(data stored in SCRATCH zone)

SWISSPROT: C5BF71_EDWI9

ID   C5BF71_EDWI9            Unreviewed;       247 AA.
AC   C5BF71;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
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=NT01EI_0419 {ECO:0000313|EMBL:ACR67657.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67657.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67657.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67657.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
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; CP001600; ACR67657.1; -; Genomic_DNA.
DR   RefSeq; WP_015869861.1; NC_012779.2.
DR   EnsemblBacteria; ACR67657; ACR67657; NT01EI_0419.
DR   GeneID; 7961244; -.
DR   KEGG; eic:NT01EI_0419; -.
DR   PATRIC; fig|634503.3.peg.378; -.
DR   eggNOG; ENOG4105C2N; Bacteria.
DR   eggNOG; COG0566; LUCA.
DR   HOGENOM; HOG000218798; -.
DR   KO; K03218; -.
DR   OMA; QVPPYEY; -.
DR   OrthoDB; 1422015at2; -.
DR   BioCyc; EICT634503:G1GVC-391-MONOMER; -.
DR   Proteomes; UP000001485; 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; C5BF71.
DR   SWISS-2DPAGE; C5BF71.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01887};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01887,
KW   ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:ACR67657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
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:ACR67657.1}.
FT   DOMAIN        4     80       SpoU_sub_bind. {ECO:0000259|SMART:
FT                                SM00967}.
FT   BINDING     197    197       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01887}.
FT   BINDING     217    217       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01887}.
FT   BINDING     226    226       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01887}.
SQ   SEQUENCE   247 AA;  27031 MW;  F7CD5699479099EC CRC64;
     MSEIIYGIHA VKALLEQDPQ RFLDVFVMKG REDRRLLPLL QQLEECGIRV QVAQRQWLDE
     KVEGAVHQGI VARVKPGRQY QENDLPDLLA GLEHPPFLLI LDGVTDPHNL GACLRSADAA
     GVDAVIVPRD RSAQLNATAK KVACGAAENV PLIRVTNLAR TIRLLQQENI WIVGTAGEAD
     HSLYQSRMTG AMALVMGAEG DGMRRLTREH CDELISIPMA GSVSSLNVSV ATGICLFEVV
     RQRSAKA
//

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