ID S7V8A6_9BACT Unreviewed; 396 AA.
AC S7V8A6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=16S rRNA (Cytosine(967)-C(5))-methyltransferase {ECO:0000313|EMBL:EPR66141.1};
DE EC=2.1.1.176 {ECO:0000313|EMBL:EPR66141.1};
GN ORFNames=ADICYQ_4839 {ECO:0000313|EMBL:EPR66141.1};
OS Cyclobacterium qasimii M12-11B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR66141.1, ECO:0000313|Proteomes:UP000014974};
RN [1] {ECO:0000313|EMBL:EPR66141.1, ECO:0000313|Proteomes:UP000014974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12-11B {ECO:0000313|EMBL:EPR66141.1,
RC ECO:0000313|Proteomes:UP000014974};
RX PubMed=23950138;
RA Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT from Arctic Marine Sediment.";
RL Genome Announc. 1:e00642-13(2013).
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:EPR66141.1}.
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DR EMBL; ATNM01000156; EPR66141.1; -; Genomic_DNA.
DR RefSeq; WP_020889953.1; NZ_ATNM01000156.1.
DR AlphaFoldDB; S7V8A6; -.
DR STRING; 641524.ADICYQ_4839; -.
DR PATRIC; fig|641524.5.peg.4796; -.
DR eggNOG; COG0144; Bacteria.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000014974; 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: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; IPR031341; Methyltr_RsmF_N.
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 Pfam; PF17125; Methyltr_RsmF_N; 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 134..395
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 346
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 396 AA; 45113 MW; 6E0AB89DDB559826 CRC64;
MKLFPNTVNA VVKALEEIFD NNRYADKVIE KVLRSNPKWG ARDRAFIAES VYEIVRWKRL
IEKLSPSHDY YLWFGTYWVL QDRTLPDWRE FKGINGEKIR LHRRKITDRA VLQSIPDWME
EMGSSQLGEK WDAELNSLNE QAQVVLRANT LKTARTDLKI KLEELEVSAY IPREYPDALV
LLKRKNVFRT PLFKEGLFEV QDASSQMVAA ALEVEPGMRV IDACAGAGGK SLHLAALMQN
KGRILAMDTE AWKLQNAKLR ARRAGISILE IKPIESNKTI KRLHESADRL LLDVPCSGLG
VLKRNPDTKW KLSEESIAKV QVLQKEILSQ YPSMLKPGGI MVYATCSILP SENHMQVAAF
LESAEGQKFE LLEETQVLSH ESGFDGFYIA KLKKKG
//