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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 synonymsQ2S463_SALRD , Q2S463 , 5245A3AFB8AF4A6A
match map segment
iprf:SAM_MT_RSMB_NOP ipfam:NusB 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   Q2S463_SALRD            Unreviewed;       427 AA.
AC   Q2S463;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   10-MAY-2017, entry version 90.
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:ABC44814.1};
GN   OrderedLocusNames=SRU_0884 {ECO:0000313|EMBL:ABC44814.1};
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44814.1, ECO:0000313|Proteomes:UP000008674};
RN   [1] {ECO:0000313|EMBL:ABC44814.1, ECO:0000313|Proteomes:UP000008674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / M31 {ECO:0000313|Proteomes:UP000008674};
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J.,
RA   Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G.,
RA   Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F.,
RA   Charlebois R.L., Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC44814.1; -; Genomic_DNA.
DR   RefSeq; WP_011403646.1; NC_007677.1.
DR   RefSeq; YP_445018.1; NC_007677.1.
DR   ProteinModelPortal; Q2S463; -.
DR   STRING; 309807.SRU_0884; -.
DR   EnsemblBacteria; ABC44814; ABC44814; SRU_0884.
DR   GeneID; 3852136; -.
DR   KEGG; sru:SRU_0884; -.
DR   PATRIC; 23424133; VBISalRub86502_0913.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; HIGLYQL; -.
DR   OrthoDB; POG091H02E2; -.
DR   Proteomes; UP000008674; 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:UP000008674};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00633812};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811925, ECO:0000313|EMBL:ABC44814.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008674};
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:ABC44814.1}.
FT   DOMAIN      150    425       SAM_MT_RSMB_NOP.
FT                                {ECO:0000259|PROSITE:PS51686}.
FT   ACT_SITE    364    364       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     264    264       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     292    292       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     311    311       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       150    425       iprf:SAM_MT_RSMB_NOP [T]
FT   MYHIT        11    106       ipfam:NusB [T]
FT   MYHIT       226    423       ipfam:Methyltr_RsmB-F [T]
SQ   SEQUENCE   427 AA;  47812 MW;  5245A3AFB8AF4A6A CRC64;
     MRTDDAFVDK LTIEDADART RRQARELVAG VTRQRRWLDF VLGEAYHGDY DSMEHRLQEI
     LRLGLYELLF QSTPTHAAVD EYVELAKQAL RPGAGNLVNG VLRTIDRDRE HIPTPDTGDD
     ANDLALRYSH PTWMVQRWLD RFGLDETTEL LRANNRRPMY SVRINPLRTS EADVAAWLDE
     HDVVNVDSPY LDRYLRLKRL QALIAGDLLD DGHVAVQDES AGLVVQLLDP QPGETLIDGC
     AAPGGKAMHA AARMEGTGTI YAVDRDEQRL ERVETAAEAQ GASEMVEAET ADLRAWAARP
     EPPQGDRVLL DVPCTGMGVL AKRAGLRWRR SMEDLEEMAE LQDELLDAAA QLVRPGGLLV
     YSTCTTEPEE NERRVEAFLA RHDGFAVESA EGHVPDEMVS DAGFLATFPH RHRMDGAFAA
     RLRRDEA
//