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Database: UniProt
Entry: D7DL30_METV0
LinkDB: D7DL30_METV0
Original site: D7DL30_METV0 
ID   D7DL30_METV0            Unreviewed;       531 AA.
AC   D7DL30;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Fmu (Sun) domain protein {ECO:0000313|EMBL:ADI28641.1};
GN   OrderedLocusNames=M301_0254 {ECO:0000313|EMBL:ADI28641.1};
OS   Methylotenera versatilis (strain 301).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylotenera.
OX   NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI28641.1, ECO:0000313|Proteomes:UP000000383};
RN   [1] {ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|Proteomes:UP000000383};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA   Chistoservova L., Kalyuzhnaya M., Woyke T.;
RT   "Complete sequence of Methylotenera sp. 301.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADI28641.1, ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|EMBL:ADI28641.1,
RC   ECO:0000313|Proteomes:UP000000383};
RX   PubMed=21622745; DOI=10.1128/JB.00404-11;
RA   Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA   Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA   Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT   "Genomes of three methylotrophs from a single niche uncover genetic and
RT   metabolic divergence of Methylophilaceae.";
RL   J. Bacteriol. 193:3757-3764(2011).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       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; CP002056; ADI28641.1; -; Genomic_DNA.
DR   RefSeq; WP_013146958.1; NC_014207.1.
DR   AlphaFoldDB; D7DL30; -.
DR   STRING; 666681.M301_0254; -.
DR   KEGG; meh:M301_0254; -.
DR   eggNOG; COG0144; Bacteria.
DR   HOGENOM; CLU_005316_0_2_4; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000000383; 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; IPR018314; Fmu/NOL1/Nop2p_CS.
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; PS01153; NOL1_NOP2_SUN; 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:UP000000383};
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          143..424
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        361
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         261
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         308
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   531 AA;  58902 MW;  1E909C1952B3ACF6 CRC64;
     MTPNLIRQAA VMLSNLLEFN SPADAKLSEF FRNNRDLGTK ERAFVAESVY GVLRRLRFLS
     AVTANDDNDP DDARKLVLAW MLRIQGMSIQ KIESMLTEQQ IEWAHTIKAK STENLPLAVQ
     ADVRDWLWEK LVAQYGEKEA LTIARSMHDA ATLDLRVNTI KGTRDDVMAK FIAENTSGES
     NVTKTPYSPI GLRMPLRLNI SRHVMFTEGQ IEVQDEGSQI LAHLVAPKRG MMVADFCAGA
     GGKTLAMGAL MRNTGRLYAF DVSEKRLHSL GQRLKRSGLS NLNAQSISSE TDPKLKRLNG
     KFDRVLVDAP CTGLGTLRRN PDLKWRQTPQ DLAELTVKQA NILARASKLT KTGGRLIYST
     CSLLRDENEQ IAENFLATHP DFKLLNAAEI LKQQQINLDT GDYLKLLPHL HNTDGFFAAV
     FEKTDGTSKP VKVATSVVAV DEAILQTAST EPKAKKAAAK PKVTKPKAAK EAAVEETLDE
     KTTVNEVVVK EKVAKPKVVK EKTVKEKIVK EKVVKEKVVK PKAVKTKAVK E
//
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