ID   T2H2_HAEPH              Reviewed;         227 AA.
AC   P00643;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Type II restriction enzyme HhaII {ECO:0000303|PubMed:12654995};
DE            Short=R.HhaII;
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease HhaII;
DE   AltName: Full=Type-2 restriction enzyme HhaII;
GN   Name=hhaIIR;
OS   Haemophilus parahaemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10014 / CCUG 3716 / NCTC 8479 / 536;
RX   PubMed=6315538; DOI=10.1016/0378-1119(83)90083-5;
RA   Schoner B., Kelly S., Smith H.O.;
RT   "The nucleotide sequence of the HhaII restriction and modification genes
RT   from Haemophilus haemolyticus.";
RL   Gene 24:227-236(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC   STRAIN=ATCC 10014 / CCUG 3716 / NCTC 8479 / 536;
RX   PubMed=3248721; DOI=10.1016/0378-1119(88)90240-5;
RA   Chandrasegaran S., Wu L.P., Valda E., Smith H.O.;
RT   "Overproduction and purification of the M.HhaII methyltransferase from
RT   Haemophilus haemolyticus.";
RL   Gene 74:15-21(1988).
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'-GANTC-3' and cleaves after G-1.
CC       {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   -!- SUBUNIT: Homodimer.
CC   -!- CAUTION: Strain ATCC 10014 was originally thought to originate from
CC       H.haemolyticus. {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; K00508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M24624; AAA24964.1; -; Genomic_DNA.
DR   PIR; A00788; NDHIH2.
DR   RefSeq; WP_005707040.1; NZ_MUXY01000022.1.
DR   AlphaFoldDB; P00643; -.
DR   REBASE; 1118; HhaII.
DR   BRENDA; 3.1.21.4; 2531.
DR   PRO; PR:P00643; -.
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.
PE   4: Predicted;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..227
FT                   /note="Type II restriction enzyme HhaII"
FT                   /id="PRO_0000077318"
SQ   SEQUENCE   227 AA;  25910 MW;  C3067B0AADA35863 CRC64;
     MSKISNALGR KDGNSGYTRV VGNAELGQLL SRVQATVISN GNELERLITQ RCNLIENIDV
     FIEDTTRGNN VQNGVYLCLK KTFKKSKKYA ESVKGIEPDM LIFIVESYRV CKVIELKDGD
     AFDTKKSQGE KEHLEKFATL FGAKIPFVTD YYICSFNQND KKLIMAGFKG VFSLEHILTG
     KELCQILGIS YQEILDIRRR DTEENFAYLI AEMMKIPEVR EEVKKHF