TRMB_BOVIN
ID TRMB_BOVIN Reviewed; 277 AA.
AC Q2YDF1;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_03055};
DE AltName: Full=Methyltransferase-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03055};
DE AltName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03055};
DE AltName: Full=miRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
GN Name=METTL1 {ECO:0000255|HAMAP-Rule:MF_03055};
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methyltransferase that mediates the formation of N(7)-
CC methylguanine in a subset of RNA species, such as tRNAs, mRNAs and
CC microRNAs (miRNAs). Catalyzes the formation of N(7)-methylguanine at
CC position 46 (m7G46) in tRNA. Also acts as a methyltransferase for a
CC subset of internal N(7)-methylguanine in mRNAs. Internal N(7)-
CC methylguanine methylation of mRNAs regulates translation. Also
CC methylates a specific subset of miRNAs, such as let-7. N(7)-
CC methylguanine methylation of let-7 miRNA promotes let-7 miRNA
CC processing by disrupting an inhibitory secondary structure within the
CC primary miRNA transcript (pri-miRNA). Acts as a regulator of embryonic
CC stem cell self-renewal and differentiation. {ECO:0000255|HAMAP-
CC Rule:MF_03055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a guanosine in mRNA + S-adenosyl-L-methionine = an N(7)-
CC methylguanosine in mRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60508, Rhea:RHEA-COMP:15584, Rhea:RHEA-COMP:15585,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; Evidence={ECO:0000255|HAMAP-Rule:MF_03055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60509;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a guanosine in miRNA + S-adenosyl-L-methionine = an N(7)-
CC methylguanosine in miRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60512, Rhea:RHEA-COMP:15587, Rhea:RHEA-COMP:15588,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; Evidence={ECO:0000255|HAMAP-Rule:MF_03055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60513;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03055};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03055}.
CC -!- SUBUNIT: Forms a complex with WDR4. {ECO:0000255|HAMAP-Rule:MF_03055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03055}.
CC -!- PTM: Phosphorylation at Ser-28 inactivates its catalytic activity but
CC does not affect the interaction with WDR4. {ECO:0000255|HAMAP-
CC Rule:MF_03055}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_03055}.
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DR EMBL; BT029912; ABM06158.1; -; mRNA.
DR EMBL; BC110252; AAI10253.1; -; mRNA.
DR RefSeq; NP_001039542.1; NM_001046077.2.
DR AlphaFoldDB; Q2YDF1; -.
DR SMR; Q2YDF1; -.
DR STRING; 9913.ENSBTAP00000022487; -.
DR PaxDb; Q2YDF1; -.
DR PRIDE; Q2YDF1; -.
DR Ensembl; ENSBTAT00000022487; ENSBTAP00000022487; ENSBTAG00000016908.
DR GeneID; 511197; -.
DR KEGG; bta:511197; -.
DR CTD; 4234; -.
DR VEuPathDB; HostDB:ENSBTAG00000016908; -.
DR VGNC; VGNC:31400; METTL1.
DR eggNOG; KOG3115; Eukaryota.
DR GeneTree; ENSGT00390000017840; -.
DR HOGENOM; CLU_050910_3_0_1; -.
DR InParanoid; Q2YDF1; -.
DR OMA; DLHNWMV; -.
DR OrthoDB; 1417652at2759; -.
DR TreeFam; TF314083; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000016908; Expressed in digestive system secreted substance and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025763; Trm8_euk.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR PANTHER; PTHR23417; PTHR23417; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00091; TIGR00091; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..277
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000284065"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 108..109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 141..142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 161
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 239..241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT MOD_RES 28
FT /note="Phosphoserine; by PKB and RPS6KA3"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP6, ECO:0000255|HAMAP-
FT Rule:MF_03055"
SQ SEQUENCE 277 AA; 31323 MW; 4860363A97727ADC CRC64;
MAGTETGDAA GTEAPQPQKR YYRQRAHSNP MADHTLRYPV KPEDMDWSEL YPEFFAPLPQ
NQSHDDPKDK KEKRAQAQVE FADIGCGYGG LLVELSPLFP DTLILGLEIR VKVSDYVQDR
IRALRAAPGG GFQNIACLRS NAMKHLPNFF HKGQLTKMFF LFPDPHFKRT KHKWRIISPT
LLAEYAYVLR VGGLVYTITD VLELHEWMCT HFEGHPLFER VPLEELSEDP IVGHLGTSTE
EGKKVLRNGG KNFPAIFRRI QDPALPAVTP TPTPPGH
