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Database: UniProt
Entry: C6M476_NEISI
LinkDB: C6M476_NEISI
Original site: C6M476_NEISI 
ID   C6M476_NEISI            Unreviewed;       249 AA.
AC   C6M476;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
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=NEISICOT_01319 {ECO:0000313|EMBL:EET44989.1};
OS   Neisseria sicca ATCC 29256.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=547045 {ECO:0000313|EMBL:EET44989.1, ECO:0000313|Proteomes:UP000005365};
RN   [1] {ECO:0000313|EMBL:EET44989.1, ECO:0000313|Proteomes:UP000005365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29256 {ECO:0000313|EMBL:EET44989.1,
RC   ECO:0000313|Proteomes:UP000005365};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUL-2009) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EET44989.1}.
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DR   EMBL; ACKO02000006; EET44989.1; -; Genomic_DNA.
DR   RefSeq; WP_003757497.1; NZ_ACKO02000006.1.
DR   AlphaFoldDB; C6M476; -.
DR   STRING; 490.A6J88_07255; -.
DR   eggNOG; COG0566; Bacteria.
DR   Proteomes; UP000005365; Unassembled WGS sequence.
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          6..82
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   249 AA;  27273 MW;  F100C71E3921034F CRC64;
     MANQRLIYGF HAVNARLWQN PKSITELYVQ EGKNDARTRD VLEKAANENV RVHFADADRL
     NAISKGARHQ GVVGFIDASK NHVHLEDVLE NLSEPPLLLI LDGITDPHNL GACLRTADAM
     GVHAVIAPKD KSAGLNATVS KVACGAAETV PYITVTNLAR TLRELKEYGI WIIGTDMGGD
     SDLYHCDLPD SAAWVMGNEG EGMRRLTREH CDMLVSIPMF GTVESMNVSV SAGMVLSETR
     RQRVLKAEK
//
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