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Database: UniProt
Entry: A0A2N7VDH3_9BURK
LinkDB: A0A2N7VDH3_9BURK
Original site: A0A2N7VDH3_9BURK 
ID   A0A2N7VDH3_9BURK        Unreviewed;       465 AA.
AC   A0A2N7VDH3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:PMS15211.1};
GN   ORFNames=C0Z18_28250 {ECO:0000313|EMBL:PMS15211.1};
OS   Trinickia dabaoshanensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Trinickia.
OX   NCBI_TaxID=564714 {ECO:0000313|EMBL:PMS15211.1, ECO:0000313|Proteomes:UP000235616};
RN   [1] {ECO:0000313|EMBL:PMS15211.1, ECO:0000313|Proteomes:UP000235616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GIMN1.004 {ECO:0000313|EMBL:PMS15211.1,
RC   ECO:0000313|Proteomes:UP000235616};
RA   Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA   Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA   Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA   James E.K.;
RT   "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT   further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT   gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT   diazotrophy and nodulation in the Burkholderiaceae.";
RL   Submitted (JAN-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: 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:PMS15211.1}.
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DR   EMBL; PNYA01000034; PMS15211.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N7VDH3; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000235616; 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:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 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; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF77; SUN PROTEIN; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
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:UP000235616};
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          187..464
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        401
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         348
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   465 AA;  50168 MW;  A7F5E0CBF2ECE4E0 CRC64;
     MKSIKKKDKG AAKGSPKDNR AAGRPSGARP NAARPNAARP HAARRDSALH GFLIGQTETL
     LAEILKFTGP ADAATSRFFR AHPKLGHAER GIIAEAVFAV LRRRMEFAHL AESGSGNPTR
     RLALLGLMQT AGRAAVAPFV SEAEGAWLEH VSKIDPASLP LRVRTNLPEW IVEALAKRFD
     EQELAQLAAA LNYPAPLDLR VNPIKANREQ VLDALQASGI EAGATPFAPL GVRVSGKPAL
     TKLQPFEDGW IEVQDEGSQL LCALVAPRRG EMVVDFCAGA GGKTLALGAA MRSTGRLYAF
     DVSDRRLAKL KPRLARSGLS NVHPVLIDSE QDAKIKRLAG KIDRVLVDAP CSGLGTLRRN
     PDLKWRQSPA SVEELVPKQG SILASAARLV KPGGRLVYAT CSMLEAENEA IVTQFLADHP
     DFTLIPAGKV LAEQRIEIEM GDYLSLWPHR HATDGFFAAV LERRA
//
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