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 02-NOV-2016, entry version 85.
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};
GN 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
RT transformation 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.,
RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA 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.,
RA Gray C., 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
CC 23S rRNA. {ECO:0000255|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: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}.
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 ProteinModelPortal; P31777; -.
DR STRING; 71421.HI0441; -.
DR EnsemblBacteria; AAC22100; AAC22100; HI_0441.
DR GeneID; 949523; -.
DR KEGG; hin:HI0441; -.
DR PATRIC; 20189435; VBIHaeInf48452_0461.
DR eggNOG; ENOG4105D6S; Bacteria.
DR eggNOG; COG2961; LUCA.
DR KO; K07115; -.
DR OMA; TYAIWYP; -.
DR PhylomeDB; P31777; -.
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-HAMAP.
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.
DR Pfam; PF04378; RsmJ; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 2.
PE 1: Evidence at protein level;
KW Complete proteome; Methyltransferase; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 281 Ribosomal RNA large subunit
FT methyltransferase J.
FT /FTId=PRO_0000169568.
FT REGION 144 145 S-adenosyl-L-methionine binding.
FT {ECO:0000255|HAMAP-Rule:MF_00934}.
FT ACT_SITE 165 165 Proton acceptor. {ECO:0000255|HAMAP-
FT Rule:MF_00934}.
FT BINDING 19 19 S-adenosyl-L-methionine.
FT {ECO:0000255|HAMAP-Rule:MF_00934}.
FT BINDING 42 42 S-adenosyl-L-methionine; via carbonyl
FT oxygen. {ECO:0000255|HAMAP-
FT Rule:MF_00934}.
FT BINDING 101 101 S-adenosyl-L-methionine.
FT {ECO:0000255|HAMAP-Rule:MF_00934}.
FT BINDING 119 119 S-adenosyl-L-methionine.
FT {ECO:0000255|HAMAP-Rule:MF_00934}.
FT BINDING 165 165 S-adenosyl-L-methionine.
FT {ECO:0000255|HAMAP-Rule:MF_00934}.
FT SITE 4 4 Interaction with substrate rRNA.
FT {ECO:0000255|HAMAP-Rule:MF_00934}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 33 279 ipfam:RsmJ [T]
FT MYHIT 2 267 ihamap:23SrRNA_methyltr_J [T]
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
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