RLMH_UREP2
ID RLMH_UREP2 Reviewed; 159 AA.
AC B1AIG8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=UPA3_0187;
OS Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=505682;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA Methe B.A., Glass J., Waites K., Shrivastava S.;
RT "Genome sequence of Ureaplasma parvum serovar 3.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000942; ACA32822.1; -; Genomic_DNA.
DR RefSeq; WP_006688906.1; NC_010503.1.
DR AlphaFoldDB; B1AIG8; -.
DR SMR; B1AIG8; -.
DR EnsemblBacteria; ACA32822; ACA32822; UPA3_0187.
DR GeneID; 29672634; -.
DR KEGG; upa:UPA3_0187; -.
DR HOGENOM; CLU_100552_0_0_14; -.
DR OMA; NEPYHHQ; -.
DR OrthoDB; 1783583at2; -.
DR Proteomes; UP000002162; 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.
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_1000082824"
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; 18245 MW; DF4B103A8A34D415 CRC64;
MMIKIISVGK LKQKAFVDLI NDYLKRINHY LKCQEIVVSD EPEPVQISNK SLEQIKSKEA
SKIFKNINQN DFVIALIIES NIISSETLAK KIQQWLNTFS HDICFIIGGS NGLHESIYER
ANYHLSMSKM TFAHGLAKVM LCEQIYRALS ILNNGKYHK
