RLMI_SALCH
ID RLMI_SALCH Reviewed; 403 AA.
AC Q57QS3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 83.
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=SCH_1032;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(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=AAX64938.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017220; AAX64938.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_023234842.1; NC_006905.1.
DR AlphaFoldDB; Q57QS3; -.
DR SMR; Q57QS3; -.
DR EnsemblBacteria; AAX64938; AAX64938; SCH_1032.
DR KEGG; sec:SCH_1032; -.
DR HOGENOM; CLU_014042_0_0_6; -.
DR Proteomes; UP000000538; 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..403
FT /note="Ribosomal RNA large subunit methyltransferase I"
FT /id="PRO_0000366241"
FT DOMAIN 9..88
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01857"
SQ SEQUENCE 403 AA; 45202 MW; 1F70D7BADB4712A2 CRC64;
MTESTFPQYP RLVLSKGREK SLLRRHPWVF SGAVSRLEGK ANLGETIDIV DHQGKWLARG
AWSPASQIRA RVWTFDKAES IDIAFFTRRL RQAQQWRDWL AKKDGLDSYR LIAGESDGLP
GVTIDRFGHF LVLQLLSAGA EYQRAALISA LQTCYPDCAI YDRSDVAVRK KEGMALTQGP
VTGELPPALL PIEEYGMKLL VDIQGGHKTG YYLDQRDSRL ATRRYVENQR VLNCFSYTGG
FAVSALMGGC RQVVSVDTSQ DALDIARQNV ELNQLDLSKA EFVRDDVFKL LRAYREHGEK
FDVIIMDPPK FVENKSQLMG ACRGYKDINM LAIQLLNPGG ILLTFSCSGL MTSDLFQKII
ADAAIDAGRD VQFIEQFRQA ADHPVIATYP EGLYLKGFAC RVM