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Database: UniProt
Entry: A0A0N1L9U1_9PROT
LinkDB: A0A0N1L9U1_9PROT
Original site: A0A0N1L9U1_9PROT 
ID   A0A0N1L9U1_9PROT        Unreviewed;       429 AA.
AC   A0A0N1L9U1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:KPF65484.1};
GN   ORFNames=IP88_13445 {ECO:0000313|EMBL:KPF65484.1};
OS   alpha proteobacterium AAP81b.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1523432 {ECO:0000313|EMBL:KPF65484.1, ECO:0000313|Proteomes:UP000037971};
RN   [1] {ECO:0000313|EMBL:KPF65484.1, ECO:0000313|Proteomes:UP000037971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP81b {ECO:0000313|EMBL:KPF65484.1,
RC   ECO:0000313|Proteomes:UP000037971};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-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|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:KPF65484.1}.
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DR   EMBL; LJHX01000147; KPF65484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1L9U1; -.
DR   STRING; 1523432.IP88_13445; -.
DR   PATRIC; fig|1523432.3.peg.802; -.
DR   Proteomes; UP000037971; 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:UP000037971};
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          141..429
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        365
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         249..255
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         270
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         296
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         312
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   429 AA;  45372 MW;  58DAF8873B649787 CRC64;
     MARPGTRRPQ PTGLVPGLAA RRGALKLLMA VLGRGLAIER AQEAALDGIA MAADRGLARL
     LAATALRWLP ELDALIDSAT DKPLPDDARA RHVLRIALAG WLRLATPPHA AIATALPLVE
     GGPRRLVHGV LGALSRRGAE LPAAPRLPAP FDVRWATDWG PQVAEAASRL LADEPATDLS
     LRDPAETERW ADALGGTSLL PGHVRVARKG GLTEWPGFAE GAWWVQDLAA SLPVRLLGAK
     AGDRVLDVCA APGGKTLQLA AMGCAVTALD VAEPRLAMVA ENLERTGLAA EIVTADALRW
     EPEAPFDHIL LDAPCSATGI FRRHPDVLHL KGARDLAPLT LLQAALLRKA ATWLKPGGTL
     VYATCSLDPR EGERIAERVI AGLPRWPFEA AGLPLGLVPT ADGFVRTMPG MMAADGGMDG
     FFIARLRKL
//
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