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Database: UniProt
Entry: D4LRJ5_9FIRM
LinkDB: D4LRJ5_9FIRM
Original site: D4LRJ5_9FIRM 
ID   D4LRJ5_9FIRM            Unreviewed;       469 AA.
AC   D4LRJ5;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=NOL1/NOP2/sun family putative RNA methylase {ECO:0000313|EMBL:CBL23403.1};
GN   ORFNames=CK5_20290 {ECO:0000313|EMBL:CBL23403.1};
OS   Blautia obeum A2-162.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=657314 {ECO:0000313|EMBL:CBL23403.1, ECO:0000313|Proteomes:UP000008955};
RN   [1] {ECO:0000313|EMBL:CBL23403.1, ECO:0000313|Proteomes:UP000008955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2-162 {ECO:0000313|EMBL:CBL23403.1,
RC   ECO:0000313|Proteomes:UP000008955};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Ruminococcus obeum A2-162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL23403.1, ECO:0000313|Proteomes:UP000008955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2-162 {ECO:0000313|EMBL:CBL23403.1,
RC   ECO:0000313|Proteomes:UP000008955};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; FP929054; CBL23403.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4LRJ5; -.
DR   KEGG; rob:CK5_20290; -.
DR   PATRIC; fig|657314.3.peg.1888; -.
DR   HOGENOM; CLU_005316_6_1_9; -.
DR   Proteomes; UP000008955; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; 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; IPR011023; Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00446; nop2p; 1.
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};
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          29..308
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        238
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         116..122
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         140
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         185
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   469 AA;  52603 MW;  FB33AD04A16311DE CRC64;
     MSDYNITDLL SPAFLERMQK MLGDEYEDFI KSYEAPRTYG LRVNTAKISC EEFEKIVPFP
     VTPIPWIPNG YFYPGDVRPS FCPLYQAGLY YLQEPSAMTP ASCLPVTPGE NILDLCAAPG
     GKATALGAML NGSGLLVAND ISSSRTRALL RNIELFGIAN AFVTNETPAH LKNRFPEFFH
     KILLDAPCSG EGMFRKEDAL ARDWTPEKSE ELSVLQKELI LQAADMLRPG GQLLYSTCTF
     APKEDEGVVS YLLENRPDMK LIELPAYEGF TPGVPAWGNG DPALSRCVHL FPHKMQGEGH
     FMALLRKEGR TDLIGQFSYA KPNPDTRKWL ELFFQEIGLK TLGGQAFDWN RVETRKDKVY
     YLPPVTGDFR GLTFLRNGLY LGDLKKNRFE PSEPFALALR KDDADGIISL SVNDQRLTRY
     LKGETLNIEP TEAAHTKGWH LLCVEGYPLG FGKLVGQTFK NKYPAGWRV
//
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