ID Q7VXM1_BORPE Unreviewed; 287 AA.
AC Q7VXM1;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 10-MAY-2017, entry version 61.
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=BP1730 {ECO:0000313|EMBL:CAE42017.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.,
RA Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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}.
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DR EMBL; BX640416; CAE42017.1; -; Genomic_DNA.
DR RefSeq; NP_880445.1; NC_002929.2.
DR RefSeq; WP_003816518.1; NC_002929.2.
DR ProteinModelPortal; Q7VXM1; -.
DR STRING; 257313.BP1730; -.
DR EnsemblBacteria; CAE42017; CAE42017; BP1730.
DR GeneID; 2665833; -.
DR KEGG; bpe:BP1730; -.
DR PATRIC; 21156722; VBIBorPer7866_1855.
DR eggNOG; ENOG4105D6S; Bacteria.
DR eggNOG; COG2961; LUCA.
DR HOGENOM; HOG000262479; -.
DR KO; K07115; -.
DR OMA; TYAIWYP; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0036307; F:23S rRNA (adenine(2030)-N(6))-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-HAMAP.
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:UP000002676};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934};
KW Reference proteome {ECO:0000313|Proteomes:UP000002676};
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 149 150 S-adenosyl-L-methionine binding.
FT {ECO:0000256|HAMAP-Rule:MF_00934}.
FT ACT_SITE 170 170 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 170 170 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.
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FT MYHIT 2 273 ihamap:23SrRNA_methyltr_J [T]
FT MYHIT 33 282 ipfam:RsmJ [T]
SQ SEQUENCE 287 AA; 32727 MW; 400FF41F0C8621F0 CRC64;
MFSYRHAFHA GNHADVLKHA ILVHVLDYMN RKEAPYWVVD THAGAGLYAL GSDWASKNAE
HADGVARLWE LSGLPPLLAD YVARIRDYNT DGVLRHYPGS PWLTLDVLRE RDRLRLFEMH
PSESDVLVRN LERRNERTAL RQTTVFAADG FEGVKALLPP PTRRGLVLID PSYEDKQDYR
RTLTAVREGV KRFATGTFVV WYPLVQRREA SEMARQLERL PVKSWLHATL TVRKPAADGF
GLHGSGMFLV NPPWTLHDAL KPAMPLLARE LAQDDRAGFT LQYRENP
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