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Database: UniProt
Entry: A0A0A2DW87_9PORP
LinkDB: A0A0A2DW87_9PORP
Original site: A0A0A2DW87_9PORP 
ID   A0A0A2DW87_9PORP        Unreviewed;       483 AA.
AC   A0A0A2DW87;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=HQ37_05575 {ECO:0000313|EMBL:KGN69657.1};
OS   Porphyromonas sp. COT-239 OH1446.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=1515613 {ECO:0000313|EMBL:KGN69657.1, ECO:0000313|Proteomes:UP000030150};
RN   [1] {ECO:0000313|EMBL:KGN69657.1, ECO:0000313|Proteomes:UP000030150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-239 OH1446 {ECO:0000313|Proteomes:UP000030150};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA   Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT   "Porphyromonas sp. COT-239_OH1446 Genome sequencing.";
RL   Submitted (AUG-2014) 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:KGN69657.1}.
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DR   EMBL; JRAO01000019; KGN69657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2DW87; -.
DR   STRING; 1515613.HQ37_05575; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG3270; Bacteria.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000030150; 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   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; 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   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:UP000030150};
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          1..294
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          298..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        231
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         110..116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         178
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   483 AA;  53495 MW;  57175906A32E3FBB CRC64;
     MTSVALPEAF CAQMIDLLGS DEAQELFTAL EQPSPVSIRL NRRKHTPQML EAGQPIAWSP
     LGRYLTERPS FVGDPLWHSG AYYVQEASSM ILSLIAPLMP QRSLNALDLC AAPGGKSTLL
     LDLLPEASLL VSNEVVRTRA HILQENLLKW GHPSTIVTHV MPEALGRLTS AFDLILVDAP
     CSGEGMFRKD HEARSEWSPE AVLHCASRQR SILNDIWPSL APGGLMIYST CTMNLEENEH
     MLHYITSTLG GEALSLLQLP EGIEPSPYSQ EPCYRMMPHR VSGEGLFMAI IRKGEGGKVS
     DGLSNTKRRR PRGKASAKGG REGQALTTMS AIHSWLQRGA DRHWGQSREG ELFALEEAHW
     PMLERLEAEG IHPLTSGIPV AILKGRDLIP HPALAHSTEL APKAFEEVEL TRLGAIRYLA
     GEAITLPLDL PVGWYIVCYE GNRLGFVKHL GRRSNNHYPA PWRIRQPQPL YQRLGAMPDI
     LEP
//
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