RLMC_SHEPA
ID RLMC_SHEPA Reviewed; 378 AA.
AC A8H8Q9;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, 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}; OrderedLocusNames=Spea_3635;
OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=398579;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700345 / ANG-SQ1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT "Complete sequence of Shewanella pealeana ATCC 700345.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABV88946.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000851; ABV88946.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041411099.1; NC_009901.1.
DR AlphaFoldDB; A8H8Q9; -.
DR SMR; A8H8Q9; -.
DR STRING; 398579.Spea_3635; -.
DR EnsemblBacteria; ABV88946; ABV88946; Spea_3635.
DR KEGG; spl:Spea_3635; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_0_0_6; -.
DR Proteomes; UP000002608; 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 Gene3D; 3.40.50.150; -; 1.
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_sf.
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;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW Reference proteome; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..378
FT /note="23S rRNA (uracil(747)-C(5))-methyltransferase RlmC"
FT /id="PRO_0000414824"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT BINDING 3
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT BINDING 241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT BINDING 309
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
SQ SEQUENCE 378 AA; 42277 MW; 74FD3A97629C517F CRC64;
MKCAHFDQQQ CLSCRHIKQS MSVQVAAKSQ VLSQLLSDFE VEQWHEPVFG PDSGFRNKAK
MVVLGAAHQP ILGIVTPTGE PVSLCDCNLY PEDMQLLLHR LEQFVRQAGI PPYNVDKAKG
ELKFILLTRS QIKGEYLLRF VLKSHKSIER IERELPKLLS EYPQIKVVSV NIQPVHMAIL
EGEEEIFLTE ETRLSEQFND VPLFIRPKSF FQTHPQIAAK LYQTAREWVA ELKPSSLWDL
FCGVGGFGLH CASKTIPLTG IEISSEAIAC AKISAETMGL TQVDFTALDS TGFAQGCDAT
DKPDVVIVNP PRRGIGESLC QSLSDFAPKA ILYSSCNPHT LAKDLANIQG YHIQKVQLFD
MFPHTDHFEV LVMLVKPS
