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Database: UniProt
Entry: A0A328BK80_9CAUL
LinkDB: A0A328BK80_9CAUL
Original site: A0A328BK80_9CAUL 
ID   A0A328BK80_9CAUL        Unreviewed;       428 AA.
AC   A0A328BK80;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=rRNA methyltransferase {ECO:0000313|EMBL:RAK67872.1};
GN   ORFNames=DJ019_05305 {ECO:0000313|EMBL:RAK67872.1};
OS   Phenylobacterium kunshanense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=1445034 {ECO:0000313|EMBL:RAK67872.1, ECO:0000313|Proteomes:UP000249524};
RN   [1] {ECO:0000313|EMBL:RAK67872.1, ECO:0000313|Proteomes:UP000249524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BUT-10 {ECO:0000313|EMBL:RAK67872.1,
RC   ECO:0000313|Proteomes:UP000249524};
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA   Winkler M.E.;
RL   Submitted (MAY-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|ARBA:ARBA00007494,
CC       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:RAK67872.1}.
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DR   EMBL; QFYS01000002; RAK67872.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328BK80; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000249524; 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:UP000249524};
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          139..427
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        361
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         245..251
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         266
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         292
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         308
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   428 AA;  44828 MW;  C36306753A82423D CRC64;
     MSETDDIRGL PARAAALDLL TTALSRRAGL DEGLSHPAMA ALEPRDRAFA RALVMATLRW
     LGPIDTALQS RLKKPPPERI VNVLRLGAAQ LLVLKTPAHA AVGATVDLCA AQKGGESFKG
     LVNAVLRGLT REPPDLADPS LMAPTWLAAR WRSAYGAADA DAIAALVGEE PATDITLQDP
     ADAAELAVPL EAAPLPGGGL RVGLKGEVST WPGFADGRWW VQDASAAVPA RLLEVQKGQA
     ALDLCAAPGG KTLQMAAAGA KVTAVDRSAG RIKRVSENLK RTGLGAEVVV ADAADWSDGR
     TFDAVLLDAP CSATGTLRRH PDVLWVASPA DVPKLAAVQS RLLDSAARRT KPGGRLVYCV
     CSLEPEEGEG QVAAFLARNK AFRLEPMTPG EGGAPEASLR ADGTLRILPH HRPGGTDGFY
     VARMRRDG
//
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