ID E5B682_ERWAM Unreviewed; 478 AA.
AC E5B682;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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:CBX80902.1};
GN Synonyms=rsmF {ECO:0000256|HAMAP-Rule:MF_01579};
GN ORFNames=EAIL5_2082 {ECO:0000313|EMBL:CBX80902.1};
OS Erwinia amylovora ATCC BAA-2158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX80902.1};
RN [1] {ECO:0000313|EMBL:CBX80902.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX80902.1};
RA Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E.,
RA Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.;
RT "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity
RT Restricted to Rubus Plants.";
RL J. Bacteriol. 193:785-786(2011).
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; FR719191; CBX80902.1; -; Genomic_DNA.
DR AlphaFoldDB; E5B682; -.
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; 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};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW 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 30..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 478 AA; 53309 MW; BC9624367B34897D CRC64;
MPHISRVFFP PAFLEQMQQL LPDANDFARF IAISQQPLRR SLRVNTLKIS VDDFLQLVKP
YQWALTPIPW CPEGFWISRD DADKLPLGST AEHLAGLFYI QEASSMLPVS ALFAGGNMPQ
RVMDMAAAPG SKTTQIAACM GDRGAILANE YSASRVKVLH ANLSRCGISN TAMTHFDGRV
FGSALPECFD AVLLDAPCSG EGVVRKDADA LRNWSATSTA EIAATQRDLI NSAFHALRPG
GTLVYSTCTL NRSENQQVVR WLLEQYPDAV AIEPLNTLFN GAEQVATAEG FLHVFPHIFD
SEGFFVARLR KVSSVARLSQ PTYKVGKPPF SPLSRQQQQE VSDAAAKVGL RWKTELKLWQ
RDKEIWLFPA GIEPLLGRVR FSRIGLKLAE TFTKGYRWQH HAAVALADAR SENAFEVNSH
EAEEWYRGRD IYPDRSLPGD ELIICHQKQP IGIAKKVGSR IKNNYPRELV RDGKLFSV
//
