Y788_STRMU
ID Y788_STRMU Reviewed; 451 AA.
AC Q8DUV4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Uncharacterized RNA methyltransferase SMU_788;
DE EC=2.1.1.-;
GN OrderedLocusNames=SMU_788;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01024}.
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DR EMBL; AE014133; AAN58507.1; -; Genomic_DNA.
DR RefSeq; NP_721201.1; NC_004350.2.
DR RefSeq; WP_002261942.1; NC_004350.2.
DR AlphaFoldDB; Q8DUV4; -.
DR SMR; Q8DUV4; -.
DR STRING; 210007.SMU_788; -.
DR PRIDE; Q8DUV4; -.
DR EnsemblBacteria; AAN58507; AAN58507; SMU_788.
DR KEGG; smu:SMU_788; -.
DR PATRIC; fig|210007.7.peg.698; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_7_0_9; -.
DR OMA; FYAGDMK; -.
DR PhylomeDB; Q8DUV4; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002792; TRAM_dom.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; PTHR11061; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS50926; TRAM; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..451
FT /note="Uncharacterized RNA methyltransferase SMU_788"
FT /id="PRO_0000162029"
FT DOMAIN 1..59
FT /note="TRAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT ACT_SITE 408
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 312
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 333
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 381
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 451 AA; 50838 MW; B0590A197CD33EBE CRC64;
MLKKNDIVEV EISDLSHDGA GIAKVDGLVF FVDNALPTEK IRMRVLKVKK NIAFGKVESY
LAKSAYRSDN LTVDYLRTGI ADLGHLTYGQ QLNFKRKQVI NSLSKIAGIS DIEVADTLGM
DNPTAYRNKA QVPVRRVNGQ LETGFFRKNS HALMPIEDYY IQDKEIDRLI NFTRDLLRRF
DLKPYDEKEQ TGLIRNLVVR RGHYTGQIML VLVTTRSKIF RIEQMIEKII SEFPAVKSII
QNINDRNTNA IFGSEFRTLY GEDTIEDTML GNRYIISAQS FYQVNTVMAE KLYQTAIDFS
DLTPDDTVID AYSGIGTIGL SFAKKVKDVY GVEVIEAAVR DAEKNAALNN ITNVHYVADS
AEKAMASWSK RGIKPDVILV DPPRKGLTES FIEASTAMQP RKITYISCAP ATMARDVKLY
EELGYKLVKV QPVDLFPQTH HVECVALLVK A