ID E0S1Q8_BUTPB Unreviewed; 470 AA.
AC E0S1Q8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=23S rRNA methyltransferase {ECO:0000313|EMBL:ADL33733.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:ADL33733.1};
GN OrderedLocusNames=bpr_I0991 {ECO:0000313|EMBL:ADL33733.1};
OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS (Clostridium proteoclasticum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL33733.1, ECO:0000313|Proteomes:UP000001299};
RN [1] {ECO:0000313|EMBL:ADL33733.1, ECO:0000313|Proteomes:UP000001299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51982 / DSM 14932 / B316
RC {ECO:0000313|Proteomes:UP000001299};
RX PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z.,
RA Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.;
RT "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T)
RT highlights adaptation to a polysaccharide-rich environment.";
RL PLoS ONE 5:E11942-E11942(2010).
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; CP001810; ADL33733.1; -; Genomic_DNA.
DR RefSeq; WP_013280389.1; NC_014387.1.
DR AlphaFoldDB; E0S1Q8; -.
DR STRING; 515622.bpr_I0991; -.
DR KEGG; bpb:bpr_I0991; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_7_2_9; -.
DR Proteomes; UP000001299; Chromosome 1.
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; 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; 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; 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:UP000001299};
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 ACT_SITE 422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 422
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 329
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 350
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 395
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 470 AA; 52761 MW; 5AC4992CE13DE38A CRC64;
MKKKDIIEGI VKRVEFPNKG IVETEEGKVI VKGVLPDQKV SVQIQKVRKD RAEGRLVEVL
EEPSDSIESP CIHFGKCGGC SYLTMPYVKE LGLKEQQVRA LLKPAMDRQT ERFTWEGIKT
SPVKFAYRNK MEFSFGDEVM GGPLCLGMHK KGSFYDIVTV SGCRIVDDDY RAILSATLDY
FSPMYASGEI SFYHRMKQTG YLRHLLVRKA VRTGDILVDI ITTTQEEHDL TGFKDALLGL
SLSGRITGIL HTKNDSLADA VIDEGTEILY GQDFFYEHLL GLKFRITPFS FFQTNSLSAE
VLYQTVRSYI KSLYDQKKIS KDGIIYDLYS GTGTIAQLLA PVANKVIGVE IVEEAVEAAK
ENAKLNNLDN CEFIAGDVLK VLDEIEDKPD MIILDPPRDG INPKALQKII GYGVKYMIYV
SCKPTSLARD LEVLQENGYV MTRAVAVDQF PWTSHVETVV LLTKTTDKEV
//
