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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 synonymsQ31PM7_SYNE7 , Q31PM7 , 8EE76347DF9C2F7D
match map segment
ipfam:NusB iprf:SAM_MT_RSMB_NOP ipfam:Methyltr_RsmB-F  
Legends: 1, ACT_SITE Nucleophile. {ECO:0000256|PROSITE- ProRule:PRU01023}; 2, BINDING S-adenosyl-L-methionine. {ECO:0000256|PROSITE-ProRule:PRU01023}. 
ID   Q31PM7_SYNE7            Unreviewed;       451 AA.
AC   Q31PM7;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   10-MAY-2017, entry version 81.
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=Synpcc7942_0962 {ECO:0000313|EMBL:ABB56992.1};
OS   Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB56992.1, ECO:0000313|Proteomes:UP000002717};
RN   [1] {ECO:0000313|Proteomes:UP000002717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 {ECO:0000313|Proteomes:UP000002717};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC
RT   7942.";
RL   Submitted (AUG-2005) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; CP000100; ABB56992.1; -; Genomic_DNA.
DR   RefSeq; WP_011377807.1; NC_007604.1.
DR   ProteinModelPortal; Q31PM7; -.
DR   STRING; 1140.Synpcc7942_0962; -.
DR   PRIDE; Q31PM7; -.
DR   EnsemblBacteria; ABB56992; ABB56992; Synpcc7942_0962.
DR   KEGG; syf:Synpcc7942_0962; -.
DR   PATRIC; 23787163; VBISynElo51371_1112.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OrthoDB; POG091H02E2; -.
DR   BioCyc; SYNEL:SYNPCC7942_0962-MONOMER; -.
DR   Proteomes; UP000002717; 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:UP000002717};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00633812};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811925};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002717};
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}.
FT   DOMAIN      175    447       SAM_MT_RSMB_NOP.
FT                                {ECO:0000259|PROSITE:PS51686}.
FT   ACT_SITE    385    385       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     290    290       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     332    332       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         8    131       ipfam:NusB [T]
FT   MYHIT       175    447       iprf:SAM_MT_RSMB_NOP [T]
FT   MYHIT       253    445       ipfam:Methyltr_RsmB-F [T]
SQ   SEQUENCE   451 AA;  49824 MW;  8EE76347DF9C2F7D CRC64;
     MPRPSRGNAR WVAFQTLTTI REGAFADLAL DRHLQRSGLV GADRRLVTEL VYGCVRRQRT
     LDALIDLLAQ RPAAQQPPVL RTVLQLGLYQ LRYLEQIPTA AAVAETVQLA KQLGLGGLSG
     AVNAILRQYL RQSEERDPLP LPSDPIAALA IHQSFPDWLV QLWSDRLGLD EAEFLCHWFN
     QPPSIDLRIN PLRTERSQVQ AALEAVGIRS TPDPQLPQAL RLIDPPGPIR QLPGFDEGWW
     MVQDSSAQLI AHLVDPQPGE TVLDVCAAPG GKSTHLAELM GDRGQVIACD SSAKRLRKVQ
     ENAQRLQLSS ITTRAIDGRQ IKGIQADRIL VDAPCSGLGT LHRHADGRWR QSPDSVAELA
     QLQSEILDAA AACLKPAGTL VYATCTLHPA ENEAVIEQFL QRHPDWQMAP LAADSPFQAW
     AEANGTLRIW PHRHDRDGFF GARLQRSPAR D
//