ID A0A2A3S4L5_9GAMM Unreviewed; 181 AA. AC A0A2A3S4L5; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 16-JAN-2019, entry version 7. 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; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=1975705 {ECO:0000313|EMBL:PNK59446.1, ECO:0000313|Proteomes:UP000217719}; RN [1] {ECO:0000313|EMBL:PNK59446.1, ECO:0000313|Proteomes:UP000217719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_221 {ECO:0000313|EMBL:PNK59446.1, RC ECO:0000313|Proteomes:UP000217719}; RA Goldberg B., Campos J., Tallon L., Sadzewicz L., Sengamalay N., RA Ott S., Godinez A., Nagaraj S., Vyas G., Aluvathingal J., Nadendla S., RA Geyer C., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx RT tests."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Methylates the ribose at the nucleotide 34 wobble CC position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and CC tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S- CC adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. CC {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- CC homocysteine; Xref=Rhea:RHEA:43088, Rhea:RHEA-COMP:10333, CC Rhea:RHEA-COMP:10334, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74508, ChEBI:CHEBI:74511; CC EC=2.1.1.207; 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- CC COMP:10332, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; CC EC=2.1.1.207; 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 CC methyltransferase superfamily. RNA methyltransferase TrmH family. CC TrmL subfamily. {ECO:0000256|HAMAP-Rule:MF_01885}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 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. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000217719}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885, KW ECO:0000256|SAAS:SAAS00120900, ECO:0000313|EMBL:PNK59446.1}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01885, KW ECO:0000256|PIRSR:PIRSR029256-1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01885, KW ECO:0000256|SAAS:SAAS00121476, ECO:0000313|EMBL:PNK59446.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}. FT DOMAIN 3 154 SpoU_methylase. {ECO:0000259|Pfam: FT PF00588}. FT BINDING 82 82 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1}. FT BINDING 112 112 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_01885, ECO:0000256|PIRSR:PIRSR029256- FT 1}. FT BINDING 134 134 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1}. FT BINDING 142 142 S-adenosyl-L-methionine. FT {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 //