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TRML_GEOSE
ID   TRML_GEOSE              Reviewed;         157 AA.
AC   P32813;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Putative tRNA (cytidine(34)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885};
DE            EC=2.1.1.207 {ECO:0000255|HAMAP-Rule:MF_01885};
DE   AltName: Full=ORF3;
DE   AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 2334 / Var. Non-diastaticus;
RX   PubMed=1339360; DOI=10.1016/0378-1119(92)90438-u;
RA   Mallinder P.R., Pritchard A., Moir A.;
RT   "Cloning and characterization of a gene from Bacillus stearothermophilus
RT   var. non-diastaticus encoding a glycerol dehydrogenase.";
RL   Gene 110:9-16(1992).
CC   -!- FUNCTION: Could methylate the ribose at the nucleotide 34 wobble
CC       position in tRNA. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01885};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01885}.
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DR   EMBL; M65289; AAA22478.1; -; Genomic_DNA.
DR   PIR; JS0680; JS0680.
DR   AlphaFoldDB; P32813; -.
DR   SMR; P32813; -.
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   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; 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.
DR   TIGRFAMs; TIGR00185; tRNA_yibK_trmL; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..157
FT                   /note="Putative tRNA (cytidine(34)-2'-O)-methyltransferase"
FT                   /id="PRO_0000159821"
FT   BINDING         79
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT   BINDING         104
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT   BINDING         125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
SQ   SEQUENCE   157 AA;  18174 MW;  726E6147D740F1C1 CRC64;
     MALHVVLFQP EIPANTGNIA RTCAATNTAL HLIRPLGFST DDKMLRRAGL DYWEFVNIHY
     YDSLDHFFQQ NQNGDFYYIT KFGKRYYTSY DFSDPSKEIF FIFGRETTGL PKELLAENED
     RCLRIPMTEN VRALNLSNTA AILVYEALRQ QSFHGLS
 
 
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