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 | Q7CG06_YERPE , Q7CG06 , Q74QW5 , F6FC38B7843AFD19 |
![]() 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}; 6, ipat:N6_MTASE [T].
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ID Q7CG06_YERPE Unreviewed; 280 AA. AC Q7CG06; Q74QW5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 10-MAY-2017, entry version 88. 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=rlmJ {ECO:0000256|HAMAP-Rule:MF_00934}; GN OrderedLocusNames=YPO3976 {ECO:0000313|EMBL:CAL22556.1}; OS Yersinia pestis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=632 {ECO:0000313|Proteomes:UP000000815}; RN [1] {ECO:0000313|EMBL:CAL22556.1, ECO:0000313|Proteomes:UP000000815} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-92 / Biovar Orientalis {ECO:0000313|Proteomes:UP000000815}; RX PubMed=11586360; DOI=10.1038/35097083; RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., RA Prentice M.B., Sebaihia M., James K.D., Churcher C., Mungall K.L., RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.M., RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., RA Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S., RA Karlyshev A.V., Moule S., Oyston P.C.F., Quail M., Rutherford K., RA Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.; RT "Genome sequence of Yersinia pestis, the causative agent of plague."; RL Nature 413:523-527(2001). 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; AL590842; CAL22556.1; -; Genomic_DNA. DR PIR; AI0483; AI0483. DR RefSeq; WP_002209533.1; NZ_LT605018.1. DR RefSeq; YP_002348846.1; NC_003143.1. DR STRING; 187410.y3853; -. DR DNASU; 1148800; -. DR EnsemblBacteria; AAM87398; AAM87398; y3853. DR EnsemblBacteria; AAS63504; AAS63504; YP_3339. DR GeneID; 1176814; -. DR KEGG; ype:YPO3976; -. DR KEGG; ypj:CH55_2655; -. DR KEGG; ypk:y3853; -. DR KEGG; ypl:CH46_1081; -. DR KEGG; ypm:YP_3339; -. DR KEGG; ypv:BZ15_3729; -. DR KEGG; ypw:CH59_1924; -. DR eggNOG; ENOG4105D6S; Bacteria. DR eggNOG; COG2961; LUCA. DR HOGENOM; HOG000262479; -. DR KO; K07115; -. DR OMA; TYAIWYP; -. DR Proteomes; UP000000815; 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; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR007473; RlmJ. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF04378; RsmJ; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000815}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934}; KW Reference proteome {ECO:0000313|Proteomes:UP000000815}; 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 143 144 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT ACT_SITE 164 164 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 100 100 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT BINDING 118 118 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT BINDING 164 164 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 2 266 ihamap:23SrRNA_methyltr_J [T] FT MYHIT 241 247 ipat:N6_MTASE [T] FT MYHIT 33 278 ipfam:RsmJ [T] SQ SEQUENCE 280 AA; 32304 MW; F6FC38B7843AFD19 CRC64; MLSYRHSFHA GNHADVLKHT VQSLIIEAMK EKEKPFLYLD THAGAGRYQL SGEHAERTGE YLDGIGKLWQ RDDLPADLAP YMSAINYFNR GEKLRYYPGS PLIARHLLRE DDKIHLTELH SSDYPLLRNE FAKDERAKVQ RADGYQQLKS QLPPLSRRGF VLIDPPYEMK TDYQDVVKGI QEGYKRFATG TYALWYPVVL RQQIKRLLRD LEATGIRRIL QIELAVRPDS DQHGMTASGM IVINPPWKLE QQMNSLLPWL HNVLVPSGHG HTLVKWVVPE // |