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TRMA_CAMLR
ID   TRMA_CAMLR              Reviewed;         346 AA.
AC   B9KCK3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Cla_0969;
OS   Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=306263;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX   PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA   Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT   "The complete genome sequence and analysis of the human pathogen
RT   Campylobacter lari.";
RL   Foodborne Pathog. Dis. 5:371-386(2008).
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; CP000932; ACM64292.1; -; Genomic_DNA.
DR   RefSeq; WP_012661675.1; NC_012039.1.
DR   AlphaFoldDB; B9KCK3; -.
DR   SMR; B9KCK3; -.
DR   STRING; 306263.Cla_0969; -.
DR   EnsemblBacteria; ACM64292; ACM64292; CLA_0969.
DR   GeneID; 7410549; -.
DR   KEGG; cla:CLA_0969; -.
DR   PATRIC; fig|306263.5.peg.953; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_043022_1_0_7; -.
DR   OMA; DHMESGV; -.
DR   OrthoDB; 1421660at2; -.
DR   Proteomes; UP000007727; 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; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..346
FT                   /note="tRNA/tmRNA (uracil-C(5))-methyltransferase"
FT                   /id="PRO_0000388550"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   ACT_SITE        337
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         197
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         202
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         218
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         278
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
SQ   SEQUENCE   346 AA;  40357 MW;  637D0C1AB45248E4 CRC64;
     MHFEEKIALN KALFSSLYDK EIQCFKSPLK AYRTRAEFCI YHHENGEISY AMYENKKKIP
     IKNFEIADEK IQAYMPILLD NLNENLKHKL FGVEFLATKI DLSITLLYHK NIESITQDLQ
     ELSKKLNLKL IARSRGKKLV FNGENLKQIL NIKNKEIFYE FNNDCFIQPN TTINEKMIEW
     VIDLLEKEER KDLLELYCGY GNFTIALAKY FNKILATEIS KKNIEFALKN CDLNSIKNIS
     FTRLSSEELS QALKKEREFN RLKGIDLDGF NISHVLVDPP RAGLDVSVIE LIKKYENIIY
     ISCNPITLRE NLEILSQSHE ILNLAFFDQF ANTSHLECGV HLRLKA
 
 
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