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Database: UniProt
Entry: K2IQ08_9GAMM
LinkDB: K2IQ08_9GAMM
Original site: K2IQ08_9GAMM 
ID   K2IQ08_9GAMM            Unreviewed;       473 AA.
AC   K2IQ08;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
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:EKE72201.1};
GN   Synonyms=rsmF {ECO:0000256|HAMAP-Rule:MF_01579};
GN   ORFNames=B3C1_11534 {ECO:0000313|EMBL:EKE72201.1};
OS   Gallaecimonas xiamenensis 3-C-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Gallaecimonas.
OX   NCBI_TaxID=745411 {ECO:0000313|EMBL:EKE72201.1, ECO:0000313|Proteomes:UP000006755};
RN   [1] {ECO:0000313|EMBL:EKE72201.1, ECO:0000313|Proteomes:UP000006755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-C-1 {ECO:0000313|EMBL:EKE72201.1,
RC   ECO:0000313|Proteomes:UP000006755};
RX   PubMed=23209203; DOI=10.1128/JB.01854-12;
RA   Lai Q., Wang L., Wang W., Shao Z.;
RT   "Genome Sequence of Gallaecimonas xiamenensis Type Strain 3-C-1.";
RL   J. Bacteriol. 194:6937-6937(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:EKE72201.1}.
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DR   EMBL; AMRI01000015; EKE72201.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2IQ08; -.
DR   STRING; 745411.B3C1_11534; -.
DR   PATRIC; fig|745411.4.peg.2269; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG3270; Bacteria.
DR   Proteomes; UP000006755; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR009056; Cyt_c-like_dom.
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; PS51007; CYTC; 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   Heme {ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01579}; Reference proteome {ECO:0000313|Proteomes:UP000006755};
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          30..312
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   DOMAIN          148..266
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
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   473 AA;  52065 MW;  66E5A246C6C7D8CC CRC64;
     MSVHTKVYLP DAFLSAMDAI MPASLSRDDF VAACQRPLRR AIRVNTLKIS VADFAEQMAQ
     KGWQLETIPW CDTGFWLQRP DEDLPLGNEP EHLLGLFYVQ EASSMLPPQA LWHCLSEAPA
     KVLDVAAAPG SKTTQLAALM NNQGLLVANE YSGSRVKVLH ANLQRLGVSN CALCHFDGKV
     FGPALPDTFD AILLDAPCGG EGTIRKDPDA LKDWAQSHID AISEVQQGLI ESAFQALKVG
     GVLVYSTCTL NTQENQGVLA FLAARFGEAV ERVSLEGLFD GAEQALTEQG ELHIWPQIYD
     SEGFFVAAVR KLAKVDVPEP SFRLGKFPYT PAKGKDTQAF IQYLKDQFGF DAKLLNLWQR
     DGDFWHFPEE ANDLIGRVRL DRIGIKVAEP AGKEWKLHQD FVLAFGSQCR PLELDSAQAA
     DYLTGKDLAV DGLAAGGERV LSYQGHPIGT AKALKNKLKN RFPRELVKDK LAF
//
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