ID T3MO_ECOLX Reviewed; 644 AA. AC P12364; Q5ZND1; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 2. DT 04-NOV-2026, entry version 111. DE RecName: Full=Type III restriction-modification enzyme EcoP15I Mod subunit {ECO:0000303|PubMed:11178902}; DE Short=M.EcoP15I; DE EC=2.1.1.72 {ECO:0000305|PubMed:26067164}; DE AltName: Full=EcoP15I methyltransferase; DE AltName: Full=Type III methyltransferase M.EcoP15I {ECO:0000303|PubMed:12654995}; GN Name=mod {ECO:0000303|PubMed:2837577}; GN Synonyms=ecoP15Imod {ECO:0000303|PubMed:15464603}; OS Escherichia coli. OG Plasmid p15B. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC PLASMID=p15B; RX PubMed=2837577; DOI=10.1016/0022-2836(88)90330-0; RA Huembelin M., Suri B., Rao D.N., Hornby D.P., Eberle H., Pripfl T., RA Kenel S., Bickle T.A.; RT "Type III DNA restriction and modification systems EcoP1 and EcoP15. RT Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene and some EcoP1 RT mod mutants."; RL J. Mol. Biol. 200:23-29(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 156; 343; 472 RP AND 513. RC PLASMID=p15B; RX PubMed=15464603; DOI=10.1016/j.jbiotec.2004.06.014; RA Moencke-Buchner E., Mackeldanz P., Krueger D.H., Reuter M.; RT "Overexpression and affinity chromatography purification of the Type III RT restriction endonuclease EcoP15I for use in transcriptome analysis."; RL J. Biotechnol. 114:99-106(2004). RN [3] RP FUNCTION, AND SUBUNIT. RX PubMed=11178902; DOI=10.1006/jmbi.2000.4411; RA Janscak P., Sandmeier U., Szczelkun M.D., Bickle T.A.; RT "Subunit assembly and mode of DNA cleavage of the type III restriction RT endonucleases EcoP1I and EcoP15I."; RL J. Mol. Biol. 306:417-431(2001). RN [4] RP NOMENCLATURE, AND SUBTYPE. 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:4ZCF} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH RES AND DNA. RX PubMed=26067164; DOI=10.1038/ncomms8363; RA Gupta Y.K., Chan S.H., Xu S.Y., Aggarwal A.K.; RT "Structural basis of asymmetric DNA methylation and ATP-triggered long- RT range diffusion by EcoP15I."; RL Nat. Commun. 6:7363-7363(2015). CC -!- FUNCTION: A beta subtype methylase that binds the system-specific DNA CC recognition site 5'-CAGCAG-3' and methylates A-5 (of only 1 strand as CC the other does not have an A residue). DNA restriction requires both CC the Res and Mod subunits (PubMed:11178902, PubMed:12654995). The A-5 CC nucleotide flips into the catalytic pocket of one Mod subunit for CC modification, while the other Mod subunit makes most of the DNA CC sequence-specific contacts (PubMed:26067164). CC {ECO:0000269|PubMed:11178902, ECO:0000269|PubMed:26067164, CC ECO:0000303|PubMed:12654995}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an CC N(6)-methyl-2'-deoxyadenosine in DNA + S-adenosyl-L-homocysteine + CC H(+); Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA- CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72; CC Evidence={ECO:0000305|PubMed:26067164}; CC -!- SUBUNIT: Forms a homodimer capable of methylating the target sequence CC in the absence of Res (Probable). A heterotetramer with stoichiometry CC Res(2)Mod(2) (PubMed:11178902). A heterotrimer with stoichiometry CC Res(1)Mod(2) (PubMed:26067164). {ECO:0000269|PubMed:11178902, CC ECO:0000269|PubMed:26067164, ECO:0000305|PubMed:26067164}. CC -!- MISCELLANEOUS: This R-M system is also called EcoP15. CC {ECO:0000303|PubMed:2837577}. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {ECO:0000305}. 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; X06288; CAA29616.1; -; Genomic_DNA. DR EMBL; AJ634453; CAG24072.1; -; Genomic_DNA. DR PIR; S03208; S03208. DR PDB; 4ZCF; X-ray; 2.60 A; A/B=1-644. DR AlphaFoldDB; P12364; -. DR SMR; P12364; -. DR REBASE; 1083344; M.EcoP15I-mut1. DR REBASE; 3389; M.EcoP15I. DR BRENDA; 3.1.21.5; 2026. DR EvolutionaryTrace; P12364; -. DR PRO; PR:P12364; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR041405; T3RM_EcoP15I_C. DR Pfam; PF01555; N6_N4_Mtase; 1. DR Pfam; PF18273; T3RM_EcoP15I_C; 1. DR PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1. DR PRINTS; PR00506; D21N6MTFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Methyltransferase; Plasmid; Restriction system; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..644 FT /note="Type III restriction-modification enzyme EcoP15I Mod FT subunit" FT /id="PRO_0000088031" FT REGION 123..126 FT /note="Binding of S-adenosyl methionine" FT /evidence="ECO:0000255" FT CONFLICT 156 FT /note="E -> Q (in Ref. 1; CAA29616)" FT /evidence="ECO:0000305" FT CONFLICT 343 FT /note="K -> KQ (in Ref. 1; CAA29616)" FT /evidence="ECO:0000305" FT HELIX 14..24 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 37..44 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 63..71 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 82..86 FT /evidence="ECO:0007829|PDB:4ZCF" FT TURN 88..92 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 96..100 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 102..113 FT /evidence="ECO:0007829|PDB:4ZCF" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 117..122 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 143..150 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 154..164 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 171..188 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 189..199 FT /evidence="ECO:0007829|PDB:4ZCF" FT TURN 201..203 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 204..215 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 220..227 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 241..249 FT /evidence="ECO:0007829|PDB:4ZCF" FT TURN 251..253 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 264..279 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 283..296 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 308..310 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 313..318 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 324..326 FT /evidence="ECO:0007829|PDB:4ZCF" FT TURN 336..338 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 342..345 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 349..351 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 353..361 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 376..380 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 381..383 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 388..393 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 396..398 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 399..404 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 420..430 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 431..441 FT /evidence="ECO:0007829|PDB:4ZCF" FT TURN 443..445 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 446..455 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 457..459 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 461..468 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 480..482 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 487..500 FT /evidence="ECO:0007829|PDB:4ZCF" FT TURN 501..503 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 508..514 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 534..538 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 539..552 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 562..566 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 569..574 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 577..580 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 587..598 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 606..611 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 612..614 FT /evidence="ECO:0007829|PDB:4ZCF" FT HELIX 618..629 FT /evidence="ECO:0007829|PDB:4ZCF" FT STRAND 639..643 FT /evidence="ECO:0007829|PDB:4ZCF" SQ SEQUENCE 644 AA; 74094 MW; 01B84990BCD43A41 CRC64; MKKETIFSEV ETANSKQLAV LKANFPQCFD KNGAFIQEKL LEIIRASEVE LSKESYSLNW LGKSYARLLA NLPPKTLLAE DKTHNQQEEN KNSQHLLIKG DNLEVLKHMV NAYAEKVKMI YIDPPYNTGK DGFVYNDDRK FTPEQLSELA GIDLDEAKRI LEFTTKGSSS HSAWLTFIYP RLYIARELMR EDGTIFISID HNEFSQLKLV CDEIFGEQNH VGDLVWKNAT DNNPSNIAVE HEYIIVYTKN KEQLISEWKS NISDVKNLLV NIGEEFASKY TGNELQEKYT QWFREHRSEL WPLDRYKYID KDGIYTGSQS VHNPGKEGYR YDIIHPKTKK PCKQPLMGYR FPLDTMDRLL SEEKIIFGDD ENKIIELKVY AKDYKQKLSS VIHLDGRVAT NELKELFPEM TQPFTNAKTI KLVEDLISFA CDGEGIVLDF FAGSGTTAHT VFNLNNKNKT SYQFITVQLD EPTKDKSDAM KHGYNTIFDL TKERLIRASK KNRDQGFKVY QLMPDFRAKD ESELTLSNHT FFDDVVLTPE QYDTLLTTWC LYDGSLLTTP IEDVDLGGYK AHLCDGRLYL IAPNFTSEAL KALLQKVDSD KDFAPNKVVF YGSNFESAKQ MELNEALKSY ANKKSIELDL VVRN //