TRMA_NEIM0
ID TRMA_NEIM0 Reviewed; 367 AA.
AC A9M1Q1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, 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=NMCC_1592;
OS Neisseria meningitidis serogroup C (strain 053442).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=374833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=053442;
RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA Liang X., Xu J., Jin Q.;
RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT clone.";
RL Genomics 91:78-87(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABX73740.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000381; ABX73740.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002220458.1; NC_010120.1.
DR AlphaFoldDB; A9M1Q1; -.
DR SMR; A9M1Q1; -.
DR EnsemblBacteria; ABX73740; ABX73740; NMCC_1592.
DR KEGG; nmn:NMCC_1592; -.
DR HOGENOM; CLU_043022_0_0_4; -.
DR Proteomes; UP000001177; 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..367
FT /note="tRNA/tmRNA (uracil-C(5))-methyltransferase"
FT /id="PRO_0000388559"
FT ACT_SITE 318
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
SQ SEQUENCE 367 AA; 41780 MW; F7190EEF9A1DDC7F CRC64;
MSDYTQQLQD KKDHLKTLFA GLDVPEWEVY ESPDKHYRMR AEFRIWHEGG EMFYAMFEKG
QKAGGASLIR CDRFEAASEA VNRLMPELIA VAAQSAELRN RWYAVEFLST LSGEMLVTMI
YHKRLDNEWM QAAQALQQQL DISVIGRSRG QKIVLKQDYV TETLKVGNRD FRYRQIEGSF
TQPNAAVCQK MLEWACGAAE GLDGDLLELY CGNGNFTLPL SEKFERVLAT EISKTSVSAA
QWNIEANRIG NIKIARLSAE EFTEAYTGKR EFKRLKDGGI ALTDYAFSTI FVDPPRAGID
EETLKLVSQF DNIIYISCNP ETLRTNLDTL AETHTVERAA LFDQFPFTHH IESGVLLKKK
ILGKSKR
