ID A0A0J1FRS1_9BURK Unreviewed; 433 AA.
AC A0A0J1FRS1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:KLU22458.1};
GN ORFNames=EOS_30505 {ECO:0000313|EMBL:KLU22458.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU22458.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU22458.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(2015).
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:KLU22458.1}.
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DR EMBL; AEJF01000179; KLU22458.1; -; Genomic_DNA.
DR RefSeq; WP_047895929.1; NZ_AEJF01000179.1.
DR AlphaFoldDB; A0A0J1FRS1; -.
DR PATRIC; fig|908627.4.peg.6806; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000035963; 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};
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..418
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 355
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 282
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 302
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 433 AA; 47404 MW; 445E8EFF6C4B4EBF CRC64;
MRLHGFLIGQ TETLLADVLR FSGPADAATS RFFRAHPKLG HNERGVIAEA VFAVLRRKME
FSHLAESGSG NLARRLALLG LMQTAGLSAV KPFISADEYQ WLNQVSKIDP GSLPVRVRTN
LPQWIYDAMT KRFDTEELAL LAAALNYPAP LDLRANPIKA TRELVIKTLT EAGIDAGEMP
FAPYGVRVDG KPALTRLQPF QDGWIEVQDE GSQLLCSLVA PRRGEMIVDF CAGAGGKTLA
LGAMMRSSGR LYAFDVSDRR LAKLKPRLAR SGLSNVNPVL IDSEHDAKIK RLAGKIDRVL
VDAPCSGLGT LRRNPDLKWR QSPESVAELT PKQLSILTSA ARLVKVGGRL VYATCSMLEA
ENEGVVNQFL ATHPGFKLVP AREVLAEQRI DLDTGDYLQL WPHKHGTDGF FAAVLERLPV
AAKEAVVEEA VEE
//
