RLMJ_HAEIN
ID RLMJ_HAEIN Reviewed; 281 AA.
AC P31777;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase J {ECO:0000255|HAMAP-Rule:MF_00934};
DE EC=2.1.1.266 {ECO:0000255|HAMAP-Rule:MF_00934};
DE AltName: Full=23S rRNA (adenine(2030)-N6)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00934};
DE AltName: Full=23S rRNA m6A2030 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00934};
DE AltName: Full=ORFJ;
GN Name=rlmJ {ECO:0000255|HAMAP-Rule:MF_00934}; OrderedLocusNames=HI_0441;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-m;
RA Tomb J.-F., El-Hajj H., Smith H.O.;
RT "Nucleotide sequence of a cluster of genes involved in the transformation
RT of Haemophilus influenzae Rd.";
RL Gene 104:1-10(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
CC -!- FUNCTION: Specifically methylates the adenine in position 2030 of 23S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_00934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(2030) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyladenosine(2030) in 23S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43736, Rhea:RHEA-COMP:10668, Rhea:RHEA-COMP:10669,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.266;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00934};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00934}.
CC -!- SIMILARITY: Belongs to the RlmJ family. {ECO:0000255|HAMAP-
CC Rule:MF_00934}.
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DR EMBL; M62809; AAA25006.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22100.1; -; Genomic_DNA.
DR PIR; E64068; E64068.
DR RefSeq; NP_438602.1; NC_000907.1.
DR RefSeq; WP_005693720.1; NC_000907.1.
DR AlphaFoldDB; P31777; -.
DR SMR; P31777; -.
DR STRING; 71421.HI_0441; -.
DR EnsemblBacteria; AAC22100; AAC22100; HI_0441.
DR KEGG; hin:HI_0441; -.
DR PATRIC; fig|71421.8.peg.461; -.
DR eggNOG; COG2961; Bacteria.
DR HOGENOM; CLU_061769_0_0_6; -.
DR OMA; TYAIWYP; -.
DR PhylomeDB; P31777; -.
DR BioCyc; HINF71421:G1GJ1-456-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0036307; F:23S rRNA (adenine(2030)-N(6))-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00934; 23SrRNA_methyltr_J; 1.
DR InterPro; IPR007473; RlmJ.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR37426; PTHR37426; 1.
DR Pfam; PF04378; RsmJ; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 2.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; RNA-binding; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..281
FT /note="Ribosomal RNA large subunit methyltransferase J"
FT /id="PRO_0000169568"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00934"
FT BINDING 19
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00934"
FT BINDING 42
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00934"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00934"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00934"
FT BINDING 144..145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00934"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00934"
FT SITE 4
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00934"
SQ SEQUENCE 281 AA; 32217 MW; 5A66A59357A80F34 CRC64;
MLSYHHSFHA GNHADVLKHI VLMLILENLK LKEKGFFYLD THSGVGRYRL SSNESEKTGE
YKEGIGRLWD QTDLPEDIAR YVKMIKKLNY GGKELRYYAG SPLIAAELLR SQDRALLTEL
HPSDYPILRN NFSDDKNVTV KCDNGFQQVK ATLPPKERRG LVLIDPPYEL KDDYDLVVKA
IEEGYKRFAT GTYAIWYPVV LRQQTKRIFK GLEATGIRKI LKIELAVRPD SDQRGMTASG
MVVINPPWTL ETQMKEILPY LTKTLVPEGT GSWTVEWITP E
