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Database: UniProt
Entry: A0A0S3F3R6_9SPHN
LinkDB: A0A0S3F3R6_9SPHN
Original site: A0A0S3F3R6_9SPHN 
ID   A0A0S3F3R6_9SPHN        Unreviewed;       430 AA.
AC   A0A0S3F3R6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:ALR22334.1};
GN   ORFNames=ATN00_02730 {ECO:0000313|EMBL:ALR22334.1};
OS   Sphingobium baderi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR22334.1, ECO:0000313|Proteomes:UP000056968};
RN   [1] {ECO:0000313|EMBL:ALR22334.1, ECO:0000313|Proteomes:UP000056968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DE-13 {ECO:0000313|EMBL:ALR22334.1,
RC   ECO:0000313|Proteomes:UP000056968};
RA   Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT   "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT   para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT   Sphingobium baderi DE-13.";
RL   Submitted (NOV-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|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; CP013264; ALR22334.1; -; Genomic_DNA.
DR   RefSeq; WP_062068318.1; NZ_CP013264.1.
DR   AlphaFoldDB; A0A0S3F3R6; -.
DR   STRING; 1332080.ATN00_02730; -.
DR   KEGG; sbd:ATN00_02730; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000056968; Chromosome.
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:UP000056968};
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          150..426
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        359
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         243..249
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         264
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         290
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         306
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   430 AA;  45738 MW;  44AE512076DEAC7B CRC64;
     MARSPRPDDI PGLPARRAAL RLLDAVLRRG DPLELALHGA AQGLPSADRA LVHAIAAETL
     RHLPDLDALI DGATRQPLPD DAKARMVLRI ALVQVLALGT APHAAIATAL PLVDGGPRKL
     VHGVFSTVTR AQPVLPDPPT LPPEVAARWA AQWGEAMPET AARSFAVRPP VDVSLRDAGD
     SDRWAERLGG ISLAPGHVRL PDGAAITDLP GFGEGAWWVQ DIAASCPARL LGPGEGRAAL
     DLCAAPGGKT MQLAAAGWRV SAVDQSKKRL ERLRENMERT GLSADIVQAD LRQWKPDAPV
     DAVLLDAPCS ATGIYRRHPD VLHRIGPRQI AELAELQAEL LDRCADWVKP GGTIIYATCS
     LEQAEGEEQI ATFLDRRPDF ATRPALVAEL PAGIAPTQDG WVRTLPGALD AQGGADGFFV
     ARLERTATRV
//
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