(data stored in ACNUC9543 zone)

SWISSPROT: TRMA_YERPA

ID   TRMA_YERPA              Reviewed;         367 AA.
AC   Q1CBU2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 80.
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=YPA_0111;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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}.
DR   EMBL; CP000308; ABG12080.1; -; Genomic_DNA.
DR   RefSeq; WP_002209474.1; NZ_CP009906.1.
DR   SMR; Q1CBU2; -.
DR   EnsemblBacteria; ABG12080; ABG12080; YPA_0111.
DR   KEGG; ypa:YPA_0111; -.
DR   HOGENOM; HOG000218626; -.
DR   KO; K00557; -.
DR   OMA; DHMESGV; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01011; RNA_methyltr_TrmA; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases.
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.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q1CBU2.
DR   SWISS-2DPAGE; Q1CBU2.
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..367
FT                   /note="tRNA/tmRNA (uracil-C(5))-methyltransferase"
FT                   /id="PRO_0000281473"
FT   ACT_SITE        324
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   ACT_SITE        358
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         190
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         218
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         223
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         239
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT   BINDING         299
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
SQ   SEQUENCE   367 AA;  42413 MW;  E1A36A9382D2BEC5 CRC64;
     MTPNILPIES YDHQLAEKSA RLKAMMLPFQ APEPEIFRSP ADHYRMRAEF RVWHDEDDLY
     HIMFDQQTKQ RIRVEQFPVA SRLINRLMDA LMTAIRAEPL LRRKLFQIDY LSTLSGKLIA
     SLLYHRQLDE EWQQKALELR DQLRAQGFDL QLIGRAAKTK IMLDHDYIDE VLPVAGREMI
     YRQVENSFTQ PNAAVNIHML EWALDVTQGA TGDLLELYCG NGNFSLALAR NFERVLATEI
     AKPSVAAAQY NIAANNIDNV QIIRMSAEEF TQAMQGVREF NRLKGIDLGS YNCETIFVDP
     PRSGLDHETV KLVQAYPRIL YISCNPETLC ANLEQLQHTH KISRLALFDQ FPYTHHMECG
     VLLEKRH
//

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