ID   Y1299_STRP3             Reviewed;         451 AA.
AC   P0DG16; Q79XZ4; Q8K6K7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Uncharacterized RNA methyltransferase SpyM3_1299;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=SpyM3_1299;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
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; AE014074; AAM79906.1; -; Genomic_DNA.
DR   RefSeq; WP_002991789.1; NC_004070.1.
DR   AlphaFoldDB; P0DG16; -.
DR   SMR; P0DG16; -.
DR   EnsemblBacteria; AAM79906; AAM79906; SpyM3_1299.
DR   GeneID; 57853005; -.
DR   KEGG; spg:SpyM3_1299; -.
DR   HOGENOM; CLU_014689_7_1_9; -.
DR   OMA; YCGVGGF; -.
DR   Proteomes; UP000000564; 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:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
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   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..451
FT                   /note="Uncharacterized RNA methyltransferase SpyM3_1299"
FT                   /id="PRO_0000162038"
FT   DOMAIN          2..60
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
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         162
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         312
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         333
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         381
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   451 AA;  50739 MW;  1B038374DE6A83C5 CRC64;
     MVVKVKQKIP LKIKRMGING EGIGFYQKTL VFVPGALKGE NIFCQITAVK RNFAEAKLLT
     VNKASKNRVK PACSVYETCG GCQIMHLAYP KQLDFKDDVI RQALKKFKPT GYEQFEIRPT
     LGMKKPDHYR AKLQFQLRSF GGTVKAGLFS QGSHRLVPID NCLVQDQLTQ DIINKITQLV
     DKYKLPIYNE RKIAGIRTIM VRKAQASDQV QIIVVSSKEV RLANFIGELT KAFPQVKTVA
     LNSNRSKSSE IYGDETEILW GQEAIHEEVL DYGFALSPRA FYQLNPQQTE VLYGEVVKAL
     DVGSKDHIID AYCGVGSIGF AFAGKVKSVR GMDIIPEAIE DAQKNAKAMG FDNAYYEAGK
     AEDIIPKWYK QGYRADAIIV DPPRTGLDDK LLKTILHYQP KQMVYVSCNT STLARDLVQL
     TKVYDVHYIQ SVDMFPHTAR TEAVVKLQKR V