MTH3_HAEIN
ID MTH3_HAEIN Reviewed; 309 AA.
AC P43871;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Type II methyltransferase M.HindIII {ECO:0000303|PubMed:12654995};
DE Short=M.HindIII {ECO:0000303|PubMed:7959067};
DE EC=2.1.1.72;
DE AltName: Full=Adenine-specific methyltransferase HindIII;
DE AltName: Full=Modification methylase HindIII;
GN Name=hindIIIM {ECO:0000303|PubMed:7959067}; OrderedLocusNames=HI_1392;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16, AND FUNCTION.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7959067; DOI=10.1016/0378-1119(94)90861-3;
RA Nwankwo D.O., Moran L.S., Slatko B.E., Waite-Rees P.A., Dorner L.F.,
RA Benner J.S., Wilson G.G.;
RT "Cloning, analysis and expression of the HindIII R-M-encoding genes.";
RL Gene 150:75-80(1994).
RN [2]
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 [3]
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: A beta subtype methylase that recognizes the double-stranded
CC sequence 5'-AAGCTT-3', methylates A-1 on both strands, and protects the
CC DNA from cleavage by the HindIII endonuclease.
CC {ECO:0000269|PubMed:7959067, 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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; L15391; AAA61959.1; -; Genomic_DNA.
DR EMBL; L42023; AAC23039.1; -; Genomic_DNA.
DR RefSeq; NP_439546.1; NC_000907.1.
DR AlphaFoldDB; P43871; -.
DR SMR; P43871; -.
DR STRING; 71421.HI_1392; -.
DR REBASE; 3428; M.HindIII.
DR EnsemblBacteria; AAC23039; AAC23039; HI_1392.
DR KEGG; hin:HI_1392; -.
DR PATRIC; fig|71421.8.peg.1451; -.
DR eggNOG; COG0863; Bacteria.
DR HOGENOM; CLU_024927_5_1_6; -.
DR PhylomeDB; P43871; -.
DR BioCyc; HINF71421:G1GJ1-1420-MON; -.
DR PRO; PR:P43871; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IBA:GO_Central.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Methyltransferase;
KW Reference proteome; Restriction system; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..309
FT /note="Type II methyltransferase M.HindIII"
FT /id="PRO_0000087964"
SQ SEQUENCE 309 AA; 35550 MW; 954E04023326E061 CRC64;
MIDCIYNSDS IFEIKKLDSN SIHAIISDIP YGIDYDDWDI LHSNTNSALG GTSSAQHKTS
LFKRRGKPLN GWSEADKKRP QEYQEWVESW SNEWFRVLKS GSSVFVFAGR QFAHRVVVAF
ENSGFTFKDM LSWEKDKAPH RAQRISCVFE RRGDIANTNK WVGWRVANLR PLFEPILWFQ
KPYKTGSTLA DNLIKHEVGA WNENSLTHWN IQQGALNHSN ILKVRITSED KGYHVAQKPL
NLMKLLIDLV TKEEQIVLDP FAGSGTTLLA AKELNRHFIG YEKNNGIYNI AVNRLGIEKN
NCFYNKEKK
