ID A0A7G2HJS2_CRYPV Unreviewed; 451 AA. AC A0A7G2HJS2; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 12-OCT-2022, entry version 8. DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152}; DE EC=2.1.1.228 {ECO:0000256|HAMAP-Rule:MF_03152}; DE AltName: Full=M1G-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152}; DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152}; DE AltName: Full=tRNA methyltransferase 5 homolog {ECO:0000256|HAMAP-Rule:MF_03152}; GN ORFNames=1MB.778 {ECO:0000313|EMBL:CAD98330.1}; OS Cryptosporidium parvum. OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia; OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium. OX NCBI_TaxID=5807 {ECO:0000313|EMBL:CAD98330.1, ECO:0000313|Proteomes:UP000242991}; RN [1] {ECO:0000313|EMBL:CAD98330.1, ECO:0000313|Proteomes:UP000242991} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Iowa {ECO:0000313|EMBL:CAD98330.1}; RX PubMed=12869580; DOI=10.1101/gr.1555203; RA Bankier A.T., Spriggs H.F., Fartmann B., Konfortov B.A., Madera M., RA Vogel C., Teichmann S.A., Ivens A., Dear P.H.; RT "Integrated mapping, chromosomal sequencing and sequence analysis of RT Cryptosporidium parvum."; RL Genome Res. 13:1787-1799(2003). CC -!- FUNCTION: Specifically methylates the N1 position of guanosine-37 in CC various cytoplasmic and mitochondrial tRNAs. Methylation is not CC dependent on the nature of the nucleoside 5' of the target nucleoside. CC This is the first step in the biosynthesis of wybutosine (yW), a CC modified base adjacent to the anticodon of tRNAs and required for CC accurate decoding. {ECO:0000256|HAMAP-Rule:MF_03152}. CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)- CC methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03152}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03152}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP- CC Rule:MF_03152}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03152}. Cytoplasm CC {ECO:0000256|HAMAP-Rule:MF_03152}. Note=Predominantly in the CC mitochondria and in the nucleus. {ECO:0000256|HAMAP-Rule:MF_03152}. CC -!- SIMILARITY: Belongs to the TRM5 / TYW2 family. {ECO:0000256|HAMAP- CC Rule:MF_03152}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. TRM5/TYW2 family. {ECO:0000256|ARBA:ARBA00009775}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03152}. 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; BX538353; CAD98330.1; -; Genomic_DNA. DR Proteomes; UP000242991; Chromosome 6. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_03152; TRM5; 1. DR InterPro; IPR030382; MeTrfase_TRM5/TYW2. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR025792; tRNA_Gua_MeTrfase_euk. DR Pfam; PF02475; Met_10; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03152}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_03152}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP- KW Rule:MF_03152}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03152}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_03152}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03152}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_03152}. FT DOMAIN 161..446 FT /note="SAM_MT_TRM5_TYW2" FT /evidence="ECO:0000259|PROSITE:PS51684" FT BINDING 250 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152" FT BINDING 289..290 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152" FT BINDING 346 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152" SQ SEQUENCE 451 AA; 52762 MW; C46CC329ABF58B4D CRC64; MEELRTNIED CFDTSKIFKS YKLPFIKVKI NNCNYVQNLL KENDILFKFP RVSPIINDEK NKENKLILMG EDLLRNYYKV SDKRMKLEDR SNSELESNGD YIIELSDDFF IKIPRNVFIG LNSIDFAEYG IMDFKIEYKY LSYIECARQC IPNNIEIVSS FETIGHIAHL NLNEDNFQYR YILGKILLDK NPGIKTVVTK TGNIESTFRT YPLEVIGGEN NLKARLKEQG IIYNINIDQV YWNSRLSNER QRIVELIPRK SIVFDLTCGA GAFTLPLIKI KDCTLFSNDL NPDAIKLLKE NMISNKLKDD KVITSQKDYP EKIFKIEKNA LNLISHENDV FYWICNLPEL SLNMLKGFVQ GKKTYLEKKI QENSSFRNTM NHFFFYCFSK DPNPKKDIET RIFTFLESDP TTINSEYFSP INLSIHEVRD VSPNKKMYCA QFSMVIPIQV N //