ID   RLMI_YERPG              Reviewed;         396 AA.
AC   A9R2N9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase I {ECO:0000255|HAMAP-Rule:MF_01857};
DE            EC=2.1.1.191 {ECO:0000255|HAMAP-Rule:MF_01857};
DE   AltName: Full=23S rRNA m5C1962 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01857};
DE   AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RlmI {ECO:0000255|HAMAP-Rule:MF_01857};
GN   Name=rlmI {ECO:0000255|HAMAP-Rule:MF_01857};
GN   OrderedLocusNames=YpAngola_A3209;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 1962
CC       (m5C1962) of 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01857}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(1962) in 23S rRNA + S-adenosyl-L-methionine = 5-
CC         methylcytidine(1962) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42912, Rhea:RHEA-COMP:10382, Rhea:RHEA-COMP:10386,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.191;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01857};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01857}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI family.
CC       {ECO:0000255|HAMAP-Rule:MF_01857}.
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DR   EMBL; CP000901; ABX88119.1; -; Genomic_DNA.
DR   RefSeq; WP_002213052.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R2N9; -.
DR   SMR; A9R2N9; -.
DR   GeneID; 66842102; -.
DR   KEGG; ypg:YpAngola_A3209; -.
DR   PATRIC; fig|349746.12.peg.4270; -.
DR   OMA; VMDVFDY; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.130.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01857; 23SrRNA_methyltr_I; 1.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR041532; RlmI_PUA-like.
DR   InterPro; IPR023542; rRNA_lsu_MeTfrase_I.
DR   InterPro; IPR019614; SAM-dep_methyl-trfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF10672; Methyltrans_SAM; 1.
DR   Pfam; PF17785; PUA_3; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; RNA-binding; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..396
FT                   /note="Ribosomal RNA large subunit methyltransferase I"
FT                   /id="PRO_0000366282"
FT   DOMAIN          2..81
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01857"
SQ   SEQUENCE   396 AA;  44481 MW;  8688475852B9D3C8 CRC64;
     MTVRLILAKG REKSLLRRHP WIFSGAVQRL EGDALSGETI DILDSQGKWL ARAAYSPESQ
     ILARVWTFQQ DEVIDCAFFI RRLQQAQNWR DWLAQRDGLN GYRLIAGESD GLPGITIDRF
     QNFLVLQLLS AGAEYQRETL VSALQHCYPE CSIYDRSDVS VRKKEGLPLT QGLICGEMPP
     ALLPISENGM QLFVDIQQGH KTGFYLDQRD SRLAARNYAN GRRVLNCFSY TGAFAVAALM
     GNCQQVISVD TSQSVLDIAK QNIELNQLDL SKTEFVRDDV FQLLRSYRAQ GEKFDLIIMD
     PPKFVENKSQ LASACRGYKD INMLAIQLLR PGGILLSFSC SGLMPVDLFQ KILADAALDA
     GHDIQFIEQF RQAADHPVIA AYPEGLYLKG FACRVM