ID   RLMI_ECOSM              Reviewed;         396 AA.
AC   B1LJ30;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=EcSMS35_2151;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
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; CP000970; ACB16334.1; -; Genomic_DNA.
DR   RefSeq; WP_000116270.1; NC_010498.1.
DR   AlphaFoldDB; B1LJ30; -.
DR   SMR; B1LJ30; -.
DR   EnsemblBacteria; ACB16334; ACB16334; EcSMS35_2151.
DR   KEGG; ecm:EcSMS35_2151; -.
DR   HOGENOM; CLU_014042_0_0_6; -.
DR   OMA; VMDVFDY; -.
DR   Proteomes; UP000007011; Chromosome.
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_0000366225"
FT   DOMAIN          2..81
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01857"
SQ   SEQUENCE   396 AA;  44354 MW;  258C5052A85DCB7C CRC64;
     MSVRLVLAKG REKSLLRRHP WIFSGAVARM EGKASLGETI DIVDHQGKWL ARGAYSPASQ
     IRARVWTFDP SESIDIAFFT RRLQQAQKWR DWLAQKDGLN SYRLIAGESD GLPGITIDRF
     GNFLVLQLLS AGAEYQRAAL ISALQTLYPE CAIYDRSDVA VRKKEGMELT QGPVTGELPP
     ALLPIEEHGM KLLVDIQHGH KTGYYLDQRD SRLATRRYVE NKRVLNCFSY TGGFAVSALM
     GGCSQVVSVD TSQEALDIAR QNVELNKLDL SKAEFVRDDV FKLLRTYRDR GEKFDVIVMD
     PPKFVENKSQ LMGACRGYKD INMLAIQLLN EGGVLLTFSC SGLMTSDLFQ KIIADAAIDA
     GRDVQFIEQF RQAADHPVIA TYPEGLYLKG FACRVM