ID A0A0G4IHI0_PLABS Unreviewed; 260 AA. AC A0A0G4IHI0; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 29-MAY-2024, entry version 33. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055}; DE EC=2.1.1.33 {ECO:0000256|HAMAP-Rule:MF_03055}; DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055}; DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055}; GN ORFNames=PBRA_000466 {ECO:0000313|EMBL:CEO94681.1}; OS Plasmodiophora brassicae (Clubroot disease agent). OC Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida; OC Plasmodiophoridae; Plasmodiophora. OX NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO94681.1, ECO:0000313|Proteomes:UP000039324}; RN [1] {ECO:0000313|EMBL:CEO94681.1, ECO:0000313|Proteomes:UP000039324} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E3 {ECO:0000313|EMBL:CEO94681.1}; RA Chooi Y.-H.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46 CC (m7G46) in tRNA. {ECO:0000256|HAMAP-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:0000256|HAMAP- CC Rule:MF_03055}; CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_03055}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03055}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. TrmB family. {ECO:0000256|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; CDSF01000001; CEO94681.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0G4IHI0; -. DR STRING; 37360.A0A0G4IHI0; -. DR EnsemblProtists; CEO94681; CEO94681; PBRA_000466. DR OMA; LPNYFAK; -. DR OrthoDB; 116813at2759; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000039324; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0043527; C:tRNA methyltransferase complex; IEA:TreeGrafter. DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. 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 3: Inferred from homology; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_03055}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03055}; KW Reference proteome {ECO:0000313|Proteomes:UP000039324}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_03055}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_03055}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03055}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_03055}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_03055}. FT ACT_SITE 163 FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055" FT BINDING 74 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055" FT BINDING 97..98 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055" FT BINDING 140..141 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055" FT BINDING 160 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055" FT BINDING 237..239 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055" SQ SEQUENCE 260 AA; 29679 MW; 41D4672C674D4518 CRC64; MPRQFQMSLP FQRVQGKRFV RIRAHVNPLS FSDQYVCPDG PSSVVWKEYF PKFPGVSDDA PAGLDDTVRF VDAGCGFGGL LEALAPTFPN KMILGMEIRE QVVKHVNTRL NCLQAGSKGA SEWKSEDIPA YSNIGVCHTN VMKYMVKFFQ KGQLEKLFFL FPDPHFKRSN HRRRIISPNL LSEYAYVLQV GGLIYNVTDV EDLFNWTVTH FEAHPLFERL SEVEVAADPA VPAMFQTDEA RRVKKNNGTT FVSVWRRIQD //