ID A0A0G4IHI0_PLABS Unreviewed; 260 AA. AC A0A0G4IHI0; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 08-MAY-2019, entry version 17. 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). OC Eukaryota; Rhizaria; Cercozoa; Imbricatea; 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 CC position 46 (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- CC COMP:10189, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74480; EC=2.1.1.33; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03055, CC ECO:0000256|SAAS:SAAS01165783}; CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_03055, ECO:0000256|SAAS:SAAS01165788}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03055, CC ECO:0000256|SAAS:SAAS01165793}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. TrmB family. {ECO:0000256|HAMAP- CC Rule:MF_03055, ECO:0000256|SAAS:SAAS01165785}. 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 EnsemblProtists; CEO94681; CEO94681; PBRA_000466. DR OMA; KWRIINQ; -. DR OrthoDB; 1417652at2759; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000039324; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR025763; Trm8_euk. DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb. DR PANTHER; PTHR23417; PTHR23417; 1. DR PANTHER; PTHR23417:SF16; PTHR23417:SF16; 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000039324}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055, KW ECO:0000256|SAAS:SAAS01165782}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03055, KW ECO:0000256|SAAS:SAAS01165792}; KW Reference proteome {ECO:0000313|Proteomes:UP000039324}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03055, KW ECO:0000256|SAAS:SAAS01165794}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03055, KW ECO:0000256|SAAS:SAAS01165789}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03055, KW ECO:0000256|SAAS:SAAS01165791}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03055, KW ECO:0000256|SAAS:SAAS01165786}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_03055, KW ECO:0000256|SAAS:SAAS01165784}. FT REGION 97 98 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_03055}. FT REGION 140 141 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_03055}. FT REGION 237 239 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_03055}. FT ACT_SITE 163 163 {ECO:0000256|HAMAP-Rule:MF_03055}. FT BINDING 74 74 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_03055}. FT BINDING 160 160 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT 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 //