ID   T2H2_HAEPA              Reviewed;         358 AA.
AC   P36433;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Type II restriction enzyme HpaII {ECO:0000303|PubMed:12654995};
DE            Short=R.HpaII;
DE            EC=3.1.21.4 {ECO:0000305|PubMed:7514149};
DE   AltName: Full=Endonuclease HpaII;
DE   AltName: Full=Type-2 restriction enzyme HpaII;
GN   Name=hpaIIR {ECO:0000303|PubMed:7514149};
OS   Haemophilus parainfluenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49669;
RX   PubMed=7514149; DOI=10.1016/0378-1119(94)90348-4;
RA   Kulakauskas S., Barsomian J.M., Lubys A., Roberts R.J., Wilson G.G.;
RT   "Organization and sequence of the HpaII restriction-modification system and
RT   adjacent genes.";
RL   Gene 142:9-15(1994).
RN   [2]
RP   NOMENCLATURE, AND SUBTYPES.
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: An E and P subtype restriction enzyme that recognizes the
CC       double-stranded sequence 5'-CCGG-3' and cleaves after C-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:7514149}.
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         Evidence={ECO:0000305|PubMed:7514149};
CC   -!- SUBUNIT: Homodimer.
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; L17342; AAA20482.1; -; Genomic_DNA.
DR   AlphaFoldDB; P36433; -.
DR   REBASE; 1159; HpaII.
DR   PRO; PR:P36433; -.
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   InterPro; IPR019062; Restrct_endonuc_II_HpaII.
DR   Pfam; PF09561; RE_HpaII; 1.
PE   4: Predicted;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..358
FT                   /note="Type II restriction enzyme HpaII"
FT                   /id="PRO_0000077325"
SQ   SEQUENCE   358 AA;  40926 MW;  ECB312180C80303E CRC64;
     MTEFFSGNRG EWSEPYALFK LLADGQLYLG DSQLNKLGIV MPILSILRQE KNYESSYILH
     NNSQNIIVTY NNEKFTVPIS GFQEKAVLLL SEIKNASGNR AFSIPSIDDF LKKLGFTHLS
     ASSSSKSDIH IVVHDLRTGI TPTLGFSIKS QLGSPATLLN ASKATNFTFK IYNLKDKQIE
     YINSLSGIKE KIKEIFSQDG KLEFVKVESC KFSNNLTLID TKLPEILAEM ILLYYSSKLN
     KIDDVTEHIS RLNPLNYNLS CNHNYYEYKV KHFLNDVALG MRPDDVWLGQ YDATGGYLVV
     KEDGELLCYH IYSKNSFEDY LYCNTKFDTP SSSRHDFGHI YQVNHDFFIK LNVQIRFL