ID A0A1N6VH16_9GAMM Unreviewed; 477 AA.
AC A0A1N6VH16;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=rsmF {ECO:0000256|HAMAP-Rule:MF_01579};
GN ORFNames=SAMN05880558_105195 {ECO:0000313|EMBL:SIQ77190.1};
OS Aeromonas sp. RU39B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1907416 {ECO:0000313|EMBL:SIQ77190.1, ECO:0000313|Proteomes:UP000186911};
RN [1] {ECO:0000313|EMBL:SIQ77190.1, ECO:0000313|Proteomes:UP000186911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU39B {ECO:0000313|EMBL:SIQ77190.1,
RC ECO:0000313|Proteomes:UP000186911};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FTMJ01000005; SIQ77190.1; -; Genomic_DNA.
DR RefSeq; WP_076575547.1; NZ_FTMJ01000005.1.
DR AlphaFoldDB; A0A1N6VH16; -.
DR STRING; 1907416.SAMN05880558_105195; -.
DR InParanoid; A0A1N6VH16; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000186911; 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};
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 28..312
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 248
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01579,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 126..132
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 150
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 177
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 195
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 477 AA; 52893 MW; 4F59557C64A0493D CRC64;
MHQNSYIPDA FLAHIAGILP SHLSLDEFVA CCRRPLRRSI RVNTLKITVA AFIERMQARG
WQLDPVPWCD TGFWLTRPAD DTVPLGNTAE HLAGLFYIQE ASSMMPVTAL FAANGIEQAE
MVLDGAAAPG SKTTQMAALM GNRGMLIANE FSASRIKGLF SNIQRCGVTN VALTHFDARV
FGQWLPETFD AILLDAPCSG EGTIRKDEDA LRNWSIASIN EIAATQKALL ESAFHALKPG
GVMVYSTCTL SHQENQDVCA FLRERFGDAL SVEPLGDLFP GASESCTPEG YLHIWPQIYD
SEGFFVARLR KHTSVPNTMF KPGKLGKFPF TPLAARDAEL LRHDITTQFG VTMAGELYGR
EGEIWLFPTP LSQVMGKIRF DRIGIKLAET FKKGYRLTHE WALAFGDRAN RQVVELDVAL
AREFMMGRDV RPDAESGQGE VVVRYQGYTL GIGKWVGNRI KNSLPRDLVR DGNLFES
//
