V7; -.
DR STRING; 40296.A0A0A2L3V7; -.
DR HOGENOM; CLU_004729_2_0_1; -.
DR OMA; ELFRGKQ; -.
DR OrthoDB; 1130801at2759; -.
DR PhylomeDB; A0A0A2L3V7; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR039772; Bin3-like.
DR InterPro; IPR010675; Bin3_C.
DR InterPro; IPR024160; BIN3_SAM-bd_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12315; BICOID-INTERACTING PROTEIN RELATED; 1.
DR Pfam; PF06859; Bin3; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51515; BIN3_SAM; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU367087};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU00848};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367087}.
FT DOMAIN 1..242
FT /note="Bin3-type SAM"
FT /evidence="ECO:0000259|PROSITE:PS51515"
SQ SEQUENCE 242 AA; 27232 MW; 02630C4EB57CDA00 CRC64;
MAEACHHDPP ATELSNAERF KATHLAARHG NYHQYYAKFR APTVPDERLS ILPSEILRNA
RVIDLGCNAG KLTYEAIAHC GAAASVGVDI DPWLVEQAKA AYPEGPCTFE HFDFVDASAY
TGTALGKFDV VLLLSVTKWI HLNNGDSGML TLFAHIQSIL NEGGYLVVEP QPMSNYARAS
KKNKELREMY KTIQIRPPFE DELKAQGFER ILQFERDEEG FARPVHVWKK KYHSMINEDG
LK
//
