ID A0A0F4NI25_9VIBR Unreviewed; 459 AA.
AC A0A0F4NI25;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase F {ECO:0000256|HAMAP-Rule:MF_01579};
DE EC=2.1.1.178 {ECO:0000256|HAMAP-Rule:MF_01579};
DE AltName: Full=16S rRNA m5C1407 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01579};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmF {ECO:0000256|HAMAP-Rule:MF_01579};
GN Name=yebU {ECO:0000313|EMBL:KJY82468.1};
GN Synonyms=rsmF {ECO:0000256|HAMAP-Rule:MF_01579};
GN ORFNames=TW81_13635 {ECO:0000313|EMBL:KJY82468.1};
OS Vibrio galatheae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579748 {ECO:0000313|EMBL:KJY82468.1, ECO:0000313|Proteomes:UP000033673};
RN [1] {ECO:0000313|EMBL:KJY82468.1, ECO:0000313|Proteomes:UP000033673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2757 {ECO:0000313|EMBL:KJY82468.1,
RC ECO:0000313|Proteomes:UP000033673};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
CC -!- FUNCTION: Specifically methylates the cytosine at position 1407
CC (m5C1407) of 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_01579}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1407) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(1407) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42756, Rhea:RHEA-COMP:10223, Rhea:RHEA-COMP:10224,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.178;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01579};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01579}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC ECO:0000256|HAMAP-Rule:MF_01579, 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:KJY82468.1}.
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DR EMBL; JXXV01000024; KJY82468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4NI25; -.
DR STRING; 579748.TW81_13635; -.
DR PATRIC; fig|579748.3.peg.2820; -.
DR Proteomes; UP000033673; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.10.450.720; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01579; 16SrRNA_methyltr_F; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023545; rRNA_ssu_MeTfrase_F.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR048457; YebU_pre-PUA_dom.
DR NCBIfam; TIGR00446; nop2p; 1.
DR PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR Pfam; PF13636; Methyltranf_PUA; 1.
DR Pfam; PF21150; YebU_pre-PUA_dom; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01579};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01579}; Reference proteome {ECO:0000313|Proteomes:UP000033673};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01579}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_01579};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01579};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01579}.
FT DOMAIN 14..295
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 231
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01579,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 109..115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01579,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01579,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01579,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01579,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 459 AA; 51064 MW; 7C2E0E1CE0C75A5A CRC64;
MRSILPQQLN MEDFIAACQR PLRKSLRVNT LKISVADFIE RAKDKGWQLE PVPWCKTGFW
IEADESVVPL GNTAEHMSGL FYIQEASSMM PVSALFAQNS QFTSVLDMAA APGSKTTQIA
AEMNNHGVLV ANEFSASRVK VLHANVERCG VRNAALSNYD GRVFGGWLPE QFDAVLIDAP
CSGEGTVRKD ADAMKNWSKA SVLSISDTQK DLIESAFHAL KPGGVMVYST CTLSIEENQQ
VCHHLKQVFA DQVEFESLTD LFPHADKALT AEGFLHIFPQ VYDCEGFFVA RIRKLGSVDA
PKVKKRLGKF PFEKASAKLQ ADIQSQLKAA LDIDFPQDTS VWLRDKDVWL FPNALEPMLG
EFRFSRMGIK IAETHKKGYR WQHQVATTLA TGNEATAVVL SVDDAREWFM GRDVRPENVT
GSGEVIVKLA NDVIGLGKWV GNRIKNGLPR ELVRDKNLF
//
