ID A0A1W6YZ32_9BORD Unreviewed; 495 AA.
AC A0A1W6YZ32;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=rRNA methyltransferase {ECO:0000313|EMBL:ARP86251.1};
GN ORFNames=CAL13_08595 {ECO:0000313|EMBL:ARP86251.1};
OS Bordetella genomosp. 9.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416803 {ECO:0000313|EMBL:ARP86251.1, ECO:0000313|Proteomes:UP000194139};
RN [1] {ECO:0000313|EMBL:ARP86251.1, ECO:0000313|Proteomes:UP000194139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU17164 {ECO:0000313|EMBL:ARP86251.1,
RC ECO:0000313|Proteomes:UP000194139};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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; CP021109; ARP86251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6YZ32; -.
DR Proteomes; UP000194139; 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:UP000194139};
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 163..444
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 380
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 307
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 327
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 495 AA; 53433 MW; 3E63F7F4F08D06D6 CRC64;
MKMKKPHRAG GKPAAPRAGG ADRARPSFAA IRLDQVQKVL GEVLQWSSPA DAALTKWLRA
HPALGGRDRA EVSEAAYDVL RNLRRYRRFA ETGVGPAARR LAILGLTATL GRDALREALS
PEENEWLQHI ALIDPATLPR AVRASLPDWL EERLGTLENA DALIEALNRP APLDIRVNPL
KTDRDTVLRG LTDGPAARYA PKPTPFSPWG IRLSGRPPVN RWPQFEAGEI EVQDEGSQLL
ALLMAPRRGE MVIDFCAGAG GKTLLLGALM RSTGRLYAFD VSAARLARAK PRFARSGLSN
VVPVVIDSEN DTRVKRLAGK AQRVLVDAPC SGIGTLRRNP DLKWRQHPEA LQELGALQTR
ILASAARCVA PGGRLVYATC SLLPEENEAQ AEIFLAAHPE FERVDAAALI AARCEGLALT
GPYMQLRPDV HGTDGFFAAV FERRKGDALS TTEAAAESVK ARAATAVPMP QGEPEAELEP
ESRQPQVNAG EGSAG
//