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Database: UniProt
Entry: A0A139NRH0_9STRE
LinkDB: A0A139NRH0_9STRE
Original site: A0A139NRH0_9STRE 
ID   A0A139NRH0_9STRE        Unreviewed;       435 AA.
AC   A0A139NRH0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=tRNA and rRNA cytosine-C5-methylase {ECO:0000313|EMBL:KXT78646.1};
GN   ORFNames=STRDD13_00537 {ECO:0000313|EMBL:KXT78646.1};
OS   Streptococcus sp. DD13.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1777881 {ECO:0000313|EMBL:KXT78646.1, ECO:0000313|Proteomes:UP000070387};
RN   [1] {ECO:0000313|EMBL:KXT78646.1, ECO:0000313|Proteomes:UP000070387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD13 {ECO:0000313|EMBL:KXT78646.1,
RC   ECO:0000313|Proteomes:UP000070387};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT78646.1}.
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DR   EMBL; LQRH01000022; KXT78646.1; -; Genomic_DNA.
DR   RefSeq; WP_067101485.1; NZ_KQ969506.1.
DR   AlphaFoldDB; A0A139NRH0; -.
DR   STRING; 1777881.STRDD13_00537; -.
DR   PATRIC; fig|1777881.3.peg.564; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000070387; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd21147; RsmF_methylt_CTD1; 1.
DR   Gene3D; 2.30.130.60; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF17125; Methyltr_RsmF_N; 1.
DR   Pfam; PF13636; Methyltranf_PUA; 1.
DR   Pfam; PF17126; RsmF_methylt_CI; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000070387};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          1..282
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        221
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         99..105
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   435 AA;  48368 MW;  A4D9B7E99EBED032 CRC64;
     MNLPADFQKK YLDLLGDDAP PFLESFQKEA ESGFRINPLK EQIPHFSHAI PDMNWSFYGK
     VSGKSVEHVT GVVYSQEPAA QVVGQVASPK EGMKVLDLAA APGGKSTHLL SYLKNSGLLV
     SNEISTKRSK ILVENIERFG ARNVVVTNES AQNLAKVFPA YFDMIVLDAP CSGEGMFRKD
     PDAMQYWSVD YPSQCARLQK EILTSAIEML AEDGELIYST CTWSPEENEE IVHWLLEQGD
     FELLDIPKIN GMLPGIGLPE TARMYPHHFK GEGQFVAKLR YTGARSKRRA SKITKKVSRE
     QELLWKQFKE ANLIGDVSGR LEAFGSHLYL VPEELPDLSS LKIARNGLYL GECKKNRFEP
     SYALGIALKR SEVQKSIDLT SEQFVLYVSG NTVAVDSSLE NGWYQVRAGG NGLGFAKIVS
     GTLKNSFPKG LRFQA
//
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