ID   MTHB_HAEPH              Reviewed;         336 AA.
AC   P50193;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Type II methyltransferase M2.HphI {ECO:0000303|PubMed:12654995};
DE            Short=M2.HphI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase HphIB;
DE   AltName: Full=M.HphI(A);
DE   AltName: Full=Modification methylase HphIB;
DE            Short=M.HphIB;
GN   Name=hphIBM; Synonyms=hphIMA {ECO:0000303|PubMed:8759008};
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 49700;
RX   PubMed=8759008; DOI=10.1093/nar/24.14.2760;
RA   Lubys A., Lubiene J., Kulakauskkas S., Stankevicius K., Timinskas A.,
RA   Janulaitis A.;
RT   "Cloning and analysis of the genes encoding the type IIS restriction-
RT   modification system HphI from Haemophilus parahaemolyticus.";
RL   Nucleic Acids Res. 24:2760-2766(1996).
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: An alpha subtype methylase that recognizes the double-
CC       stranded sequence 5'-GGTGA-3', probably methylates A-5 on the top
CC       strand, and protects the DNA from cleavage by the HphI endonuclease.
CC       {ECO:0000269|PubMed:8759008, 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   -!- MISCELLANEOUS: Both this methylase and M1.HphI protect DNA from
CC       cleavage by HphI. {ECO:0000269|PubMed:8759008}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X85374; CAA59691.1; -; Genomic_DNA.
DR   PIR; S70708; S70708.
DR   AlphaFoldDB; P50193; -.
DR   REBASE; 3661; M2.HphI.
DR   PRO; PR:P50193; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; -; 2.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
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..336
FT                   /note="Type II methyltransferase M2.HphI"
FT                   /id="PRO_0000087952"
SQ   SEQUENCE   336 AA;  39609 MW;  3BD144C7772C4FDF CRC64;
     MNNPKYPKVN YIGNKEKIAE WICEQLPVDV RTIADVFSGG CSFSFEAKKR GYQVIANDIL
     NINYQLALAL IVNNQEILTA CDVDFIFSNP PKSGFMTKNY SDVFFFKEEC RELDAIRANI
     LKLNNTYKQA LAFALMRRAM IRKMPYSRFT ISWEKVKQLR DEEYSYSKYG RRRAYHNQSF
     EFHFRENLNS YNQAVFNNGN IHQAYNEDVF ELLDHIQADA VYLDPPYTGT MNNYFGFYGL
     LDSYMSGEIR QPFDNHFMDK NQAVELFEKL IEKLKPFKYW LLSYNNVSRP NREELTAMLS
     RNGRKVTVLE TPHVYKVTGK ENKQKHTELL FLVENR