(data stored in ACNUC7421 zone)

SWISSPROT: A1AZJ7_PARDP

ID   A1AZJ7_PARDP            Unreviewed;       257 AA.
AC   A1AZJ7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 70.
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=Pden_0579 {ECO:0000313|EMBL:ABL68691.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68691.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000489; ABL68691.1; -; Genomic_DNA.
DR   RefSeq; WP_011746924.1; NC_008686.1.
DR   PRIDE; A1AZJ7; -.
DR   EnsemblBacteria; ABL68691; ABL68691; Pden_0579.
DR   KEGG; pde:Pden_0579; -.
DR   eggNOG; ENOG4105D6S; Bacteria.
DR   eggNOG; COG2961; LUCA.
DR   HOGENOM; HOG000262479; -.
DR   KO; K07115; -.
DR   OMA; TYAIWYP; -.
DR   BioCyc; PDEN318586:G1GW1-587-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; IPR002052; DNA_methylase_N6_adenine_CS.
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.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AZJ7.
DR   SWISS-2DPAGE; A1AZJ7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
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      139    140       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   ACT_SITE    160    160       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                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-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     160    160       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}.
SQ   SEQUENCE   257 AA;  28173 MW;  A77A715E2FF7600B CRC64;
     MLSYQHAYHA GNLADLYKHA LLASILAYLT AKPKPLSYLE THAGRGLYDL SSPEADKTGE
     AAAGITRALA ENWLPADHPL CLALDAVRAR HGASAYPGSP LIARHFLRPG DVAHLAELHP
     AEHEALAEIA GFAHLHRQDG FQMAQAICPP TPRRGLLLID PSYEVKADYD AIPRQIAKLA
     RKWNVGVIVL WYPILTDLRH APMVEALRRN HPEALVSEVR FPPARPGHGM VGSGMVVLNP
     PYGLAEEALR IEALYDR
//

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