ID   Y1346_STRP1             Reviewed;         462 AA.
AC   Q99Z86; Q48Y56;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Uncharacterized RNA methyltransferase SPy_1346/M5005_Spy1098;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=SPy_1346, M5005_Spy1098;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ51716.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004092; AAK34177.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51716.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_269456.1; NC_002737.2.
DR   AlphaFoldDB; Q99Z86; -.
DR   SMR; Q99Z86; -.
DR   STRING; 1314.HKU360_01131; -.
DR   PaxDb; Q99Z86; -.
DR   EnsemblBacteria; AAK34177; AAK34177; SPy_1346.
DR   KEGG; spy:SPy_1346; -.
DR   KEGG; spz:M5005_Spy1098; -.
DR   PATRIC; fig|160490.10.peg.1176; -.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   OMA; FYAGDMK; -.
DR   Proteomes; UP000000750; Chromosome.
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   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..462
FT                   /note="Uncharacterized RNA methyltransferase
FT                   SPy_1346/M5005_Spy1098"
FT                   /id="PRO_0000162035"
FT   DOMAIN          12..70
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        419
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         294
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         323
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         344
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         392
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   462 AA;  51732 MW;  7D0DB1E41443CD84 CRC64;
     MVSPRKGKRI RMLKKNDIIQ VAISDLSHEG AGVAKHDGFV FFVDNALPEE VIDMRVLKVN
     KNSGFGKVEA YHYLSSARNA DVNLTYLRTG IADLGHLTYE DQLTFKKKQV QDSLYKIAGI
     SDVTVESTIG MTEPLAYRNK AQVPVRRVNG QLETGFFRKH SHDLIPISDY YIQDKEIDRL
     INFTRDLLRR FDIKPYDETE QTGLLRNIVV RRGHYSGEMM LVLVTTRPKV FRVDQVIEKI
     VEAFPAVVSI IQNINDKNTN AIFGKDFKTL YGKDTITDSM LGNNYAISAQ SFYQVNTVMA
     EKLYQTAIAF SDLSKDDIVI DAYSGIGTIG LSFAKTVKAV YGVEVIEAAV RDAQQNAALN
     GITNAYFVAD TAEHAMATWA KDGIKPSVIL VDPPRKGLTE SFIQASVAMG PQKITYVSCN
     PATMARDIKR YQELGYKLAK VQPVDLFPQT HHVECVVLLI KE