ID MTP2_PROHU Reviewed; 336 AA. AC P11409; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 24-JAN-2024, entry version 127. DE RecName: Full=Type II methyltransferase M.PvuII {ECO:0000303|PubMed:12654995}; DE Short=M.PvuII {ECO:0000303|PubMed:2662138}; DE EC=2.1.1.113; DE AltName: Full=Modification methylase PvuII; DE AltName: Full=N-4 cytosine-specific methyltransferase PvuII; GN Name=pvuIIM {ECO:0000303|PubMed:2662138}; OS Proteus hauseri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Proteus. OX NCBI_TaxID=183417; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / RC NCTC 4175 / NRRL B-3405; RX PubMed=2662138; DOI=10.1093/nar/17.11.4161; RA Tao T., Walter J., Brennan K.J., Cotterman M.M., Blumenthal R.M.; RT "Sequence, internal homology and high-level expression of the gene for a RT DNA-(cytosine N4)-methyltransferase, M.Pvu II."; RL Nucleic Acids Res. 17:4161-4175(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80, AND SEQUENCE REVISION TO 44. RC STRAIN=ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / RC NCTC 4175 / NRRL B-3405; RX PubMed=7607491; DOI=10.1016/0378-1119(94)00704-v; RA Adams G.M., Blumenthal R.M.; RT "Gene pvuIIW: a possible modulator of PvuII endonuclease subunit RT association."; RL Gene 157:193-199(1995). RN [3] 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 [4] {ECO:0007744|PDB:1BOO} RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 14-336, AND SUBUNIT. RX PubMed=9207015; DOI=10.1093/nar/25.14.2702; RA Gong W., O'Gara M., Blumenthal R.M., Cheng X.; RT "Structure of Pvu II DNA-(cytosine N4) methyltransferase, an example of RT domain permutation and protein fold assignment."; RL Nucleic Acids Res. 25:2702-2715(1997). CC -!- FUNCTION: A beta subtype methylase, recognizes the double-stranded CC sequence 5'-CAGCTG-3', methylates C-4 on both strands, and protects the CC DNA from cleavage by the PvuII endonuclease. CC {ECO:0000303|PubMed:12654995}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)- CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9207015}. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4) CC subfamily. {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; X13778; CAA32026.1; -; Genomic_DNA. DR EMBL; AF305615; AAA96336.1; -; Genomic_DNA. DR PIR; S04739; S04739. DR RefSeq; WP_010904457.1; NZ_PGWU01000024.1. DR PDB; 1BOO; X-ray; 2.80 A; A=14-336. DR PDBsum; 1BOO; -. DR AlphaFoldDB; P11409; -. DR SMR; P11409; -. DR STRING; 1354271.M997_3410; -. DR DrugBank; DB01752; S-adenosyl-L-homocysteine. DR REBASE; 182811; M.DspNSZ14ORF374P. DR REBASE; 3485; M.PvuII. DR BRENDA; 2.1.1.113; 14542. DR EvolutionaryTrace; P11409; -. DR PRO; PR:P11409; -. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0008170; F:N-methyltransferase activity; IDA:CAFA. DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IDA:CAFA. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR017985; MeTrfase_CN4_CS. DR InterPro; IPR001091; RM_Methyltransferase. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS00093; N4_MTASE; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Methyltransferase; Repeat; Restriction system; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..336 FT /note="Type II methyltransferase M.PvuII" FT /id="PRO_0000087931" FT REPEAT 11..113 FT /note="1" FT REPEAT 181..293 FT /note="2" FT REGION 196..215 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 44 FT /note="D -> E (in Ref. 1; CAA32026)" FT /evidence="ECO:0000305" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:1BOO" FT STRAND 26..33 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 35..38 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:1BOO" FT STRAND 47..52 FT /evidence="ECO:0007829|PDB:1BOO" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 68..86 FT /evidence="ECO:0007829|PDB:1BOO" FT STRAND 87..97 FT /evidence="ECO:0007829|PDB:1BOO" FT STRAND 105..108 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 111..121 FT /evidence="ECO:0007829|PDB:1BOO" FT STRAND 126..134 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 144..148 FT /evidence="ECO:0007829|PDB:1BOO" FT STRAND 157..168 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:1BOO" FT STRAND 221..224 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 232..240 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 253..262 FT /evidence="ECO:0007829|PDB:1BOO" FT STRAND 268..271 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 278..285 FT /evidence="ECO:0007829|PDB:1BOO" FT STRAND 289..295 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 297..304 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:1BOO" FT HELIX 314..325 FT /evidence="ECO:0007829|PDB:1BOO" SQ SEQUENCE 336 AA; 38365 MW; 084371A667F86B91 CRC64; MMTLNLQTMS SNDMLNFGKK PAYTTSNGSM YIGDSLELLE SFPDESISLV MTSPPFALQR KKEYGNLEQH EYVDWFLSFA KVVNKKLKPD GSFVVDFGGA YMKGVPARSI YNFRVLIRMI DEVGFFLAED FYWFNPSKLP SPIEWVNKRK IRVKDAVNTV WWFSKTEWPK SDITKVLAPY SDRMKKLIED PDKFYTPKTR PSGHDIGKSF SKDNGGSIPP NLLQISNSES NGQYLANCKL MGIKAHPARF PAKLPEFFIR MLTEPDDLVV DIFGGSNTTG LVAERESRKW ISFEMKPEYV AASAFRFLDN NISEEKITDI YNRILNGESL DLNSII //