MTF1_PLAOK
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 03-AUG-2022, entry version 108.
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; Firmicutes; 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 / LMG
RC 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; -; 1.
DR Gene3D; 3.40.50.150; -; 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 PANTHER; PTHR30481; PTHR30481; 1.
DR Pfam; PF02086; MethyltransfD12; 2.
DR PIRSF; PIRSF036638; M_m6A_StsI; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 2.
DR TIGRFAMs; TIGR00571; dam; 1.
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
