TRMB_XENLA
ID TRMB_XENLA Reviewed; 273 AA.
AC Q6NU94;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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;
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 (APR-2004) 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. {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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_03055}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC068703; AAH68703.1; -; mRNA.
DR RefSeq; NP_001084693.1; NM_001091224.1.
DR AlphaFoldDB; Q6NU94; -.
DR SMR; Q6NU94; -.
DR DNASU; 414654; -.
DR GeneID; 414654; -.
DR KEGG; xla:414654; -.
DR CTD; 414654; -.
DR Xenbase; XB-GENE-6252283; mettl1.L.
DR OMA; DLHNWMV; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 414654; Expressed in blastula and 19 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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: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; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..273
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000370559"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 109..110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 142..143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 240..242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
SQ SEQUENCE 273 AA; 31843 MW; 9E0BE0D49811ADAC CRC64;
MADTQAMASD RGVAVTLPQK RYYRQRAHSN PMADHTFQYP VKPEVMDWSE YYPEFFKPLV
PDCAHDDAKD LQERKEQHQV EFADVGCGYG GLLVALSPLF PNTLMLGLEI RVKVSDYVQD
RIKSLRASHL GQYQNIACIR SNAMKYLPNF FKKGQLSKMF FLFPDPHFKK TKHKWRIISP
TLLAEYSYAL RVGGMVYTIT DVEEVHEWMV KHFTEHPLFE RVEKEELVSD IIVDKLGTST
EEGKKVQRNK GQNFLAVFRR IENRTFIQRD SQQ
