ID   MTHC_HAEIF              Reviewed;         502 AA.
AC   P17744;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Type II methyltransferase M.HincII {ECO:0000303|PubMed:12654995};
DE            Short=M.HincII {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase HincII;
DE   AltName: Full=Modification methylase HincII;
GN   Name=hincIIM {ECO:0000303|PubMed:2374714};
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=RC;
RX   PubMed=2374714; DOI=10.1093/nar/18.13.3903;
RA   Ito H., Sadaoka A., Kotani H., Hiraoka N., Nakamura T.;
RT   "Cloning, nucleotide sequence, and expression of the HincII restriction-
RT   modification system.";
RL   Nucleic Acids Res. 18:3903-3911(1990).
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 gamma subtype methylase that recognizes the double-stranded
CC       sequence 5'-GTYRAC-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the HincII endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:2374714}.
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; X52124; CAA36369.1; -; Genomic_DNA.
DR   AlphaFoldDB; P17744; -.
DR   SMR; P17744; -.
DR   PRO; PR:P17744; -.
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; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; RM_methylase_Eco57I-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF07669; Eco57I; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
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..502
FT                   /note="Type II methyltransferase M.HincII"
FT                   /id="PRO_0000087973"
SQ   SEQUENCE   502 AA;  58776 MW;  2536FA72B2F1720A CRC64;
     MDESKKISLG QFFTPTHIVK YMIGLMTKNK NASILEPSSG NGVFLDSLIQ LGYTNLTSYE
     IDGDIISHPF VINSSFITSY DKPQYDSIIG NPPYVRWKNL SELQKKELKD NSIWKMYCNS
     LCDYFYIFII KSILQLKVGG ELIFICPDYF FSTKNAEGLR KFLINNGSFE KIILFNESKV
     FHGVSSSVVI FKYIKGKNID NINIINIDSK SPIKSEDIES LGESYYIPRF SSSDVWVTSP
     NHIKVALDKF ESYCKTIKKV QQKSLFDDLS FLDKAFQMND INYSELELLN SICVAKAKHL
     DAFCFSGYTR YKLILDDNNE DKLITYFPNF FYEFNNYKDY LLKRYSYNKY LPYWEVAFLR
     NFSLFSKNEK KIFVPCKERI SKKSNFRFSL VDEFIYPTQD VTALYKKENV KESIEYITAY
     LNSKAVFLWM KYKGVVKGNV VEFSEKPLTN IPFRRIDWQL KSEKKIHDDI TNLVRKYLSN
     KEFSILHEIN LNLEKLGIKV EI