ID   RLMI_SHEDO              Reviewed;         397 AA.
AC   Q12JE5;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 87.
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}; OrderedLocusNames=Sden_3155;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
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., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE56431.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000302; ABE56431.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041405863.1; NC_007954.1.
DR   AlphaFoldDB; Q12JE5; -.
DR   SMR; Q12JE5; -.
DR   STRING; 318161.Sden_3155; -.
DR   EnsemblBacteria; ABE56431; ABE56431; Sden_3155.
DR   KEGG; sdn:Sden_3155; -.
DR   eggNOG; COG1092; Bacteria.
DR   HOGENOM; CLU_014042_0_0_6; -.
DR   OrthoDB; 468283at2; -.
DR   Proteomes; UP000001982; 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; Reference proteome; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..397
FT                   /note="Ribosomal RNA large subunit methyltransferase I"
FT                   /id="PRO_0000366258"
FT   DOMAIN          2..80
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01857"
SQ   SEQUENCE   397 AA;  44105 MW;  D13248B8EB54E7EE CRC64;
     MAIRIKLKPG RERSLERRHP WVFSNGIHNV NGGKPQAGDT VDVVAHDGRW LGRGAWSPES
     QIQVRIWTFD KEEAIDADFF ARRIQRAQAG REDLIREQGL TGYRLIAAES DGLPGITIDR
     YADVLVCQLL NTGAEKWRDT LVEQLALQFP GCAIYERSDV DSRKKEGLAP VQGLLHGELP
     AMPIIIEENG IKIAVDVVKG HKTGFYLDQR DNRAIAARFV KGKSVLNCFC YTGTFGLYAA
     KAGAASIENV DVSALALQTA RDNMAINGLD DSHVNYHEAD VFKLLRQYRD EGKTFDVIVL
     DPPKFADNKS QLNGACRGYK DINMIAMQLL NPGGILLTFS CSGLMESDLF QKVVADAALD
     AKREVQFVER MHQASDHPIS SAFPEGYYLK GLVARVW