ID A0A075R3N0_BRELA Unreviewed; 452 AA.
AC A0A075R3N0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Ribosomal RNA large subunit methyltransferase I {ECO:0000313|EMBL:AIG25743.1};
DE EC=2.1.1.191 {ECO:0000313|EMBL:AIG25743.1};
GN ORFNames=BRLA_c014040 {ECO:0000313|EMBL:AIG25743.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG25743.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG25743.1, ECO:0000313|Proteomes:UP000005850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG25743.1,
RC ECO:0000313|Proteomes:UP000005850};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI family.
CC {ECO:0000256|ARBA:ARBA00038091}.
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DR EMBL; CP007806; AIG25743.1; -; Genomic_DNA.
DR RefSeq; WP_003338208.1; NZ_CP007806.1.
DR AlphaFoldDB; A0A075R3N0; -.
DR STRING; 1042163.BRLA_c014040; -.
DR KEGG; blr:BRLA_c014040; -.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_0_0_9; -.
DR Proteomes; UP000005850; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd21153; PUA_RlmI; 1.
DR CDD; cd11572; RlmI_M_like; 1.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR Gene3D; 3.30.750.80; RNA methyltransferase domain (HRMD) like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR041532; RlmI-like_PUA.
DR InterPro; IPR019614; SAM-dep_methyl-trfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42873:SF1; METHYLTRANS_SAM DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42873; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE; 1.
DR Pfam; PF10672; Methyltrans_SAM; 1.
DR Pfam; PF17785; PUA_3; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AIG25743.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005850};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AIG25743.1}.
FT DOMAIN 2..87
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 452 AA; 51382 MW; 27606ABBDA143E64 CRC64;
MTKVLLQRNR KKRLEAGHPW VFQSEVLEIQ GDFLAGDIVE ICNHQGHFLA KGYINPDSQM
IVRVMSYNPK EEIDYDFFVR RFREAKETRE RFVNNPRACR VIYGEADFLP GLIVDRYNDV
LVMQVLSMGM DIRLDMIKMA LIEVFEPAGI YLRNDVPVRE LEGLEQGKGV LYGECPAEIE
IEENGLKYVV DIVEGQKTGF FYDQRENRAA IAPLMTGWGE KHGIKLLPIG EDDEPIYDKK
GKKRDVLPKM DEAGQPIQRP VDRRGKVMKN PFWDGAEVLE CFTHTGSFTL NACKHGAKKV
TALDISEHAI ETAKRNVGLN GYLHRVDFVV ANAFDYLREN VEAGKNWDVV ILDPPAFAKS
RGAVKGACRG YKDINLHGMK LVRPGGYLVT ASCSYHMSPD LFLETIQQAA YDAKKILRLI
EWRGAGKDHP QISGADEGHY LKFAIFEVRD RK
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