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Database: UniProt
Entry: A0A0Q7FUY8_9FLAO
LinkDB: A0A0Q7FUY8_9FLAO
Original site: A0A0Q7FUY8_9FLAO 
ID   A0A0Q7FUY8_9FLAO        Unreviewed;       404 AA.
AC   A0A0Q7FUY8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KQW98777.1};
GN   ORFNames=ASC72_11610 {ECO:0000313|EMBL:KQW98777.1};
OS   Flavobacterium sp. Root420.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1736533 {ECO:0000313|EMBL:KQW98777.1, ECO:0000313|Proteomes:UP000051729};
RN   [1] {ECO:0000313|EMBL:KQW98777.1, ECO:0000313|Proteomes:UP000051729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root420 {ECO:0000313|EMBL:KQW98777.1,
RC   ECO:0000313|Proteomes:UP000051729};
RX   PubMed=26633631; DOI=10.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA   Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA   McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQW98777.1}.
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DR   EMBL; LMEF01000030; KQW98777.1; -; Genomic_DNA.
DR   RefSeq; WP_056193668.1; NZ_LMEF01000030.1.
DR   AlphaFoldDB; A0A0Q7FUY8; -.
DR   STRING; 1736533.ASC72_11610; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000051729; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent 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; IPR001678; MeTrfase_RsmB/NOP2.
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:SF53; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE B-RELATED; 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};
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          142..403
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        354
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         256
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         283
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   404 AA;  46309 MW;  375C8582A4CE2833 CRC64;
     MRLHRNLVYT TIDSLNAIFN EGEYADKVVA RALKKDKRWG SSDRKFVAET IYEIVRWKRL
     YAEIAEVKEP FDRDNLWRMF AVWAVLRGYP IPDWRQLEGT PERKIKGRFD ELSKIRALKE
     SIPDWMDELG VKELGEKVWS TEIAAQNQPA KVILRTNTLK GTKESLRNTL MDLNIETEYL
     KDQPEALVLK ERANVFLTDA FKQGLFEVQD ANSQLVAGFL DVKPGMRVVD TCAGAGGKTL
     HIASLMENKG QLIAMDLYES KLKQLKLRAK RNGAFNIEYR IIDTTKVIKK LHEKADRVLI
     DAPCSGLGVL KRNPDAKWKL QPEFIDNIRK VQSEVLESYS KIVKPGGKLV YATCSVLPSE
     NQEQVEKFLK TEIGKQFTFI KDRKILASES GFDGFYMALL ERKA
//
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