ID   MTF1_PLAOK              Reviewed;         647 AA.
AC   P14871; Q47911;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   13-SEP-2023, entry version 112.
DE   RecName: Full=Type II methyltransferase M.FokI {ECO:0000303|PubMed:12654995};
DE            Short=M.FokI {ECO:0000303|PubMed:2684765, ECO:0000303|PubMed:2784436};
DE            EC=2.1.1.72 {ECO:0000305|PubMed:2647724, ECO:0000305|PubMed:2684765};
DE   AltName: Full=Adenine-specific methyltransferase FokI;
DE   AltName: Full=Modification methylase FokI;
GN   Name=fokIM {ECO:0000303|PubMed:2684765}; Synonyms=mfoKI;
OS   Planomicrobium okeanokoites (Planococcus okeanokoites) (Flavobacterium
OS   okeanokoites).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planomicrobium.
OX   NCBI_TaxID=244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, SUBUNIT, AND
RP   MOTIF.
RC   STRAIN=ATCC 33414 / DSM 15489 / NBRC 12536 / NCIMB 561 / CIP 105082 /
RC   LMG 4030 / VKM B-1175;
RX   PubMed=2784436; DOI=10.1016/s0021-9258(18)83613-4;
RA   Kita K., Kotani H., Sugisaki H., Takanami M.;
RT   "The fokI restriction-modification system. I. Organization and nucleotide
RT   sequences of the restriction and modification genes.";
RL   J. Biol. Chem. 264:5751-5756(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24, FUNCTION,
RP   DOMAIN, AND MOTIF.
RX   PubMed=2684765; DOI=10.1016/0378-1119(89)90284-9;
RA   Looney M.C., Moran L.S., Jack W.E., Feehery G.R., Benner J.S., Slatko B.E.,
RA   Wilson G.G.;
RT   "Nucleotide sequence of the FokI restriction-modification system: separate
RT   strand-specificity domains in the methyltransferase.";
RL   Gene 80:193-208(1989).
RN   [3]
RP   FUNCTION, DOMAIN, MOTIF, AND MUTAGENESIS OF ASP-218 AND ASP-548.
RX   PubMed=2647724; DOI=10.1016/s0021-9258(18)83614-6;
RA   Sugisaki H., Kita K., Takanami M.;
RT   "The FokI restriction-modification system. II. Presence of two domains in
RT   FokI methylase responsible for modification of different DNA strands.";
RL   J. Biol. Chem. 264:5757-5761(1989).
RN   [4]
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 asymmetric
CC       double-stranded sequence 5'-GGATG-3', methylates A-3 of both strands,
CC       and protects the DNA from cleavage by the FokI endonuclease.
CC       {ECO:0000269|PubMed:2647724, ECO:0000269|PubMed:2684765,
CC       ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:2784436}.
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         Evidence={ECO:0000305|PubMed:2647724, ECO:0000305|PubMed:2684765};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2784436}.
CC   -!- DOMAIN: The 2 adenine-specific methylase motifs of the protein
CC       participate in modification of the two strands; the first motif
CC       modifies the sequence 5'-GGATG-3', the second motif modifies the
CC       sequence 5'-CATCC-5'. {ECO:0000269|PubMed:2647724,
CC       ECO:0000269|PubMed:2684765}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; J04623; AAA24926.1; -; Genomic_DNA.
DR   EMBL; M28828; AAA24933.1; -; Genomic_DNA.
DR   PIR; JQ0033; JQ0033.
DR   AlphaFoldDB; P14871; -.
DR   SMR; P14871; -.
DR   REBASE; 3405; M.FokI.
DR   PRO; PR:P14871; -.
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; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR012186; Ade-mod_methylase_MStsI.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00571; dam; 1.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR   Pfam; PF02086; MethyltransfD12; 2.
DR   PIRSF; PIRSF036638; M_m6A_StsI; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   PROSITE; PS00092; N6_MTASE; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Methyltransferase; Repeat;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..647
FT                   /note="Type II methyltransferase M.FokI"
FT                   /id="PRO_0000087960"
FT   MOTIF           218..221
FT                   /note="Adenine-specific methylase 1"
FT                   /evidence="ECO:0000269|PubMed:2647724,
FT                   ECO:0000305|PubMed:2684765, ECO:0000305|PubMed:2784436"
FT   MOTIF           548..551
FT                   /note="Adenine-specific methylase 2"
FT                   /evidence="ECO:0000269|PubMed:2647724,
FT                   ECO:0000305|PubMed:2684765, ECO:0000305|PubMed:2784436"
FT   MUTAGEN         218
FT                   /note="D->G: Methylates only 5'-GGATG-3' strand. Loss of
FT                   methylation; when associated with A-548."
FT                   /evidence="ECO:0000269|PubMed:2647724"
FT   MUTAGEN         548
FT                   /note="D->A: Methylates only 5'-CATCC-3' strand. Loss of
FT                   methylation; when associated with G-218."
FT                   /evidence="ECO:0000269|PubMed:2647724"
FT   CONFLICT        190
FT                   /note="G -> V (in Ref. 2; AAA24933)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   647 AA;  75626 MW;  66F7D05F17345836 CRC64;
     MRFIGSKVNL LDNIQEVIEE NVKDDAHVFM DLFSGTGIVG ENFKKDYQVL SNDSLYFSYI
     LLKAKIENNS IPNFSELKKI GIKEPLHYLE NEEFEISHEF FLTHNYSPYM GCERMYFTVE
     NASRIDFIRL TLNRWKNESL INELEFAYLL AILIEAVPFI SNISGTYGAY LKHWDKRALG
     KLKLRTLDIG NNHYANKTYN EDANSLIEKV YGDILYIDPP YNGRQYISNY HLLETIALYD
     YPEIYGKTGL RPYVESKSLY CQKKEVGNAF NHLIEKANFR HILVSYSSEG LLLEEEIESI
     LKSHGLPETY RIYKMPYRKY KSKHKQEASE LHEYIFYIQK DIALTNSVKS NKKIEVGKHK
     TNSYIKSPLN YVGGKHKLLN QIVPLFPDKI DTFVDLFSGG FNVGINVNAN KIIATDINTY
     VVEVLDTMKK TSVEEVIAHI ERRIEEYGLS KSNEEGFKAF RNYYNKTKKP LDLYTLICYS
     FNYQFRFNNN QEYNNPFGRE RSQFSPALKK KLVLFIEALH EKNVQFVCSE FEHFNFSQLD
     QNDLVYCDPP YLITTGSYND GNRGFKDWNR LQEIKLLDIL DHLNSKGVYF ALSNVLSHKG
     LENELLLEWS KKYNIHHLQH SYSNSSHNTT RGESQEVLIT NYTNYTK
//