ID S3DGC0_9GAMM Unreviewed; 425 AA.
AC S3DGC0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=16S rRNA (cytosine(967)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00012140};
DE EC=2.1.1.176 {ECO:0000256|ARBA:ARBA00012140};
DE AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000256|ARBA:ARBA00030399};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000256|ARBA:ARBA00031088};
GN ORFNames=O1U_0786 {ECO:0000313|EMBL:EPE37482.1};
OS Candidatus Photodesmus katoptron Akat1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photodesmus.
OX NCBI_TaxID=1236703 {ECO:0000313|EMBL:EPE37482.1, ECO:0000313|Proteomes:UP000053688};
RN [1] {ECO:0000313|EMBL:EPE37482.1, ECO:0000313|Proteomes:UP000053688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Akat1 {ECO:0000313|EMBL:EPE37482.1,
RC ECO:0000313|Proteomes:UP000053688};
RX PubMed=24118864; DOI=10.1111/1462-2920.12302;
RA Hendry T.A., de Wet J.R., Dunlap P.V.;
RT "Genomic signatures of obligate host dependence in the luminous bacterial
RT symbiont of a vertebrate.";
RL Environ. Microbiol. 16:2611-2622(2014).
CC -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC of 16S rRNA. {ECO:0000256|ARBA:ARBA00002724}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42748, Rhea:RHEA-COMP:10219, Rhea:RHEA-COMP:10220,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.176;
CC Evidence={ECO:0000256|ARBA:ARBA00000588};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {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:EPE37482.1}.
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DR EMBL; AMSD01000002; EPE37482.1; -; Genomic_DNA.
DR RefSeq; WP_016504114.1; NZ_AMSD01000002.1.
DR AlphaFoldDB; S3DGC0; -.
DR STRING; 28176.CF66_3034; -.
DR PATRIC; fig|1236703.3.peg.814; -.
DR eggNOG; COG0144; Bacteria.
DR eggNOG; COG0781; Bacteria.
DR Proteomes; UP000053688; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.287.730; Helix hairpin bin; 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; IPR004573; rRNA_ssu_MeTfrase_B.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00563; rsmB; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000053688};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..425
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 252..258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 275
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"
FT BINDING 320
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 425 AA; 49130 MW; BA3029DAD52D24DC CRC64;
MNVRVLATRI LFQVLNKGNS FTRTLNVAKN NIKPKDEAFL KELCYGVFRY LLRLELIANY
LIHYPFKKTD KQIFYYLILV GIYQLSFMRI PWHAAVYETV KSSKILGAKN LSRLINAILR
NYLRNKDKLD EMAITEHSGK YNHPNWILDK LKKNYPKEWQ FIVEANNKKA PMWLRVNRQY
HTRNEYLNLL DDLGIQYTIH SIADNAIKLA SACKVDILPG FKKGWISVQD ASAQLSVNYL
KPKENELILD CCAAPGGKTT HILEYTNTAK VVALDINPTR LNNLHNNLER LKLKANVICG
DARYPKKWWK GDKFDKILLD VPCSSTGVIR RHPDIKWLRN SNDIDTLSEL QSEIIDAMWQ
ELKSDGIMVY STCSVIPEEN KLQIKSFLER TKNAILIGSK TDHPGYQILP GDEDMDGFYY
AVVKK
//
