(data stored in ACNUC1104 zone)

SWISSPROT: D3VII8_XENNA

ID   D3VII8_XENNA            Unreviewed;       245 AA.
AC   D3VII8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=23S rRNA (guanosine-2'-O-)-methyltransferase RlmB {ECO:0000256|HAMAP-Rule:MF_01887};
DE            EC=2.1.1.185 {ECO:0000256|HAMAP-Rule:MF_01887};
DE   AltName: Full=23S rRNA (guanosine2251 2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01887};
DE   AltName: Full=23S rRNA Gm2251 2'-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01887};
GN   Name=rlmB {ECO:0000256|HAMAP-Rule:MF_01887};
GN   OrderedLocusNames=XNC1_0464 {ECO:0000313|EMBL:CBJ88538.1};
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:CBJ88538.1, 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:CBJ88538.1, 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 ribose of guanosine 2251 in
CC       23S rRNA. {ECO:0000256|HAMAP-Rule:MF_01887}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine =
CC         2'-O-methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:24140, Rhea:RHEA-COMP:10239,
CC         Rhea:RHEA-COMP:10241, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74445;
CC         EC=2.1.1.185; Evidence={ECO:0000256|HAMAP-Rule:MF_01887};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01887}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01887}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding
CC       methyltransferase superfamily. RNA methyltransferase TrmH family.
CC       RlmB subfamily. {ECO:0000256|HAMAP-Rule:MF_01887}.
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DR   EMBL; FN667742; CBJ88538.1; -; Genomic_DNA.
DR   RefSeq; WP_013183284.1; NC_014228.1.
DR   STRING; 406817.XNC1_0464; -.
DR   EnsemblBacteria; CBJ88538; CBJ88538; XNC1_0464.
DR   KEGG; xne:XNC1_0464; -.
DR   eggNOG; ENOG4105C2N; Bacteria.
DR   eggNOG; COG0566; LUCA.
DR   HOGENOM; HOG000218798; -.
DR   KO; K03218; -.
DR   OMA; QVPPYEY; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_01887; 23SrRNA_methyltr_B; 1.
DR   InterPro; IPR024915; 23S_rRNA_MeTrfase_RlmB.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR004441; rRNA_MeTrfase_TrmH.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR013123; SpoU_subst-bd.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   Pfam; PF08032; SpoU_sub_bind; 1.
DR   SMART; SM00967; SpoU_sub_bind; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00186; rRNA_methyl_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VII8.
DR   SWISS-2DPAGE; D3VII8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01887};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01887,
KW   ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:CBJ88538.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01887};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01887};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01887,
KW   ECO:0000256|SAAS:SAAS00477754, ECO:0000313|EMBL:CBJ88538.1}.
FT   DOMAIN        4     80       SpoU_sub_bind. {ECO:0000259|SMART:
FT                                SM00967}.
FT   BINDING     196    196       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01887}.
FT   BINDING     216    216       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01887}.
FT   BINDING     225    225       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01887}.
SQ   SEQUENCE   245 AA;  26897 MW;  401753DB53B9619D CRC64;
     MSEIIYGIHA VKALLESDPQ RFMEVYVLKG REDRRLTPLF QELESIGITV QLANRQWLDA
     QTEGAVHQGI IARVKPGRQY QENDLPDLLS QLDRPFLLVL DGVTDPHNLG ACLRTADAAG
     VDAVIVPRDR SAQLNATAKK VACGAAENVP LIRVTNLART LRLLQEHNIW IVGTAGEATH
     ALYESKLTGP MALVMGAEGE GMRRLTREHC DELISIPMAG SVSSLNVSVA TGVCLFEIVR
     QRRSQ
//

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