(data stored in ACNUC1104 zone)

SWISSPROT: D3VIM1_XENNA

ID   D3VIM1_XENNA            Unreviewed;       209 AA.
AC   D3VIM1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000256|HAMAP-Rule:MF_01547, ECO:0000256|SAAS:SAAS00088961};
DE            EC=2.1.1.166 {ECO:0000256|HAMAP-Rule:MF_01547, ECO:0000256|SAAS:SAAS00359536};
DE   AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547};
DE   AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547};
GN   Name=rlmE {ECO:0000256|HAMAP-Rule:MF_01547};
GN   Synonyms=ftsJ {ECO:0000256|HAMAP-Rule:MF_01547,
GN   ECO:0000313|EMBL:CBJ88571.1}, rrmJ {ECO:0000256|HAMAP-Rule:MF_01547};
GN   OrderedLocusNames=XNC1_0497 {ECO:0000313|EMBL:CBJ88571.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88571.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88571.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Specifically methylates the uridine in position 2552 of
CC       23S rRNA at the 2'-O position of the ribose in the fully assembled
CC       50S ribosomal subunit. {ECO:0000256|HAMAP-Rule:MF_01547,
CC       ECO:0000256|SAAS:SAAS00088962}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-
CC         O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42720, Rhea:RHEA-COMP:10202,
CC         Rhea:RHEA-COMP:10203, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74478;
CC         EC=2.1.1.166; Evidence={ECO:0000256|HAMAP-Rule:MF_01547,
CC         ECO:0000256|SAAS:SAAS01120683};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01547,
CC       ECO:0000256|SAAS:SAAS00088964}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RNA methyltransferase RlmE family.
CC       {ECO:0000256|HAMAP-Rule:MF_01547}.
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DR   EMBL; FN667742; CBJ88571.1; -; Genomic_DNA.
DR   RefSeq; WP_010845213.1; NC_014228.1.
DR   STRING; 406817.XNC1_0497; -.
DR   EnsemblBacteria; CBJ88571; CBJ88571; XNC1_0497.
DR   KEGG; xne:XNC1_0497; -.
DR   eggNOG; ENOG4105F7M; Bacteria.
DR   eggNOG; COG0293; LUCA.
DR   HOGENOM; HOG000162367; -.
DR   KO; K02427; -.
DR   OMA; HRQTDHL; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR004512; rRNA_MeTrfase_gammaproteobac.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01728; FtsJ; 1.
DR   PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00438; rrmJ; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VIM1.
DR   SWISS-2DPAGE; D3VIM1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000256|SAAS:SAAS00437003};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000256|SAAS:SAAS00461497, ECO:0000313|EMBL:CBJ88571.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000256|SAAS:SAAS00319237};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000256|PIRSR:PIRSR005461-1, ECO:0000256|SAAS:SAAS00461490};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000256|SAAS:SAAS00461492, ECO:0000313|EMBL:CBJ88571.1}.
FT   DOMAIN       31    206       FtsJ. {ECO:0000259|Pfam:PF01728}.
FT   ACT_SITE    164    164       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01547, ECO:0000256|PIRSR:PIRSR005461-
FT                                1}.
FT   BINDING      63     63       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01547}.
FT   BINDING      65     65       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01547}.
FT   BINDING      83     83       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01547}.
FT   BINDING      99     99       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01547}.
FT   BINDING     124    124       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01547}.
SQ   SEQUENCE   209 AA;  23402 MW;  6498648CAEE9873B CRC64;
     MANKKRSASS SRWLQEHFSD KYVLQAQKKG LRSRAWFKLD EIQQSDKIFK PGMTVVDLGA
     APGGWSQYVV SQIGNSGRVI ACDLLPMDPI VGVDFLQGDF RDELVLKTLL ERVGDNKVQV
     VMSDMAPNMS GTPAVDIPRS MYLIELALDM CRDVLAPGGS FIVKVFQGEG FDEYLREIRS
     LFAKIKIRKP EASRARSREV YIVATGRKV
//

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