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Database: UniProt
Entry: A0A3M9LZW5_9MICO
LinkDB: A0A3M9LZW5_9MICO
Original site: A0A3M9LZW5_9MICO 
ID   A0A3M9LZW5_9MICO        Unreviewed;       505 AA.
AC   A0A3M9LZW5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=rRNA small subunit methyltransferase B {ECO:0000313|EMBL:RNI18163.1};
GN   ORFNames=EFY87_18380 {ECO:0000313|EMBL:RNI18163.1};
OS   Flexivirga caeni.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Flexivirga.
OX   NCBI_TaxID=2294115 {ECO:0000313|EMBL:RNI18163.1, ECO:0000313|Proteomes:UP000271678};
RN   [1] {ECO:0000313|EMBL:RNI18163.1, ECO:0000313|Proteomes:UP000271678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BO-16 {ECO:0000313|EMBL:RNI18163.1,
RC   ECO:0000313|Proteomes:UP000271678};
RA   Im W.T.;
RT   "Draft genome of Simplicispira Flexivirga sp. BO-16.";
RL   Submitted (NOV-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}.
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:RNI18163.1}.
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DR   EMBL; RJJQ01000024; RNI18163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M9LZW5; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000271678; 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:UP000271678};
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          206..502
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        435
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         309..315
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         335
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         364
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         382
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   505 AA;  53356 MW;  962E36BB83CDE5F3 CRC64;
     MNDEQQRGGY RDERGRQRPE SRRAGGKNRT AVRPADRRRG GDPTRKAAWQ VSRAVAGGAY
     ANLELPKVLR AAGLHGRDAA FATELTYGAI RMRGLYDAII EFASGRPVSQ IDPPVLDTLR
     LGAHQILGMR VPPHAAASET VALAREVNGT GASGFVNAVL RRITERTREE WIREVTAGRP
     RDEALAVEHS HPAWVVRALR GSLRSGGVTD EAHLEDALVA LLEADNAAPA VSLVARPGLA
     TVAELVEAGA EASQLSPVGA VLPGGDPADI PAVRQTRAAV QDEGSQLVAL ALAAAPRDGD
     GPQEWLDLCA GPGGKAALLA ALSTSQQNVT VFVNEVNEHR TELVRRTMRA AIDAGAEVMI
     GTGDGRELGA EEPDTYDRIL VDAPCTGLGA LRRRPEARWR RTPADVGELT AIQAELLASA
     LDAAKPGGVV AYVTCSPHVA ETTAVVDSVT EGRGDATVED ARGLFRDASG SQISDLGDGP
     TVQLWPHVHG TDAMFFALLR KTVTS
//
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