Y3644_MYCBP
ID Y3644_MYCBP Reviewed; 322 AA.
AC A1KPR5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Uncharacterized tRNA/rRNA methyltransferase BCG_3644c;
DE EC=2.1.1.-;
GN OrderedLocusNames=BCG_3644c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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DR EMBL; AM408590; CAL73633.1; -; Genomic_DNA.
DR RefSeq; WP_003419423.1; NC_008769.1.
DR AlphaFoldDB; A1KPR5; -.
DR SMR; A1KPR5; -.
DR PRIDE; A1KPR5; -.
DR KEGG; mbb:BCG_3644c; -.
DR HOGENOM; CLU_021322_0_0_11; -.
DR OMA; QVPPYEY; -.
DR Proteomes; UP000001472; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
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 PANTHER; PTHR46429; PTHR46429; 1.
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;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..322
FT /note="Uncharacterized tRNA/rRNA methyltransferase
FT BCG_3644c"
FT /id="PRO_0000379571"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 33952 MW; C02D12F7512B171D CRC64;
MPGNSRRRGA VRKSGTKKGA GVGSGGQRRR GLEGRGPTPP AHLRPHHPAA KRARAQPRRP
VKRADETETV LGRNPVLECL RAGVPATALY VALGTEADER LTECVARAAD SGIAIVELLR
ADLDRMTANH LHQGIALQVP PYNYAHPDDL LAAALDQPPA LLVALDNLSD PRNLGAIVRS
VAAFGGHGVL IPQRRSASVT AVAWRTSAGA AARIPVARAT NLTRTLKGWA DRGVRVIGLD
AGGGTALDDV DGTDSLVVVV GSEGKGLSRL VRQNCDEVVS IPMAAQAESL NASVAAGVVL
AAIARQRRRP REPREQTQNR MI