RLMH_CLOBK
ID RLMH_CLOBK Reviewed; 159 AA.
AC B1IH25;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase H {ECO:0000255|HAMAP-Rule:MF_00658};
DE EC=2.1.1.177 {ECO:0000255|HAMAP-Rule:MF_00658};
DE AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00658};
DE AltName: Full=23S rRNA m3Psi1915 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00658};
DE AltName: Full=rRNA (pseudouridine-N3-)-methyltransferase RlmH {ECO:0000255|HAMAP-Rule:MF_00658};
GN Name=rlmH {ECO:0000255|HAMAP-Rule:MF_00658}; OrderedLocusNames=CLD_0914;
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- FUNCTION: Specifically methylates the pseudouridine at position 1915
CC (m3Psi1915) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00658}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine =
CC H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:42752, Rhea:RHEA-COMP:10221, Rhea:RHEA-
CC COMP:10222, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:74486; EC=2.1.1.177;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00658};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00658}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00658}.
CC -!- SIMILARITY: Belongs to the RNA methyltransferase RlmH family.
CC {ECO:0000255|HAMAP-Rule:MF_00658}.
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DR EMBL; CP000939; ACA44922.1; -; Genomic_DNA.
DR RefSeq; WP_003400968.1; NC_010516.1.
DR AlphaFoldDB; B1IH25; -.
DR SMR; B1IH25; -.
DR EnsemblBacteria; ACA44922; ACA44922; CLD_0914.
DR KEGG; cbb:CLD_0914; -.
DR HOGENOM; CLU_100552_0_0_9; -.
DR OMA; NEPYHHQ; -.
DR Proteomes; UP000008541; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070038; F:rRNA (pseudouridine-N3-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd18081; RlmH-like; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_00658; 23SrRNA_methyltr_H; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR003742; RlmH-like.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR33603; PTHR33603; 1.
DR Pfam; PF02590; SPOUT_MTase; 1.
DR PIRSF; PIRSF004505; MT_bac; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00246; tRNA_RlmH_YbeA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..159
FT /note="Ribosomal RNA large subunit methyltransferase H"
FT /id="PRO_0000366582"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00658"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00658"
FT BINDING 127..132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00658"
SQ SEQUENCE 159 AA; 18076 MW; E83FEE8310BE5428 CRC64;
MNISIISVGK IKEKFLKAAI DEYSKRLSKY CKLNIIEVTD EKTPDNASLK EENIIKEKEG
NLILKHIKDN SFVIALDLKG KAITSEEFSD LIENCRLTGN STIAFVIGGS LGLSEQVLSR
ANYKLSFSKM TFPHQLFRVM LLEQVYRAFR ILCGEPYHK
