ID A0A2D9KIZ4_9ALTE Unreviewed; 154 AA. AC A0A2D9KIZ4; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 07-APR-2021, entry version 12. DE RecName: Full=tRNA (cytidine(34)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885}; DE EC=2.1.1.207 {ECO:0000256|HAMAP-Rule:MF_01885}; DE AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmL {ECO:0000256|HAMAP-Rule:MF_01885}; GN Name=trmL {ECO:0000256|HAMAP-Rule:MF_01885, GN ECO:0000313|EMBL:MAP22667.1}; GN ORFNames=CL582_17200 {ECO:0000313|EMBL:MAP22667.1}; OS Alteromonadaceae bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae. OX NCBI_TaxID=1916082 {ECO:0000313|EMBL:MAP22667.1, ECO:0000313|Proteomes:UP000227212}; RN [1] {ECO:0000313|Proteomes:UP000227212} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the RT Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Methylates the ribose at the nucleotide 34 wobble position in CC the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). CC Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH CC of the wobble nucleotide. {ECO:0000256|HAMAP-Rule:MF_01885}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S- CC adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O- CC methyluridine(34) in tRNA(Leu) + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:43088, Rhea:RHEA-COMP:10333, Rhea:RHEA-COMP:10334, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74508, ChEBI:CHEBI:74511; EC=2.1.1.207; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01885}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine(34) in tRNA + S-adenosyl-L-methionine = 2'-O- CC methylcytidine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:43084, Rhea:RHEA-COMP:10331, Rhea:RHEA-COMP:10332, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.207; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01885}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01885}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885}. CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase CC superfamily. RNA methyltransferase TrmH family. TrmL subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01885}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01885}. 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:MAP22667.1}. 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; NZSW01000146; MAP22667.1; -; Genomic_DNA. DR EnsemblBacteria; MAP22667; MAP22667; CL582_17200. DR Proteomes; UP000227212; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-UniRule. DR CDD; cd18094; SpoU-like_TrmL; 1. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_01885; tRNA_methyltr_TrmL; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR016914; tRNA_cyt/urid_MeTfrase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR PANTHER; PTHR42971; PTHR42971; 1. DR Pfam; PF00588; SpoU_methylase; 1. DR PIRSF; PIRSF029256; SpoU_TrmH_prd; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00185; tRNA_yibK_trmL; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_01885, ECO:0000313|EMBL:MAP22667.1}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01885, KW ECO:0000256|PIRSR:PIRSR029256-1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01885, ECO:0000313|EMBL:MAP22667.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}. FT DOMAIN 2..142 FT /note="SpoU_methylase" FT /evidence="ECO:0000259|Pfam:PF00588" FT BINDING 100 FT /note="S-adenosyl-L-methionine; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1" FT BINDING 122 FT /note="S-adenosyl-L-methionine; via amide nitrogen and FT carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1" FT BINDING 130 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1" SQ SEQUENCE 154 AA; 17625 MW; E12854FD2B542B5E CRC64; MLDIVLYQPE IPPNTGNIIR LCANTGYALH LIEPLGFDWD DKRVRRAGLD YHEFAEVKRY ANFDAYLAER NPKRVFACTT KGKAFHSDVQ YQAGDALLFG PETRGLPDDI IESLPPAQRV RIPMLPDSRS MNLSNAVSVF VYESWRQFGY EQAR //