ID   MTH2_HAEPH              Reviewed;         228 AA.
AC   P00473;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Type II methyltransferase M.HhaII {ECO:0000303|PubMed:6315538};
DE            Short=M.HhaII {ECO:0000303|PubMed:3248721};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase HhaII;
DE   AltName: Full=Modification methylase HhaII;
GN   Name=hhaIIM {ECO:0000303|PubMed:3248721};
OS   Haemophilus parahaemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 10014 / CCUG 3716 / NCTC 8479 / 536;
RX   PubMed=6315538; DOI=10.1016/0378-1119(83)90083-5;
RA   Schoner B., Kelly S., Smith H.O.;
RT   "The nucleotide sequence of the HhaII restriction and modification genes
RT   from Haemophilus haemolyticus.";
RL   Gene 24:227-236(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-51, AND FUNCTION.
RC   STRAIN=ATCC 10014 / CCUG 3716 / NCTC 8479 / 536;
RX   PubMed=3248721; DOI=10.1016/0378-1119(88)90240-5;
RA   Chandrasegaran S., Wu L.P., Valda E., Smith H.O.;
RT   "Overproduction and purification of the M.HhaII methyltransferase from
RT   Haemophilus haemolyticus.";
RL   Gene 74:15-21(1988).
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).
CC   -!- FUNCTION: A beta subtype methylase, recognizes the double-stranded
CC       sequence 5'-GANTC-3', methylates A-2 on both strands, and protects the
CC       DNA from cleavage by the HhaII endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:3248721,
CC       ECO:0000305|PubMed:6315538}.
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   -!- CAUTION: Strain ATCC 10014 was originally thought to originate from
CC       H.haemolyticus. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=K00508; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M24624; AAA24963.1; -; Genomic_DNA.
DR   EMBL; K00508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JS0103; XYHIH2.
DR   RefSeq; WP_005707043.1; NZ_MUXY01000022.1.
DR   AlphaFoldDB; P00473; -.
DR   SMR; P00473; -.
DR   STRING; 735.B0185_09590; -.
DR   REBASE; 3422; M.HhaII.
DR   PRO; PR:P00473; -.
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; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00506; D21N6MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Methyltransferase;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3248721"
FT   CHAIN           2..228
FT                   /note="Type II methyltransferase M.HhaII"
FT                   /id="PRO_0000087972"
SQ   SEQUENCE   228 AA;  26432 MW;  FABEEED916927505 CRC64;
     MFSHQDYLSF VNKKNKMNGI DLFKLIPDKA VKIAFFDPQY RGVLDKMSYG NEGKGRGKER
     AALPQMTDEI IQQFINEFER VLLPNGYLFL WVDKFHLVEG VKPWLENTPS LSVVDMLTWD
     KQKIGMGYRT RRRSEYLVVI QKEPKKAKIT WTLHNIPDVW AEKLQSKPHT HSKPIEMQKQ
     LILATTQEGD LILDPASGGY SVFECCKQTN RNFIGCDLIF GDDENEQD