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TRMA_TOLAT
ID   TRMA_TOLAT              Reviewed;         367 AA.
AC   C4L9A7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=tRNA/tmRNA (uracil-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_01011};
DE            EC=2.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01011};
DE   AltName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE   AltName: Full=tRNA(m5U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE            Short=RUMT {ECO:0000255|HAMAP-Rule:MF_01011};
DE   AltName: Full=tmRNA (uracil(341)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
GN   Name=trmA {ECO:0000255|HAMAP-Rule:MF_01011}; OrderedLocusNames=Tola_0377;
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dual-specificity methyltransferase that catalyzes the
CC       formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and
CC       that of position 341 (m5U341) in tmRNA (transfer-mRNA).
CC       {ECO:0000255|HAMAP-Rule:MF_01011}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(54) in tRNA = 5-
CC         methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42712, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:10193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.35;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01011};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(341) in tmRNA = 5-
CC         methyluridine(341) in tmRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43612, Rhea:RHEA-COMP:10630, Rhea:RHEA-COMP:10631,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01011};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. TrmA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01011}.
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DR   EMBL; CP001616; ACQ92006.1; -; Genomic_DNA.
DR   RefSeq; WP_012728605.1; NC_012691.1.
DR   AlphaFoldDB; C4L9A7; -.
DR   SMR; C4L9A7; -.
DR   STRING; 595494.Tola_0377; -.
DR   EnsemblBacteria; ACQ92006; ACQ92006; Tola_0377.
DR   KEGG; tau:Tola_0377; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_043022_0_0_6; -.
DR   OMA; DHMESGV; -.
DR   OrthoDB; 1421660at2; -.
DR   Proteomes; UP000009073; Chromosome.
DR   GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01011; RNA_methyltr_TrmA; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR011869; TrmA_MeTrfase.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR47790; PTHR47790; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02143; trmA_only; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..367
FT                   /note="tRNA/tmRNA (uracil-C(5))-methyltransferase"
FT                   /id="PRO_1000213200"
FT   ACT_SITE        325
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   ACT_SITE        359
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         191
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         219
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         224
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         240
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         300
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
SQ   SEQUENCE   367 AA;  42126 MW;  486048CA5A8D8212 CRC64;
     MTNAVHSDAL YQQQLHEKQQ RLTQLLAPFQ APEPEVFASA PSHYRMRAEF RIWHEGVDEL
     YYVMFNSETK QRYYVHEFPT GSQLINRLMP RLLELIRGNH TLKYKLFQID FLTTLSGEAL
     ISLLYHKTLN EAWQPAATEL RQALRAEFGE VDVVGRAHKQ KIVLEREYVL EQLQVGDRTL
     EYMQVENSFT QPNAGMNQQM LGWATDVTAD CQGDLLELYC GNGNFSLALA KNFNRVLATE
     IAKPSVHAAQ HNIAVNKIDN VQILRMSAEE FTQAMNGERE FNRLKGIDLQ SYQCNTILVD
     PPRAGLDPAT VAMIQAYEQI LYISCNPETL CDNLKTLCQT HNIARCALFD QFPFTHHMES
     GVWLVRK
 
 
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