ID   T2D1_DESNO              Reviewed;         240 AA.
AC   P05301;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Type II restriction enzyme DdeI {ECO:0000303|PubMed:12654995};
DE            Short=R.DdeI {ECO:0000303|PubMed:2823226};
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease DdeI;
DE   AltName: Full=Type-2 restriction enzyme DdeI;
GN   Name=ddeIR; Synonyms=ddeR;
OS   Desulfomicrobium norvegicum (strain DSM 1741 / NCIMB 8310) (Desulfovibrio
OS   baculatus (strain Norway 4)) (Desulfovibrio desulfuricans (strain Norway
OS   4)).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfomicrobiaceae; Desulfomicrobium.
OX   NCBI_TaxID=52561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=2823226; DOI=10.1093/nar/15.20.8249;
RA   Sznyter L.A., Slatko B., Moran L., O'Donnell K.H., Brooks J.E.;
RT   "Nucleotide sequence of the DdeI restriction-modification system and
RT   characterization of the methylase protein.";
RL   Nucleic Acids Res. 15:8249-8266(1987).
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: A P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-CTNAG-3' and cleaves after C-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:2823226}.
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; Y00449; CAA68504.1; -; Genomic_DNA.
DR   AlphaFoldDB; P05301; -.
DR   STRING; 52561.SAMN05421830_1264; -.
DR   REBASE; 770; DdeI.
DR   OrthoDB; 9811614at2; -.
DR   PRO; PR:P05301; -.
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..240
FT                   /note="Type II restriction enzyme DdeI"
FT                   /id="PRO_0000077299"
SQ   SEQUENCE   240 AA;  27808 MW;  AE0A7821F2F41356 CRC64;
     MKAATDQELR KLIVLYNNVM EVMEHDAAKS MRDDNRAYGG FVRAAKGKIQ ELITERLVRT
     VWDVEMGENP ERLSINSKKI KIPILRSYVD SINDENLKKY ISSNILKYSY GLSVDKHVFI
     DNKFVLGIEC KAYTENAMLK RILVDFYLLK TKFPKLNCFL FQLESQLGGD YSECNKFPIG
     SYPTRTIMSY FKNVDLNIVT LLEGERKVDR PINKPQFFKP LKVEHLEVAI GYLQESLSEI
//