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Database: UniProt
Entry: A0A0R1VTK4_9LACO
LinkDB: A0A0R1VTK4_9LACO
Original site: A0A0R1VTK4_9LACO 
ID   A0A0R1VTK4_9LACO        Unreviewed;       460 AA.
AC   A0A0R1VTK4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KRM09096.1};
GN   ORFNames=FC15_GL001743 {ECO:0000313|EMBL:KRM09096.1};
OS   Lapidilactobacillus concavus DSM 17758.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lapidilactobacillus.
OX   NCBI_TaxID=1423735 {ECO:0000313|EMBL:KRM09096.1, ECO:0000313|Proteomes:UP000051315};
RN   [1] {ECO:0000313|EMBL:KRM09096.1, ECO:0000313|Proteomes:UP000051315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17758 {ECO:0000313|EMBL:KRM09096.1,
RC   ECO:0000313|Proteomes:UP000051315};
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:KRM09096.1}.
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DR   EMBL; AZFX01000059; KRM09096.1; -; Genomic_DNA.
DR   RefSeq; WP_057824792.1; NZ_AZFX01000059.1.
DR   AlphaFoldDB; A0A0R1VTK4; -.
DR   STRING; 1423735.FC15_GL001743; -.
DR   PATRIC; fig|1423735.3.peg.1811; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000051315; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0001510; P:RNA methylation; IEA:GOC.
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: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.
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:UP000051315};
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          8..66
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        418
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        418
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         293
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         322
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         343
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         391
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   460 AA;  51704 MW;  A190CF7BFD153515 CRC64;
     MKESNSVVVE VGQRFPLTIK KIGINGEGIG YFQHKVTFVP GLLPDEVAVV EATQVTDRYI
     RAKVHQLRHR STQRATTVPE IAEKVGGLEL AHLKYDQQVF YKNDLIKQAL EKYRPRGYQH
     YDFLPPIGAD NPWGYRNKAQ FPIKINDEGQ LISGLYQPNT QNLVDLPEMP TQSPLTLSIV
     RRLLPILTEL KMPIYDAKTN AGIIKAVAVR ESQLHHQVQL TFITNSKKMP HKQALLIAIA
     EQLPEVSGIF QNLNQTKQGL FWGDETWKLA GEDYLEEQVG ERRFLLSPRA FLQLNLPQTE
     KLYRVVTDFL EPQSTETLLD AYAGVGTIGL SLAKRVKSVV GIEQIPEAVA DAQRNAAHNH
     IQNATYHLGK VESELPKLQA AGENFSAMIV DPPRVGLAPQ LIETILNARP KKLIYISCNE
     STLAQNLVKL TQAYVVDKIQ MVDMFPQTAR VEAVVKLVLR
//
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