ID A0A1W1V0F3_PEPAS Unreviewed; 420 AA.
AC A0A1W1V0F3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=23S rRNA (Uracil1939-C5)-methyltransferase {ECO:0000313|EMBL:SMB86770.1};
GN ORFNames=SAMN00017477_0945 {ECO:0000313|EMBL:SMB86770.1};
OS Peptoniphilus asaccharolyticus DSM 20463.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=573058 {ECO:0000313|EMBL:SMB86770.1, ECO:0000313|Proteomes:UP000192368};
RN [1] {ECO:0000313|EMBL:SMB86770.1, ECO:0000313|Proteomes:UP000192368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20463 {ECO:0000313|EMBL:SMB86770.1,
RC ECO:0000313|Proteomes:UP000192368};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FWWR01000009; SMB86770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1V0F3; -.
DR STRING; 573058.SAMN00017477_0945; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000192368; 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; 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};
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..52
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 378
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 378
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 303
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 351
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 420 AA; 48080 MW; 61CC06A9EE8CF0FA CRC64;
MDVKIIDFDH KGRGFGRYEG KSLFLDGGVI GDTVSFEVTE SKKKFDIGRI TEIIEPSIDR
VESKCPYSKK CGGCDFLEYK YSMQKKWKRD NVSATMQKIG GVDTKVEPTI GMENPFYYRN
HIQLKVEDGK LGYYAKNSNT LVEVKRCLIA EKEMNKAIDV LRNWKDLKSV DEIVVRQNNV
SELMIVLITK TEVKKVNGLL SELLDLNLKS LFINYRKNSR FRFGREFKKV YGEDYIEDEL
CGFKFRLSAE SFFQVNRIQT EKLYKTAVNY MEIKPDDVVM DLYSGIGSIS LLMTGAKEVV
GVEVVGAAVE NARQNSELNG KYNTRFIAGK VEDVIDKLVE EGTRFNKIML DPPRAGVDES
VIEKINELQP ERIVYVSCNP STQAKDLKLF KDYKVEKIQP VDMFCNSVHC ECICQLSRVN
//