ID A0A0R1JR74_9LACO Unreviewed; 456 AA.
AC A0A0R1JR74;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=TrmA family tRNA (Uracil-5-)-methyltransferase {ECO:0000313|EMBL:KRK71715.1};
GN ORFNames=FD02_GL001958 {ECO:0000313|EMBL:KRK71715.1};
OS Lacticaseibacillus nasuensis JCM 17158.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1291734 {ECO:0000313|EMBL:KRK71715.1, ECO:0000313|Proteomes:UP000051804};
RN [1] {ECO:0000313|EMBL:KRK71715.1, ECO:0000313|Proteomes:UP000051804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17158 {ECO:0000313|EMBL:KRK71715.1,
RC ECO:0000313|Proteomes:UP000051804};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
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:KRK71715.1}.
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DR EMBL; AZDJ01000026; KRK71715.1; -; Genomic_DNA.
DR RefSeq; WP_056951227.1; NZ_AZDJ01000026.1.
DR AlphaFoldDB; A0A0R1JR74; -.
DR STRING; 1291734.FD02_GL001958; -.
DR PATRIC; fig|1291734.4.peg.2010; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000051804; Unassembled WGS sequence.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002792; TRAM_dom.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR NCBIfam; TIGR00479; rumA; 1.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS50926; TRAM; 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|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000051804};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01024}.
FT DOMAIN 7..65
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 287
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 316
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 337
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 385
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 456 AA; 49932 MW; E34CC601D39AA7AA CRC64;
MAVETAPVTK NQELTVTITD LTYEGMGVAK VGDFPLFVAA ALPGEEALIH VVKLQKHFGF
ARVVKLLKTS PDRVAPRDHA YAQTGIAPLQ HLAYPAQLKF KQHQLENVFE KQHLAITVKP
TLGMATPSGY RNKAQIPVRL VNGELTTGFY KQRSHDLIPL EDFYIQDPAI DAAIIVVRDL
LRQYGLTAYD ERTNTGLVRH IMVRRGYYSH ELMIVLVVTS WSVPHLDTIA QALAKQLPEL
ASFMLNLNDQ RTNVVLGRKS RVVSGNDYLT DQLLGNTFHI SAPSFYQVNP QQTEVLYGQA
IAAAGLTGSE TVIDAYSGIG TISLALAKHA KQVYGVEVVP SAVADAKKNA QLNGLDNVTF
TLGKAEEVMQ TWREQALPVD ALVVDPPRKG LAPEFIAATG VLLPPRIVYV SCNPATLARD
IAALTEFGYS ATTTQPVDMF PQTTHIESVT VLTLTR
//
