ID MTS9_STAAU Reviewed; 430 AA. AC P23737; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 02-SEP-2026, entry version 127. DE RecName: Full=Type II methyltransferase M.Sau96I {ECO:0000303|PubMed:12654995}; DE Short=M.Sau96I {ECO:0000303|PubMed:2204026}; DE EC=2.1.1.37 {ECO:0000269|PubMed:2204026}; DE AltName: Full=Cytosine-specific methyltransferase Sau96I; DE AltName: Full=Modification methylase Sau96I; GN Name=sau96IM {ECO:0000303|PubMed:2204026}; OS Staphylococcus aureus. OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1280; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=PS96; RX PubMed=2204026; DOI=10.1093/nar/18.16.4659; RA Szilak L., Venetianer P., Kiss A.; RT "Cloning and nucleotide sequence of the genes coding for the Sau96I RT restriction and modification enzymes."; RL Nucleic Acids Res. 18:4659-4664(1990). RN [2] RP NOMENCLATURE. RX PubMed=12654995; DOI=10.1093/nar/gkg274; RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A., RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K., RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S., RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A., RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S., RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V., RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E., RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W., RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.; RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing RT endonucleases and their genes."; RL Nucleic Acids Res. 31:1805-1812(2003). CC -!- FUNCTION: A methylase that recognizes the double-stranded sequence 5'- CC GGNCC-3', methylates C-4 on both strands, and protects the DNA from CC cleavage by the Sau96I endonuclease. {ECO:0000269|PubMed:2204026, CC ECO:0000303|PubMed:12654995}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5- CC methyl-2'-deoxycytidine in DNA + S-adenosyl-L-homocysteine + H(+); CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018, CC ECO:0000269|PubMed:2204026}; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE- CC ProRule:PRU01016}. 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; X53096; CAA37260.1; -; Genomic_DNA. DR PIR; S12705; S12705. DR RefSeq; WP_001238815.1; NZ_AP017922.1. DR AlphaFoldDB; P23737; -. DR SMR; P23737; -. DR REBASE; 182835; M.Bli37ORF2575P. DR REBASE; 182836; M.Bli14ORF1492P. DR REBASE; 182841; M.Bli34ORF1606P. DR REBASE; 195420; M.BliB11ORF1170P. DR REBASE; 204712; M.Bso1395ORF4807P. DR REBASE; 3496; M.Sau96I. DR PATRIC; fig|1280.3540.peg.2442; -. DR PRO; PR:P23737; -. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; EXP:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0044027; P:negative regulation of gene expression via chromosomal CpG island methylation; IEA:TreeGrafter. DR CDD; cd00315; Cyt_C5_DNA_methylase; 1. DR CDD; cd00093; HTH_XRE; 1. DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1. DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR050390; C5-Methyltransferase. DR InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR031303; C5_meth_CS. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00675; dcm; 1. DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1. DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1. DR Pfam; PF00145; DNA_methylase; 1. DR Pfam; PF01381; HTH_3; 1. DR PRINTS; PR00105; C5METTRFRASE. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS00094; C5_MTASE_1; 1. DR PROSITE; PS00095; C5_MTASE_2; 1. DR PROSITE; PS50943; HTH_CROC1; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. PE 1: Evidence at protein level; KW DNA-binding; Methyltransferase; Restriction system; KW S-adenosyl-L-methionine; Transcription; Transcription regulation; KW Transferase. FT CHAIN 1..430 FT /note="Type II methyltransferase M.Sau96I" FT /id="PRO_0000087908" FT DOMAIN 9..63 FT /note="HTH cro/C1-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257" FT DOMAIN 99..429 FT /note="SAM-dependent MTase C5-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" FT ACT_SITE 174 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016, FT ECO:0000255|PROSITE-ProRule:PRU10018" SQ SEQUENCE 430 AA; 49284 MW; 884FBD96F4890651 CRC64; MRLNKGSIIE KMKNQNIKTQ TELAEKIDIS KSQLSFMFSD EYEPLKKNVI KLADVLKVSP NDIILDEEDQ MPINSDFNRY DYKLDEFIDV SNVRKNKDYN VFETFAGAGG LALGLESAGL STYGAVEIDK NAAETLRINR PKWKVIENDI EFIADNLDEF IDEEIDILSG GYPCQTFSYA GKRNGFADTR GTLFYPYSKI LSKLKPKAFI AENVRGLVNH DDGKTLEVML KVFIKEGYEV YWNILNSWNY DVAQKRERIV IIGIREDLVK EQKYPFRFPL AQVYKPVLKD VLKDVPKSKV TAYSDKKREV MKLVPPGGCW VDLPEQIAKD YMGKSWYSGG GKRGMARRIS WDEPCLTLTT SPSQKQTERC HPDETRPFSI REYARIQSFP DEWEFSGGVG AQYRQIGNAV PVNLAKYIGK SLVHYLNQFN //