RLMI_VIBVY
ID RLMI_VIBVY Reviewed; 397 AA.
AC Q7ML80;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, 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}; OrderedLocusNames=VV1548;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC94311.1; -; Genomic_DNA.
DR RefSeq; WP_011150172.1; NC_005139.1.
DR AlphaFoldDB; Q7ML80; -.
DR SMR; Q7ML80; -.
DR STRING; 672.VV93_v1c14530; -.
DR EnsemblBacteria; BAC94311; BAC94311; BAC94311.
DR KEGG; vvy:VV1548; -.
DR PATRIC; fig|196600.6.peg.1530; -.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_0_0_6; -.
DR OMA; VMDVFDY; -.
DR OrthoDB; 468283at2; -.
DR Proteomes; UP000002675; Chromosome I.
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_0000366278"
FT DOMAIN 2..80
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01857"
SQ SEQUENCE 397 AA; 44470 MW; 4977C3D3F005D87E CRC64;
MSAAIYLVKG REKSVVRRHP WIFSRGIDRV EGNPQLGETV DVYGHDGKWL AKAAYSPESQ
IRARVWSFEK QDVNRAFFVK RIQDAQLLRE DVIERDGLTG YRLIAAESDG MPGVTIDRYQ
NFFVCQLLSA GAEHQKQNIV DALIEVFPDC NVYERSDVSV RKKEGLQETT GVLHGEMPPK
SVVIEENGVK ISVDIVGGHK TGFYLDQRDS RQQAMKYVKD KEVLNCFSYT GGFGLYALKG
GAKRVINADV SQPALDTAKF NAELNEFDIS KKRAVFLNAD VFKLLREYRD QGTKFDVVIM
DPPKFAESKA QLNGACRGYK DINMLAMQIL KPGGTLLTYS CSGLMDQVLF QKIIADAAVD
AGRSVKFVER FEQAADHPTD TAYPEGFYLK GFACKVL