ID A0A3G6ZMZ3_9MICO Unreviewed; 454 AA.
AC A0A3G6ZMZ3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=rRNA small subunit methyltransferase B {ECO:0000313|EMBL:AZC13967.1};
GN ORFNames=DT073_09805 {ECO:0000313|EMBL:AZC13967.1};
OS Microbacterium sp. ABRD28.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2268461 {ECO:0000313|EMBL:AZC13967.1, ECO:0000313|Proteomes:UP000280903};
RN [1] {ECO:0000313|EMBL:AZC13967.1, ECO:0000313|Proteomes:UP000280903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABRD_28 {ECO:0000313|EMBL:AZC13967.1};
RA Jin H.M.;
RT "Genome sequence of Microbacterium sp. ABRD28.";
RL Submitted (JUL-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|PROSITE-ProRule:PRU01023}.
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DR EMBL; CP031015; AZC13967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G6ZMZ3; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000280903; 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 Gene3D; 1.10.940.10; NusB-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; 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:UP000280903};
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 153..454
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 383
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 263..269
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 288
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 314
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 330
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 454 AA; 48047 MW; FAA5039C84EE2E40 CRC64;
MSALNPARLV AFETIRSVHD SDAYANLLLP TAIRRAGLDA ADAGLATELT YGTLRRENTY
DAVIAVAAAR AVDLIDPPVL DAIRLGVHQL LSTRVASHAA VNESVELARR AAGRSAGGFA
NAVLRRVSRD TPGDWMTRIG ETARSDDERR GLLTSHPVWV VRAFRRALAA EGRADELDEL
LHADNVSPRV TFAALPGLAE VPQGARRTDF SPVGFRSPGG DPEAQVTASG GRIRVQDEGS
QIAALALTRA RPARAGERWL DLCAGPGGKT AILAAEALAA GAQLEANEVN PARAGLVRQS
VAGVPLDVPV SEEDGRTRAR AGGYDRILVD APCTGLGALR RRPEARWRKS PSDVADLVDL
QRGLLDAAID GLTPGGLVAY VTCSPHLAET AGVVADIVRA RGDDVEELDA RAVITAFSAS
DPDLLPQADG SGRAQLWPHR HNTDAMSISL LRRR
//