ID   T2H1_HAEPH              Reviewed;         379 AA.
AC   P50191;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Type II restriction enzyme HphI {ECO:0000303|PubMed:12654995};
DE            Short=R.HphI;
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease HphI;
DE   AltName: Full=Type-2 restriction enzyme HphI;
GN   Name=hphIR {ECO:0000303|PubMed:8759008};
OS   Haemophilus parahaemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 49700;
RX   PubMed=8759008; DOI=10.1093/nar/24.14.2760;
RA   Lubys A., Lubiene J., Kulakauskkas S., Stankevicius K., Timinskas A.,
RA   Janulaitis A.;
RT   "Cloning and analysis of the genes encoding the type IIS restriction-
RT   modification system HphI from Haemophilus parahaemolyticus.";
RL   Nucleic Acids Res. 24:2760-2766(1996).
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).
CC   -!- FUNCTION: An S subtype restriction enzyme that recognizes the double-
CC       stranded sequences 5'-GGTGA-3' and 5'-TCACC-3' and cleaves respectively
CC       13 bases after G-1 and 7 bases before T-1, leaving a single 3'
CC       protruding nucleotide. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:8759008}.
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; X85374; CAA59692.1; -; Genomic_DNA.
DR   PIR; S70709; S70709.
DR   AlphaFoldDB; P50191; -.
DR   SMR; P50191; -.
DR   REBASE; 1160; HphI.
DR   PRIDE; P50191; -.
DR   PRO; PR:P50191; -.
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; IPR003615; HNH_nuc.
DR   Pfam; PF13391; HNH_2; 1.
PE   4: Predicted;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..379
FT                   /note="Type II restriction enzyme HphI"
FT                   /id="PRO_0000077326"
SQ   SEQUENCE   379 AA;  45321 MW;  771488C513C74E34 CRC64;
     MQIYETYWEI TNEYGYNTER FVETLKICVE YIDEIKLVNP NYTETDYSSV IYNELQMRLQ
     SSPILQSTRK GFEGKPKNET SIRKSINQLV KSGFINPFLT GYHSLAKEYL QTKVNKKRNF
     LFSRIVYESS NFSYAITDKP DIKVRHINFL VNTLIENFEG KLSKNEIIAL MLMDLRTYNG
     NYYPIDELRN FIRLNQNYIS EFKERKYNQI TYLWGLLSKL DEIYQKDEFI CLEEDKKRVF
     GDLEDTQYLR KRDPYLHRLY KHQLQEESAE YCGGIKCMLE KLAYPVLIAS HIKPFIQSDD
     NEAYDPNNGL LLSRTLDSLF DLKYISFDDN GNMLKSARLS DDVWQYWRNI KLDSVLLNEK
     RKQYLKFHRE LMEKEDSKN