MTP2_PROHU
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 03-AUG-2022, entry version 123.
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; Proteobacteria; 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 / NCTC
RC 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 / NCTC
RC 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 PDB; 1BOO; X-ray; 2.80 A; A=14-336.
DR PDBsum; 1BOO; -.
DR AlphaFoldDB; P11409; -.
DR SMR; P11409; -.
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:0032775; P:DNA methylation on adenine; IDA:CAFA.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:0090124; P:N-4 methylation of cytosine; IDA:CAFA.
DR Gene3D; 3.40.50.150; -; 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; SSF53335; 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
