RLMH_BACSU
ID RLMH_BACSU Reviewed; 159 AA.
AC Q45601;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
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}; Synonyms=yydA;
GN OrderedLocusNames=BSU40230;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA Kasahara Y., Nakai S., Ogasawara N.;
RT "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT Bacillus subtilis genome.";
RL DNA Res. 4:155-159(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=16460560; DOI=10.1186/1471-2105-7-53;
RA von Grotthuss M., Plewczynski D., Ginalski K., Rychlewski L.,
RA Shakhnovich E.I.;
RT "PDB-UF: database of predicted enzymatic functions for unannotated protein
RT structures from structural genomics.";
RL BMC Bioinformatics 7:53-53(2006).
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; D78193; BAA11281.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16060.1; -; Genomic_DNA.
DR PIR; H70090; H70090.
DR RefSeq; NP_391903.1; NC_000964.3.
DR RefSeq; WP_003243164.1; NZ_JNCM01000034.1.
DR PDB; 1TO0; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-159.
DR PDBsum; 1TO0; -.
DR AlphaFoldDB; Q45601; -.
DR SMR; Q45601; -.
DR STRING; 224308.BSU40230; -.
DR PaxDb; Q45601; -.
DR PRIDE; Q45601; -.
DR EnsemblBacteria; CAB16060; CAB16060; BSU_40230.
DR GeneID; 937752; -.
DR KEGG; bsu:BSU40230; -.
DR PATRIC; fig|224308.179.peg.4351; -.
DR eggNOG; COG1576; Bacteria.
DR InParanoid; Q45601; -.
DR OMA; NEPYHHQ; -.
DR PhylomeDB; Q45601; -.
DR BioCyc; BSUB:BSU40230-MON; -.
DR EvolutionaryTrace; Q45601; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..159
FT /note="Ribosomal RNA large subunit methyltransferase H"
FT /id="PRO_0000198090"
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"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1TO0"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:1TO0"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1TO0"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:1TO0"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:1TO0"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1TO0"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1TO0"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1TO0"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1TO0"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1TO0"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:1TO0"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1TO0"
FT HELIX 134..152
FT /evidence="ECO:0007829|PDB:1TO0"
SQ SEQUENCE 159 AA; 18073 MW; 7438A57C259BD602 CRC64;
MNINIVTIGK LKEKYLKQGI EEYTKRLSAY AKIDIIELPD EKAPENLSDQ DMKIIKDKEG
DRILSKISPD AHVIALAIEG KMKTSEELAD TIDKLATYGK SKVTFVIGGS LGLSDTVMKR
ADEKLSFSKM TFPHQLMRLI LVEQIYRAFR INRGEPYHK
