ID Q8DUW5_STRMU Unreviewed; 385 AA. AC Q8DUW5; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 31-MAY-2011, entry version 45. DE SubName: Full=Putative uncharacterized protein; GN OrderedLocusNames=SMU_776; OS Streptococcus mutans. OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700610 / UA159 / Serotype c; RX MEDLINE=22295063; PubMed=12397186; DOI=10.1073/pnas.172501299; RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., RA Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., RA Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., RA 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). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS). RA Nan J., Wang K.T., Su X.D.; RT "A putative sam-dependent methyltransferase from Streptococcus RT mutans."; RL Submitted (OCT-2005) to the PDB data bank. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-HOMOCYSTEINE. RA Wang K.-T., Nan J., Su X.-D.; RT "Crystal structure of SMU.776 complexed with SAH."; RL Submitted (JAN-2010) to the PDB data bank. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; AE014133; AAN58496.1; -; Genomic_DNA. DR RefSeq; NP_721190.1; NC_004350.1. DR PDB; 2B78; X-ray; 2.00 A; A=1-385. DR PDB; 3LDF; X-ray; 2.23 A; A=1-385. DR PDBsum; 2B78; -. DR PDBsum; 3LDF; -. DR ProteinModelPortal; Q8DUW5; -. DR SMR; Q8DUW5; 1-385. DR EnsemblBacteria; EBSTRT00000014034; EBSTRP00000013516; EBSTRG00000014034. DR GeneID; 1028166; -. DR GenomeReviews; AE014133_GR; SMU_776. DR KEGG; smu:SMU.776; -. DR NMPDR; fig|210007.1.peg.703; -. DR GeneTree; EBGT00050000027121; -. DR HOGENOM; HBG514942; -. DR OMA; YLNDGAM; -. DR ProtClustDB; CLSK876711; -. DR BioCyc; SMUT210007:SMU_776-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR InterPro; IPR015947; PUA-like. DR InterPro; IPR019614; SAM-dep_methyl-trfase. DR Pfam; PF10672; Methyltrans_SAM; 1. DR SUPFAM; SSF88697; PUA-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT REGION 220 222 S-adenosyl-L-homocysteine binding. FT REGION 242 246 S-adenosyl-L-homocysteine binding. FT REGION 270 272 S-adenosyl-L-homocysteine binding. FT REGION 292 297 S-adenosyl-L-homocysteine binding. FT BINDING 196 196 S-adenosyl-L-homocysteine. FT BINDING 226 226 S-adenosyl-L-homocysteine. SQ SEQUENCE 385 AA; 43682 MW; D025EF430B79A23B CRC64; MIKLMVGSFA EKKLKRGVQL LSSRDYPNLN LDNQVVQLYS DADIFLGTAY LSKQNKGVGW LISPKKVSLN VTYFIKLFQW SKDKRKNFAH SKLTTAYRLF NQDGDSFGGV TIDCYGDFVL FSWYNSFVYQ IRDEIVAAFR QVYPNFLGAY EKIRFKGIDN VSAHLYGQEA PEQFLILENG ISYNVFLNDG LMTGIFLDQR QVRNELINGS AAGKTVLNLF SYTAAFSVAA AMGGAMATTS VDLAKRSRAL SLAHFEANHL DMANHQLVVM DVFDYFKYAR RHHLTYDIII IDPPSFARNK KEVFSVSKDY HKLIRQGLEI LSENGLIIAS TNAANMTVSQ FKKQIEKGFG KQKHTYLDLQ QLPSDFAVNV QDESSNYLKV FTIKV //