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 | RecName: Full=Ribosomal RNA large subunit methyltransferase J {ECO:0000256|HAMAP-Rule:MF_00934}; EC=2.1.1.266 {ECO:0000256|HAMAP-Rule:MF_00934}; AltName: Full=23S rRNA (adenine(2030)-N6)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934}; AltName: Full=23S rRNA m6A2030 methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934}; |
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MyHits synonyms | Q8E8K5_SHEON , Q8E8K5 , EEC5450349083575 |
![]() Legends: 1, ACT_SITE Proton acceptor. {ECO:0000256|HAMAP- Rule:MF_00934}; 2, BINDING S-adenosyl-L-methionine. {ECO:0000256|HAMAP-Rule:MF_00934}; 3, BINDING S-adenosyl-L-methionine; via carbonyl oxygen. {ECO:0000256|HAMAP- Rule:MF_00934}; 4, SITE Interaction with substrate rRNA. {ECO:0000256|HAMAP-Rule:MF_00934}; 5, REGION S-adenosyl-L-methionine binding. {ECO:0000256|HAMAP-Rule:MF_00934}.
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ID Q8E8K5_SHEON Unreviewed; 281 AA. AC Q8E8K5; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 10-MAY-2017, entry version 67. DE RecName: Full=Ribosomal RNA large subunit methyltransferase J {ECO:0000256|HAMAP-Rule:MF_00934}; DE EC=2.1.1.266 {ECO:0000256|HAMAP-Rule:MF_00934}; DE AltName: Full=23S rRNA (adenine(2030)-N6)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934}; DE AltName: Full=23S rRNA m6A2030 methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934}; GN Name=yhiR {ECO:0000313|EMBL:AAN57618.1}; GN Synonyms=rlmJ {ECO:0000256|HAMAP-Rule:MF_00934}; GN OrderedLocusNames=SO_4659 {ECO:0000313|EMBL:AAN57618.1}; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN57618.1, ECO:0000313|Proteomes:UP000008186}; RN [1] {ECO:0000313|EMBL:AAN57618.1, ECO:0000313|Proteomes:UP000008186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN57618.1, RC ECO:0000313|Proteomes:UP000008186}; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A., RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S., RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., RA Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., RA Vamathevan J., Weidman J., Impraim M., Lee K., Berry K., Lee C., RA Mueller J., Khouri H., Gill J., Utterback T.R., McDonald L.A., RA Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). CC -!- FUNCTION: Specifically methylates the adenine in position 2030 of CC 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_00934}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + adenine(2030) in 23S CC rRNA = S-adenosyl-L-homocysteine + N(6)-methyladenine(2030) in 23S CC rRNA. {ECO:0000256|HAMAP-Rule:MF_00934}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00934}. CC -!- SIMILARITY: Belongs to the RlmJ family. {ECO:0000256|HAMAP- CC Rule:MF_00934}. 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; AE014299; AAN57618.1; -; Genomic_DNA. DR RefSeq; NP_720174.1; NC_004347.2. DR RefSeq; WP_011074253.1; NC_004347.2. DR ProteinModelPortal; Q8E8K5; -. DR PaxDb; Q8E8K5; -. DR EnsemblBacteria; AAN57618; AAN57618; SO_4659. DR GeneID; 1172243; -. DR KEGG; son:SO_4659; -. DR PATRIC; 23528985; VBISheOne101494_4518. DR eggNOG; ENOG4105D6S; Bacteria. DR eggNOG; COG2961; LUCA. DR HOGENOM; HOG000262479; -. DR KO; K07115; -. DR OMA; TYAIWYP; -. DR OrthoDB; POG091H04AQ; -. DR PhylomeDB; Q8E8K5; -. DR Proteomes; UP000008186; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0036307; F:23S rRNA (adenine(2030)-N(6))-methyltransferase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central. DR HAMAP; MF_00934; 23SrRNA_methyltr_J; 1. DR InterPro; IPR007473; RlmJ. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF04378; RsmJ; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008186}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934}; KW Reference proteome {ECO:0000313|Proteomes:UP000008186}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00934}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_00934}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00934}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00934}. FT REGION 145 146 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT ACT_SITE 166 166 Proton acceptor. {ECO:0000256|HAMAP- FT Rule:MF_00934}. FT BINDING 19 19 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT BINDING 42 42 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00934}. FT BINDING 102 102 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT BINDING 120 120 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT BINDING 166 166 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT SITE 4 4 Interaction with substrate rRNA. FT {ECO:0000256|HAMAP-Rule:MF_00934}. CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 2 268 ihamap:23SrRNA_methyltr_J [T] FT MYHIT 33 278 ipfam:RsmJ [T] SQ SEQUENCE 281 AA; 31780 MW; EEC5450349083575 CRC64; MLSYRHGYHA GNYADVLKHA MLLQTLQLMH KKDKPLVYID THAGAGGYAL TDEFAQKTGE YLDGVAKLWN KTDLPKSLQD YVDAVRHFNE DNPEELNFYP GSPAFIDMDL GPKDRMVLHE LHGTDHLLLD EYFEQDKQVK VIKGDGLKGL IAAVPPLERR ALVLVDPSYE IKTDYQTVAD TLIKAHKRFA TGVFMLWYPV VNRAQTEEML SRLANSGIKR QLRIEQAIKP DSNEFGMTAA GLWVINPPWQ LDEIANEMVD YLGKTLGQAD GHVSVKWEVG E // |