RLMH_THEMA
ID RLMH_THEMA Reviewed; 151 AA.
AC Q9WZU8;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=TM_0844;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 2-151.
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; AE000512; AAD35926.1; -; Genomic_DNA.
DR PIR; E72326; E72326.
DR RefSeq; NP_228653.1; NC_000853.1.
DR RefSeq; WP_004080783.1; NZ_CP011107.1.
DR PDB; 1O6D; X-ray; 1.66 A; A=2-151.
DR PDBsum; 1O6D; -.
DR AlphaFoldDB; Q9WZU8; -.
DR SMR; Q9WZU8; -.
DR STRING; 243274.THEMA_00420; -.
DR EnsemblBacteria; AAD35926; AAD35926; TM_0844.
DR KEGG; tma:TM0844; -.
DR eggNOG; COG1576; Bacteria.
DR InParanoid; Q9WZU8; -.
DR OMA; NEPYHHQ; -.
DR OrthoDB; 1783583at2; -.
DR EvolutionaryTrace; Q9WZU8; -.
DR Proteomes; UP000008183; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..151
FT /note="Ribosomal RNA large subunit methyltransferase H"
FT /id="PRO_0000198200"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00658"
FT BINDING 119..124
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:1O6D"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:1O6D"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1O6D"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:1O6D"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:1O6D"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1O6D"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1O6D"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:1O6D"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1O6D"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:1O6D"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1O6D"
FT HELIX 126..144
FT /evidence="ECO:0007829|PDB:1O6D"
SQ SEQUENCE 151 AA; 17591 MW; 1A08C07987AC5DE4 CRC64;
MRVRIAVIGK LDGFIKEGIK HYEKFLRRFC KPEVLEIKRV HRGSIEEIVR KETEDLTNRI
LPGSFVMVMD KRGEEVSSEE FADFLKDLEM KGKDITILIG GPYGLNEEIF AKAHRVFSLS
KMTFTHGMTV LIVLEQIFRA FKIIHGENYH Y
