(data stored in ACNUC9543 zone)

SWISSPROT: RLMC_YERPA

ID   RLMC_YERPA              Reviewed;         376 AA.
AC   Q1CAC8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 77.
DE   RecName: Full=23S rRNA (uracil(747)-C(5))-methyltransferase RlmC {ECO:0000255|HAMAP-Rule:MF_01012};
DE            EC=2.1.1.189 {ECO:0000255|HAMAP-Rule:MF_01012};
DE   AltName: Full=23S rRNA(m5U747)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01012};
GN   Name=rlmC {ECO:0000255|HAMAP-Rule:MF_01012}; Synonyms=rumB;
GN   OrderedLocusNames=YPA_0626;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 747
CC       (m5U747) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-
CC         methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42628, Rhea:RHEA-COMP:10154, Rhea:RHEA-COMP:10155,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.189;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01012};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. RlmC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01012}.
DR   EMBL; CP000308; ABG12594.1; -; Genomic_DNA.
DR   RefSeq; WP_002208756.1; NZ_CP009906.1.
DR   SMR; Q1CAC8; -.
DR   EnsemblBacteria; ABG12594; ABG12594; YPA_0626.
DR   KEGG; ypa:YPA_0626; -.
DR   HOGENOM; HOG000218547; -.
DR   KO; K03212; -.
DR   OMA; SCQWLEK; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01012; 23SrRNA_methyltr_RlmC; 1.
DR   InterPro; IPR011825; 23SrRNA_MeTrfase_RlmC.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02085; meth_trns_rumB; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q1CAC8.
DR   SWISS-2DPAGE; Q1CAC8.
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..376
FT                   /note="23S rRNA (uracil(747)-C(5))-methyltransferase RlmC"
FT                   /id="PRO_0000282022"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   METAL           3
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   METAL           11
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   METAL           14
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   METAL           87
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         212
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         241
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         262
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         307
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
SQ   SEQUENCE   376 AA;  42202 MW;  EE0FB4775CE9BB44 CRC64;
     MHCAQYTAGR CRSCQWLDKP YPQQLADKQH HLESLLAGHA VTQWLAPVFG RESAFRNKAK
     MVVSGSVERP LLGMLHRDGT PVDLCACPLY PPSFEPVFTV LKTFIARAGL TPYNVARKRG
     ELKFLLLTES TYNGELMLRF VLRSETKLAQ LIAALPWLQQ QLPQLAVISA NIQPVHMAIL
     EGEREIPLTE QQALPERFNQ VPLYIRPQSF FQTNPQVAAS LYATARQWVQ EHEVHSMWDL
     FCGVGGFGLH CAGPETQLTG IEINAEAIAC ARQSAEQLGL KNVSFAALDS TRFATAEAQI
     PELVLVNPPR RGIGRELCDY LSQMAPKFIL YSSCNAETMA KDISLLAGYH IERVQLFDMF
     PHTSHYEVLT LLTLRR
//

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