(data stored in SCRATCH zone)

SWISSPROT: D3UWD2_XENBS

ID   D3UWD2_XENBS            Unreviewed;       365 AA.
AC   D3UWD2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase M {ECO:0000256|HAMAP-Rule:MF_01551, ECO:0000256|SAAS:SAAS00058276};
DE            EC=2.1.1.186 {ECO:0000256|HAMAP-Rule:MF_01551, ECO:0000256|SAAS:SAAS00058274};
DE   AltName: Full=23S rRNA (cytidine2498-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01551};
DE   AltName: Full=23S rRNA 2'-O-ribose methyltransferase RlmM {ECO:0000256|HAMAP-Rule:MF_01551};
GN   Name=ygdE {ECO:0000313|EMBL:CBJ79641.1};
GN   Synonyms=rlmM {ECO:0000256|HAMAP-Rule:MF_01551};
GN   OrderedLocusNames=XBJ1_0492 {ECO:0000313|EMBL:CBJ79641.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79641.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
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:CBJ79641.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79641.1,
RC   ECO:0000313|Proteomes:UP000002045};
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: Catalyzes the 2'-O-methylation at nucleotide C2498 in
CC       23S rRNA. {ECO:0000256|HAMAP-Rule:MF_01551,
CC       ECO:0000256|SAAS:SAAS00368255}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine =
CC         2'-O-methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42788, Rhea:RHEA-COMP:10244,
CC         Rhea:RHEA-COMP:10245, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748;
CC         EC=2.1.1.186; Evidence={ECO:0000256|HAMAP-Rule:MF_01551,
CC         ECO:0000256|SAAS:SAAS01122283};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01551,
CC       ECO:0000256|SAAS:SAAS00058275}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01551,
CC       ECO:0000256|SAAS:SAAS00058272}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RNA methyltransferase RlmE family.
CC       RlmM subfamily. {ECO:0000256|HAMAP-Rule:MF_01551,
CC       ECO:0000256|SAAS:SAAS00559244}.
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DR   EMBL; FN667741; CBJ79641.1; -; Genomic_DNA.
DR   RefSeq; WP_012987097.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0492; -.
DR   EnsemblBacteria; CBJ79641; CBJ79641; XBJ1_0492.
DR   GeneID; 8830115; -.
DR   KEGG; xbo:XBJ1_0492; -.
DR   PATRIC; fig|406818.4.peg.451; -.
DR   eggNOG; ENOG4105EZ6; Bacteria.
DR   eggNOG; COG2933; LUCA.
DR   HOGENOM; HOG000247137; -.
DR   KO; K06968; -.
DR   OMA; PVDWMVC; -.
DR   BioCyc; XBOV406818:XBJ1_RS02130-MONOMER; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01551; 23SrRNA_methyltr_M; 1.
DR   InterPro; IPR040739; RlmM_FDX.
DR   InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR011224; rRNA_MeTrfase_M.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF18125; RlmM_FDX; 1.
DR   PIRSF; PIRSF028774; UCP028774; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UWD2.
DR   SWISS-2DPAGE; D3UWD2.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01551,
KW   ECO:0000256|SAAS:SAAS00445589};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01551,
KW   ECO:0000256|SAAS:SAAS00445585, ECO:0000313|EMBL:CBJ79641.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01551,
KW   ECO:0000256|SAAS:SAAS00058273};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01551,
KW   ECO:0000256|SAAS:SAAS00445586};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01551,
KW   ECO:0000256|SAAS:SAAS00445596, ECO:0000313|EMBL:CBJ79641.1}.
FT   DOMAIN        1     70       RlmM_FDX. {ECO:0000259|Pfam:PF18125}.
FT   DOMAIN      186    279       FtsJ. {ECO:0000259|Pfam:PF01728}.
FT   REGION      221    224       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01551}.
FT   COILED      310    330       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    306    306       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01551}.
FT   BINDING     188    188       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01551}.
FT   BINDING     240    240       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01551}.
FT   BINDING     260    260       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01551}.
FT   BINDING     277    277       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01551}.
SQ   SEQUENCE   365 AA;  42039 MW;  6D3B828F2891E8EF CRC64;
     MNKVALYCRP GFEKECAAEI TDKAGKKGIY GFARVKENSG YVLFECYQHD DADRLIREIP
     FGELIFARQM VVVGELLKNL PQEDRITPIL GMLTGVIERA GELRVEVPDN DESKELMTFC
     RKFTVPLRHA MRQEKFLLAK ESANRPVIHV LFIAPGCCYV GYSYSNNNSR FYMGIPRLKF
     PSDAPSRSTL KLEEAFHVFI PHDEWEERLG SGLYAVDLGA CPGGWTYQLV KRGMIVHAVD
     NGLMADSLMD TGQVKHHRVD GFKFEPTVKN VYWLVCDMVE QPAKVAHLMT DWLVKSWCRE
     AIFNLKLPMK KRYEEVAQIL QKIEQQLKEN GVNAQIQAKH LYHDREEVTV HVRRIWSAYA
     MTRDF
//

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