ID   C0MCX8_STRS7            Unreviewed;       275 AA.
AC   C0MCX8;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Hemolysin-like protein {ECO:0000313|EMBL:CAW99954.1};
GN   OrderedLocusNames=SZO_13760 {ECO:0000313|EMBL:CAW99954.1};
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483 {ECO:0000313|Proteomes:UP000001368};
RN   [1] {ECO:0000313|EMBL:CAW99954.1, ECO:0000313|Proteomes:UP000001368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70 {ECO:0000313|EMBL:CAW99954.1,
RC   ECO:0000313|Proteomes:UP000001368};
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- SIMILARITY: Belongs to the TlyA family.
CC       {ECO:0000256|ARBA:ARBA00029460}.
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DR   EMBL; FM204884; CAW99954.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MCX8; -.
DR   KEGG; seq:SZO_13760; -.
DR   PATRIC; fig|40041.11.peg.1461; -.
DR   eggNOG; COG1189; Bacteria.
DR   HOGENOM; CLU_058015_3_0_9; -.
DR   Proteomes; UP000001368; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:InterPro.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR004538; Hemolysin_A/TlyA.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR047048; TlyA.
DR   NCBIfam; TIGR00478; tly; 1.
DR   PANTHER; PTHR32319; BACTERIAL HEMOLYSIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR32319:SF0; BACTERIAL HEMOLYSIN-LIKE PROTEIN; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   PIRSF; PIRSF005578; TlyA; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          62..244
FT                   /note="Ribosomal RNA methyltransferase FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
SQ   SEQUENCE   275 AA;  30347 MW;  FDCC5FCEE60A6165 CRC64;
     MAKERVDVLA YRQGLFETRE QAKRGVMAGL VISAISGLRF DKPGEKIDEE IELRLKGEKL
     KYVSRGGLKL EKALQVFGIS VQDKVTIDIG ASTGGFTDVM LQAGARLVYA VDVGTNQLVW
     KLRQDSRVRS MEQYNFRYAK LADFSEGQPA FASIDVSFIS LSLILPALCS LLQEGAEAVA
     LIKPQFEAGR EQIGKKGIVK DRLIHEKVIK QVTDTALNCG FIVKGLDFSP IQGGHGNIEF
     LAHLVKGKDS KAIDDQLIQS LVSSAHKEFK QHEKE
//