T1MH_METJA
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 03-AUG-2022, entry version 110.
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}.
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DR EMBL; L77118; AAC37111.1; -; Genomic_DNA.
DR PIR; A64515; A64515.
DR AlphaFoldDB; Q60297; -.
DR SMR; Q60297; -.
DR STRING; 243232.MJ_ECL42; -.
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 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 OMA; YEYLMGM; -.
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: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; IPR002052; DNA_methylase_N6_adenine_CS.
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.
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
