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Database: UniProt
Entry: A0A150H7M8_9MICO
LinkDB: A0A150H7M8_9MICO
Original site: A0A150H7M8_9MICO 
ID   A0A150H7M8_9MICO        Unreviewed;       469 AA.
AC   A0A150H7M8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:KXZ58102.1};
DE            EC=2.1.1.176 {ECO:0000313|EMBL:KXZ58102.1};
GN   Name=rsmB {ECO:0000313|EMBL:KXZ58102.1};
GN   ORFNames=Bravens_01138 {ECO:0000313|EMBL:KXZ58102.1};
OS   Brevibacterium ravenspurgense.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=479117 {ECO:0000313|EMBL:KXZ58102.1, ECO:0000313|Proteomes:UP000243589};
RN   [1] {ECO:0000313|EMBL:KXZ58102.1, ECO:0000313|Proteomes:UP000243589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG56047 {ECO:0000313|EMBL:KXZ58102.1,
RC   ECO:0000313|Proteomes:UP000243589};
RA   Bernier A.-M., Burdz T., Huynh C., Pachecho A.L., Wiebe D., Bonner C.,
RA   Bernard K.;
RT   "Use of Whole Genome Sequencing to ascertain that Brevibacterium
RT   massiliense (Roux, Raoult 2009) is a later heterotypic synonym of
RT   Brevibacterium ravenspurgense (Mages 2008).";
RL   Submitted (JAN-2016) 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:KXZ58102.1}.
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DR   EMBL; LQQC01000010; KXZ58102.1; -; Genomic_DNA.
DR   RefSeq; WP_062021165.1; NZ_LQQC01000010.1.
DR   AlphaFoldDB; A0A150H7M8; -.
DR   PATRIC; fig|479117.4.peg.1135; -.
DR   Proteomes; UP000243589; 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:UP000243589};
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          176..468
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        396
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         274..280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         299
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         325
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         343
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   469 AA;  50404 MW;  AEE1465936D98EDA CRC64;
     MSRPDARRSR GRNNPQKANL ARILAWEVLV AVDEDDAYAN LLLPRKIART RLRADDAALA
     TELTYGTLRA RGLYDAIIAE AASRKVDTLE IPVLNAMRMG AHQLLAMRIP DHAAVGETVA
     VIKQSLPRAS GIVNAVLRRI GERSYDDWLA LMTAGLPEDQ AKSLRYSHPA WIVSALREAL
     EAHGRSSAEI DLLLQSHNDP APVVLTALPG LDRSELPGTP TELSPLGVIL DRGDPGNLEA
     VRTGRARVQD EGSQLTALTL LEAEAPEGEW LDMCAGPGGK TAILAATAAE RGVPVTALDA
     SGHRADLVVD STRAFADTVE VFKGDGREFA EAYPGEFTRV LVDVPCSGLG ALRRRPEARW
     RRSSEDVRTL RPLQDGLLRA AWQACAPGGV IAYSTCSPHK HETLDVVRAF AADTPAVQIL
     NTPDHLARVT GQPAESFASS AVGDGAAAQL WSHVHETDGM FICLIRCPA
//
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