ID Y1703_LISMO Reviewed; 459 AA. AC Q8Y6I1; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=Uncharacterized RNA methyltransferase lmo1703; DE EC=2.1.1.-; GN OrderedLocusNames=lmo1703; OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e). OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=169963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-679 / EGD-e; RX PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D., RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE- CC ProRule:PRU01024}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL591981; CAC99781.1; -; Genomic_DNA. DR PIR; AG1287; AG1287. DR RefSeq; NP_465228.1; NC_003210.1. DR RefSeq; WP_003733116.1; NZ_CP023861.1. DR AlphaFoldDB; Q8Y6I1; -. DR SMR; Q8Y6I1; -. DR STRING; 169963.gene:17594384; -. DR PaxDb; 169963-lmo1703; -. DR DNASU; 985603; -. DR EnsemblBacteria; CAC99781; CAC99781; CAC99781. DR GeneID; 985603; -. DR KEGG; lmo:lmo1703; -. DR PATRIC; fig|169963.11.peg.1746; -. DR eggNOG; COG2265; Bacteria. DR HOGENOM; CLU_014689_7_1_9; -. DR OrthoDB; 9804590at2; -. DR PhylomeDB; Q8Y6I1; -. DR BioCyc; LMON169963:LMO1703-MONOMER; -. DR Proteomes; UP000000817; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 2.40.50.1070; -; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR030390; MeTrfase_TrmA_AS. DR InterPro; IPR030391; MeTrfase_TrmA_CS. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR002792; TRAM_dom. DR InterPro; IPR010280; U5_MeTrfase_fam. DR NCBIfam; TIGR00479; rumA; 1. DR PANTHER; PTHR11061:SF45; -; 1. DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1. DR Pfam; PF01938; TRAM; 1. DR Pfam; PF05958; tRNA_U5-meth_tr; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1. DR PROSITE; PS50926; TRAM; 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; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..459 FT /note="Uncharacterized RNA methyltransferase lmo1703" FT /id="PRO_0000162001" FT DOMAIN 5..63 FT /note="TRAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00208" FT ACT_SITE 415 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024" FT BINDING 76 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 82 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 85 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 166 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 290 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024" FT BINDING 319 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024" FT BINDING 340 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024" FT BINDING 388 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024" SQ SEQUENCE 459 AA; 51325 MW; A582F57A42595F06 CRC64; MNQNPVEEGQ KFPLTIRRMG INGEGIGYFK KAVVFVPGAI TGEEVVVEAV KVRDRFTEAK LNKIRKKSPN RVTAPCPVYE ACGGCQLQHV AYSAQLELKR DIVIQSIEKH TKIDPTKLKI RPTIGMEDPW RYRNKSQFQT RMVGSGQVET GLFGANSHQL VPIEDCIVQQ PVTIKVTNFV RDLLEKYGVP IYDEKAGSGI VRTIVVRTGV KTGETQLVFI TNSKKLPKKR EMLAEIEAAL PEVTSIMQNV NQAKSSLIFG DETFLLAGKE SIEEKLMELE FDLSARAFFQ LNPFQTERLY QEVEKALVLT GSETLVDAYC GVGTIGQAFA GKVKEVRGMD IIPESIEDAK RNAEKNGIEN VYYEVGKAED VLPKWVKEGF RPDAVIVDPP RSGCDQGLIK SLLDVEAKQL VYVSCNPSTL ARDLALLAKK YRIRYMQPVD MFPQTAHVET VVLLQLKDK //