ID Q8P7B5_XANCP Unreviewed; 302 AA.
AC Q8P7B5;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 10-MAY-2017, entry version 72.
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=XCC2696 {ECO:0000313|EMBL:AAM41968.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 /
OS NCPPB 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM41968.1, ECO:0000313|Proteomes:UP000001010};
RN [1] {ECO:0000313|EMBL:AAM41968.1, ECO:0000313|Proteomes:UP000001010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC {ECO:0000313|Proteomes:UP000001010};
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA Almeida N.F.Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA Katsuyama A.M., Kishi L.T., Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F.,
RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA Pereira H.A.Jr., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing
RT host specificities.";
RL Nature 417:459-463(2002).
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; AE008922; AAM41968.1; -; Genomic_DNA.
DR RefSeq; NP_638044.1; NC_003902.1.
DR RefSeq; WP_011037826.1; NC_003902.1.
DR ProteinModelPortal; Q8P7B5; -.
DR STRING; 190485.XCC2696; -.
DR EnsemblBacteria; AAM41968; AAM41968; XCC2696.
DR GeneID; 999618; -.
DR KEGG; xcc:XCC2696; -.
DR PATRIC; 24076370; VBIXanCam115730_2875.
DR eggNOG; ENOG4105D6S; Bacteria.
DR eggNOG; COG2961; LUCA.
DR HOGENOM; HOG000262479; -.
DR KO; K07115; -.
DR OMA; TYAIWYP; -.
DR Proteomes; UP000001010; 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 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:UP000001010};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934};
KW Reference proteome {ECO:0000313|Proteomes:UP000001010};
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 159 160 S-adenosyl-L-methionine binding.
FT {ECO:0000256|HAMAP-Rule:MF_00934}.
FT ACT_SITE 185 185 Proton acceptor. {ECO:0000256|HAMAP-
FT Rule: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-
FT Rule:MF_00934}.
FT BINDING 116 116 S-adenosyl-L-methionine.
FT {ECO:0000256|HAMAP-Rule:MF_00934}.
FT BINDING 134 134 S-adenosyl-L-methionine.
FT {ECO:0000256|HAMAP-Rule:MF_00934}.
FT BINDING 185 185 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}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 32 298 ipfam:RsmJ [T]
FT MYHIT 1 288 ihamap:23SrRNA_methyltr_J [T]
SQ SEQUENCE 302 AA; 33075 MW; CE0386CE72A1FEFF CRC64;
MNYRHAFHAG NHADVLKHIA LLALIDTLKR KDTPFFVLDT HAGRGRYQLG GEESRKTNEA
DAGVMRLMAE ATLPEVVERY LRAVQADNAA VARPAVPGQK AARPTAGIQI NHYPGSPLLA
AQALRAQDRM AFCELQPDEA QALKTLFAND SRVRVHAGDG YAAIRAFLPP RAGEVKIGRG
LVLIDPPYES QGAEYPQVIA SVREALARWP QAICMVWYPI KLRRSLQPFM RKAAALPAKS
VLMAELQVHP DDSPLRLTGS GLLIVNAPWQ FDQVLAPALP ALKAHLGEAG ASTRLEWLRQ
EG
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