T2C2_HAEIF
ID T2C2_HAEIF Reviewed; 258 AA.
AC P17743;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Type II restriction enzyme HincII {ECO:0000303|PubMed:12654995};
DE Short=R.HincII {ECO:0000303|PubMed:2374714};
DE EC=3.1.21.4;
DE AltName: Full=Endonuclease HincII;
DE AltName: Full=Type-2 restriction enzyme HincII;
GN Name=hincIIR;
OS Haemophilus influenzae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, AND FUNCTION.
RC STRAIN=RC;
RX PubMed=2374714; DOI=10.1093/nar/18.13.3903;
RA Ito H., Sadaoka A., Kotani H., Hiraoka N., Nakamura T.;
RT "Cloning, nucleotide sequence, and expression of the HincII restriction-
RT modification system.";
RL Nucleic Acids Res. 18:3903-3911(1990).
RN [2]
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-258.
RX PubMed=11742344; DOI=10.1038/nsb741;
RA Horton N.C., Dorner L.F., Perona J.J.;
RT "Sequence selectivity and degeneracy of a restriction endonuclease mediated
RT by DNA intercalation.";
RL Nat. Struct. Biol. 9:42-47(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-257.
RX PubMed=15491133; DOI=10.1021/bi0490082;
RA Etzkorn C., Horton N.C.;
RT "Ca2+ binding in the active site of HincII: implications for the catalytic
RT mechanism.";
RL Biochemistry 43:13256-13270(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-257.
RX PubMed=15476804; DOI=10.1016/j.jmb.2004.08.082;
RA Etzkorn C., Horton N.C.;
RT "Mechanistic insights from the structures of HincII bound to cognate DNA
RT cleaved from addition of Mg2+ and Mn2+.";
RL J. Mol. Biol. 343:833-849(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-257.
RX PubMed=15993893; DOI=10.1016/j.jmb.2005.05.063;
RA Little E.J., Horton N.C.;
RT "DNA-induced conformational changes in type II restriction endonucleases:
RT the structure of unliganded HincII.";
RL J. Mol. Biol. 351:76-88(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-258.
RX PubMed=16675462; DOI=10.1074/jbc.m512339200;
RA Joshi H.K., Etzkorn C., Chatwell L., Bitinaite J., Horton N.C.;
RT "Alteration of sequence specificity of the type II restriction endonuclease
RT HincII through an indirect readout mechanism.";
RL J. Biol. Chem. 281:23852-23869(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 2-258.
RX PubMed=18762194; DOI=10.1016/j.jmb.2008.08.032;
RA Babic A.C., Little E.J., Manohar V.M., Bitinaite J., Horton N.C.;
RT "DNA distortion and specificity in a sequence-specific endonuclease.";
RL J. Mol. Biol. 383:186-204(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
RX PubMed=19081059; DOI=10.1016/j.str.2008.09.009;
RA Little E.J., Babic A.C., Horton N.C.;
RT "Early interrogation and recognition of DNA sequence by indirect readout.";
RL Structure 16:1828-1837(2008).
CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC stranded sequence 5'-GTYRAC-3' and cleaves after Y-3.
CC {ECO:0000269|PubMed:2374714, 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; X52124; CAA36370.1; -; Genomic_DNA.
DR PIR; S10323; S10323.
DR PDB; 1KC6; X-ray; 2.60 A; A/B/C/D=2-258.
DR PDB; 1TW8; X-ray; 2.80 A; A/B/C/D=2-258.
DR PDB; 1TX3; X-ray; 2.50 A; A/B/C/D=2-258.
DR PDB; 1XHU; X-ray; 2.95 A; A/B/C/D=2-258.
DR PDB; 1XHV; X-ray; 2.50 A; A/B/C/D=2-258.
DR PDB; 2AUD; X-ray; 2.10 A; A=2-258.
DR PDB; 2GIE; X-ray; 2.60 A; A/B/C/D=2-258.
DR PDB; 2GIG; X-ray; 1.83 A; A/B=2-258.
DR PDB; 2GIH; X-ray; 2.50 A; A/B=2-258.
DR PDB; 2GII; X-ray; 2.30 A; A/B=2-258.
DR PDB; 2GIJ; X-ray; 1.93 A; A/B=2-258.
DR PDB; 3E3Y; X-ray; 2.13 A; A/B=2-258.
DR PDB; 3E40; X-ray; 2.10 A; A/B=2-258.
DR PDB; 3E41; X-ray; 2.73 A; A/B=2-258.
DR PDB; 3E42; X-ray; 2.68 A; A/B=2-258.
DR PDB; 3E43; X-ray; 2.73 A; A/B=2-258.
DR PDB; 3E44; X-ray; 2.52 A; A/B=2-258.
DR PDB; 3E45; X-ray; 2.78 A; A/B=2-258.
DR PDB; 3EBC; X-ray; 2.55 A; A/B=1-258.
DR PDBsum; 1KC6; -.
DR PDBsum; 1TW8; -.
DR PDBsum; 1TX3; -.
DR PDBsum; 1XHU; -.
DR PDBsum; 1XHV; -.
DR PDBsum; 2AUD; -.
DR PDBsum; 2GIE; -.
DR PDBsum; 2GIG; -.
DR PDBsum; 2GIH; -.
DR PDBsum; 2GII; -.
DR PDBsum; 2GIJ; -.
DR PDBsum; 3E3Y; -.
DR PDBsum; 3E40; -.
DR PDBsum; 3E41; -.
DR PDBsum; 3E42; -.
DR PDBsum; 3E43; -.
DR PDBsum; 3E44; -.
DR PDBsum; 3E45; -.
DR PDBsum; 3EBC; -.
DR AlphaFoldDB; P17743; -.
DR SMR; P17743; -.
DR DIP; DIP-48338N; -.
DR BRENDA; 3.1.21.4; 2529.
DR EvolutionaryTrace; P17743; -.
DR PRO; PR:P17743; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 3.40.600.10; -; 1.
DR InterPro; IPR037057; DNA_rep_MutH/T2_RE_sf.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR015307; Restrct_endonuc_II_HincII.
DR Pfam; PF09226; Endonuc-HincII; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW Restriction system.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2374714"
FT CHAIN 2..258
FT /note="Type II restriction enzyme HincII"
FT /id="PRO_0000077319"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:2GIG"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2GIG"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1TW8"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2GIH"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:2GIG"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:2GIG"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:2GIG"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2AUD"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:2GIG"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:2GIG"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2GIH"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:2GIG"
FT STRAND 162..176
FT /evidence="ECO:0007829|PDB:2GIG"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2GIG"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2GIG"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:2GIJ"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 223..249
FT /evidence="ECO:0007829|PDB:2GIG"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:2GIG"
SQ SEQUENCE 258 AA; 29871 MW; 9FE82017F7C15A47 CRC64;
MSFIKPIYQD INSILIGQKV KRPKSGTLSG HAAGEPFEKL VYKFLKENLS DLTFKQYEYL
NDLFMKNPAI IGHEARYKLF NSPTLLFLLS RGKAATENWS IENLFEEKQN DTADILLVKD
QFYELLDVKR RNISKSAQAP NIISAYKLAQ TCAKMIDNKE FDLFDINYLE VDSELNGEDL
VCVSTSFAEL FKSEPSELYI NWAAAMQIQF HVRDLDQGFN GTREEWAKSY LKHFVTQAEQ
RAISMIDKFV KPFKKYIL
