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Database: UniProt
Entry: A0A0R2MM63_9LACO
LinkDB: A0A0R2MM63_9LACO
Original site: A0A0R2MM63_9LACO 
ID   A0A0R2MM63_9LACO        Unreviewed;       456 AA.
AC   A0A0R2MM63;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Putative rna methyltransferase lp 1151 {ECO:0000313|EMBL:KRO14815.1};
GN   ORFNames=IV64_GL000387 {ECO:0000313|EMBL:KRO14815.1};
OS   Lactiplantibacillus xiangfangensis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=942150 {ECO:0000313|EMBL:KRO14815.1, ECO:0000313|Proteomes:UP000051783};
RN   [1] {ECO:0000313|EMBL:KRO14815.1, ECO:0000313|Proteomes:UP000051783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26013 {ECO:0000313|EMBL:KRO14815.1,
RC   ECO:0000313|Proteomes:UP000051783};
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:KRO14815.1}.
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DR   EMBL; JQCL01000006; KRO14815.1; -; Genomic_DNA.
DR   RefSeq; WP_057705193.1; NZ_JQCL01000006.1.
DR   AlphaFoldDB; A0A0R2MM63; -.
DR   STRING; 942150.IV64_GL000387; -.
DR   PATRIC; fig|942150.3.peg.394; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000051783; 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          6..64
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;  51084 MW;  BB581E840C2DE8AF CRC64;
     MKTNLPVHNG EELDVTIIDL TYQGMGVAKV DNYPIFIENA LPEEKITVKV TKTTKNFAFG
     DVVKINQVSP HRVNPKGRVY RQTGIAPLQH LEYSEQLKFK QHQVAELFAK VHMDDVEVLP
     TIGMENPTQY RNKAQVPVRQ VQGKLTTGFY KKNSHQLMPI EDYYIQDPEI DKAIVVIRDI
     LRKYHEAAYD EFHHSGTIRT IMVRRGYYSH EMMVVIVTRT KHLPMADVVV QEIQAALPEV
     VSVIQNINQK KTNVILGPDN NVLAGKSTID DQLLGLTFAI SAQSFYQVNP QQTEKLYQLA
     IDQAGLTGNE TVIDAYSGIG TISLTMAQHA KQVYGVEIVP AAIENAKQNA NKNGITNAKF
     VLGSAEDVMA KWEEEGIKPD VVVVDPPRKG LDAEFIKSTG EMAPKKVVYI SCNPSTLVRD
     VQRFGEYGYE ISAPVQPVDQ FPQTPHIECV TVLTRK
//
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