ID   T1MH_METJA              Reviewed;         558 AA.
AC   Q60297;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Type I restriction enzyme MjaIX methylase subunit;
DE            Short=M protein;
DE            EC=2.1.1.72 {ECO:0000250|UniProtKB:P08957};
DE   AltName: Full=Type I methyltransferase M.MjaIX {ECO:0000303|PubMed:12654995};
DE            Short=M.MjaIX {ECO:0000303|PubMed:12654995};
GN   OrderedLocusNames=MJECL42;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OG   Plasmid large ECE.
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 A-2 on the
CC       bottom strand of the sequence 5'-CCAN(5)GTR-3'. In the presence of the
CC       R 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 N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L77118; AAC37111.1; -; Genomic_DNA.
DR   PIR; A64515; A64515.
DR   AlphaFoldDB; Q60297; -.
DR   SMR; Q60297; -.
DR   REBASE; 155513; M.VscVS05ORF3158P.
DR   REBASE; 188606; M.AsoACEORF2384P.
DR   REBASE; 191852; M.Apa1447ORF2799P.
DR   REBASE; 191856; M.Apa1447ORF3031P.
DR   REBASE; 191865; M.Apa1342ORF2767P.
DR   REBASE; 191868; M.Apa1342ORF2943P.
DR   REBASE; 191872; M.Apa1342ORF3157P.
DR   REBASE; 191885; M.Apa1468ORF2991P.
DR   REBASE; 191888; M.Apa1468ORF3072P.
DR   REBASE; 204130; M.Keu1446ORF147P.
DR   REBASE; 211764; M.RspL182ORF2217P.
DR   REBASE; 3910; M.MjaIX.
DR   REBASE; 618873; M.LspCC1II.
DR   PaxDb; 243232-MJ_ECL42; -.
DR   DNASU; 1450824; -.
DR   EnsemblBacteria; AAC37111; AAC37111; MJ_ECL42.
DR   KEGG; mja:MJ_ECL42; -.
DR   eggNOG; arCOG02632; Archaea.
DR   HOGENOM; CLU_013049_4_1_2; -.
DR   InParanoid; Q60297; -.
DR   OrthoDB; 45790at2157; -.
DR   PhylomeDB; Q60297; -.
DR   PRO; PR:Q60297; -.
DR   Proteomes; UP000000805; Plasmid large ECE.
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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR   PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 1.
DR   Pfam; PF12161; HsdM_N; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Plasmid; Reference proteome;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..558
FT                   /note="Type I restriction enzyme MjaIX methylase subunit"
FT                   /id="PRO_0000088029"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         227..232
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT   BINDING         256..258
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT   BINDING         283
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
SQ   SEQUENCE   558 AA;  64552 MW;  0DD8568C71C3AF37 CRC64;
     MATLDKFLSI KENDEKTKKK ESKKKSSKSN KTSESLVSHD HFELTPEFEN QLWKVADKLR
     KKMEVHQYKY VVLGLIFLRA LTCRFYERRK EIEEELSNPN SELYTEDPEL RKMILEDEDF
     YLSEGVLYLP KETRWDYFVE NVMSPNIGEI IDTAIEILEE KYPDRLKDVI PKIYAQSPLD
     NHDYSYLINK FSEISFGKEH RVKDVFGRIY EYFLGKFTEV EGKLGGKFYT PRSLTKLIVD
     VLDVKGGSIF DPACGSGGFF VSALEKLERE GIDINELSIY GQDSDPMAYR LTKMNLIIRG
     AEGDIRIDDS YHDDKFMDMT FDYVVANPPF NDSEWDANRI KPDDPRLRIG NKKVPVPPNG
     NANYMWILHF IYHTAPNGKA GFVMANGALS AGNVEGEIRK AIIENDLVYG IVACPPKLFY
     NVSLPVSLWF IRKEKPDYMK GKVLFINAKN LYKQISRRQN ILTEEHIKKI VDKFRMFESG
     EDEDKINELG FAKVATIDEI AKNGYVLTPG RYVGVKIEDD GIPFEVKMKE YSEELKKLLD
     EEEKLRNKVK EILDALGF
//