ID   RLMI_VIBVU              Reviewed;         397 AA.
AC   Q8D992;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=VV1_2713;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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; AE016795; AAO11058.1; -; Genomic_DNA.
DR   RefSeq; WP_011080553.1; NC_004459.3.
DR   AlphaFoldDB; Q8D992; -.
DR   SMR; Q8D992; -.
DR   EnsemblBacteria; AAO11058; AAO11058; VV1_2713.
DR   KEGG; vvu:VV1_2713; -.
DR   HOGENOM; CLU_014042_0_0_6; -.
DR   OMA; VMDVFDY; -.
DR   Proteomes; UP000002275; 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; RNA-binding; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..397
FT                   /note="Ribosomal RNA large subunit methyltransferase I"
FT                   /id="PRO_0000366277"
FT   DOMAIN          2..80
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01857"
SQ   SEQUENCE   397 AA;  44460 MW;  B23830F9DE041635 CRC64;
     MSAAIYLVKG REKSVVRRHP WIFSRGIDRV EGNPQLGETV DVYGHDGKWL AKAAYSPESQ
     IRARVWSFEK QDINRAFFVK RIQDAQLLRE DVIERDGLTG YRLIAAESDG MPGVTIDRYQ
     NFFVCQLLSA GAEHQKQNIV DALIEVFPDC NVYERSDVSV RKKEGLQETT GVLHGEMPPK
     SVVIEENGVK ISVDIVGGHK TGFYLDQRDS RQQAMKYVKD KEVLNCFSYT GGFGLYALKG
     GAKRVINADV SQPALDTAKF NAELNEFDIS KKRAVFLNAD VFKLLREYRD QGTKFDVVIM
     DPPKFAESKA QLNGACRGYK DINMLAFEIL KSGGTLLTYS CSGLMDLALF QKIIADAAVD
     AGRTVKFVER FEQAADHPVD TAYPEGFYLK GFACKVI