(data stored in ACNUC7421 zone)

SWISSPROT: A8FPK3_SHESH

ID   A8FPK3_SHESH            Unreviewed;       280 AA.
AC   A8FPK3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 51.
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=Ssed_0163 {ECO:0000313|EMBL:ABV34776.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34776.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34776.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34776.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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: 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; CP000821; ABV34776.1; -; Genomic_DNA.
DR   RefSeq; WP_012004302.1; NC_009831.1.
DR   ProteinModelPortal; A8FPK3; -.
DR   STRING; 425104.Ssed_0163; -.
DR   EnsemblBacteria; ABV34776; ABV34776; Ssed_0163.
DR   KEGG; sse:Ssed_0163; -.
DR   eggNOG; ENOG4105D6S; Bacteria.
DR   eggNOG; COG2961; LUCA.
DR   HOGENOM; HOG000262479; -.
DR   OMA; TYAIWYP; -.
DR   OrthoDB; POG091H04AQ; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0036307; F:23S rRNA (adenine(2030)-N(6))-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-HAMAP.
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;
DR   PRODOM; A8FPK3.
DR   SWISS-2DPAGE; A8FPK3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
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      144    145       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   ACT_SITE    165    165       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     101    101       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   BINDING     119    119       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   BINDING     165    165       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   280 AA;  31420 MW;  2E58831313E5A5FC CRC64;
     MLSYRHGYHA GNYADVLKHS VLLQVLKLMH KKPTPFVYID THAGAGGYAL SDEFAQKTGE
     YLEGVAKLWG KEDLPEPLAE YIADVTHFNQ GKPELSFYPG SPAFVDMNSY EKERMVLHEL
     HGADHAQLEE QFAGDRYIRI VKDDGLKGLI AAVPPRERRG VILVDPSYEM KTDYQDVPNA
     IIKAHKKFAT GVYMLWYPVV NRAQTEGMLK ILAQSGIKNQ LRIEQSVRAD SDEFGMTAAG
     LWIINPPWQL DSKADEILEY LSPLLNQGGG KVTMKLEVGE
//

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