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Database: UniProt
Entry: A0A221W2L2_9PSEU
LinkDB: A0A221W2L2_9PSEU
Original site: A0A221W2L2_9PSEU 
ID   A0A221W2L2_9PSEU        Unreviewed;       481 AA.
AC   A0A221W2L2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:ASO19957.1};
DE            EC=2.1.1.176 {ECO:0000313|EMBL:ASO19957.1};
GN   Name=rsmB {ECO:0000313|EMBL:ASO19957.1};
GN   ORFNames=AHOG_11570 {ECO:0000313|EMBL:ASO19957.1};
OS   Actinoalloteichus hoggarensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinoalloteichus.
OX   NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO19957.1, ECO:0000313|Proteomes:UP000204221};
RN   [1] {ECO:0000313|EMBL:ASO19957.1, ECO:0000313|Proteomes:UP000204221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO19957.1,
RC   ECO:0000313|Proteomes:UP000204221};
RA   Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA   Kalinowski J., Zotchev S.B.;
RT   "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943, type
RT   strain of Actinoalloteichus hoggarensis.";
RL   Submitted (JUL-2017) 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}.
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DR   EMBL; CP022521; ASO19957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A221W2L2; -.
DR   KEGG; ahg:AHOG_11570; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000204221; Chromosome.
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:UP000204221};
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          191..475
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         295..301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         320
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         344
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         361
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   481 AA;  50897 MW;  259339D46D1B6E4F CRC64;
     MSPSPARRDR RGGPSGPPRG RQGPRRPPTQ DAARDAALDT LTAVREKDAY ANLVLPRLLR
     DRRLTTRDAG LATELTYGAC RAFGLLDTVL GDCSDRPVDE IDGVVLDALR LGCYQLLRTR
     IPTHAAVSAT VELVRGRAGS GAAGFANAVL RRVSERTEDE WVELLAPDAT SDPIGHLALR
     HAHPRWVAEA FAAALGDARD ELAEALAADD ARPAVHLVAR PGEISSAELA AVTGGDEAPY
     SPYGVRLEAG AGDPADLEPV RERLAGVQDE GSQLAALALT RPPAEGSDLR WLDLCAGPGG
     KAALLGALVS LDGGTLDAVE PAAHRADLIR SLVRELPVTV HVGDGRDSGL PAGGFDRVLV
     DAPCTGLGAL RRRPEARWRR RPSDVAELAR LQGELLRAAF ELVRPGGVVA YVVCSPHLSE
     TVEVARQAAR LPGVVQLDAR PFFPDVPALG DGPGVQLWPH RHGTDAMFCA LFRREAAAPT
     A
//
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