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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=16S rRNA (cytosine(967)-C(5))-methyltransferase {ECO:0000256|SAAS:SAAS00672440}; EC=2.1.1.176 {ECO:0000256|SAAS:SAAS00672440};
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MyHits synonymsQ6F1S0_MESFL , Q6F1S0 , 6A676F6D5D3EF1CE
match map segment
ipfam:Methyltr_RsmB-F iprf:SAM_MT_RSMB_NOP ipfam:NusB  
Legends: 1, ACT_SITE Nucleophile. {ECO:0000256|PROSITE- ProRule:PRU01023}; 2, BINDING S-adenosyl-L-methionine. {ECO:0000256|PROSITE-ProRule:PRU01023}. 
ID   Q6F1S0_MESFL            Unreviewed;       425 AA.
AC   Q6F1S0;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   10-MAY-2017, entry version 89.
DE   RecName: Full=16S rRNA (cytosine(967)-C(5))-methyltransferase {ECO:0000256|SAAS:SAAS00672440};
DE            EC=2.1.1.176 {ECO:0000256|SAAS:SAAS00672440};
GN   OrderedLocusNames=Mfl196 {ECO:0000313|EMBL:AAT75553.1};
OS   Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS   (Acholeplasma florum).
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales;
OC   Entomoplasmataceae; Mesoplasma.
OX   NCBI_TaxID=265311 {ECO:0000313|EMBL:AAT75553.1, ECO:0000313|Proteomes:UP000006647};
RN   [1] {ECO:0000313|EMBL:AAT75553.1, ECO:0000313|Proteomes:UP000006647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1
RC   {ECO:0000313|Proteomes:UP000006647};
RA   Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA   Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R.,
RA   Nusbaum C.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967
CC       (m5C967) of 16S rRNA. {ECO:0000256|SAAS:SAAS00672432}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(967) in 16S
CC       rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(967) in 16S
CC       rRNA. {ECO:0000256|SAAS:SAAS00672435}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00633808}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01023,
CC       ECO:0000256|SAAS:SAAS00811926}.
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DR   EMBL; AE017263; AAT75553.1; -; Genomic_DNA.
DR   RefSeq; WP_011183093.1; NC_006055.1.
DR   RefSeq; YP_053437.1; NC_006055.1.
DR   ProteinModelPortal; Q6F1S0; -.
DR   STRING; 265311.Mfl196; -.
DR   EnsemblBacteria; AAT75553; AAT75553; Mfl196.
DR   GeneID; 2898042; -.
DR   KEGG; mfl:Mfl196; -.
DR   PATRIC; 22473119; VBIMesFlo3168_0197.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; NDCLIAN; -.
DR   OrthoDB; POG091H02E2; -.
DR   Proteomes; UP000006647; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.940.10; -; 1.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; SSF48013; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00563; rsmB; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006647};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00633812};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811925, ECO:0000313|EMBL:AAT75553.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006647};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811931};
KW   rRNA processing {ECO:0000256|SAAS:SAAS00633795};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811929};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811925, ECO:0000313|EMBL:AAT75553.1}.
FT   DOMAIN      156    425       SAM_MT_RSMB_NOP.
FT                                {ECO:0000259|PROSITE:PS51686}.
FT   ACT_SITE    378    378       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     281    281       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     308    308       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     324    324       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       244    404       ipfam:Methyltr_RsmB-F [T]
FT   MYHIT       156    425       iprf:SAM_MT_RSMB_NOP [T]
FT   MYHIT         8    128       ipfam:NusB [T]
SQ   SEQUENCE   425 AA;  48553 MW;  6A676F6D5D3EF1CE CRC64;
     MILVETNNSR KIAFEILKKV FKNKSFSNIL LNDVSKMPIS DKFKNLIFAI VHGTITNQIL
     LDHVSRKLID VKKTNIDIQI LLWMSIYQLR FLKTIPQYAV VNESVMIAKS VNHKFSGLLN
     ACLKKVIKNE EELFDFSFKS ENQKICIENS FPKNLFNLIE KGYGKDIAKK VAIDSNQKPV
     ISFRVNTLKI SENDFFEKYK DEYELEKTEI KNCLISKKAI VKSDAYTSGQ ITIQDPASIL
     VGNVLNPTKG SKVLDMCSAP GGKLTHLSMI MENTGQVTGF EISENKIKLI EENIKRLDCK
     NISLKCGDAT LINEKENFDF ILLDAPCSGF GVLKRKPEIK INNIEINNIN NIVNIQEKLL
     DTAYYNLKQQ GVMVYSTCTI NPAENQNQIK KFIEKYKDIK IISENQLFGY EMNTDGFYIC
     KMIKE
//