Entry bact:Q7VXM1_BORPE

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.
CC   --------------------------------------------------------------------------
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
//