T1MH_HAEIN
ID T1MH_HAEIN Reviewed; 443 AA.
AC Q57168; O05053;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Type I restriction enzyme HindI methylase subunit;
DE Short=M protein;
DE EC=2.1.1.72 {ECO:0000269|PubMed:4591672};
DE AltName: Full=Type I methyltransferase M.HindI {ECO:0000303|PubMed:12654995};
DE Short=M.HindI {ECO:0000303|PubMed:12654995};
DE AltName: Full=Type I restriction enzyme HindVIIP methylase subunit;
GN Name=hsdM {ECO:0000303|PubMed:7542800}; OrderedLocusNames=HI_1287;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP FUNCTION AS A METHYLASE, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=4591672; DOI=10.1016/0022-2836(73)90515-9;
RA Roy P.H., Smith H.O.;
RT "DNA methylases of Hemophilus influenzae Rd. I. Purification and
RT properties.";
RL J. Mol. Biol. 81:427-444(1973).
RN [3]
RP PARTIAL RECOGNITION SEQUENCE.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=4544320; DOI=10.1016/0022-2836(73)90516-0;
RA Roy P.H., Smith H.O.;
RT "DNA methylases of Hemophilus influenzae Rd. II. Partial recognition site
RT base sequences.";
RL J. Mol. Biol. 81:445-459(1973).
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: 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 adenosines in the sequence
CC 5'-RAACN(5)TAG-3'. Methylation protects against cleavage by HindI
CC (PubMed:4591672) (Probable). In the presence of the R subunit the
CC complex can also act as an endonuclease, binding to the same target
CC sequence but cutting the DNA some distance from this site. Whether the
CC DNA is cut or modified depends on the methylation state of the target
CC sequence. When the target site is unmodified, the DNA is cut. When the
CC target site is hemimethylated, the complex acts as a maintenance MTase
CC modifying the DNA so that both strands become methylated (Probable)
CC (PubMed:12654995). After locating a non-methylated recognition site,
CC the enzyme complex serves as a molecular motor that translocates DNA in
CC an ATP-dependent manner until a collision occurs that triggers cleavage
CC (By similarity). {ECO:0000250|UniProtKB:P08957,
CC ECO:0000269|PubMed:4591672, ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:4544320, ECO:0000305|PubMed:4591672}.
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:0000269|PubMed:4591672};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 nM for S-adenosyl-L-methionine {ECO:0000269|PubMed:4591672};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S; the restriction enzyme has stoichiometry
CC R(2)M(2)S(1) while the methyltransferase is M(2)S(1).
CC {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; L42023; AAC22936.1; -; Genomic_DNA.
DR PIR; G64114; G64114.
DR RefSeq; NP_439439.2; NC_000907.1.
DR AlphaFoldDB; Q57168; -.
DR SMR; Q57168; -.
DR STRING; 71421.HI_1287; -.
DR REBASE; 203814; M.Lbr1106ORF30P.
DR REBASE; 231750; M.Sen4839ORF3820P.
DR REBASE; 3426; M.HindI.
DR EnsemblBacteria; AAC22936; AAC22936; HI_1287.
DR KEGG; hin:HI_1287; -.
DR PATRIC; fig|71421.8.peg.1339; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_4_1_6; -.
DR OMA; NSADWAW; -.
DR PhylomeDB; Q57168; -.
DR PRO; PR:Q57168; -.
DR Proteomes; UP000000579; Chromosome.
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; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..443
FT /note="Type I restriction enzyme HindI methylase subunit"
FT /id="PRO_0000088027"
FT BINDING 117..122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT BINDING 146..148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT BINDING 173
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
SQ SEQUENCE 443 AA; 49732 MW; 70573FBFFA78594C CRC64;
MPASARWQAL QEVSILNTGA ELPWGGKFSG VAKLIDDAFD AIEKDNEKLK GVLQRISGYA
VNEDTLRGLI ILFSDTHFTR PTYNGEPVHL GAKDILGHVY EYFLSRFAQA EGKRSGQYFT
PKSIVSLIVE MLEPYSGRVY DPAMGSGGFF VQTERFITAH QGNINNVSIY GQEFNPTTWK
LAAMNMAIRG IDYDFGKYNA DSFTQPQHID KKMDFIMANP HFNDKEWWNE SLADDPRWAY
GTPPKGNANF AWLQHMIYHL SPNGKIALLL ANGSMSSQTN NEGEIRKAII NADLVECMVA
LPGQLFTNTK IPACIWFLNR NKKRKGEVLF IDARQIGYMK DRVLRDFTAD DIAKIADTLH
AWQTSDGYED QAAFCKSATL EEIKNNDFVL TPGRYVGTAE QEDDGVPFAE KMQNLTALLK
EQFAKSAELE AEIKKNLGGL GYE
