(data stored in ACNUC10821 zone)

SWISSPROT: RLMH_LISMF

ID   RLMH_LISMF              Reviewed;         159 AA.
AC   Q724B0;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 85.
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};
GN   OrderedLocusNames=LMOf2365_0314;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Specifically methylates the pseudouridine at position
CC       1915 (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-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:42752, Rhea:RHEA-
CC         COMP:10221, Rhea:RHEA-COMP:10222, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65314,
CC         ChEBI:CHEBI:74486; EC=2.1.1.177; Evidence={ECO:0000255|HAMAP-
CC         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}.
DR   EMBL; AE017262; AAT03101.1; -; Genomic_DNA.
DR   RefSeq; WP_003722913.1; NC_002973.6.
DR   SMR; Q724B0; -.
DR   EnsemblBacteria; AAT03101; AAT03101; LMOf2365_0314.
DR   KEGG; lmf:LMOf2365_0314; -.
DR   HOGENOM; HOG000218433; -.
DR   KO; K00783; -.
DR   OMA; NGEPYHK; -.
DR   BioCyc; LMON265669:G1G0V-330-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070038; F:rRNA (pseudouridine-N3-)-methyltransferase activity; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; Q724B0.
DR   SWISS-2DPAGE; Q724B0.
KW   Cytoplasm; Methyltransferase; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    159       Ribosomal RNA large subunit
FT                                methyltransferase H.
FT                                /FTId=PRO_0000198139.
FT   REGION      127    132       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00658}.
FT   BINDING      76     76       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00658}.
FT   BINDING     108    108       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00658}.
SQ   SEQUENCE   159 AA;  17741 MW;  F70490E973C91B3A CRC64;
     MNIQIVTVGK LKEKYLVQGI AEYLKRLSAY AKVTIVEVPD EKAPEVLSDA EMKQVKDKEG
     ARILAKIPDD AHVIALAIDG KMKSSEEFAA DLDKLATYGK SKVTFVIGGS LGLSEAVLKR
     SNERISFGRL TLPHQLMRLV LVEQVYRAFR IVRGEPYHK
//

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