RLMI_SHIBS
ID RLMI_SHIBS Reviewed; 396 AA.
AC Q31YN0;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 91.
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=SBO_2264;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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=ABB66828.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000036; ABB66828.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000116300.1; NC_007613.1.
DR AlphaFoldDB; Q31YN0; -.
DR SMR; Q31YN0; -.
DR EnsemblBacteria; ABB66828; ABB66828; SBO_2264.
DR KEGG; sbo:SBO_2264; -.
DR HOGENOM; CLU_014042_0_0_6; -.
DR Proteomes; UP000007067; 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_0000366267"
FT DOMAIN 2..81
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01857"
SQ SEQUENCE 396 AA; 44328 MW; DEE6CC72602B3E0B CRC64;
MSVRLVLAKG REKSLLRRHP WVFSGAVARM EGKASLGETI DIVDHQGKWL ARGAYSPASQ
IRARVWTFDP SESIDIAFFS RRLQQAQKWR DWLAQKDGLD SYRLIAGESD GLPGITIDRF
GNFLVLQLLS AGAEYQRAAL VSALQTLYPE CAIYDRSDVA VRKKEGMELT LGLVTGELPP
ALLPIEEHGM KLLVDIQHGH KTGYYLDQRD SRLATRRYVE NKRVLNCFSY TGGFAVSALM
GGCSQVVSVD TSQEALDIAR QNVELNKLDL SKAEFVRDDV FKLLRTYRDR GEKFDVIVMD
PPKFVENKSQ LMGACRGYKD INMLAIQLLN EGGILLTFSC SGLMTSDLFQ KIIADAAIDA
GRDVQFIEQF RQAADHPVIA TYPEGLYLKG FACRVM