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 27-MAR-2024, entry version 133. 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; Pseudomonadota; 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}. 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; 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 OrthoDB; 9816043at2; -. DR PhylomeDB; P43871; -. DR BioCyc; HINF71421:G1GJ1-1420-MONOMER; -. DR PRO; PR:P43871; -. 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; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR001091; RM_Methyltransferase. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1. DR PANTHER; PTHR13370:SF33; TYPE II METHYLTRANSFERASE M.MJAV; 1. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 //