(data stored in SCRATCH zone)

SWISSPROT: Q3IEX0_PSEHT

ID   Q3IEX0_PSEHT            Unreviewed;       279 AA.
AC   Q3IEX0;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 62.
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=PSHAa0298 {ECO:0000313|EMBL:CAI85397.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85397.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85397.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85397.1; -; Genomic_DNA.
DR   RefSeq; WP_011327011.1; NC_007481.1.
DR   ProteinModelPortal; Q3IEX0; -.
DR   STRING; 326442.PSHAa0298; -.
DR   EnsemblBacteria; CAI85397; CAI85397; PSHAa0298.
DR   KEGG; pha:PSHAa0298; -.
DR   PATRIC; fig|326442.8.peg.284; -.
DR   eggNOG; ENOG4105D6S; Bacteria.
DR   eggNOG; COG2961; LUCA.
DR   HOGENOM; HOG000262479; -.
DR   KO; K07115; -.
DR   OMA; TYAIWYP; -.
DR   OrthoDB; POG091H04AQ; -.
DR   Proteomes; UP000006843; Chromosome I.
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; Q3IEX0.
DR   SWISS-2DPAGE; Q3IEX0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
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      143    144       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   ACT_SITE    164    164       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     100    100       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   BINDING     118    118       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00934}.
FT   BINDING     164    164       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   279 AA;  31743 MW;  8895B777CF97B0D0 CRC64;
     MLSYRHSFHA GNPADVLKHL VLAQVLGYQT LKDKPLDYID THSGAGFFEL AAADAQKTQE
     YQDGIEKLWQ HTSKHSALND YIALIKSFNQ TANLEFYPGS PKIAEHFLRR QDKGWFFELH
     PRDLLLLEEN MQGKRSIRVR GENGFAGLVG LLPPASRRAC VLIDPPYEVK DDYDTVITTL
     MQAYQRFATG TYMIWYPVVD RSRIDNMEQD LIDSGMRNIQ LFELATKADT DVHGMTASGM
     IVINPPWKLK QVMDEVLPEL VSILSESSGF YRSEQLVAE
//

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