ID T2D3_HAEIN Reviewed; 300 AA. AC P43870; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-SEP-2023, entry version 130. DE RecName: Full=Type II restriction enzyme HindIII {ECO:0000303|PubMed:7542800}; DE Short=R.HindIII {ECO:0000303|PubMed:7959067}; DE EC=3.1.21.4; DE AltName: Full=Endonuclease HindIII; DE AltName: Full=Type-2 restriction enzyme HindIII; GN Name=hindIIIR {ECO:0000303|PubMed:7959067}; OrderedLocusNames=HI_1393; 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 1-26, 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 P subtype restriction enzyme that recognizes the double- CC stranded sequence 5'-AAGCTT-3' and cleaves after A-1. CC {ECO:0000269|PubMed:7959067, ECO:0000303|PubMed:12654995}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage of DNA to give specific double- CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; 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; AAA61958.1; -; Genomic_DNA. DR EMBL; L42023; AAC23040.1; -; Genomic_DNA. DR PIR; H64121; H64121. DR RefSeq; NP_439547.1; NC_000907.1. DR PDB; 2E52; X-ray; 2.00 A; A/B/C/D=1-300. DR PDB; 3A4K; X-ray; 2.17 A; A/B/C/D=1-300. DR PDB; 3WVG; X-ray; 2.25 A; A/B/C/D=1-300. DR PDB; 3WVH; X-ray; 2.54 A; A/B/C/D=1-300. DR PDB; 3WVI; X-ray; 2.55 A; A/B/C/D=1-300. DR PDB; 3WVK; X-ray; 2.00 A; A/B/C/D=1-300. DR PDB; 3WVP; X-ray; 2.30 A; A/B/C/D=1-300. DR PDBsum; 2E52; -. DR PDBsum; 3A4K; -. DR PDBsum; 3WVG; -. DR PDBsum; 3WVH; -. DR PDBsum; 3WVI; -. DR PDBsum; 3WVK; -. DR PDBsum; 3WVP; -. DR AlphaFoldDB; P43870; -. DR SMR; P43870; -. DR STRING; 71421.HI_1393; -. DR BindingDB; P43870; -. DR ChEMBL; CHEMBL5004; -. DR DrugCentral; P43870; -. DR REBASE; 1151; HindIII. DR EnsemblBacteria; AAC23040; AAC23040; HI_1393. DR KEGG; hin:HI_1393; -. DR PATRIC; fig|71421.8.peg.1452; -. DR eggNOG; ENOG5032WDH; Bacteria. DR HOGENOM; CLU_079600_0_0_6; -. DR OrthoDB; 977705at2; -. DR BioCyc; HINF71421:G1GJ1-1421-MONOMER; -. DR BRENDA; 3.1.21.4; 2529. DR EvolutionaryTrace; P43870; -. DR PRO; PR:P43870; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR CDD; cd22330; HindIII-like; 1. DR Gene3D; 6.10.250.1510; -; 1. DR Gene3D; 3.40.91.70; Type II restriction endonuclease, HindIII; 1. DR InterPro; IPR019043; Restrct_endonuc_II_HindIII. DR InterPro; IPR038373; Restrct_endonuc_II_HindIII_sf. DR Pfam; PF09518; RE_HindIII; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Restriction system. FT CHAIN 1..300 FT /note="Type II restriction enzyme HindIII" FT /id="PRO_0000077321" FT HELIX 5..15 FT /evidence="ECO:0007829|PDB:2E52" FT TURN 16..18 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 21..33 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 37..47 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 59..78 FT /evidence="ECO:0007829|PDB:2E52" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:2E52" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:3WVK" FT STRAND 94..103 FT /evidence="ECO:0007829|PDB:2E52" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 122..125 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 127..133 FT /evidence="ECO:0007829|PDB:2E52" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:2E52" FT STRAND 137..144 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:2E52" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 155..163 FT /evidence="ECO:0007829|PDB:2E52" FT STRAND 165..169 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 170..178 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 190..193 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 195..200 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 213..224 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 228..261 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 265..275 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 278..293 FT /evidence="ECO:0007829|PDB:2E52" FT HELIX 295..298 FT /evidence="ECO:0007829|PDB:2E52" SQ SEQUENCE 300 AA; 34952 MW; 62F62AC4B18E841B CRC64; MKKSALEKLL SLIENLTNQE FKQATNSLIS FIYKLNRNEV IELVRSIGIL PEAIKPSSTQ EKLFSKAGDI VLAKAFQLLN LNSKPLEQRG NAGDVIALSK EFNYGLVADA KSFRLSRTAK NQKDFKVKAL SEWREDKDYA VLTAPFFQYP TTKSQIFKQS LDENVLLFSW EHLAILLQLD LEETNIFSFE QLWNFPKKQS KKTSVSDAEN NFMRDFNKYF MDLFKIDKDT LNQLLQKEIN FIEERSLIEK EYWKKQINII KNFTREEAIE ALLKDINMSS KIETIDSFIK GIKSNDRLYL //