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Database: UniProt
Entry: A0A0F0LRL0_9MICO
LinkDB: A0A0F0LRL0_9MICO
Original site: A0A0F0LRL0_9MICO 
ID   A0A0F0LRL0_9MICO        Unreviewed;       454 AA.
AC   A0A0F0LRL0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:KJL35763.1};
DE            EC=2.1.1.176 {ECO:0000313|EMBL:KJL35763.1};
GN   Name=rsmB {ECO:0000313|EMBL:KJL35763.1};
GN   ORFNames=RR49_02196 {ECO:0000313|EMBL:KJL35763.1};
OS   Microbacterium ginsengisoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=400772 {ECO:0000313|EMBL:KJL35763.1, ECO:0000313|Proteomes:UP000033451};
RN   [1] {ECO:0000313|EMBL:KJL35763.1, ECO:0000313|Proteomes:UP000033451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18659 {ECO:0000313|EMBL:KJL35763.1,
RC   ECO:0000313|Proteomes:UP000033451};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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: 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:KJL35763.1}.
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DR   EMBL; JYIY01000077; KJL35763.1; -; Genomic_DNA.
DR   RefSeq; WP_045248101.1; NZ_JYIY01000077.1.
DR   AlphaFoldDB; A0A0F0LRL0; -.
DR   STRING; 400772.RR49_02196; -.
DR   PATRIC; fig|400772.4.peg.2212; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000033451; 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; 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:UP000033451};
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          151..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         261..267
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         286
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         312
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;  48158 MW;  0EBF5653692C202F CRC64;
     MTAPARRVAF EVIRAVHADD AYANLLLPAA ITRAGLSSAD AALATELTYG TLRREGTYDA
     VISLAAGRDI ALIDPPVLDA LRLGAHQILA TRIASHAAVH DTVDLVRREI GPAVTGFANA
     VLRRISRDNP GDWFSRIADE ARSDDERLAL RFSHPVWVIR AFRRALAAEG RADELEALLT
     ADNAAPGVTM AALPGLVDPD ADSACTPYSP VGFRLAGGDP EPVITAAGGR VRVQDEGSQL
     VALALSRHAP VRAGERWLDL CAGPGGKTAL LAAEALAHGA VLDANEPVPA RAGLVRRSVA
     AVPLPVDVSE LDGRERAASA AGAYDRILVD APCTGLGALR RRPEARWRKQ SSDVADLTPL
     QRELLSSAVG ALTPGGVVAY VTCSPHLAET QGVVADVRRE WGDALEPVDA REVLQRVARR
     PLDLPEPASD DGHAQLWPHR HGTDGMFLAL LRRR
//
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