Entry bact:Q5NF64_FRATT

ID   Q5NF64_FRATT            Unreviewed;       426 AA.
AC   Q5NF64;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   10-MAY-2017, entry version 84.
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:CAG46016.1};
GN   OrderedLocusNames=FTT_1383 {ECO:0000313|EMBL:CAG46016.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG46016.1, ECO:0000313|Proteomes:UP000001174};
RN   [1] {ECO:0000313|EMBL:CAG46016.1, ECO:0000313|Proteomes:UP000001174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M.,
RA   Fuxelius H.H., Garcia E., Halltorp G., Johansson D., Isherwood K.,
RA   Karp P., Larsson E., Lui Y., Michell S., Prior J., Prior R.,
RA   Sjostedt A., Svensson K., Thompson N., Vergez L., Wagg J., Wren B.,
RA   Lindler L.E., Andersson S.G., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(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; AJ749949; CAG46016.1; -; Genomic_DNA.
DR   RefSeq; WP_003029619.1; NZ_CP010290.1.
DR   RefSeq; YP_170328.1; NC_006570.2.
DR   STRING; 177416.FTT_1383; -.
DR   EnsemblBacteria; AJI69410; AJI69410; BZ14_1397.
DR   EnsemblBacteria; CAG46016; CAG46016; FTT_1383.
DR   GeneID; 3190743; -.
DR   KEGG; ftu:FTT_1383; -.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; NDCLIAN; -.
DR   Proteomes; UP000001174; 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:UP000001174};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00633812};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811925, ECO:0000313|EMBL:CAG46016.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001174};
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:CAG46016.1}.
FT   ACT_SITE    365    365       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     268    268       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     296    296       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         1    121       ipfam:NusB [T]
FT   MYHIT       157    423       iprf:SAM_MT_RSMB_NOP [T]
FT   MYHIT       233    421       ipfam:Methyltr_RsmB-F [T]
SQ   SEQUENCE   426 AA;  49000 MW;  6B46E9146EFDBA1A CRC64;
     MNTRAIAAKT ILDILDNKYS LLTIGQKLVK LNLLEQDKSF IKLLCYEFFR HYYSLEKIIA
     LYLTQKTKVK AKVLIMLGAL QIFEIKQPYY ATINETVAAC KVLKIIWAKK LVNRILREMT
     RNIEYITSIY TQNKAIDMPE WLCDTLKKQY PNDHLVIAQA INAKADMFIR LNQNKDNKKV
     LDYFDKNNIG YSFTNLKDCI KLDQAIDVKY NQLFQQGYFT IQDISAQYAG HIIKAANNDK
     ILDACAAPGG KTSHILECAP QADITAIDII DKRLELLREN LERLSENHNV NVFKHDLTLP
     LAGKFNKIIL DAPCSALGTI RRNPDIKVLR TPNDIQAIKS LQSKILANLW NNNLTDNGYL
     LYITCSILAE ENQQQIKEFL AKNNNAEIIE IDILEKYKTS YGYQLLPSQQ DGDGFYYCLL
     KKNPYF
//