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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 synonymsQ7TVA8_PROMA , Q7TVA8 , F319AF12173B6F59
match map segment
iprf:SAM_MT_RSMB_NOP ipfam:Methyltr_RsmB-F ipfam:NusB  
Legends: 1, ACT_SITE Nucleophile. {ECO:0000256|PROSITE- ProRule:PRU01023}; 2, BINDING S-adenosyl-L-methionine. {ECO:0000256|PROSITE-ProRule:PRU01023}. 
ID   Q7TVA8_PROMA            Unreviewed;       438 AA.
AC   Q7TVA8;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   10-MAY-2017, entry version 95.
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:AAP99468.1};
GN   OrderedLocusNames=Pro_0422 {ECO:0000313|EMBL:AAP99468.1};
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539 {ECO:0000313|EMBL:AAP99468.1, ECO:0000313|Proteomes:UP000001420};
RN   [1] {ECO:0000313|EMBL:AAP99468.1, ECO:0000313|Proteomes:UP000001420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120 {ECO:0000313|Proteomes:UP000001420};
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F.,
RA   Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B.,
RA   Scanlan D.J., Tandeau de Marsac N., Weissenbach J., Wincker P.,
RA   Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120,
RT   a nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAP99468.1; -; Genomic_DNA.
DR   RefSeq; NP_874816.1; NC_005042.1.
DR   RefSeq; WP_011124577.1; NC_005042.1.
DR   ProteinModelPortal; Q7TVA8; -.
DR   STRING; 167539.Pro0422; -.
DR   EnsemblBacteria; AAP99468; AAP99468; Pro_0422.
DR   GeneID; 1461804; -.
DR   KEGG; pma:Pro_0422; -.
DR   PATRIC; 23027463; VBIProMar8617_0432.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   KO; K03500; -.
DR   OMA; HIGLYQL; -.
DR   OrthoDB; POG091H02E2; -.
DR   Proteomes; UP000001420; 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:UP000001420};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00633812};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00811925, ECO:0000313|EMBL:AAP99468.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001420};
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:AAP99468.1}.
FT   DOMAIN      174    438       SAM_MT_RSMB_NOP.
FT                                {ECO:0000259|PROSITE:PS51686}.
FT   ACT_SITE    390    390       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     289    289       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     316    316       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     337    337       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       174    438       iprf:SAM_MT_RSMB_NOP [T]
FT   MYHIT       252    417       ipfam:Methyltr_RsmB-F [T]
FT   MYHIT         9    130       ipfam:NusB [T]
SQ   SEQUENCE   438 AA;  48759 MW;  F319AF12173B6F59 CRC64;
     MLKKGLLSRL AAWEILQTVG RGAYSDIAID HSFRKYSLSI ADRALATELA CGAIRQRLVL
     DCWIDCLAKV SAEKQPPLLR WLLHVGLYQI FYMDRIPVSA AVNTTVELAK KKNLKSLAPV
     VNAILREAIR ARDLGKELPG LIEPQDRLSL KHSIPTWLAY ELIEWKGEKG AEIIAKAFNQ
     APAIDLRVNS KRSSVKSLRQ KFQDSGIESK LIETCPYGLT VTSGAGDLRQ WPGYEQGEWS
     VQDRSAQWVV PLLEPRSGEV VLDACSAPGG KTTHLAELMN DIGEIWAVDR SPKRLQKVSL
     NAARLGHHCI KFLSADATNL IELKPSWKGY FNKILLDVPC SGLGTLARNP DARWRMSPSQ
     IEGLIQLQFN LLEGILPLLK PGGRIVYSTC TIHPDENFRQ IEKFVSMHQP LNLERQKQIW
     PGDAQGGDGF YAAIIDSG
//