ID S9UXD9_9TRYP Unreviewed; 372 AA. AC S9UXD9; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 05-JUN-2019, entry version 22. 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; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC Strigomonadinae; Strigomonas. OX NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY15195.1}; RN [1] {ECO:0000313|EMBL:EPY15195.1} 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., RA Brocchi M., Colabardini A.C., de Araujo Lima B., Machado C.R., RA de Almeida Soares C.M., Probst C.M., de Menezes C.B., Thompson C.E., RA Bartholomeu D.C., Gradia D.F., Pavoni D.P., Grisard E.C., RA Fantinatti-Garboggini F., Marchini F.K., Rodrigues-Luiz G.F., RA Wagner G., Goldman G.H., Fietto J.L., Elias M.C., Goldman M.H., RA 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 RT Their Respective Endosymbionts Reveals New Aspects of the RT Trypanosomatidae Family."; RL PLoS ONE 8:E60209-E60209(2013). RN [2] {ECO:0000313|EMBL:EPY15195.1} RP NUCLEOTIDE SEQUENCE. RA Motta M.C.M., Martins A.C.A., Preta C.M.C.C., Silva R., de Souza S.S., RA Klein C.C., de Almeida L.G.P., Cunha O.L., Colabardini A.C., RA Lima B.A., Machado C.R., Soares C.M.A., de Menezes C.B.A., RA Bartolomeu D.C., Grisard E.C., Fantinatti-Garboggini F., RA Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L.R., RA Ciapina L.P., Brocchi M., Elias M.C., Goldman M.H.S., Sagot M.-F., RA Pereira M., Stoco P.H., Teixeira S.M.R., de Mendonca-Neto R.P., RA Maciel T.E.F., Mendes T.A.O., Urmenyi T.P., Teixeira M.M.G., RA de Camargo E.F.P., de Sousa W., Schenkman S., de Vasconcelos A.T.R.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions CC 32 and 34 of the tRNA anticodon loop of substrate tRNAs. CC {ECO:0000256|HAMAP-Rule:MF_03162}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L- CC methionine = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in CC tRNA + 2 H(+) + 2 S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:42396, Rhea:RHEA-COMP:10246, Rhea:RHEA- CC COMP:10247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74445, CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.205; CC Evidence={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 CC methyltransferase superfamily. RNA methyltransferase RlmE family. CC TRM7 subfamily. {ECO:0000256|HAMAP-Rule:MF_03162}. 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: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 EnsemblProtists; EPY15195; EPY15195; STCU_12263. DR OrthoDB; 1362679at2759; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0002181; P:cytoplasmic translation; IEA:UniProtKB-UniRule. DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:UniProtKB-UniRule. 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; IPR015507; rRNA-MeTfrase_E. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR10920:SF12; PTHR10920:SF12; 1. DR Pfam; PF01728; FtsJ; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03162}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03162, KW ECO:0000313|EMBL:EPY15195.1}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03162}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03162, KW ECO:0000313|EMBL:EPY15195.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03162}. FT DOMAIN 21 225 FtsJ. {ECO:0000259|Pfam:PF01728}. FT REGION 304 372 Disordered. {ECO:0000256|MobiDB-lite: FT S9UXD9}. FT COMPBIAS 331 349 Pro-rich. {ECO:0000256|MobiDB-lite: FT S9UXD9}. FT COMPBIAS 351 372 Polyampholyte. {ECO:0000256|MobiDB-lite: FT S9UXD9}. FT ACT_SITE 182 182 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_03162}. FT BINDING 56 56 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_03162}. FT BINDING 58 58 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_03162}. FT BINDING 90 90 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_03162}. FT BINDING 106 106 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_03162}. FT BINDING 142 142 S-adenosyl-L-methionine. FT {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 //