ID RLMI_YERPE Reviewed; 396 AA.
AC Q7CHM1; Q74VH3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 105.
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=YPO1445, y2725, YP_1336;
OS Yersinia pestis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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; AL590842; CAL20096.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86277.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61579.1; -; Genomic_DNA.
DR PIR; AF0176; AF0176.
DR RefSeq; WP_002213052.1; NZ_WUCM01000066.1.
DR RefSeq; YP_002346466.1; NC_003143.1.
DR AlphaFoldDB; Q7CHM1; -.
DR SMR; Q7CHM1; -.
DR STRING; 214092.YPO1445; -.
DR PaxDb; 214092-YPO1445; -.
DR DNASU; 1147672; -.
DR EnsemblBacteria; AAS61579; AAS61579; YP_1336.
DR GeneID; 66842102; -.
DR KEGG; ype:YPO1445; -.
DR KEGG; ypk:y2725; -.
DR KEGG; ypm:YP_1336; -.
DR PATRIC; fig|214092.21.peg.1771; -.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_0_0_6; -.
DR OMA; VMDVFDY; -.
DR OrthoDB; 9805492at2; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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 CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd21153; PUA_RlmI; 1.
DR CDD; cd11572; RlmI_M_like; 1.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR Gene3D; 3.30.750.80; RNA methyltransferase domain (HRMD) like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR023542; RLMI.
DR InterPro; IPR041532; RlmI-like_PUA.
DR InterPro; IPR019614; SAM-dep_methyl-trfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42873:SF1; METHYLTRANS_SAM DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42873; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE; 1.
DR Pfam; PF10672; Methyltrans_SAM; 1.
DR Pfam; PF17785; PUA_3; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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..396
FT /note="Ribosomal RNA large subunit methyltransferase I"
FT /id="PRO_0000366280"
FT DOMAIN 2..81
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01857"
SQ SEQUENCE 396 AA; 44481 MW; 8688475852B9D3C8 CRC64;
MTVRLILAKG REKSLLRRHP WIFSGAVQRL EGDALSGETI DILDSQGKWL ARAAYSPESQ
ILARVWTFQQ DEVIDCAFFI RRLQQAQNWR DWLAQRDGLN GYRLIAGESD GLPGITIDRF
QNFLVLQLLS AGAEYQRETL VSALQHCYPE CSIYDRSDVS VRKKEGLPLT QGLICGEMPP
ALLPISENGM QLFVDIQQGH KTGFYLDQRD SRLAARNYAN GRRVLNCFSY TGAFAVAALM
GNCQQVISVD TSQSVLDIAK QNIELNQLDL SKTEFVRDDV FQLLRSYRAQ GEKFDLIIMD
PPKFVENKSQ LASACRGYKD INMLAIQLLR PGGILLSFSC SGLMPVDLFQ KILADAALDA
GHDIQFIEQF RQAADHPVIA AYPEGLYLKG FACRVM
//
