ID A0A2A3S4L5_9GAMM Unreviewed; 181 AA. AC A0A2A3S4L5; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 24-JAN-2024, entry version 23. 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 ORFNames=A6J60_000105 {ECO:0000313|EMBL:PNK59446.1}, A6J60_013255 GN {ECO:0000313|EMBL:PNK61733.1}; OS Psychrobacter sp. FDAARGOS_221. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Psychrobacter. OX NCBI_TaxID=1975705 {ECO:0000313|EMBL:PNK59446.1, ECO:0000313|Proteomes:UP000217719}; RN [1] {ECO:0000313|Proteomes:UP000217719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_221 {ECO:0000313|Proteomes:UP000217719}; RA Hoffmann M., Allard M., Evans P., Brown E., Tallon L., Sadzewicz L., RA Sengamalay N., Ott S., Godinez A., Nagaraj S., Vavikolanu K., RA Aluvathingal J., Nadendla S., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:PNK59446.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FDAARGOS_221 {ECO:0000313|EMBL:PNK59446.1}; RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J., RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Vyas G., RA Aluvathingal J., Nadendla S., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (DEC-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: 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:PNK59446.1}. 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; NWFK02000001; PNK59446.1; -; Genomic_DNA. DR EMBL; NWFK02000001; PNK61733.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2A3S4L5; -. DR OrthoDB; 9789043at2; -. DR Proteomes; UP000217719; 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 GO; GO:0030488; P:tRNA methylation; 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; TrmL. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR PANTHER; PTHR42971; TRNA (CYTIDINE(34)-2'-O)-METHYLTRANSFERASE; 1. DR PANTHER; PTHR42971:SF1; TRNA (CYTIDINE(34)-2'-O)-METHYLTRANSFERASE; 1. DR Pfam; PF00588; SpoU_methylase; 1. DR PIRSF; PIRSF029256; SpoU_TrmH_prd; 1. DR SUPFAM; SSF75217; alpha/beta knot; 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}; 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}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}. FT DOMAIN 3..154 FT /note="tRNA/rRNA methyltransferase SpoU type" FT /evidence="ECO:0000259|Pfam:PF00588" FT BINDING 82 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1" FT BINDING 112 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1" FT BINDING 134 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1" FT BINDING 142 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1" SQ SEQUENCE 181 AA; 20350 MW; 1DFBB86F8781934E CRC64; MTIHIVLVHP RIPNNTGSAI RLCANTGAQL HLVEPLGFDL EDKKLRRAGL DYHEYANMQV HKDWEQAKQA LNQAGCERMV ALTTKLSHPF YEYDFAQTDS GDKIENIALV FGSETAGLAD DIRADIGEKN WLRLPMLPDS RSLNLANSVS ICLYEVWRQQ GFVGDEGRST GYTELTPYDP K //