T2D3_HAEIN
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 03-AUG-2022, entry version 127.
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; Proteobacteria; 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;
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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 BioCyc; HINF71421:G1GJ1-1421-MON; -.
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 Gene3D; 3.40.91.70; -; 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
