ID F7RJE9_9GAMM Unreviewed; 389 AA.
AC F7RJE9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=23S rRNA (uracil(747)-C(5))-methyltransferase RlmC {ECO:0000256|HAMAP-Rule:MF_01012};
DE EC=2.1.1.189 {ECO:0000256|HAMAP-Rule:MF_01012};
DE AltName: Full=23S rRNA(m5U747)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01012};
GN Name=rlmC {ECO:0000256|HAMAP-Rule:MF_01012};
GN ORFNames=SOHN41_00486 {ECO:0000313|EMBL:EGM71572.1};
OS Shewanella sp. HN-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM71572.1, ECO:0000313|Proteomes:UP000002956};
RN [1] {ECO:0000313|EMBL:EGM71572.1, ECO:0000313|Proteomes:UP000002956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM71572.1,
RC ECO:0000313|Proteomes:UP000002956};
RX PubMed=21868804; DOI=10.1128/JB.05578-11;
RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA Hur H.G.;
RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT Arsenic-Sulfide Nanotubes.";
RL J. Bacteriol. 193:5039-5040(2011).
CC -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 747
CC (m5U747) in 23S rRNA. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01012}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGM71572.1}.
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DR EMBL; AFOZ01000013; EGM71572.1; -; Genomic_DNA.
DR RefSeq; WP_007645143.1; NZ_AFOZ01000013.1.
DR AlphaFoldDB; F7RJE9; -.
DR STRING; 327275.SOHN41_00486; -.
DR Proteomes; UP000002956; Unassembled WGS sequence.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR02085; meth_trns_rumB; 1.
DR NCBIfam; TIGR00479; rumA; 1.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 {ECO:0000256|HAMAP-Rule:MF_01012};
KW Iron {ECO:0000256|HAMAP-Rule:MF_01012};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01012};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01012};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01012}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_01012};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01012};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01012}.
FT ACT_SITE 348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 348
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 274
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 321
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 389 AA; 43211 MW; 115A708AE9797F22 CRC64;
MSAAIVSAKS QCGYFNLGQC QSCRHIQVPM AQQVAAKTQE LQQLLAPFVS NPLDIFQAPI
FGDASGFRNK AKMVALGAAH APVLGIVSPS GEAVSLCDCL LYPTDMQALL HRLERFVQQA
GIPPYRVDKA KGELKFILLT RSQVRGEYLL RFVLRSQDAI PRIERELPAL LLEFPQIKVV
SVNIQPIHMA ILEGDEEIFL TENTRLEERF NDVPLFIRPK SFFQTNPLVA AKLYQTAREW
VAQFEPKSLW DLFCGVGGFG LHCASKDIPL TGIEIEAEAI VCAKMSAQIM GLDKVQFMAL
DSTDFAKGEA AETKPDLIIV NPPRRGIGEA LCQSLSEFAP KAILYSSCNP KTLAKDLTHI
HGYRLTKVQL FDLFPHTDHF EVLAMLVKE
//
