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   27-MAR-2024, entry version 98.
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: Catalytic component of METTL1-WDR4 methyltransferase complex
CC       that mediates the formation of N(7)-methylguanine in a subset of RNA
CC       species, such as tRNAs, mRNAs and microRNAs (miRNAs). Catalyzes the
CC       formation of N(7)-methylguanine at position 46 (m7G46) in a large
CC       subset of tRNAs that contain the 5'-RAGGU-3' motif within the variable
CC       loop. M7G46 interacts with C13-G22 in the D-loop to stabilize tRNA
CC       tertiary structure and protect tRNAs from decay. Also acts as a
CC       methyltransferase for a subset of internal N(7)-methylguanine in mRNAs.
CC       Internal N(7)-methylguanine methylation of mRNAs in response to stress
CC       promotes their relocalization to stress granules, thereby suppressing
CC       their translation. Also methylates a specific subset of miRNAs.
CC       {ECO:0000250|UniProtKB:Q5XJ57}.
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: Catalytic component of the METTL1-WDR4 complex, composed of
CC       mettl1 and 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   AGR; Xenbase:XB-GENE-6252283; -.
DR   CTD; 414654; -.
DR   Xenbase; XB-GENE-6252283; mettl1.L.
DR   OMA; LPNYFAK; -.
DR   OrthoDB; 116813at2759; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 414654; Expressed in blastula and 19 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0106143; C:tRNA (m7G46) methyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106004; P:tRNA (guanine-N7)-methylation; ISS:UniProtKB.
DR   GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1.
DR   PANTHER; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR23417:SF16; TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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   REGION          166..174
FT                   /note="AlphaC helix"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   REGION          240..248
FT                   /note="Alpha6 helix"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
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
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         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
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         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
//