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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 synonymsD8GRX4_CLOLD , D8GRX4 , 157FCAB09D07F64A
match map segment
ipfam:NusB ipfam:Methyltr_RsmB-F iprf:SAM_MT_RSMB_NOP  
Legends: 1, ACT_SITE Nucleophile. {ECO:0000256|PROSITE- ProRule:PRU01023}; 2, BINDING S-adenosyl-L-methionine. {ECO:0000256|PROSITE-ProRule:PRU01023}. 
ID   D8GRX4_CLOLD            Unreviewed;       443 AA.
AC   D8GRX4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   10-MAY-2017, entry version 44.
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   Name=sun {ECO:0000313|EMBL:ADK14327.1};
GN   OrderedLocusNames=CLJU_c12590 {ECO:0000313|EMBL:ADK14327.1};
OS   Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK14327.1, ECO:0000313|Proteomes:UP000001656};
RN   [1] {ECO:0000313|EMBL:ADK14327.1, ECO:0000313|Proteomes:UP000001656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55383 / DSM 13528 / PETC
RC   {ECO:0000313|Proteomes:UP000001656};
RX   PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA   Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA   Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT   "Clostridium ljungdahlii represents a microbial production platform
RT   based on syngas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
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; CP001666; ADK14327.1; -; Genomic_DNA.
DR   RefSeq; WP_013237924.1; NZ_LITS01000006.1.
DR   STRING; 748727.CLJU_c12590; -.
DR   EnsemblBacteria; ADK14327; ADK14327; CLJU_c12590.
DR   KEGG; clj:CLJU_c12590; -.
DR   PATRIC; 42483714; VBICloLju82977_1228.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; HIGLYQL; -.
DR   OrthoDB; POG091H02E2; -.
DR   Proteomes; UP000001656; 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:UP000001656};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00633812};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811925, ECO:0000313|EMBL:ADK14327.1};
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:ADK14327.1}.
FT   ACT_SITE    381    381       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     283    283       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     310    310       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     328    328       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         4    126       ipfam:NusB [T]
FT   MYHIT       245    439       ipfam:Methyltr_RsmB-F [T]
FT   MYHIT       169    442       iprf:SAM_MT_RSMB_NOP [T]
SQ   SEQUENCE   443 AA;  51029 MW;  157FCAB09D07F64A CRC64;
     MNGARSTAVE ILNEVLGSNA YSNKVLNTYL NKNNLNKKDK ALVTEIVYGT LKYMYTIDTI
     LDDFIKSSLK KMNIDIVNIL RISIYQLRYL DKIPEFAVVN EAVELSKKKS KGLSKLVNGV
     LRNYLRNKDN LHCEHKDNKI DNLCFKYSFP RWMTLLFIHQ YGEAVGESIL QSLNYIPKVT
     VRVNGLKIDY KSVWDELLKN GYDIQKGKIC KEAVVINRGS NIEENPLFKK GYITVQDESA
     MLVAHIVDPE ENMTVLDMCS APGGKSCHMA ELMKNTGVIY AYDLHENKLR FVEENANRMD
     IKNIKCNKLD AEKYVEQFEA TADRVLIDVP CSGLGIVRKK PEIKWNKSMK SLNSLINVQR
     KIMLNASRYV KDGGKLIYST CTLNKSENED NINWFIRENP QYKLEKIYCG DFDNIIYHKE
     GYITILPDDN MDGFFIAKMI KHR
//