(data stored in ACNUC7421 zone)

SWISSPROT: Q3KJ54_PSEPF

ID   Q3KJ54_PSEPF            Unreviewed;       279 AA.
AC   Q3KJ54;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
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=Pfl01_0458 {ECO:0000313|EMBL:ABA72202.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72202.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72202.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72202.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Specifically methylates the adenine in position 2030 of
CC       23S rRNA. {ECO:0000256|HAMAP-Rule:MF_00934}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(2030) in 23S rRNA + S-adenosyl-L-methionine =
CC         H(+) + N(6)-methyladenosine(2030) in 23S rRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:43736, Rhea:RHEA-COMP:10668,
CC         Rhea:RHEA-COMP:10669, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74449;
CC         EC=2.1.1.266; Evidence={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; CP000094; ABA72202.1; -; Genomic_DNA.
DR   RefSeq; WP_011332124.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0458; -.
DR   EnsemblBacteria; ABA72202; ABA72202; Pfl01_0458.
DR   KEGG; pfo:Pfl01_0458; -.
DR   eggNOG; ENOG4105D6S; Bacteria.
DR   eggNOG; COG2961; LUCA.
DR   HOGENOM; HOG000262479; -.
DR   KO; K07115; -.
DR   OMA; TYAIWYP; -.
DR   BioCyc; PFLU205922:G1G4S-463-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0036307; F:23S rRNA (adenine(2030)-N(6))-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00934; 23SrRNA_methyltr_J; 1.
DR   InterPro; IPR007473; RlmJ.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR37426; PTHR37426; 1.
DR   Pfam; PF04378; RsmJ; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJ54.
DR   SWISS-2DPAGE; Q3KJ54.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934};
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      142    143       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   COILED      169    189       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    163    163       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00934}.
FT   BINDING      18     18       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   BINDING      41     41       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00934}.
FT   BINDING      99     99       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   BINDING     117    117       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   BINDING     163    163       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   SITE          3      3       Interaction with substrate rRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
SQ   SEQUENCE   279 AA;  31711 MW;  753A857920F2F1C4 CRC64;
     MNYRHAFHAG NHADVFKHLT LTRLIALMSR KEQPFAYLDS HAGIGLYDLQ GDQANRTGEY
     LEGIARLWDQ PDLPALTADY MNVLHEMNPD GQLRYYPGSP ELARRLTRSQ DRVLLNEKHP
     EDGVLLKDNM KGDRRVAVHL GEGWHVARAL LPVAEKRAVM LIDPPFEKLD EMQRCAASLR
     EAISRMRQTV AAIWYPVKDQ RALRRFYQDL AGTGAPKLLR VELLVHPLDT PNSLNGSGLA
     IANPPWGLEE ELRELLPWLS KKLGQTQGGW QMDWLIAES
//

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