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Database: UniProt
Entry: A0A3D8K5E9_9BURK
LinkDB: A0A3D8K5E9_9BURK
Original site: A0A3D8K5E9_9BURK 
ID   A0A3D8K5E9_9BURK        Unreviewed;       477 AA.
AC   A0A3D8K5E9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-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:RDV00107.1};
GN   ORFNames=DWV00_07005 {ECO:0000313|EMBL:RDV00107.1};
OS   Trinickia dinghuensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Trinickia.
OX   NCBI_TaxID=2291023 {ECO:0000313|EMBL:RDV00107.1, ECO:0000313|Proteomes:UP000256838};
RN   [1] {ECO:0000313|EMBL:RDV00107.1, ECO:0000313|Proteomes:UP000256838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DHOM06 {ECO:0000313|EMBL:RDV00107.1,
RC   ECO:0000313|Proteomes:UP000256838};
RA   Gao Z.-H., Qiu L.-H.;
RT   "Paraburkholderia sp. DHOM06 isolated from forest soil.";
RL   Submitted (AUG-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:RDV00107.1}.
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DR   EMBL; QRGA01000003; RDV00107.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8K5E9; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000256838; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; 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; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00563; rsmB; 1.
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   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:UP000256838};
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          195..477
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        403
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         283..289
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         305
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         331
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         350
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   477 AA;  50797 MW;  5B1F80DB26D24E3D CRC64;
     MTRSAPTRRK APKAGAAQFS TLHLAPDSLG FALDCAALAV GAVRTGTALP AALAAVQASM
     PAAAAASARG AIQDLAYRTL RRLGTVDWLV GQLVNKAPPA HVGNVLSCAL ALLIDDERHA
     AYTSFTVVDQ AVTAIGARRE CVFAKGLVNA VLRNFLRERE AWLEKAQADA VAASNYPLWW
     AEAVRRAWPD AWQRVLAAGN APGPLTLRVN ARRSTVAEYL QTLDSNGIAA DAIGPYAVRL
     ATPLPVDRIP GFSQGVVSVQ DAGAQLAAER LDVRDGMRVL DACAAPGGKT GHILELADVD
     LVALESDPAR AARIEENLTR LGLRANVTVG DAGTPAAWHD GQPFDRILAD VPCSASGIVR
     RHPDVRWLRR ATDIPALVTE QRRILDALWP LVAPGGELLY VTCSIFPEEC EEQARWFEST
     HEDAVRLDAP GQLLPAGLPA AASPSVSLST GTHAAKSERP GADIDHDGFY YARFQKR
//
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