ID A0A1I4DJA2_9RHOB Unreviewed; 422 AA.
AC A0A1I4DJA2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=16S rRNA (Cytosine967-C5)-methyltransferase {ECO:0000313|EMBL:SFK93592.1};
GN ORFNames=SAMN04488036_103229 {ECO:0000313|EMBL:SFK93592.1};
OS Shimia haliotis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1280847 {ECO:0000313|EMBL:SFK93592.1, ECO:0000313|Proteomes:UP000198851};
RN [1] {ECO:0000313|EMBL:SFK93592.1, ECO:0000313|Proteomes:UP000198851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28453 {ECO:0000313|EMBL:SFK93592.1,
RC ECO:0000313|Proteomes:UP000198851};
RA de Groot N.N.;
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; FOSZ01000003; SFK93592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4DJA2; -.
DR STRING; 1280847.SAMN04488036_103229; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000198851; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.940.10; NusB-like; 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; IPR035926; NusB-like_sf.
DR InterPro; IPR006027; NusB_RsmB_TIM44.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF01029; NusB; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF48013; NusB-like; 1.
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 132..422
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 240..246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 301
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 422 AA; 45071 MW; E8C2061123C47E9B CRC64;
MSKSGMQTRR SAVYLLDQVM GEGRLMSEVI GSGALERLEP ADRARAQRLA MDTLRGLERA
DRVLQKHLKK VPALTVQNVL RLGTVELCQG GAAHGVVNDA VEIIAKNKHH AGLKGLVNAV
LRKVDADGQA EWDRLRIPRM PKWLRKPLAQ AYGSDVMLGI EAAHFNGAPL DLTAKGDAAA
LADTIGGELL PTGSVRVPVG QQVSALAGYE AGDWWVQDAA AALPAKILNV QAGEKVLDLC
AAPGGKTMQM AAAGAEVAAV DDNPSRMARV EENLKRTGLS ATLVVGDAMA QQGAYDAILL
DAPCSATGTM RRHPDLPFAK DGSEFGDLIG MQEVFLDHAL SLLKPGGRLV FCTCSLLPDE
GEVQVEESVA RWSGVSVDRD AVLIEGVDPD WVTEEGGLRL RPDYWADRGG MDGFYMALLR
KA
//