ID   BN3D2_XENLA             Reviewed;         255 AA.
AC   Q7T0L7;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Pre-miRNA 5'-monophosphate methyltransferase;
DE            EC=2.1.1.-;
DE   AltName: Full=BCDIN3 domain-containing protein;
GN   Name=bcdin3d;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: O-methyltransferase that specifically monomethylates 5'-
CC       monophosphate of cytoplasmic histidyl tRNA (tRNA(His)), acting as a
CC       capping enzyme by protecting tRNA(His) from cleavage by DICER1. Also
CC       able, with less efficiently, to methylate the 5' monophosphate of a
CC       subset of pre-miRNAs, acting as a negative regulator of miRNA
CC       processing. The 5' monophosphate of pre-miRNAs is recognized by DICER1
CC       and is required for pre-miRNAs processing: methylation at this position
CC       reduces the processing of pre-miRNAs by DICER1. Was also reported to
CC       mediate dimethylation of pre-miR-145; however dimethylation cannot be
CC       reproduced by another group which observes a monomethylation of pre-
CC       miR-145. {ECO:0000250|UniProtKB:Q7Z5W3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-phospho)-ribonucleoside-RNA + S-adenosyl-L-
CC         methionine = a 5'-end (5'-methylphospho)-ribonucleoside-RNA + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:58656, Rhea:RHEA-COMP:15179,
CC         Rhea:RHEA-COMP:15181, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138282, ChEBI:CHEBI:142776;
CC         Evidence={ECO:0000250|UniProtKB:Q7Z5W3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-phospho)-ribonucleoside-RNA + 2 S-adenosyl-L-
CC         methionine = a 5'-end (5'-bismethylphospho)-ribonucleoside-RNA + 2 S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:58640, Rhea:RHEA-COMP:15179,
CC         Rhea:RHEA-COMP:15182, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138282, ChEBI:CHEBI:142777;
CC         Evidence={ECO:0000250|UniProtKB:Q7Z5W3};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7Z5W3}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC056133; AAH56133.1; -; mRNA.
DR   RefSeq; NP_001079900.1; NM_001086431.1.
DR   AlphaFoldDB; Q7T0L7; -.
DR   SMR; Q7T0L7; -.
DR   MaxQB; Q7T0L7; -.
DR   DNASU; 379590; -.
DR   GeneID; 379590; -.
DR   KEGG; xla:379590; -.
DR   CTD; 379590; -.
DR   Xenbase; XB-GENE-5859397; bcdin3d.L.
DR   OMA; GNFMNYY; -.
DR   OrthoDB; 1185441at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 379590; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008173; F:RNA methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:2000632; P:negative regulation of pre-miRNA processing; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 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; PTHR12315; 1.
DR   Pfam; PF06859; Bin3; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51515; BIN3_SAM; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..255
FT                   /note="Pre-miRNA 5'-monophosphate methyltransferase"
FT                   /id="PRO_0000420471"
FT   DOMAIN          41..253
FT                   /note="Bin3-type SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00848"
FT   BINDING         32
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT   BINDING         96
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT   BINDING         121..122
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT   BINDING         150
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
SQ   SEQUENCE   255 AA;  28629 MW;  2B31F0C678DD1D95 CRC64;
     MSNSESVPHV DPGAAPYGNF PNYYSFNPPE NRISLLPAEL LHKLFRKPAE SDSSTQPLLG
     LDVGCNTGDL SVALYNHLTE PHSKSSDVPV HFLCCDIDPD LITRARASNP FPDFISYATL
     DIMDSSAVRG PVNDFLQQFA RSTFDIAFCM SVTMWIHLNY GDQGLVTFLG HLANLCDYLL
     VEPQPWKCYR SAARRLRKLG RQDFDHFHSL SIRGDMAENI TQILTAEGAA KLIHIFGNTS
     WDRSLLLFKI QRHPC