ID Q1DB20_MYXXD Unreviewed; 427 AA.
AC Q1DB20;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Methyltransferase, RsmB/NOP family {ECO:0000313|EMBL:ABF92880.1};
GN OrderedLocusNames=MXAN_1909 {ECO:0000313|EMBL:ABF92880.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF92880.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF92880.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF92880.1; -; Genomic_DNA.
DR RefSeq; WP_011552009.1; NC_008095.1.
DR AlphaFoldDB; Q1DB20; -.
DR STRING; 246197.MXAN_1909; -.
DR EnsemblBacteria; ABF92880; ABF92880; MXAN_1909.
DR GeneID; 41359323; -.
DR KEGG; mxa:MXAN_1909; -.
DR eggNOG; COG0144; Bacteria.
DR HOGENOM; CLU_005316_0_2_7; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000002402; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002402};
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 157..425
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 364
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 272
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 311
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 427 AA; 46335 MW; FCF9223E80E02B10 CRC64;
MVPALSTVPF DPLSRLHLQP WSALAGLGPV AADAIAQVLA GSAAERVLDR TLRDRRSLTR
EQRLALKEAV FNVGLWRRRL GFLLGREDAA PLFLLHALMH GLAGVPAVES AALAGLGDGA
PPPLVSAPPP TLALRASLPD WLADHFAREF GPEADDFCAH LNVPGPITLR ANVLRTSREA
LAERLRSEGV ETRPGPWSPL ALHIEGPRPN LYGLRSLQEG LFEVQDEGSQ LLGLLVEARP
GETVLDLCAG AGGKTLQLGA DMKDSGRLLA YDPDPERLDR LLQRSSRAHL TRVQVLRSLP
ESLDADRVLV DAPCSELGSL RRGPDQRFRI QPEVLTRFPA LQQDILQRGA RLVRPGGRLV
YATCTVNRAE NEDVVAAFLA SRPDFRLVRP GAGWLSDACL RDGFLFVAPH RHGTDAFFAA
VLERTAG
//
