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Database: UniProt
Entry: J1F411_9LACO
LinkDB: J1F411_9LACO
Original site: J1F411_9LACO 
ID   J1F411_9LACO            Unreviewed;       458 AA.
AC   J1F411;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=tRNA (Uracil-5-)-methyltransferase {ECO:0000313|EMBL:KRN09711.1};
GN   ORFNames=FD00_GL000853 {ECO:0000313|EMBL:KRN09711.1};
OS   Liquorilactobacillus mali KCTC 3596 = DSM 20444.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1046596 {ECO:0000313|EMBL:KRN09711.1, ECO:0000313|Proteomes:UP000050898};
RN   [1] {ECO:0000313|EMBL:KRN09711.1, ECO:0000313|Proteomes:UP000050898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20444 {ECO:0000313|EMBL:KRN09711.1,
RC   ECO:0000313|Proteomes:UP000050898};
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:KRN09711.1}.
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DR   EMBL; AYYH01000020; KRN09711.1; -; Genomic_DNA.
DR   RefSeq; WP_003688510.1; NZ_BACP01000059.1.
DR   AlphaFoldDB; J1F411; -.
DR   PATRIC; fig|1046596.6.peg.924; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000050898; 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};
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          5..63
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        411
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         286
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         315
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         336
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         384
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   458 AA;  51256 MW;  D13AB6584A7380DB CRC64;
     MSKPPVAKNQ KLTLTISDLT YQGMGVGKVE HYPLFIENAL PDEVVDITVI KVSKNYGFAK
     VINRHNDSPL RTAGIDKTYT QTGIAPLQHL KYDAQLSFKR NQVVELLKKS HLEEVEVAPV
     LGMDKPIHYR NKAQVPVRMV KNRLETGFFK KNSHNFVPME DYLIQDERID EVIKAVRDIL
     RKFMISAYDE KTHKGVVRHI IVRRGHYSHE VMVVLVTRAK KIPESDEVVG EILKACPDVR
     TVVQNINQEK TNVILGKTEK ILAGDGHITD SLNGINFEIS AHSFYQVNSV QTEKIYQKVV
     EAAELTGKET VIDAYCGIGT ISLNLAQKAA KVYGVEIVPE AIDDAKKNAT ANNIDNAIFE
     VGTASDWMAK WSEEGIKPDV VVFDPPRKGL ESEVINSTAK LAPAKIVYVS CNPATLVRDI
     QLFTEKGYQV AKPIQPVDQF PMTTHIESIT VLTRTENN
//
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