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Database: UniProt
Entry: U1JS69_9GAMM
LinkDB: U1JS69_9GAMM
Original site: U1JS69_9GAMM 
ID   U1JS69_9GAMM            Unreviewed;       521 AA.
AC   U1JS69;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
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:ERG19842.1};
GN   Synonyms=rsmF {ECO:0000256|HAMAP-Rule:MF_01579};
GN   ORFNames=PCIT_04295 {ECO:0000313|EMBL:ERG19842.1};
OS   Pseudoalteromonas citrea DSM 8771.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1117314 {ECO:0000313|EMBL:ERG19842.1, ECO:0000313|Proteomes:UP000016487};
RN   [1] {ECO:0000313|EMBL:ERG19842.1, ECO:0000313|Proteomes:UP000016487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8771 {ECO:0000313|Proteomes:UP000016487};
RX   PubMed=22535931; DOI=10.1128/JB.00265-12;
RA   Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA   He H.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of type strains of seven species of the marine bacterium
RT   Pseudoalteromonas.";
RL   J. Bacteriol. 194:2746-2747(2012).
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|HAMAP-Rule:MF_01579,
CC       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:ERG19842.1}.
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DR   EMBL; AHBZ02000047; ERG19842.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1JS69; -.
DR   STRING; 1117314.PCIT_04295; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG3270; Bacteria.
DR   Proteomes; UP000016487; 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   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; 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; 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:UP000016487};
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          68..352
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        288
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01579,
FT                   ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         166..172
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         190
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         217
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         235
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   521 AA;  58368 MW;  1C64979FC85ED93C CRC64;
     MSREDWSIQY DNLNFENPLS HYHAVLKLPH FNQTCNTERH LDSKTYIPEA FIDDVKTYLP
     THLTLDDFLQ ACKSPLRRSV RVNTLKMSVS DFKSYCAAHD WSIEPVPWCD SGFWLTRSET
     EEHSLPIGNT ELHLSGCIYV QEASSMLPPV ALKHAIEDSD TVLDMASAPG SKTSQLSAMM
     DNKGVLIANE LSSSRLKVLA ANMKRMGIAN CALSHFDAAI FGDYMYECFD SILLDAPCSG
     EGTVRKDADA LKNWSIESNI DIADVQKKLI RSAFMALKPG GTLVYSTCTL TPLENQQVCD
     ELLNAFPDAI KTDDLSSLFP DATRATTEEG YLHVWPQIYD SEGFFIARFI KTASVENTAQ
     KTKKGSFPFA VSEKKLQQQF FDLAKKQFGI EQTTISGQLM SRDKELWLFP DGFHNVENKI
     KYSRMGIQVG TTHKNGIRLE HEFATALGQL ACKNNYAMSQ NEAKDYFNGK DIRLDCAVNV
     TGEVILTLCG APVGLGKWQK QKIKNSLPRD LVSDSQLITW V
//
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