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Database: UniProt
Entry: A0A0L6TYC0_9FIRM
LinkDB: A0A0L6TYC0_9FIRM
Original site: A0A0L6TYC0_9FIRM 
ID   A0A0L6TYC0_9FIRM        Unreviewed;       454 AA.
AC   A0A0L6TYC0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KNZ41072.1};
GN   ORFNames=AKG39_14025 {ECO:0000313|EMBL:KNZ41072.1};
OS   Acetobacterium bakii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ41072.1, ECO:0000313|Proteomes:UP000036873};
RN   [1] {ECO:0000313|Proteomes:UP000036873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA   Song Y., Hwang S., Cho B.-K.;
RT   "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT   psychrophilic chemical producer through syngas fermentation.";
RL   Submitted (JUL-2015) 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:KNZ41072.1}.
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DR   EMBL; LGYO01000036; KNZ41072.1; -; Genomic_DNA.
DR   RefSeq; WP_050741034.1; NZ_UOGO01000001.1.
DR   AlphaFoldDB; A0A0L6TYC0; -.
DR   STRING; 52689.AKG39_14025; -.
DR   PATRIC; fig|52689.4.peg.2183; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000036873; 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   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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000036873};
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          7..65
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        410
FT                   /note="Nucleophile"
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         313
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         334
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         383
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   454 AA;  50165 MW;  AD68826F0A9A7FF6 CRC64;
     MNENNKIIAN GEKYTMKLID ITHSGEGLGR IENMIVFVEG GLPGDTVEVE IKNVKKTYAQ
     GRLLNIIENA PERVVPACKY FEQCGGCQLL HMSYEGQLRV KSKMVGDALE RIGGLKDIAV
     NPIIGMEDPT RYRNKAQFKV DKNGMGFYAK QSHNLVHIDD CLNQPESAAD VIRTMNAMIS
     DLNLSIYDER THKGYIRGIL HRTNLEGENM ITIIINGRDL SQRPAIVDAI LAGIPNVKSI
     FVNINREKGN VILGRKSLCI HGVPRIVEKI GDLMFSISPN SFFQVNSKQT VKLYDVIKKM
     AALKGTETVF DLYCGTGTIG LYIADKAKEV IGIESVGDAV LDARENAGLN QIDNAVFLHG
     KADEEMARIA KDENIKPDLI VLDPPRKGCE ETLLNAIGDL KTPRVIYVSC NPSTLARDLK
     IMITLGYGIL EVQPVDLFPG TGHVETVVLM SREK
//
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