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Y1703_LISMO
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   03-AUG-2022, entry version 100.
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; Firmicutes; 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}.
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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.lmo1703; -.
DR   PaxDb; Q8Y6I1; -.
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   OMA; YCGVGGF; -.
DR   PhylomeDB; Q8Y6I1; -.
DR   BioCyc; LMON169963:LMO1703-MON; -.
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   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.150; -; 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   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53335; SSF53335; 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
 
 
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