MTH1_HAEPA
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-AUG-2022, entry version 80.
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; Proteobacteria; 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}.
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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 Gene3D; 3.40.50.150; -; 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 Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 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