ID A0A702BQ96_SALBN Unreviewed; 243 AA. AC A0A702BQ96; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 27-NOV-2024, entry version 13. DE RecName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ {ECO:0000256|ARBA:ARBA00013781, ECO:0000256|RuleBase:RU362024}; DE EC=2.1.1.200 {ECO:0000256|ARBA:ARBA00012626, ECO:0000256|RuleBase:RU362024}; DE AltName: Full=tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase {ECO:0000256|ARBA:ARBA00031634, ECO:0000256|RuleBase:RU362024}; DE AltName: Full=tRNA Cm32/Um32 methyltransferase {ECO:0000256|ARBA:ARBA00032381, ECO:0000256|RuleBase:RU362024}; GN Name=trmJ {ECO:0000256|RuleBase:RU362024, GN ECO:0000313|EMBL:HAC6694191.1}; GN ORFNames=G0D16_07765 {ECO:0000313|EMBL:HAC6694191.1}; OS Salmonella bongori serovar 44:r:-. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1967585 {ECO:0000313|EMBL:HAC6694191.1}; RN [1] {ECO:0000313|EMBL:HAC6694191.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2702-77 {ECO:0000313|EMBL:HAC6694191.1}; RX PubMed=30286803; DOI=10.1186/s13059-018-1540-z; RA Souvorov A., Agarwala R., Lipman D.J.; RT "SKESA: strategic k-mer extension for scrupulous assemblies."; RL Genome Biol. 19:153-153(2018). RN [2] {ECO:0000313|EMBL:HAC6694191.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2702-77 {ECO:0000313|EMBL:HAC6694191.1}; RG NCBI Pathogen Detection Project; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or CC 2'O-methylated uridine (Um32) at position 32 in tRNA. CC {ECO:0000256|RuleBase:RU362024}. CC -!- CATALYTIC ACTIVITY: CC Reaction=uridine(32) in tRNA + S-adenosyl-L-methionine = 2'-O- CC methyluridine(32) in tRNA + S-adenosyl-L-homocysteine + H(+); CC Xref=Rhea:RHEA:42936, Rhea:RHEA-COMP:10107, Rhea:RHEA-COMP:10290, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.200; CC Evidence={ECO:0000256|ARBA:ARBA00000240, CC ECO:0000256|RuleBase:RU362024}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O- CC methylcytidine(32) in tRNA + S-adenosyl-L-homocysteine + H(+); CC Xref=Rhea:RHEA:42932, Rhea:RHEA-COMP:10288, Rhea:RHEA-COMP:10289, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.200; CC Evidence={ECO:0000256|ARBA:ARBA00000470, CC ECO:0000256|RuleBase:RU362024}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362024}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362024}. CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase CC superfamily. RNA methyltransferase TrmH family. CC {ECO:0000256|ARBA:ARBA00007228}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HAC6694191.1}. 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; DAAMHO010000007; HAC6694191.1; -; Genomic_DNA. DR AlphaFoldDB; A0A702BQ96; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0106339; F:tRNA (cytidine(32)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:TreeGrafter. DR CDD; cd18093; SpoU-like_TrmJ; 1. DR FunFam; 1.10.8.590:FF:000001; tRNA:Cm32/Um32 methyltransferase; 1. DR FunFam; 3.40.1280.10:FF:000006; Uncharacterized tRNA/rRNA methyltransferase HI_0380; 1. DR Gene3D; 1.10.8.590; -; 1. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR004384; RNA_MeTrfase_TrmJ/LasT. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR NCBIfam; TIGR00050; rRNA_methyl_1; 1. DR PANTHER; PTHR42786:SF2; TRNA (CYTIDINE_URIDINE-2'-O-)-METHYLTRANSFERASE TRMJ; 1. DR PANTHER; PTHR42786; TRNA/RRNA METHYLTRANSFERASE; 1. DR Pfam; PF00588; SpoU_methylase; 1. DR PIRSF; PIRSF004808; LasT; 1. DR SUPFAM; SSF75217; alpha/beta knot; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|RuleBase:RU362024}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, KW ECO:0000256|RuleBase:RU362024}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, KW ECO:0000256|RuleBase:RU362024}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:HAC6694191.1}; KW tRNA processing {ECO:0000256|RuleBase:RU362024}. FT DOMAIN 5..154 FT /note="tRNA/rRNA methyltransferase SpoU type" FT /evidence="ECO:0000259|Pfam:PF00588" SQ SEQUENCE 243 AA; 26618 MW; E6BAD434F8EC6096 CRC64; MLQNIRIVLV ETSHTGNMGS VARAMKTMGL TNLWLVNPLV KPDSQAIALA AGASDVIGNA QIVDTLDEAL AGCSLVVGTS ARSRTLPWPM LDPRECGLKS VAEAANTPVA LVFGRERVGL TNDELQKCHY HVAIAANPEY SSLNLAMAVQ VIAYEVRMAW LAAQENGDAA MHEETPYPLV DDLERFYGHL EQTLLSTGFI RENHPGQVMN KLRRLFTRAR PESQELNILR GMLASIEQQN KGK //