RLMI_PHOPR
ID RLMI_PHOPR Reviewed; 397 AA.
AC Q6LQ36;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 97.
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=PBPRA2194;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(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=CAG20590.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR378670; CAG20590.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041394360.1; NC_006370.1.
DR AlphaFoldDB; Q6LQ36; -.
DR SMR; Q6LQ36; -.
DR STRING; 298386.PBPRA2194; -.
DR EnsemblBacteria; CAG20590; CAG20590; PBPRA2194.
DR KEGG; ppr:PBPRA2194; -.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_0_0_6; -.
DR OrthoDB; 468283at2; -.
DR Proteomes; UP000000593; Chromosome 1.
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_0000366236"
FT DOMAIN 2..82
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01857"
SQ SEQUENCE 397 AA; 44304 MW; 376907D2E22E8ADF CRC64;
MTTSIYLVKG REKSLRRRHP WVFSRGIDRI EGNKPSMGET VEVYDNKGEW LARGAYSPQS
QIRIRVWTFD KKEVINVDFF VKRLKAAQAL RDVLAARDGL TGYRLIAAES DGLPGITIDR
YQNFLVCQLL SAGAEEQKDA LVEALNICYP ECSVYERSDV AVRKKEGLKQ RTGVLSGEEP
PKFVTIEENG IKINVDIVGG HKTGFYLDQR DSRQAAVKYV NGKRVLNCFC YTGGFGLYAL
KGGASQVVNV DVSQPALDTA RLNTEANGLP VENAEFVNAD VFKLLREYRE RGEFFDVVIM
DPPKFAESKS QLVGACRGYK DINMLAMQIL NPGGILLTYS CSGLMDNGLF QKIVADAALD
AHREVQFIER FGQAADHPLD SAYPEGFYLK GFACYVK