ID Q8DUW5_STRMU Unreviewed; 385 AA. AC Q8DUW5; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 26-FEB-2020, entry version 107. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAN58496.1}; GN OrderedLocusNames=SMU_776 {ECO:0000313|EMBL:AAN58496.1}; OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58496.1, ECO:0000313|Proteomes:UP000002512}; RN [1] {ECO:0000313|EMBL:AAN58496.1, ECO:0000313|Proteomes:UP000002512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512}; RX PubMed=12397186; DOI=10.1073/pnas.172501299; RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H., RA Najar F., 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). RN [2] {ECO:0000213|PDB:2B78} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS). RA Nan J., Wang K.T., Su X.D.; RT "A putative sam-dependent methyltransferase from Streptococcus mutans."; RL Submitted (OCT-2005) to the PDB data bank. RN [3] {ECO:0000213|PDB:3LDF} 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 {ECO:0000256|SAAS:SAAS00351055}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI family. CC {ECO:0000256|SAAS:SAAS00545036}. 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_004350.2. DR RefSeq; WP_002263895.1; NC_004350.2. 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 SMR; Q8DUW5; -. DR STRING; 210007.SMU_776; -. DR PRIDE; Q8DUW5; -. DR EnsemblBacteria; AAN58496; AAN58496; SMU_776. DR GeneID; 1028166; -. DR KEGG; smu:SMU_776; -. DR PATRIC; fig|210007.7.peg.687; -. DR eggNOG; ENOG4105DR4; Bacteria. DR eggNOG; COG1092; LUCA. DR HOGENOM; CLU_014042_1_2_9; -. DR KO; K06969; -. DR OMA; VMDVFDY; -. DR PhylomeDB; Q8DUW5; -. DR BioCyc; SMUT210007:G1FZX-746-MONOMER; -. DR EvolutionaryTrace; Q8DUW5; -. DR Proteomes; UP000002512; 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 Gene3D; 2.30.130.10; -; 1. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR036974; PUA_sf. DR InterPro; IPR041532; RlmI_PUA-like. DR InterPro; IPR019614; SAM-dep_methyl-trfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF10672; Methyltrans_SAM; 1. DR Pfam; PF17785; PUA_3; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF88697; SSF88697; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2B78, ECO:0000213|PDB:3LDF}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00428966}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00429068}; KW Reference proteome {ECO:0000313|Proteomes:UP000002512}; KW RNA-binding {ECO:0000256|SAAS:SAAS00977754}; KW rRNA processing {ECO:0000256|SAAS:SAAS00429013}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00429032}; KW Transferase {ECO:0000256|SAAS:SAAS00429003}. FT DOMAIN 10..63 FT /note="PUA_3" FT /evidence="ECO:0000259|Pfam:PF17785" FT DOMAIN 160..341 FT /note="Methyltrans_SAM" FT /evidence="ECO:0000259|Pfam:PF10672" FT REGION 242..246 FT /note="S-adenosyl-L-homocysteine binding" FT /evidence="ECO:0000213|PDB:3LDF" FT BINDING 220 FT /note="S-adenosyl-L-homocysteine; via carbonyl oxygen" FT /evidence="ECO:0000213|PDB:3LDF" FT BINDING 272 FT /note="S-adenosyl-L-homocysteine; via amide nitrogen" FT /evidence="ECO:0000213|PDB:3LDF" FT BINDING 292 FT /note="S-adenosyl-L-homocysteine" FT /evidence="ECO:0000213|PDB:3LDF" 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 //