ID Q63NE7_BURPS Unreviewed; 281 AA.
AC Q63NE7;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 10-MAY-2017, entry version 56.
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=BPSS0352 {ECO:0000313|EMBL:CAH37800.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH37800.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH37800.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH37800.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.,
RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R.,
RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I.,
RA Chillingworth T., Cronin A., Crosset B., Davis P., DeShazer D.,
RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K.,
RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A.,
RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis,
RT Burkholderia pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571966; CAH37800.1; -; Genomic_DNA.
DR RefSeq; WP_004538077.1; NZ_CP009537.1.
DR RefSeq; YP_110372.1; NC_006351.1.
DR ProteinModelPortal; Q63NE7; -.
DR STRING; 272560.BPSS0352; -.
DR EnsemblBacteria; CAH37800; CAH37800; BPSS0352.
DR GeneID; 3096091; -.
DR KEGG; bps:BPSS0352; -.
DR PATRIC; 19268348; VBIBurPse99623_4346.
DR eggNOG; ENOG4105D6S; Bacteria.
DR eggNOG; COG2961; LUCA.
DR HOGENOM; HOG000262479; -.
DR KO; K07115; -.
DR OMA; TYAIWYP; -.
DR Proteomes; UP000000605; Chromosome 2.
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:UP000000605};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605};
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 144 145 S-adenosyl-L-methionine binding.
FT {ECO:0000256|HAMAP-Rule:MF_00934}.
FT ACT_SITE 165 165 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 165 165 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 33 273 ipfam:RsmJ [T]
FT MYHIT 2 268 ihamap:23SrRNA_methyltr_J [T]
SQ SEQUENCE 281 AA; 32037 MW; 86F3AE606D166524 CRC64;
MLSYRHGFHA GNHADVLKHT VVVQLLRYLN KKDKSYWYID THAGAGVYSL FDGYAAKTGE
FGTGIEKIWD ATDLPEALSD YVDEVRALNR DGELRYYPGS PYLAWRLMRE QDRMRLFELH
STEIDVLRHN FRDAGRRAMI YAGDGFEGIK ALLPPPPRRA LVLVDPSYED KRDYAKTTAC
VEESLKRFAT GCYAIWYPQV SRPESQKFPD HLKQLQPNNW LHLSLTVSRP PSDGFGLFGS
GMFILNPPYT LVDTMKEALP YLVEALGQDS GAKFAIEHRA N
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