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Database: UniProt
Entry: X2JP37_AGGAC
LinkDB: X2JP37_AGGAC
Original site: X2JP37_AGGAC 
ID   X2JP37_AGGAC            Unreviewed;       245 AA.
AC   X2JP37;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   ORFNames=CF65_01374 {ECO:0000313|EMBL:AHN71753.1};
OS   Aggregatibacter actinomycetemcomitans HK1651.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=272556 {ECO:0000313|EMBL:AHN71753.1, ECO:0000313|Proteomes:UP000019758};
RN   [1] {ECO:0000313|EMBL:AHN71753.1, ECO:0000313|Proteomes:UP000019758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK1651 {ECO:0000313|EMBL:AHN71753.1,
RC   ECO:0000313|Proteomes:UP000019758};
RA   Gillaspy A.F., Griffin J., Najar F., Hinkle J., Lewis L.A.,
RA   McLaughlin R.E., Hartman K., Nydick C., Gipson M., Conway B., Vaughn J.,
RA   Thompson C., Gipson J., Maddera L., Carson M., Kenton S., Lai H., Roe B.A.,
RA   Orvis J., Zaitshik J., Griffin J., Scott E., Dyer D.W.;
RT   "Genome sequencing and closure of the periodontal pathogen, Aggregatibacter
RT   actinomycetemcomitans.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the ribose of guanosine 2251 in 23S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01887}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-
CC         methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:24140, Rhea:RHEA-COMP:10239, Rhea:RHEA-COMP:10241,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.185;
CC         Evidence={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 methyltransferase
CC       superfamily. RNA methyltransferase TrmH family. RlmB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01887}.
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DR   EMBL; CP007502; AHN71753.1; -; Genomic_DNA.
DR   RefSeq; WP_005544885.1; NZ_CP007502.1.
DR   AlphaFoldDB; X2JP37; -.
DR   SMR; X2JP37; -.
DR   KEGG; aah:CF65_01374; -.
DR   PATRIC; fig|272556.10.peg.962; -.
DR   eggNOG; COG0566; Bacteria.
DR   HOGENOM; CLU_021322_0_1_6; -.
DR   Proteomes; UP000019758; 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   CDD; cd18103; SpoU-like_RlmB; 1.
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; Ribosomal_eL30-like_sf.
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   NCBIfam; TIGR00186; rRNA_methyl_3; 1.
DR   PANTHER; PTHR46429; 23S RRNA (GUANOSINE-2'-O-)-METHYLTRANSFERASE RLMB; 1.
DR   PANTHER; PTHR46429:SF1; 23S RRNA (GUANOSINE-2'-O-)-METHYLTRANSFERASE RLMB; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   Pfam; PF08032; SpoU_sub_bind; 1.
DR   SMART; SM00967; SpoU_sub_bind; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
DR   SUPFAM; SSF55315; L30e-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01887};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01887};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_01887};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01887};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01887}.
FT   DOMAIN          4..80
FT                   /note="RNA 2-O ribose methyltransferase substrate binding"
FT                   /evidence="ECO:0000259|SMART:SM00967"
FT   BINDING         197
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
FT   BINDING         217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
SQ   SEQUENCE   245 AA;  27048 MW;  F7D24494DA0C0DB3 CRC64;
     MSETIYGIHA VKAFVTHYPE RLIEVWALKG RDDQRLQPLI NEIQRLGISV QFLNRQTLDK
     KAEGEVHQGI IARVHSLPEL NEHDLDRLLE QQNTPLLLVL DGVTDPHNLG ACLRTADAAG
     VNAVIVPKDK SAQLNSTARK VACGAAENVP LIRVTNLART LRELQKRHNV WVVGTAGETT
     ETLYQTKLTG ALALVMGAEG EGMRRLTREH CDQLISIPMM GSVSSLNVSV ATGVCLFEIV
     RQRLK
//
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