ID A0A0P0NK69_9SPHI Unreviewed; 389 AA.
AC A0A0P0NK69;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:ALL07995.1};
GN ORFNames=AQ505_22435 {ECO:0000313|EMBL:ALL07995.1};
OS Pedobacter sp. PACM 27299.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL07995.1, ECO:0000313|Proteomes:UP000062859};
RN [1] {ECO:0000313|EMBL:ALL07995.1, ECO:0000313|Proteomes:UP000062859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL07995.1,
RC ECO:0000313|Proteomes:UP000062859};
RA Gilbert D.G.;
RL Submitted (OCT-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}.
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DR EMBL; CP012996; ALL07995.1; -; Genomic_DNA.
DR RefSeq; WP_062550233.1; NZ_CP012996.1.
DR AlphaFoldDB; A0A0P0NK69; -.
DR STRING; 1727164.AQ505_22435; -.
DR KEGG; pep:AQ505_22435; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000062859; 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 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 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:UP000062859};
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 120..389
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 341
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 288
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 389 AA; 44995 MW; 2D012111DD0FC72B CRC64;
MRIEHQIRAF EQIFKSYDGL LPLHRFLHLY FKQNKKMGSS DRRWSSRYIY SFFRLGKALM
KEPQVQRLAI ADFLCNHTHS LVVDTYLSEF ADQIELPLKA KLALIQSVFP AFNLEDVFSF
HQNLSAEVEQ GDFFESFFTQ PDLFLRITKG HLKALLSDLQ AHEVPVKELS ETTLALPNGT
KLENIFPNQK FYQVQDLSSQ KTGLFFEPKA YDRWWDCCAA SGGKSLLLHD LEPSVQLVVS
DVRETSLNNL DDRFHEAGIK KYQKKVLDLL QNNDQDLHDY VFDGIVLDAP CSGSGTWGRT
PEMLYYFDAH KITMYNRLQK GIASNVVKYL KVGKPLIYIT CSVFKQENEE VVRFLEEMLP
LKLEKMEVVK GYKDAADTMF VARLIKTEA
//
