ID A0A1D8P4W2_9FLAO Unreviewed; 402 AA.
AC A0A1D8P4W2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:AOW19618.1};
GN ORFNames=LPB138_02510 {ECO:0000313|EMBL:AOW19618.1};
OS Urechidicola croceus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Urechidicola.
OX NCBI_TaxID=1850246 {ECO:0000313|EMBL:AOW19618.1, ECO:0000313|Proteomes:UP000176050};
RN [1] {ECO:0000313|EMBL:AOW19618.1, ECO:0000313|Proteomes:UP000176050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0138 {ECO:0000313|EMBL:AOW19618.1,
RC ECO:0000313|Proteomes:UP000176050};
RA Kim E., Yi H.;
RT "Lutibacter sp. LPB0138, isolated from marine gastropod.";
RL Submitted (OCT-2016) 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; CP017478; AOW19618.1; -; Genomic_DNA.
DR RefSeq; WP_070235734.1; NZ_CP017478.1.
DR AlphaFoldDB; A0A1D8P4W2; -.
DR STRING; 1850246.LPB138_02510; -.
DR KEGG; lul:LPB138_02510; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000176050; 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:UP000176050};
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..402
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 402 AA; 46115 MW; DBAF6DC678B682C5 CRC64;
MRLHRNLCFT VIDSLHSIFN EEEFAGKVVE KALKRDKRWG ARDRKFVAET IYDIVRWKRL
YNEIAGTKDH YSRENLWKMF AVWAVLKGID LPDWKYFEST PVRRIKGKFD EAQKTRVIKE
SIPDWMDEIA VKELGADAWS KEIAAMNQKA EVILRVNTLK IDIATLQKFL RKEEVDTEIV
RDHPSALRLV ERKNVFLTEA FKRGYFEVQD ASSQLVAPFL QVEPGMRVVD TCAGAGGKTL
HLASLMQNKG QIIAMDIYAG KLAQLKKRAK RAGVHNIDMR VIDSTKVIKK LKDSADAVLI
DAPCSGIGVL KRNPDSKWKL QPEFLDNIKK TQAEILDSYS RMVKKGGKLV YATCSILPSE
NQNQVKNFLD THKEFKFVQD RKVSPSKSGF DGFYMALLER IE
//
