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Database: UniProt
Entry: A0A3P1S7J3_9FIRM
LinkDB: A0A3P1S7J3_9FIRM
Original site: A0A3P1S7J3_9FIRM 
ID   A0A3P1S7J3_9FIRM        Unreviewed;       402 AA.
AC   A0A3P1S7J3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=16S rRNA (Cytosine(967)-C(5))-methyltransferase RsmB {ECO:0000313|EMBL:RRC93109.1};
DE            EC=2.1.1.176 {ECO:0000313|EMBL:RRC93109.1};
GN   Name=rsmB {ECO:0000313|EMBL:RRC93109.1};
GN   ORFNames=EII25_02560 {ECO:0000313|EMBL:RRC93109.1};
OS   Erysipelotrichaceae bacterium OH741_COT-311.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae.
OX   NCBI_TaxID=2491058 {ECO:0000313|EMBL:RRC93109.1, ECO:0000313|Proteomes:UP000270315};
RN   [1] {ECO:0000313|EMBL:RRC93109.1, ECO:0000313|Proteomes:UP000270315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH741_COT-311 {ECO:0000313|EMBL:RRC93109.1,
RC   ECO:0000313|Proteomes:UP000270315};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       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:RRC93109.1}.
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DR   EMBL; RQZE01000004; RRC93109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P1S7J3; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000270315; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.940.10; NusB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; NusB-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 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:UP000270315};
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          141..402
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        354
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         234..240
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         258
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         285
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   402 AA;  46865 MW;  8DDD9371B7511488 CRC64;
     MNQREIAYQL LQEIMLDGKY SNLIMRQTLM KVDPLKRGYI SEVVYGVLRN YRYLRYQWMD
     LVKHKPKNKI AILIDMAIYL LLYTNDPDYA VVNDACILAK NQKGFVNAVL RRFLARKEKK
     LHLDSFEHLG IYYSLPSWVV AMWHKQYGSE TTQKILESKL KKATMFYRLN AGYTIQDIEH
     LDVKQIDDTC FTSKYNLVHT KEFIHHVFDI QDYGSQQIVK LLQVDKHQDV LDICSAPGSK
     TVQIASALGH TGSLIACDIH LHRLQLVEEK MRSYGFLNLQ YQVCDASTVK FDKVFDRILL
     DVPCSGLGTL SHKCEIAMRI QPETIDELVA LQAKILENIT KYVKVNGYFV YSTCTLNKKE
     NEKQIEHFLL KHGNFKLVQQ RTIFPFEFDS DGFYMALCQR IK
//
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