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Database: UniProt
Entry: K2KBJ9_9RHOB
LinkDB: K2KBJ9_9RHOB
Original site: K2KBJ9_9RHOB 
ID   K2KBJ9_9RHOB            Unreviewed;       430 AA.
AC   K2KBJ9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:EKE74735.1};
GN   ORFNames=B30_03385 {ECO:0000313|EMBL:EKE74735.1};
OS   Celeribacter baekdonensis B30.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE74735.1, ECO:0000313|Proteomes:UP000006762};
RN   [1] {ECO:0000313|EMBL:EKE74735.1, ECO:0000313|Proteomes:UP000006762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B30 {ECO:0000313|EMBL:EKE74735.1,
RC   ECO:0000313|Proteomes:UP000006762};
RA   Wang W.;
RT   "Celeribacter baekdonensis B30 Genome Sequencing.";
RL   Submitted (SEP-2012) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:EKE74735.1}.
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DR   EMBL; AMRK01000001; EKE74735.1; -; Genomic_DNA.
DR   RefSeq; WP_009570606.1; NZ_AMRK01000001.1.
DR   AlphaFoldDB; K2KBJ9; -.
DR   STRING; 1208323.B30_03385; -.
DR   PATRIC; fig|1208323.3.peg.694; -.
DR   eggNOG; COG0144; Bacteria.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000006762; 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; 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:UP000006762};
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          140..430
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        363
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         248..254
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         269
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         310
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   430 AA;  46726 MW;  3C35FA445385D040 CRC64;
     MKTRSTNTPS AVAGLEARRA ALALLDAILV EKRLLSEVLL LRTKDLTPED RARAQRLVSE
     CLRVMDRCDR MLGPHLTKRP APHVMNALRL GVYEICAVGE AAHGVVNAYV ALMQERAKAS
     HFKGLVNAVL RKIDASKDKW DVLPAPMMPK WLRKPLIADF GKETVALMEA AHAKGAPLDL
     SIKGDMAGWA KTLGGTVLPT GSLRLDPSVQ VTKLEGFAEG AWWVQDAAAA LPARILAPRS
     GERVLDMCAA PGGKTMQLSA AGAIVTALDI SESRMKRVQE NLTRCGLSAE IVVSDALEYE
     GGPFDAILLD APCTATGTIR RHPDLPQVKD GSDFPGLFEL QEHLIDRALG LLKPGGRLIY
     CTCSLLIDEG EEQVRDAKLR HPDLVVDLDA LKIEGVDPDW IGDEGLRTRP DYWADFGGLD
     GFFITVLRRG
//
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