MTH1_HAEIF
ID MTH1_HAEIF Reviewed; 359 AA.
AC P20590;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Type II methyltransferase M.HinfI {ECO:0000303|PubMed:12654995};
DE Short=M.HinfI {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.72;
DE AltName: Full=Adenine-specific methyltransferase HinfI;
DE AltName: Full=Modification methylase HinfI;
GN Name=hinfIM;
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=RF;
RX PubMed=3063606; DOI=10.1016/0378-1119(88)90210-7;
RA Chandrasegaran S., Lunnen K.D., Smith H.O., Wilson G.G.;
RT "Cloning and sequencing the HinfI restriction and modification genes.";
RL Gene 70:387-392(1988).
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'-GANTC-3', methylates A-2 on both strands, and protects the
CC DNA from cleavage by the HinfI endonuclease.
CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:3063606}.
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; M22862; AAA24986.1; -; Genomic_DNA.
DR PIR; JT0391; JT0391.
DR AlphaFoldDB; P20590; -.
DR SMR; P20590; -.
DR REBASE; 3429; M.HinfI.
DR PRO; PR:P20590; -.
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; IPR040843; RAMA.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF18755; RAMA; 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..359
FT /note="Type II methyltransferase M.HinfI"
FT /id="PRO_0000087963"
FT DOMAIN 275..358
FT /note="RAMA"
FT /evidence="ECO:0000255"
SQ SEQUENCE 359 AA; 41806 MW; 128C6BB0D5480621 CRC64;
MMKENINDFL NTILKGDCIE KLKTIPNESI DLIFADPPYF MQTEGKLLRT NGDEFSGVDD
EWDKFNDFVE YDSFCELWLK ECKRILKSTG SIWVIGSFQN IYRIGYIMQN LDFWILNDVI
WNKTNPVPNF GGTRFCNAHE TMLWCSKCKK NKFTFNYKTM KHLNQEKQER SVWSLSLCTG
KERIKDEEGK KAHSTQKPES LLYKVILSSS KPNDVVLDPF FGTGTTGAVA KALGRNYIGI
EREQKYIDVA EKRLREIKPN PNDIELLSLE IKPPKVPMKT LIEADFLRVG QTLFDKNENA
ICIVTQDGNV KDNEETLSIH KMSAKYLNKT NNNGWDYFYL FRNNNFITLD SLRYEYTNQ
