ID S9UXD9_9TRYP Unreviewed; 372 AA. AC S9UXD9; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 27-NOV-2024, entry version 44. DE RecName: Full=Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03162}; DE EC=2.1.1.205 {ECO:0000256|HAMAP-Rule:MF_03162}; DE AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog {ECO:0000256|HAMAP-Rule:MF_03162}; GN ORFNames=STCU_12263 {ECO:0000313|EMBL:EPY15195.1}; OS Strigomonas culicis. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas. OX NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY15195.1, ECO:0000313|Proteomes:UP000015354}; RN [1] {ECO:0000313|EMBL:EPY15195.1, ECO:0000313|Proteomes:UP000015354} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23560078; RA Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R., RA Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M., RA Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M., RA Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F., RA Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K., RA Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C., RA Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P., RA Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P., RA de Souza W., Schenkman S., de Vasconcelos A.T.; RT "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their RT Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae RT Family."; RL PLoS ONE 8:E60209-E60209(2013). CC -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and CC 34 of the tRNA anticodon loop of substrate tRNAs. {ECO:0000256|HAMAP- CC Rule:MF_03162}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine CC = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 S- CC adenosyl-L-homocysteine + 2 H(+); Xref=Rhea:RHEA:42396, Rhea:RHEA- CC COMP:10246, Rhea:RHEA-COMP:10247, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, CC ChEBI:CHEBI:74445, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; CC EC=2.1.1.205; Evidence={ECO:0000256|ARBA:ARBA00035600, CC ECO:0000256|HAMAP-Rule:MF_03162}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03162}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. RNA methyltransferase RlmE family. TRM7 subfamily. CC {ECO:0000256|HAMAP-Rule:MF_03162}. 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:EPY15195.1}. 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; ATMH01012431; EPY15195.1; -; Genomic_DNA. DR AlphaFoldDB; S9UXD9; -. DR EnsemblProtists; EPY15195; EPY15195; STCU_12263. DR OrthoDB; 119516at2759; -. DR Proteomes; UP000015354; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0106339; F:tRNA (cytidine(32)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0106340; F:tRNA (guanine(34)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0002181; P:cytoplasmic translation; IEA:UniProtKB-UniRule. DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:UniProtKB-UniRule. DR FunFam; 3.40.50.150:FF:000220; CAMK protein kinase; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_01547; RNA_methyltr_E; 1. DR HAMAP; MF_03162; RNA_methyltr_E_TRM7; 1. DR InterPro; IPR028590; RNA_methyltr_E_TRM7. DR InterPro; IPR050082; RNA_methyltr_RlmE. DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom. DR InterPro; IPR015507; rRNA-MeTfrase_E. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1. DR PANTHER; PTHR10920:SF12; TRNA (CYTIDINE(32)_GUANOSINE(34)-2'-O)-METHYLTRANSFERASE-RELATED; 1. DR Pfam; PF01728; FtsJ; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03162}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_03162}; Reference proteome {ECO:0000313|Proteomes:UP000015354}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_03162}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03162}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_03162}. FT DOMAIN 21..225 FT /note="Ribosomal RNA methyltransferase FtsJ" FT /evidence="ECO:0000259|Pfam:PF01728" FT REGION 304..372 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 331..349 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 351..372 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 182 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162" FT BINDING 56 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162" FT BINDING 58 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162" FT BINDING 90 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162" FT BINDING 106 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162" FT BINDING 142 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162" SQ SEQUENCE 372 AA; 40102 MW; ADF8B5CC11301C70 CRC64; MGRASKDKRD IYYRKAKEEG YRARSAYKLL QIHEDYHILD PAQVQYGAVD LCAAPGSWSQ VLSSILACPP PGDVPASPAA YVPPPVIAVD LQEMAPIPHV TILQGDITST TTAQQILDLL AAANRRRGAR SADARASIVV CDGAPDVTGL HELDEYLQHQ LLLAALLITT CVLRPGGTFV TKMFRGPNTP FLVHKSELFF EEVRVVKPKS SRNASVESFL LCQRFRLPAG YVPRLRLALP PTAGEPGDVL LQVQGGSHHT PDADTYRVAA GRRTAAAEAL LVPFLSCGDL SGFDADMCYD HEVDEEHTEG GGGAAPHPAG RRAKGHVLPP VQPPLQAPYL PPPPPAPRTR DETDGSARST SPKESPTKKT KQ //