RLMI_AERS4
ID RLMI_AERS4 Reviewed; 396 AA.
AC A4SML8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=ASA_2074;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(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; CP000644; ABO90140.1; -; Genomic_DNA.
DR RefSeq; WP_005311453.1; NC_009348.1.
DR AlphaFoldDB; A4SML8; -.
DR SMR; A4SML8; -.
DR STRING; 382245.ASA_2074; -.
DR EnsemblBacteria; ABO90140; ABO90140; ASA_2074.
DR KEGG; asa:ASA_2074; -.
DR PATRIC; fig|382245.13.peg.2039; -.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_0_0_6; -.
DR OMA; VMDVFDY; -.
DR OrthoDB; 468283at2; -.
DR Proteomes; UP000000225; 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_0000366215"
FT DOMAIN 2..79
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01857"
SQ SEQUENCE 396 AA; 44382 MW; 6234AD2CEB55AF22 CRC64;
MSVFIYLVKG REKSLLRRHP WIFSKGIERV EGNPVDGDTV EIYANDGRWL ARGAWSGSSQ
IRARVWTFDK EETVDLDFFL RRLKYAQESR DPLIKRQGLT GYRLCAAESD GLPGLTIDSY
ADFLVCQILS AGAEFQRELI TQALRTLYPE CSIYERSDVA VRKKEGLKER TGVIHGETPT
EPVVIEENGV KILVDIRNGH KTGFYLDQRD NRQAVSKYTS AKRVLNCFSY TGGFGIYALK
GGAKEVVNVD LSQTALDMAR QNAELNGLDI SNTQFIRHDV FKLLREYREK GEKFDVIVLD
PPKFAESKAQ LLGACRGYKD INMLAFQLLA PGGVLLTYSC SGLMEQSLFQ KIVADAALDA
GRDAQILELL SQASDHPIGT AYPEGFYLKG LVVRAR