Y5079_MYCMM
ID Y5079_MYCMM Reviewed; 310 AA.
AC B2HJ20;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Uncharacterized tRNA/rRNA methyltransferase MMAR_5079;
DE EC=2.1.1.-;
GN OrderedLocusNames=MMAR_5079;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000854; ACC43483.1; -; Genomic_DNA.
DR RefSeq; WP_012396601.1; NC_010612.1.
DR AlphaFoldDB; B2HJ20; -.
DR SMR; B2HJ20; -.
DR STRING; 216594.MMAR_5079; -.
DR EnsemblBacteria; ACC43483; ACC43483; MMAR_5079.
DR GeneID; 64258340; -.
DR KEGG; mmi:MMAR_5079; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_0_0_11; -.
DR OMA; QVPPYEY; -.
DR OrthoDB; 1422015at2; -.
DR Proteomes; UP000001190; 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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..310
FT /note="Uncharacterized tRNA/rRNA methyltransferase
FT MMAR_5079"
FT /id="PRO_0000379575"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 32508 MW; 5202801C3696F721 CRC64;
MAGNSQRRGA IRKSGTKKGT SVGSGGQRRR GLEGRGPTPP AHMRPNHPAA KRAKAQQRRP
ARGRTDETET VLGRNPVLEC LRAGVPSTAL YVALGVEADE RLTESVSRAA DSGIPILEVP
RTDLDRMTAN HLHQGIALQV PPYNYAHPDD LLAAALDTPP ALLVALDNIS DPRNLGAIVR
SVAAFGGHGV LIPQRRSASV TAVAWRTSAG AAARMPVARA TNLTRALKDW ADRGVRVVGL
DAGGDTAIDD LDGSDPIVVV VGSEGKGLSR LVRQTCDEVV SVPMAGPTES LNASVAAGVV
LAEIARQRRT