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Database: UniProt
Entry: A0A2V5KBW6_9BACL
LinkDB: A0A2V5KBW6_9BACL
Original site: A0A2V5KBW6_9BACL 
ID   A0A2V5KBW6_9BACL        Unreviewed;       464 AA.
AC   A0A2V5KBW6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:PYI56482.1};
GN   ORFNames=DLM86_05785 {ECO:0000313|EMBL:PYI56482.1};
OS   Paenibacillus flagellatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2211139 {ECO:0000313|EMBL:PYI56482.1, ECO:0000313|Proteomes:UP000247476};
RN   [1] {ECO:0000313|EMBL:PYI56482.1, ECO:0000313|Proteomes:UP000247476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DXL2 {ECO:0000313|EMBL:PYI56482.1,
RC   ECO:0000313|Proteomes:UP000247476};
RA   Dai X.;
RT   "Paenibacillus flagellatus sp. nov., isolated from selenium mineral soil.";
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|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:PYI56482.1}.
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DR   EMBL; QJVJ01000002; PYI56482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5KBW6; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000247476; 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   CDD; cd21147; RsmF_methylt_CTD1; 1.
DR   Gene3D; 2.30.130.60; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF17125; Methyltr_RsmF_N; 1.
DR   Pfam; PF13636; Methyltranf_PUA; 1.
DR   Pfam; PF17126; RsmF_methylt_CI; 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:UP000247476};
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          23..332
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          289..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        242
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         120..126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         144
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         189
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   464 AA;  50924 MW;  8F0AE0BEB2A29382 CRC64;
     MIELPQRFIE RIREQLGPEA EAFIGTYDEP RTQGLRLNPL KLGGPATGAN GHESFRDELI
     RRFGLTPVPW CRDGYYYDEA TKPGKHPYHQ AGLYYIQEPS AMSAAELLDV QPGELVLDLA
     AAPGGKTTQI AGALAGRGLL VSNDIHPARA KILSENVERF GIANAVVTNA SPDELAAKFS
     GAFDKIMLDA PCSGEGMFRK DPEAILEWSP DHVRMCAARQ LDILDSAARL LKPGGTLAYS
     TCTFNREENE EALERFVERY PAFSVVRTER IWPHRHKGEG HFVALLRRQT DEEPASTAAT
     SGRRDERCRR TDPADRSVRE AMKLAEAMLR DVVPGFDLPA GEPVLFGEQL YWLPSVPGFP
     LRARDLNGLR TLRPGLHLAH VKKDRAEPAH SLAMAISTRQ ARSVASFDAD GPEAGAYWRG
     ETVPAPDGVN GWTAVAVDGY PIGWAKASGG QLKNHLPKGL RRPG
//
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