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Database: UniProt
Entry: A0A087C184_9BIFI
LinkDB: A0A087C184_9BIFI
Original site: A0A087C184_9BIFI 
ID   A0A087C184_9BIFI        Unreviewed;       429 AA.
AC   A0A087C184;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=SAM-dependent methyl transferase {ECO:0000313|EMBL:KFI77034.1};
DE            EC=2.1.1.190 {ECO:0000313|EMBL:KFI77034.1};
GN   ORFNames=BMON_0590 {ECO:0000313|EMBL:KFI77034.1};
OS   Bifidobacterium mongoliense DSM 21395.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437603 {ECO:0000313|EMBL:KFI77034.1, ECO:0000313|Proteomes:UP000029082};
RN   [1] {ECO:0000313|EMBL:KFI77034.1, ECO:0000313|Proteomes:UP000029082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21395 {ECO:0000313|EMBL:KFI77034.1,
RC   ECO:0000313|Proteomes:UP000029082};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KFI77034.1}.
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DR   EMBL; JGZE01000010; KFI77034.1; -; Genomic_DNA.
DR   RefSeq; WP_033511172.1; NZ_JGZE01000010.1.
DR   AlphaFoldDB; A0A087C184; -.
DR   STRING; 1437603.GCA_000771525_00199; -.
DR   eggNOG; COG2265; Bacteria.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000029082; 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   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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000029082};
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          1..57
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        383
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        383
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         251
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         284
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         308
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         356
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   429 AA;  46940 MW;  59BE87CD84BC2B2E CRC64;
     MQTTVRIERY ADQGRCVGHV DGRVVFVRFA LPGELVNVAL DEPHERKDRF WTGEVVEVLE
     ASDRRVAPVW PLAGPLADGG GVGGADLIHV SLPGQLDWKS TVITEQMHRL GHVDLPKVGV
     ESMAGDEALS GLHWRTRIEM IADDEGRPSM RRRESHQRVP IDTMPLASQA LLAVADHCGV
     WRGGFDPGAS IRLAVPEPRD QGDGDLLTDI GENYALMVGD EVKAGSAKLH ESADIDGTRF
     AYDVHADGFW QVHRRAPMVL PDHVLRCVRA LLDGRPHATV WDLYSGAGLF TLPLAKKAAD
     TVHMLSVEGS KPAVRQAREN LTRAGIDTVE AHSGDVARAL RFVPRHLAHP DVVVLDPPRA
     GARAAVCRRI AESGAHGVVY VACDPTSLAR DTATFADEGY RLTDIHAFDI YPMTHHVETV
     AVFERAQHR
//
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