MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
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
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
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
- MyHits
Description | SubName: Full=16S rRNA m(5)C 967 methyltransferase {ECO:0000313|EMBL:CCC78930.1}; EC=2.1.1.- {ECO:0000313|EMBL:CCC78930.1}; |
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MyHits synonyms | F9UNZ1_LACPL , F9UNZ1 , BBC9C9F4021A2545 |
![]() Legends: 1, ACT_SITE Nucleophile. {ECO:0000256|PROSITE- ProRule:PRU01023}; 2, BINDING S-adenosyl-L-methionine. {ECO:0000256|PROSITE-ProRule:PRU01023}; 3, ipat:NOL1_NOP2_SUN [T].
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ID F9UNZ1_LACPL Unreviewed; 447 AA. AC F9UNZ1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 10-MAY-2017, entry version 44. DE SubName: Full=16S rRNA m(5)C 967 methyltransferase {ECO:0000313|EMBL:CCC78930.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:CCC78930.1}; GN Name=sunL {ECO:0000313|EMBL:CCC78930.1}; GN OrderedLocusNames=lp_1617 {ECO:0000313|EMBL:CCC78930.1}; OS Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC78930.1, ECO:0000313|Proteomes:UP000000432}; RN [1] {ECO:0000313|EMBL:CCC78930.1, ECO:0000313|Proteomes:UP000000432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1 RC {ECO:0000313|Proteomes:UP000000432}; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., RA De Vos W.M., Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WCFS1; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.F.T.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL Submitted (JUN-2011) 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:SAAS00637407}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL935263; CCC78930.1; -; Genomic_DNA. DR RefSeq; WP_011101476.1; NC_004567.2. DR RefSeq; YP_004889444.1; NC_004567.2. DR ProteinModelPortal; F9UNZ1; -. DR STRING; 220668.lp_1617; -. DR EnsemblBacteria; CCC78930; CCC78930; lp_1617. DR GeneID; 1063708; -. DR KEGG; lpl:lp_1617; -. DR eggNOG; ENOG4105CYJ; Bacteria. DR eggNOG; COG0144; LUCA. DR KO; K03500; -. DR OMA; HIGLYQL; -. DR BioCyc; LPLA220668:G137Z-1386-MONOMER; -. DR Proteomes; UP000000432; 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; IPR018314; Fmu/NOL1/Nop2p_CS. 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; PS01153; NOL1_NOP2_SUN; 1. DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000432}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00633812}; KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023, KW ECO:0000256|SAAS:SAAS00637415, ECO:0000313|EMBL:CCC78930.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000432}; KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023, KW ECO:0000256|SAAS:SAAS00637422}; KW rRNA processing {ECO:0000256|SAAS:SAAS00633795}; KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023, KW ECO:0000256|SAAS:SAAS00637399}; KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01023, KW ECO:0000256|SAAS:SAAS00637415, ECO:0000313|EMBL:CCC78930.1}. FT DOMAIN 171 447 SAM_MT_RSMB_NOP. FT {ECO:0000259|PROSITE:PS51686}. FT ACT_SITE 386 386 Nucleophile. {ECO:0000256|PROSITE- FT ProRule:PRU01023}. FT BINDING 286 286 S-adenosyl-L-methionine. FT {ECO:0000256|PROSITE-ProRule:PRU01023}. FT BINDING 314 314 S-adenosyl-L-methionine. FT {ECO:0000256|PROSITE-ProRule:PRU01023}. FT BINDING 333 333 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 247 445 ipfam:Methyltr_RsmB-F [T] FT MYHIT 8 129 ipfam:NusB [T] FT MYHIT 171 447 iprf:SAM_MT_RSMB_NOP [T] FT MYHIT 327 338 ipat:NOL1_NOP2_SUN [T] SQ SEQUENCE 447 AA; 50117 MW; BBC9C9F4021A2545 CRC64; MSTVGNTPRW LAVAALAKIK NGAYSNLQLN QLINDHQMDR RDINLLTNMV YGVIQHRLTL EYWLTPFVRH PHQIDPWVRE LLLSALYQWQ YLDKIPQRAV FNETIEIAKV KGHPGIRRFV TGVLHQMDRS GLPSFDAIKN PDERLSVTYS MPIWLIQELR RQLGAEKMER ILSSLNQPAK QALRVNPALS TVEDVTTALI NDGLTITPSE ISPLGLIATD GQAINTEAMR YGMFTVQDES AQLVVPALNP QPNDRVLDAC AAPGGKTTQI AASLDAEQGG TVVALDIHAN KVKLIGQNAA RMHVADRVEA TELDARKVET QFNAESFDRI LVDAPCSGLG LMRRKPEIRY EKQLQDSLNL QRIQLAILTA VAPTLKKGGI MTYSTCTILQ QENQDVITKF LADHPDFELQ TTPTERDLKT DRTEKTLSIY PDDYLSDGFF IACLRKK // |