ID E6LMS0_9FIRM Unreviewed; 471 AA.
AC E6LMS0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=NOL1/NOP2/sun family protein {ECO:0000313|EMBL:EFU76879.1};
GN ORFNames=HMPREF0381_1255 {ECO:0000313|EMBL:EFU76879.1};
OS Lachnoanaerobaculum saburreum DSM 3986.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnoanaerobaculum.
OX NCBI_TaxID=887325 {ECO:0000313|EMBL:EFU76879.1, ECO:0000313|Proteomes:UP000003434};
RN [1] {ECO:0000313|EMBL:EFU76879.1, ECO:0000313|Proteomes:UP000003434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3986 {ECO:0000313|EMBL:EFU76879.1,
RC ECO:0000313|Proteomes:UP000003434};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-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: 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:EFU76879.1}.
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DR EMBL; AEPW01000050; EFU76879.1; -; Genomic_DNA.
DR RefSeq; WP_008751022.1; NZ_GL622296.1.
DR AlphaFoldDB; E6LMS0; -.
DR eggNOG; COG0144; Bacteria.
DR HOGENOM; CLU_005316_6_1_9; -.
DR Proteomes; UP000003434; 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};
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 26..312
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 250
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 128..134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 471 AA; 53834 MW; 518987E9DBA6B182 CRC64;
MIQEKDLPKA YKDAMQKLLG EDYKAYIKSL DEKPYVGIRT NLLKLDSDRL KELLDRDFKS
VPWVKEGFYF EEERGVLTTP SIKYNKKINS ISKNPYYFAG LYYIQEPSAM TPASIAKIKP
GDKVLDLCAA PGGKSTQIAS YLQGEGLLVT NDFSASRVKA LQKNVEVSGI DNVLITNEDP
KHLSEVYSEY FDKIIVDAPC SGEGMFRRDS AVFKAYLGRG PESFTGIQVG ILNEAAKMLK
SGGTLVYSTC TYSSIEDEGS LISFLENHND FDIDRITPEF GFEESKQLPG TVRLFPHKLK
GEGHFVARLK KQDGKKYIEL KENGTVKNKK KQKPPKLPKE LLDFLKKINR KWDYERIFIN
KDYAYYLPKD ALIDKSLHYI RTGLLLGEIK KNRFEPFQAL AMNIKSDEWE NPLDLSATDE
RVVKYLKGET IEADDEYSGI RLVCVDGFSL GFVKQNKRSC KNKYYQGWRW V
//
