ID   MTH1_HAEPA              Reviewed;         314 AA.
AC   P29538;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-MAY-2023, entry version 83.
DE   RecName: Full=Type II methyltransferase M.HpaI {ECO:0000303|PubMed:12654995};
DE            Short=M.HpaI {ECO:0000303|PubMed:1542567};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase HpaI;
DE   AltName: Full=Modification methylase HpaI;
GN   Name=hpaIM;
OS   Haemophilus parainfluenzae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49669;
RX   PubMed=1542567; DOI=10.1093/nar/20.4.705;
RA   Ito H., Shimato H., Sadaoka A., Kotani H., Kimizuka F., Kato I.;
RT   "Cloning and expression of the HpaI restriction-modification genes.";
RL   Nucleic Acids Res. 20:705-709(1992).
RN   [2]
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).
CC   -!- FUNCTION: A beta subtype methylase that recognizes the double-stranded
CC       sequence 5'-GTTAAC-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the HpaI endonuclease.
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 + H(+) + S-adenosyl-L-
CC         homocysteine; 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   -!- 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; D10668; BAA01519.1; -; Genomic_DNA.
DR   PIR; S28681; S28681.
DR   AlphaFoldDB; P29538; -.
DR   SMR; P29538; -.
DR   REBASE; 154999; M.VscVS12ORF3208P.
DR   REBASE; 157604; M.Rso10709ORF1624P.
DR   REBASE; 204128; M.Keu1446ORF2975P.
DR   REBASE; 3431; M.HpaI.
DR   PRO; PR:P29538; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..314
FT                   /note="Type II methyltransferase M.HpaI"
FT                   /id="PRO_0000087965"
SQ   SEQUENCE   314 AA;  37393 MW;  F72298845BF2778B CRC64;
     MDQRLICSNA IKALKNLEEN SIDLIITDPP YNLGKDYGTT DDNLNFNKYL EFSHEWLEEC
     YRVLKPHGTI YIFMGMKYIS YIYKILEQDL GMYFNSWITW YYTQGIGKTR GYSPRHDDIL
     MFTKHPKKFT FNLDRIRVPQ KYYRSVNNMR GANPSNVWEF SHVHYCNKNR KPHPTQKPEA
     LYERMILASS NEGDIVLDPF VGSGTLNFVC KHLNRSGIGI DINKEYIEMA KERLDSEFNG
     FDSIDERMKR CPNDLSDPVI RKQYIINHIN WFLKNHENAR EEFLNEVKTK YYKKMTQEEK
     RLLDKENNLS FDFS
//