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Database: UniProt
Entry: A0A0R1LX77_9LACO
LinkDB: A0A0R1LX77_9LACO
Original site: A0A0R1LX77_9LACO 
ID   A0A0R1LX77_9LACO        Unreviewed;       463 AA.
AC   A0A0R1LX77;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=tRNA (Uracil-5-)-methyltransferase {ECO:0000313|EMBL:KRL00263.1};
GN   ORFNames=FC81_GL000040 {ECO:0000313|EMBL:KRL00263.1};
OS   Liquorilactobacillus capillatus DSM 19910.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423731 {ECO:0000313|EMBL:KRL00263.1, ECO:0000313|Proteomes:UP000051621};
RN   [1] {ECO:0000313|EMBL:KRL00263.1, ECO:0000313|Proteomes:UP000051621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19910 {ECO:0000313|EMBL:KRL00263.1,
RC   ECO:0000313|Proteomes:UP000051621};
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:KRL00263.1}.
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DR   EMBL; AZEF01000053; KRL00263.1; -; Genomic_DNA.
DR   RefSeq; WP_057746278.1; NZ_AZEF01000053.1.
DR   AlphaFoldDB; A0A0R1LX77; -.
DR   STRING; 1423731.FC81_GL000040; -.
DR   PATRIC; fig|1423731.3.peg.43; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000051621; 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:0006396; P:RNA processing; IEA:InterPro.
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; 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:SF45; -; 1.
DR   PANTHER; PTHR11061; RNA M5U 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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000051621};
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          12..70
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        420
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        420
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         295
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         324
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         345
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         393
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   463 AA;  52894 MW;  1135C0ABD11C304A CRC64;
     MVADYRDKNK QLIKVGQCFP LTIKRLGING EGIGYYKHKV IFVAGALVQE VIVAEIISVR
     PNYATAKIHR IRKRSQDRIE KKDQYDVGGI ELEHLRYTQQ LEFKRDVIRQ SLEKFKPTGY
     KTYKLLPTIG MQTPFEYRNK AQFQVRKNQQ GQVIAGLYRR NSHDLVALPT FSTQRPLTMQ
     IMRTVCEILQ ELEIPIYDEK KNSGIIKTLV VRESWAEKNA QLTFITNSTK LPHKKQLLEK
     VASRLPMIVS VMQNINQGRA SLVWGDKTLC LAGKDYLLEK LGNIQFKLSA QAFFQLNPEQ
     TEKMYLEIKK ALALKKDELL IDAYCGAGTI GLFVAEQAKE VRGMDIVAAA IADARFNARL
     NGYTNTQYVT GKAEEVIPKW VEEGLVPHAL VVDPPRTGLD KRLIKTILEV KPTKFVYVSC
     NPSTLARDLV QLTRVYRVDY IQSIDMFPQT ARCEAVVKLI RKK
//
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