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Database: UniProt
Entry: V5HMC0_9VIBR
LinkDB: V5HMC0_9VIBR
Original site: V5HMC0_9VIBR 
ID   V5HMC0_9VIBR            Unreviewed;       476 AA.
AC   V5HMC0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
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   ECO:0000313|EMBL:GAD90345.1};
GN   ORFNames=VHA01S_040_00250 {ECO:0000313|EMBL:GAD90345.1};
OS   Vibrio halioticoli NBRC 102217.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1219072 {ECO:0000313|EMBL:GAD90345.1, ECO:0000313|Proteomes:UP000017800};
RN   [1] {ECO:0000313|EMBL:GAD90345.1, ECO:0000313|Proteomes:UP000017800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102217 {ECO:0000313|EMBL:GAD90345.1,
RC   ECO:0000313|Proteomes:UP000017800};
RA   Ichikawa N., Kimura A., Ohji S., Hosoyama A., Fujita N.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAD90345.1, ECO:0000313|Proteomes:UP000017800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102217 {ECO:0000313|EMBL:GAD90345.1,
RC   ECO:0000313|Proteomes:UP000017800};
RA   Isaki S., Kimura A., Ohji S., Hosoyama A., Fujita N., Hashimoto M.,
RA   Hosoyama Y., Yamazoe A.;
RT   "Whole genome shotgun sequence of Vibrio halioticoli NBRC 102217.";
RL   Submitted (NOV-2013) 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}.
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:GAD90345.1}.
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DR   EMBL; BAUJ01000040; GAD90345.1; -; Genomic_DNA.
DR   RefSeq; WP_023404688.1; NZ_BAUJ01000040.1.
DR   AlphaFoldDB; V5HMC0; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG3270; Bacteria.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000017800; 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   476 AA;  53480 MW;  77FEB39FF9C8AE63 CRC64;
     MHQNVYIPDE FIELIAQQMP SHLKLDELLE ACRRPLKRSI RVNTLKISVE EFKQQATEMG
     WTLTPIPWCA EGFWLDDVDE SSTSLGNTSQ HLAGLFYIQE ASSMMPVTAL FEQLDVNDEF
     RVLDMAAAPG SKTTQIASHI GKDGLVIANE FSASRVKILF GNLMRCGVGN MAMTNFDARV
     FGSWLPETFD AILLDAPCSG EGSLRKDADA MKNWSLSSVE EIASTQKDLI ESAFHALKPN
     GTLVYSTCTL NLQENQQVVQ HLLDTFADCI EVEPLQQLFD GAELSATEEG YLHVYPQVYD
     CEGFFIARFK KTASVTAPAV KKRLGKFPFQ LLSAKECDAV TKSLSTTLGI TIPSSFSLWQ
     RDNEVWLFPK LIEPLLGQMR FQRIGIKLAE AHKKGYRWQH QGVVAMSEHN ETNAIDLTLE
     EAREWYMGRD IRPLQSAGKG EILVRYDNVT IGLGKWVGNR VKNGLPREMV RDNNLF
//
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