BN3D2_BOVIN
ID BN3D2_BOVIN Reviewed; 292 AA.
AC Q29S19;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=RNA 5'-monophosphate methyltransferase {ECO:0000250|UniProtKB:Q7Z5W3};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q7Z5W3};
DE AltName: Full=BCDIN3 domain-containing protein;
GN Name=BCDIN3D;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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 -!- SUBUNIT: Interacts with DICER1; the interaction may be mediated by RNA.
CC {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; BC113219; AAI13220.1; -; mRNA.
DR RefSeq; NP_001068684.1; NM_001075216.1.
DR AlphaFoldDB; Q29S19; -.
DR SMR; Q29S19; -.
DR STRING; 9913.ENSBTAP00000023645; -.
DR PaxDb; Q29S19; -.
DR GeneID; 505650; -.
DR KEGG; bta:505650; -.
DR CTD; 144233; -.
DR eggNOG; KOG2899; Eukaryota.
DR HOGENOM; CLU_082749_0_0_1; -.
DR InParanoid; Q29S19; -.
DR OrthoDB; 1185441at2759; -.
DR TreeFam; TF324061; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
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:0008175; F:tRNA methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; IBA:GO_Central.
DR GO; GO:2000632; P:negative regulation of pre-miRNA processing; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; 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..292
FT /note="RNA 5'-monophosphate methyltransferase"
FT /id="PRO_0000289264"
FT DOMAIN 53..274
FT /note="Bin3-type SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00848"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT BINDING 110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT BINDING 135..136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5W3"
SQ SEQUENCE 292 AA; 33490 MW; 570600352C1CA6A8 CRC64;
MAASTEQATG GVEKTAAEEK PRVLEPGAAP FGNFPHYSRF HPPEQRLRLL PPELLRRLFP
QSPETRPILG LDVGCNSGDL SVALYKHFLS LHDGETCLDA SRELHLLCCD IDPVLVERAE
KECPFPDGLT FITLDFMNQR TRKVLLSSFL SQFGRSVFDI GFCMSVTMWI HLNHGDQGLW
EFLAHLSSLC RYLLVEPQPW KCYRAAARRL RKLGLHDFDH FRSLAIRGDM ASQIVQILTQ
DHGMELVCCF GNTKWDRSLL LFRTKQATET HPIPESLIEE GKERNRIRFW RE
