RLMC_HAEDU
ID RLMC_HAEDU Reviewed; 213 AA.
AC Q7VNM5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Putative 23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
DE EC=2.1.1.189;
DE AltName: Full=23S rRNA(m5U747)-methyltransferase;
GN Name=rlmC; Synonyms=rumB; OrderedLocusNames=HD_0478;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 747
CC (m5U747) in 23S rRNA. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-
CC methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42628, Rhea:RHEA-COMP:10154, Rhea:RHEA-COMP:10155,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.189;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. RlmC subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01024}.
CC -!- CAUTION: Could be the product of a pseudogene. The N-terminus is much
CC shorter than in related proteins. {ECO:0000305}.
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DR EMBL; AE017143; AAP95434.1; -; Genomic_DNA.
DR RefSeq; WP_010944487.1; NC_002940.2.
DR AlphaFoldDB; Q7VNM5; -.
DR SMR; Q7VNM5; -.
DR STRING; 233412.HD_0478; -.
DR PRIDE; Q7VNM5; -.
DR EnsemblBacteria; AAP95434; AAP95434; HD_0478.
DR KEGG; hdu:HD_0478; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_099436_0_0_6; -.
DR OMA; HTTHYET; -.
DR Proteomes; UP000001022; Chromosome.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; PTHR11061; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 5: Uncertain;
KW Methyltransferase; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..213
FT /note="Putative 23S rRNA (uracil(747)-C(5))-
FT methyltransferase RlmC"
FT /id="PRO_0000161929"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 43
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 213 AA; 24113 MW; EA5A57982794B1EE CRC64;
MRRALIFLAS PHFFAPNFFI FIYAKRISTP QIPLFIRPQG FFQTNPKVAS QLYATVQQWV
KILPINHLWD LFCGVGGFGL HCAKALQDQG KPVTLTGIEI SAAAIESATQ SAQKLALNNV
TFASLDAAQF ALKDRQQTPE LVIVNPPRRG IGKDLAEFLN QLNIPYLIYS SCNAESMVKD
FAYLTHYQLH RVQLFDMFPH TTHYETVTLL IRK
