T1M1_METJA
ID T1M1_METJA Reviewed; 577 AA.
AC Q57596;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Type I restriction enzyme MjaVII methylase subunit;
DE Short=M protein;
DE EC=2.1.1.72 {ECO:0000250|UniProtKB:P08957};
DE AltName: Full=Type I methyltransferase M.MjaVII {ECO:0000303|PubMed:12654995};
DE Short=M.MjaVII {ECO:0000303|PubMed:12654995};
GN OrderedLocusNames=MJ0132;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(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: The subtype gamma methyltransferase (M) subunit of a type I
CC restriction enzyme. The M and S subunits together form a
CC methyltransferase (MTase) that methylates A-3 on the top and bottom
CC strands of the sequence 5'-CAAN(7)TGG-3'. In the presence of the R
CC subunit the complex can also act as an endonuclease, binding to the
CC same target sequence but cutting the DNA some distance from this site.
CC Whether the DNA is cut or modified depends on the methylation state of
CC the target sequence. When the target site is unmodified, the DNA is
CC cut. When the target site is hemimethylated, the complex acts as a
CC maintenance MTase modifying the DNA so that both strands become
CC methylated. After locating a non-methylated recognition site, the
CC enzyme complex serves as a molecular motor that translocates DNA in an
CC ATP-dependent manner until a collision occurs that triggers cleavage.
CC {ECO:0000250|UniProtKB:P08957, 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 Evidence={ECO:0000250|UniProtKB:P08957};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000250|UniProtKB:P08957}.
CC -!- MISCELLANEOUS: Type I restriction and modification enzymes are complex,
CC multifunctional systems which require ATP, S-adenosyl methionine and
CC Mg(2+) as cofactors and, in addition to their endonucleolytic and
CC methylase activities, are potent DNA-dependent ATPases.
CC {ECO:0000250|UniProtKB:P08957}.
CC -!- SIMILARITY: Belongs to the N4/N6-methyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB98113.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB98113.1; ALT_FRAME; Genomic_DNA.
DR PIR; D64316; D64316.
DR AlphaFoldDB; Q57596; -.
DR STRING; 243232.MJ_0132; -.
DR REBASE; 3902; M.MjaVII.
DR EnsemblBacteria; AAB98113; AAB98113; MJ_0132.
DR KEGG; mja:MJ_0132; -.
DR eggNOG; arCOG02632; Archaea.
DR HOGENOM; CLU_013049_1_0_2; -.
DR PhylomeDB; Q57596; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..577
FT /note="Type I restriction enzyme MjaVII methylase subunit"
FT /id="PRO_0000106710"
FT BINDING 251..256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT BINDING 281..283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT BINDING 306
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305"
FT BINDING 335..336
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
SQ SEQUENCE 577 AA; 67315 MW; 650D178C2FE6EC2F CRC64;
MLLEFADLDN WVKKRGSILF KKFKYEPFTL EEADKALKEE GIEAENTKEL LSILRRKEII
IAKKDPKDKR KRLYQFVKSA KKPTKDNLIR NLKYCADLIR TSVDYKVLLV FLFYKAISDK
YLALVEKFVS EGYSKTQAYL MANRSYLTLY DEDEGKLYVW HEIVKSRETI MELANALNKI
ANLNDNLKDL SKLVEVLGLI GFINEDNMHI LEELVRVYNE MDFSEIDYDA IGDAYQWILS
YFAPQKCKEG EVYTPVEVVR LIVNLLDIEK DSEVLDPACG SGTMLIESYR YVKDNYGGEI
YLYGQERNEI MAILAKLNLI LHGVDSEEYE IYIGDSLKNP KIWRGEVDYT IANPPWNLDG
YNEDVLKENP DVRRIYNTFV RGGYPPKQSA DWAWVQLMLY FARKKVGIVL DSGALFRGGK
EKKIRKEIVE KDLIEAIILL PEKLFYNVTA PGIVMILNKN KPEERKGKIL FINASLEFEK
HPEVRRLNRL GEENIDKIVD VYENWEDIEG FSRVVDLEEI RKNDYNLNVS LYVFPVEEKE
DIDLRKELEE FKEIEKKEKE VLDEVIGYVE GILRAGS
