(data stored in ACNUC7421 zone)

SWISSPROT: RLMH_RHOPS

ID   RLMH_RHOPS              Reviewed;         160 AA.
AC   Q13DN3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAY-2019, entry version 64.
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=RPD_0568;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE37806.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000283; ABE37806.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041805603.1; NC_007958.1.
DR   SMR; Q13DN3; -.
DR   STRING; 316057.RPD_0568; -.
DR   PRIDE; Q13DN3; -.
DR   EnsemblBacteria; ABE37806; ABE37806; RPD_0568.
DR   KEGG; rpd:RPD_0568; -.
DR   eggNOG; ENOG4108UXA; Bacteria.
DR   eggNOG; COG1576; LUCA.
DR   HOGENOM; HOG000218433; -.
DR   KO; K00783; -.
DR   OrthoDB; 1783583at2; -.
DR   BioCyc; RPAL316057:RPD_RS02915-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
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.
PE   3: Inferred from homology;
DR   PRODOM; Q13DN3.
DR   SWISS-2DPAGE; Q13DN3.
KW   Complete proteome; Cytoplasm; Methyltransferase; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    160       Ribosomal RNA large subunit
FT                                methyltransferase H.
FT                                /FTId=PRO_0000260598.
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   160 AA;  17508 MW;  8AA6A9C5D68896F2 CRC64;
     MRLTVIAIGK LKQGPERELA ERYRGRFDDL GRKLGFRGLD IHEIAESRAR DAAGRMAEEA
     AAIAALIAEG SSLVTLDERG KSVDSAAFAA QLGRWRDESV PGTIFVIGGA DGLLPELRRK
     AKLCLSFGAA TWPHQMVRVM LLEQIYRAAT ILAGHPYHRA
//

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