TRMA_NEIGO
ID TRMA_NEIGO Reviewed; 225 AA.
AC P55134;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=tRNA/tmRNA (uracil-C(5))-methyltransferase;
DE EC=2.1.1.-;
DE EC=2.1.1.35;
DE AltName: Full=tRNA (uracil(54)-C(5))-methyltransferase;
DE AltName: Full=tRNA(m5U54)-methyltransferase;
DE Short=RUMT;
DE AltName: Full=tmRNA (uracil(341)-C(5))-methyltransferase;
DE Flags: Fragment;
GN Name=trmA;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8441767; DOI=10.1006/plas.1993.1005;
RA Sarandopoulos S., Davies J.K.;
RT "Lack of substantial sequence homology between the cryptic plasmid and
RT chromosome of Neisseria gonorrhoeae.";
RL Plasmid 29:41-49(1993).
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). {ECO:0000250}.
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 -!- 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;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. TrmA subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01024}.
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DR EMBL; M90807; AAA63404.1; -; Genomic_DNA.
DR AlphaFoldDB; P55134; -.
DR SMR; P55134; -.
DR PRIDE; P55134; -.
DR GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; -; 1.
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.
PE 3: Inferred from homology;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN <1..>225
FT /note="tRNA/tmRNA (uracil-C(5))-methyltransferase"
FT /id="PRO_0000161866"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT NON_TER 1
FT NON_TER 225
SQ SEQUENCE 225 AA; 25680 MW; 9AB84BA4C8B7215B CRC64;
IRCDRFDAAS EAVNCLMPEL IAVAAQSAEL RNHWYAVEFL STLSGEMLVT MIYHKRLDDE
WMKAAQALQQ QLDISVIGRS RGQKIVLKQD YVTETLRVGD RDFHYRQIEG SFTQPNAAVC
RKMLEWACAR RKAWGGDLLE LYCGNGNFTL PLSRYFRQVL ATEISKTSVS AAQWNIEANW
IGNIKIARLS AEEFTEAYTG KREFTRLKES GIVLTDYAFS TIFVD
