ID Q1ZL49_PHOAS Unreviewed; 368 AA.
AC Q1ZL49;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=tRNA/tmRNA (uracil-C(5))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01011};
DE EC=2.1.1.35 {ECO:0000256|HAMAP-Rule:MF_01011};
DE AltName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01011};
DE AltName: Full=tRNA(m5U54)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01011};
DE Short=RUMT {ECO:0000256|HAMAP-Rule:MF_01011};
DE AltName: Full=tmRNA (uracil(341)-C(5))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01011};
GN Name=trmA {ECO:0000256|HAMAP-Rule:MF_01011};
GN ORFNames=VAS14_23129 {ECO:0000313|EMBL:EAS62988.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS62988.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS62988.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS62988.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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:0000256|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:0000256|HAMAP-
CC 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:0000256|HAMAP-Rule:MF_01011};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. TrmA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01011}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAS62988.1}.
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DR EMBL; AAOJ01000012; EAS62988.1; -; Genomic_DNA.
DR RefSeq; WP_005372566.1; NZ_CH902603.1.
DR AlphaFoldDB; Q1ZL49; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_043022_0_0_6; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000001603; Unassembled WGS sequence.
DR GO; GO:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; IEA:UniProtKB-UniRule.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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_sf.
DR InterPro; IPR011869; TrmA_MeTrfase.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR NCBIfam; TIGR02143; trmA_only; 1.
DR PANTHER; PTHR47790; TRNA/TMRNA (URACIL-C(5))-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR47790:SF2; TRNA_TMRNA (URACIL-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01011};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01011};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01011};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01011}.
FT ACT_SITE 326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 326
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT ACT_SITE 360
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 301
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 368 AA; 42875 MW; C01B8D293D491BA9 CRC64;
MTSTILNTAG YQQQLDEKAE RIQNIFVDFD TPELEVFASP AEHYRMRAEF RVWHEGEDLF
YIMFNQETRE KYRVDQFPAA SRLINDLMPM LVDAIKPIKA LRHKLFQVDF LSTLSGEILV
SMLYHRQLDD EWTAEAKQLK QRLNDEGFKL NLIGRARKMK IVLDQDYVIE QLKVHDRTLT
YKQVENSFTQ PNGEVAQKML EWAVDCTQDS EGDLLELYCG NGNFSLALAQ NFERVLATEL
AKPSVDSAQY NIAVNNIDNV QIIRMSAEDF TDAMEGKREF RRLKDQNVDL QSYNCNTIFV
DPPRSGMDEG TCRMVQGYER IMYISCNPET LKENLDILCE THKITRFALF DQFPYTHHME
AGVLLERK
//
