ID D2Q7M8_BIFDB Unreviewed; 329 AA.
AC D2Q7M8;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=SpoU rRNA methylase family protein {ECO:0000313|EMBL:ADB10790.1};
DE EC=2.1.1.34 {ECO:0000313|EMBL:ADB10790.1};
GN Name=spoU {ECO:0000313|EMBL:ADB10790.1};
GN OrderedLocusNames=BDP_2236 {ECO:0000313|EMBL:ADB10790.1};
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB10790.1, ECO:0000313|Proteomes:UP000008693};
RN [1] {ECO:0000313|EMBL:ADB10790.1, ECO:0000313|Proteomes:UP000008693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC {ECO:0000313|Proteomes:UP000008693};
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(2009).
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family.
CC {ECO:0000256|ARBA:ARBA00007228}.
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DR EMBL; CP001750; ADB10790.1; -; Genomic_DNA.
DR RefSeq; WP_003838445.1; NC_013714.1.
DR AlphaFoldDB; D2Q7M8; -.
DR STRING; 401473.BDP_2236; -.
DR GeneID; 69535818; -.
DR KEGG; bde:BDP_2236; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_0_0_11; -.
DR Proteomes; UP000008693; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0141100; F:tRNA (guanine(18)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd18103; SpoU-like_RlmB; 1.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
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 Methyltransferase {ECO:0000313|EMBL:ADB10790.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008693};
KW Transferase {ECO:0000313|EMBL:ADB10790.1}.
FT DOMAIN 69..145
FT /note="RNA 2-O ribose methyltransferase substrate binding"
FT /evidence="ECO:0000259|SMART:SM00967"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 329 AA; 34986 MW; 0D80D6705E870B16 CRC64;
MAMKKGPTKG SGGKHRNALR GKGPTPKAEN RVYHKAYKAK KVADRRKMAD PRLAARRRVA
KFASESDDLV IGRNAVLEAL RCGVPASTLY IAARIEHDDR TREIVRLAGI HGLHLMEADR
LEMDRIARSS NHQGIVMKAQ PFQYSSLAEL VERADKKSRA MEAANSAAAR IAARPLFIAL
DGVTDPQNLG AVIRSAAAFG ANGVILPERR SASVTAAAWK VSAGAAAHMP VARVVNLTKA
IESLKERGYY SIGLDGGGDA LVGETGFETD PLVVVLGSEG NGLSRLVRST CDVIAGIPMS
SMVESLNASV AAGITLYAVA RARREAANN
//
