ID MTH3_HAEAE Reviewed; 330 AA. AC P20589; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 13-SEP-2023, entry version 115. DE RecName: Full=Type II methyltransferase M.HaeIII {ECO:0000303|PubMed:12654995}; DE Short=M.HaeIII {ECO:0000303|PubMed:1932026}; DE EC=2.1.1.37 {ECO:0000269|PubMed:1932026}; DE AltName: Full=Cytosine-specific methyltransferase HaeIII; DE AltName: Full=Modification methylase HaeIII; GN Name=haeIIIM; OS Haemophilus aegyptius. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=197575; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 11116 / CCUG 25716 / NCTC 8502 / 180-a; RX PubMed=3248732; DOI=10.1016/0378-1119(88)90248-x; RA Slatko B.E., Croft R., Moran L.S., Wilson G.G.; RT "Cloning and analysis of the HaeIII and HaeII methyltransferase genes."; RL Gene 74:45-50(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 11116 / CCUG 25716 / NCTC 8502 / 180-a; RA Zhang B.-H., Wilson G.G.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 62-81, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND RP DNA-BINDING. RX PubMed=1932026; DOI=10.1021/bi00110a002; RA Chen L., McMillan A.M., Chang W., Ezak-Nipkay K., Lane W.S., Verdine G.L.; RT "Direct identification of the active-site nucleophile in a DNA (cytosine- RT 5)-methyltransferase."; RL Biochemistry 30:11018-11025(1991). RN [4] 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). RN [5] {ECO:0007744|PDB:1DCT} RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH DNA, AND SUBUNIT. RX PubMed=7606780; DOI=10.1016/0092-8674(95)90060-8; RA Reinisch K.M., Chen L., Verdine G.L., Lipscomb W.N.; RT "The crystal structure of HaeIII methyltransferase covalently complexed to RT DNA: an extrahelical cytosine and rearranged base pairing."; RL Cell 82:143-153(1995). RN [6] {ECO:0007744|PDB:3UBT} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF MUTANT SER-71 IN COMPLEX WITH RP ATP, SUBUNIT, AND MUTAGENESIS OF CYS-71. RX PubMed=23012373; DOI=10.1074/jbc.m112.413054; RA Didovyk A., Verdine G.L.; RT "Structural origins of DNA target selection and nucleobase extrusion by a RT DNA cytosine methyltransferase."; RL J. Biol. Chem. 287:40099-40105(2012). CC -!- FUNCTION: A methylase, recognizes the double-stranded sequence 5'-GGCC- CC 3', methylates C-3 on both strands, and protects the DNA from cleavage CC by the HaeIII endonuclease. {ECO:0000269|PubMed:1932026, 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 + H(+) + S-adenosyl-L-homocysteine; 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:1932026}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23012373, CC ECO:0000269|PubMed:7606780}. 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; M24625; AAA24970.1; -; Genomic_DNA. DR EMBL; AF051375; AAC05696.1; -; Genomic_DNA. DR PIR; JS0102; JS0102. DR RefSeq; WP_013527695.1; NZ_UGHG01000002.1. DR PDB; 1DCT; X-ray; 2.80 A; A/B=1-324. DR PDB; 3UBT; X-ray; 2.50 A; A/B/Y=1-330. DR PDBsum; 1DCT; -. DR PDBsum; 3UBT; -. DR AlphaFoldDB; P20589; -. DR SMR; P20589; -. DR REBASE; 3410; M.HaeIII. DR BRENDA; 2.1.1.37; 2525. DR EvolutionaryTrace; P20589; -. DR PRO; PR:P20589; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR CDD; cd00315; Cyt_C5_DNA_methylase; 1. DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR031303; C5_meth_CS. 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 PRINTS; PR00105; C5METTRFRASE. 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; PS51679; SAM_MT_C5; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Direct protein sequencing; DNA-binding; KW Methyltransferase; Nucleotide-binding; Restriction system; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..330 FT /note="Type II methyltransferase M.HaeIII" FT /id="PRO_0000087878" FT DOMAIN 1..327 FT /note="SAM-dependent MTase C5-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" FT ACT_SITE 71 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016, FT ECO:0000255|PROSITE-ProRule:PRU10018, FT ECO:0000269|PubMed:1932026" FT BINDING 29 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007744|PDB:3UBT" FT BINDING 50..51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007744|PDB:3UBT" FT BINDING 260 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007744|PDB:3UBT" FT MUTAGEN 71 FT /note="C->S: No longer has methyltransferase activity, FT binds DNA in a wild-type manner." FT /evidence="ECO:0000269|PubMed:23012373" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 12..19 FT /evidence="ECO:0007829|PDB:3UBT" FT STRAND 23..29 FT /evidence="ECO:0007829|PDB:3UBT" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 35..41 FT /evidence="ECO:0007829|PDB:3UBT" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:3UBT" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:3UBT" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:1DCT" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:1DCT" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 89..101 FT /evidence="ECO:0007829|PDB:3UBT" FT STRAND 104..110 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 113..116 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:1DCT" FT HELIX 121..133 FT /evidence="ECO:0007829|PDB:3UBT" FT STRAND 135..143 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:3UBT" FT STRAND 154..162 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:3UBT" FT STRAND 189..191 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:3UBT" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:1DCT" FT STRAND 255..258 FT /evidence="ECO:0007829|PDB:3UBT" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:3UBT" FT TURN 266..268 FT /evidence="ECO:0007829|PDB:1DCT" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 277..284 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 297..305 FT /evidence="ECO:0007829|PDB:3UBT" FT HELIX 310..326 FT /evidence="ECO:0007829|PDB:3UBT" SQ SEQUENCE 330 AA; 37686 MW; 928C6D5390DBED25 CRC64; MNLISLFSGA GGLDLGFQKA GFRIICANEY DKSIWKTYES NHSAKLIKGD ISKISSDEFP KCDGIIGGPP CQSWSEGGSL RGIDDPRGKL FYEYIRILKQ KKPIFFLAEN VKGMMAQRHN KAVQEFIQEF DNAGYDVHII LLNANDYGVA QDRKRVFYIG FRKELNINYL PPIPHLIKPT FKDVIWDLKD NPIPALDKNK TNGNKCIYPN HEYFIGSYST IFMSRNRVRQ WNEPAFTVQA SGRQCQLHPQ APVMLKVSKN LNKFVEGKEH LYRRLTVREC ARVQGFPDDF IFHYESLNDG YKMIGNAVPV NLAYEIAKTI KSALEICKGN //