TRM7_CAEEL
ID TRM7_CAEEL Reviewed; 337 AA.
AC Q22031;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03162};
DE EC=2.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03162};
DE AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog {ECO:0000255|HAMAP-Rule:MF_03162};
GN ORFNames=R74.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and
CC 34 of the tRNA anticodon loop of substrate tRNAs. {ECO:0000255|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 H(+) +
CC 2 S-adenosyl-L-homocysteine; 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:0000255|HAMAP-Rule:MF_03162};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_03162}.
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DR EMBL; Z36238; CAA85279.2; -; Genomic_DNA.
DR PIR; B88422; B88422.
DR PIR; T24259; T24259.
DR RefSeq; NP_497843.1; NM_065442.5.
DR AlphaFoldDB; Q22031; -.
DR SMR; Q22031; -.
DR STRING; 6239.R74.7; -.
DR EPD; Q22031; -.
DR PaxDb; Q22031; -.
DR PeptideAtlas; Q22031; -.
DR EnsemblMetazoa; R74.7.1; R74.7.1; WBGene00011281.
DR GeneID; 175543; -.
DR KEGG; cel:CELE_R74.7; -.
DR UCSC; R74.7; c. elegans.
DR CTD; 175543; -.
DR WormBase; R74.7; CE23932; WBGene00011281; -.
DR eggNOG; KOG1099; Eukaryota.
DR GeneTree; ENSGT00730000111146; -.
DR HOGENOM; CLU_009422_1_1_1; -.
DR InParanoid; Q22031; -.
DR OMA; GLHDMDI; -.
DR OrthoDB; 1362679at2759; -.
DR PhylomeDB; Q22031; -.
DR PRO; PR:Q22031; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00011281; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 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; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10920:SF12; PTHR10920:SF12; 1.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..337
FT /note="Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-
FT methyltransferase"
FT /id="PRO_0000155586"
FT REGION 304..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 53
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
SQ SEQUENCE 337 AA; 37611 MW; 4A92E487252779DF CRC64;
MGKTSRDKRD IYYRLAKENK WRARSAFKLM QIDDEFQILK GVRRAVDLCA APGSWSQVLS
KRLYEEDQEA KIVAIDLQPM APIPGVIQLQ GDITSVDTAN QVIKHFSGEK SDIVICDGAP
DVTGIHSLDE FMQAELILAA FNITSHVLKE GGNFLAKIFR SRNSSLLYAQ MKKYFKKVYL
AKPRSSRQSS CEAFVLCLDY SPPEGFVPTM GKTSLDATDA SAISPDIIDG FVTCGDLSGW
DSEKSYPLDI DACFPKGEID EEQKKRYEFK DVVQPPTDPA YKAALDKKKS GVFAKMSADL
NRQLKAELSR GKDQKKTPAE NVPSVEELEK AAEKFQL
