© 1991 Oxford University Press
Nucleic Acids Research, Vol. 19, Supplement 2077
Restriction enzymes and their isoschizomers
Richard J.Roberts and Dana Macelis
Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724-2202, USA
INTRODUCTION
ACKNOWLEDGMENTS
Since the last compilation of restriction enzymes, (1) 442 new
entries have been added including 13 new specificities. A
complete list of these new enzymes can be found in Table I. With
the growing size of the restriction enzyme database and the
recognition that the most widespread use of the information is
as a database for computer programs predicting restriction
enzyme cleavage patterns, Table n contains a listing of all
prototype restriction enzymes (Types I, II and HI) together with
their commercially available isoschizomers. It should be noted
that an alternative compilation of these enzymes has recently been
produced (3).
During the previous year the names of several restriction
enzymes have been changed by the original authors.
Special thanks are due to the many individuals who have so kindly
communicated their unpublished results for inclusion in this
compilation. Work from the authors' laboratory is supported by
the N.I.H. (GM40537).
Old Name
Prototype
HalB6l
EcoKl
PsA
SacU
Noel
Clal
Hamaa
NgoAIE
NgoAIV
PgHMl
Spa
SsrB6l
UbaUCni
UbaUOSl
UballOlU
UbalHHl
Mwll05I
L*oll06I
Ww 11081
Uball
Hpal
Espl
AvalU
Dpnl
Ksp632l
PpuMl
PpuMl
Recognition
Sequence
G1AATTC
CTGCA1G
CCGCIGG
GtCCGGC
AT1CGAT
CCGC
GTTIAAC
GC1TNAGC
ATGCA1T
GATC
CTCTTC (1/5)
GACNNNINNGTC
RGGWCCY
TCGTAG
RGtGWCCY
New Name
Hall
Ham
NgoFUl
NgoFW
PgK
Aril
Ssri
BpullO/21
MphllOil
MphllOlU
REFERENCES
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
12.
13.
14.
15.
16.
17.
18.
19.
20.
Eamlltol
EamllOSl
MlullO6l
/y?1108I
PJU.TI
21.
22.
23.
24.
The complete database is available in many formats including
the styles shown in Tables I and n, or as a flat file arranged in
fields that can easily be reformatted. It is possible to get regular
monthly updates or specialized versions of the database by
electronic mail. For instance, files containing the database in
formats that can be used directly by the UWGCG, IGSuite and
other computer software packages are available. Anyone who
wishes to be included on the electronic mailing list for these
regular monthly updates should send a request to
[email protected] by e-mail.
In forming Table I all endonucleases cleaving DNA at a specific
sequence have been considered to be restriction enzymes,
although in most cases there is no direct genetic evidence for
the presence of a restriction modification system. The
endonucleases are named in accordance with the proposal of
Smith and Nathans (4).
25.
26.
27.
28.
29.
30.
31.
32.
33.
34.
35.
36.
37.
Roberts, R.J. (1990) Nucl. Acids Res. 18:2331-2365
Roberts, R.J. (1985) Nucl. Acids Res. 12:rl65-r200.
Kessler, C. and Mania, V. (1990) Gene 92: 1-248.
Smith, H.O. and Nathans, D. (1973) J. Mol. Biol., 81:419-423.
Barbes, C , Yebra, MJ., Novella, I.S., Sanchez, J. unpublished observations.
Chen, W., Pan, X., Chen, Z. unpublished observations.
Chen, Z. unpublished observations.
Chen, Z., Yang, R., Chen, B., Li, R. (1989) Fudan Xuebao, Ziran Kexueban
28: 96-101
Clark, D. unpublished observations.
Clark, D.R., Klein, S., Roberts, R.J. unpublished observations.
Cowan, D., Ward, J., Morgan, R. unpublished observations.
Degtyarcv, S.K. unpublished observations.
Earle-Hughes, J., Roberts, R.J. unpublished observations.
Elgar, G. unpublished observations.
Foerg, E., Saporito, L., Huang, S., Yang, J., Allen, M.M. (1990) FEMS
Microbiol. Letts. 69: 105-108
Frey, B., Lechner, M., Jarsch, M., Schmitz, G. unpublished observations.
Glatman, L.I., Terekhov, A.A., Kalnin, K.V., Bolotin, A.P., Rebentish,
B.A. (1990) Mol. Genet. Mikrobiol. Virusol. 3: 32
Grones, J. unpublished observations.
Grones, J., Tuma, J. unpublished observations.
Inagaki, K., Dou, D., Kite, K., Hiraoka, N., Kishimoto, N., Sugio, T.,
Tano, T. (1990) J. Ferment. Bioeng. 69: 60-62
Inagaki, K., Dou, D., Kobayashi, F., Hiraoka, N., Kishimoto, N.,Tano,
T. unpublished observations.
Inagaki, K., Kobayashi, F., Dou, D., Nomura, Y., Hiraoka, N., Kishimoto,
N. and Tano, T. unpublished observations.
Inagaki, K., Kobayashi, F., Dou, D., Nomura, Y., Kotani, H., Kishimoto,
N., Sugio, T. and Tano, T. (1990) Nucl. Acids Res. 18: 6155
Inagaki, K., Morimoto, Y., Hiraoka, N., Sugio, T., Tano, T. unpublished
observations.
Inagaki, K., Morimoto, Y., Sugio, T., Tano, T. unpublished observations.
Ishikawa, T., Yamada, Y. (1990) J. Gen. Appl. Microbiol. 36: 127-135
Janulaitis, A.A. unpublished observations.
Janulaitis, A.A., Kazlauslriene, R., Petrusyte, M. unpublished observations.
Janulaitis A., BitinaheJ., Jagelavicius M., NaurcckieneS., Vaitkevknus D.,
Maneliene Z., Kiuduliene L., Butkus V. unpublished observations.
Janulaitis A., BitinaheJ., Maneliene Z., Kiuduliene L., Butkus V. unpublished
observations.
Janulaitis A., Gilvonauskaite R., Petrusyte M. unpublished observations.
Janulaitis A., GrigaiteR., BrdnaheJ., MandieneZ., Butkus V., Kiuduliene
L. unpublished observations.
Janulaitis A., Grigaite R., Trinkunaite L., Maneliene Z., Bitinaite J.,
Kiuduliene L., Butkus V. unpublished observations.
Janulaitis A., Jagelavicius M., Bitinaite J. unpublished observations.
Janulaitis, A., Lazareviciute L., Bitinaite J., Maneliene Z., Kiuduliene L.,
Butkus V. unpublished observations.
Janulaitis A., Petrusyte M. unpublished observations.
Janulaitis A., Petrusyte M., Maneliene Z., Capskaya L., Kiuduliene L.,
Butkus V. unpublished observations.
2078 Nucleic Acids Research, Vol. 19, Supplement
38. Karginov, V.A., KovaJenko, S.P., Kotesnikov, V.A., Chikaev, N.A., Serov,
C D . , Repin, V.E. unpublished observations.
39. Klein, S., Roberts, R.J. unpublished observations.
40. Kotani, H., Nomura, Y., Kawashima, Y., Sagawa, H., Takagi, M., Kita,
A., Ito, H., Kato, I. (1990) Nucl. Acids Res. 18: 5637-5640
41. Leung, S.M., Kam, K.M., Shaw, P.C. unpublished observations.
42. Li, Y., Fu, P., Shi, L-Y. (1990) Chinese Biochem. J. 6: 309-313
43. Mise, K. unpublished observations.
44. Miyahara, M. and Mise, K. unpublished observations.
45. Morgan, R. unpublished observations.
46. Morgan, R., Reinecke, S. unpublished observations.
47. Muro-Pastor, A.M., Herrero, A., Rores, E. (1991) FEMS Microbiol. Lett
77: 1-4
48. Mushtaq, R., Sohail, A., Arif, A., Niazi, I.K. unpublished observations.
49. Nelson, M. unpublished observations.
50. Ochiai, H., Shibata, H., Sawa, Y., Ashida, N. (1989) Bull. Fac. Agr. Shimane
Univ. 23: 184-191
51. Polisson, C. unpublished observations.
52. Polisson, C , Barsomian, J. unpublished observations.
53. Polisson, C , Meloni, A. unpublished observations.
54. Polisson, C , Morgan, R.D. (1990) Nucl. Acids Res. 18: 5911
55. Prihodko, G.G., Degtyarev, S.K., Rechkunova, N.I., Sosnovsev, S.V.,
Tchigikov, V.E. (1990) Biotekhnologiya 1: 12-16
56. Repin, V.E., Andreeva, I.S., Sizov, A.A., Khomov, V.V. unpublished
observations.
57. Repin, V.E., Rechkunova, N.I., Degtyarev, S.K., Hachaturyan, A.A.,
Afrikyan, E.K. (1989) Biol. J. Armenia 42: 969-972
58. Repin, V.E., Serov, G.D., Lebedev, L.R. unpublished observations.
59. Rina, M., Stratidakis, I., Bouriotis, V. (1990) Nucl. Acis Res. 18: 6161
60. Ronka, J., Tenkanen, T., Hjorleifsdottir, S. unpublished observations.
61. Ryu, C.J., Lee, C.H., Yoo, O.J. (1989) Korean Biochem. J. 22: 444-447
62. Serov, G.D., Tercschenko, T.A., Puchkova, L.I., Repin, V.E. unpublished
observations.
63. Simcox, T.G. unpublished observations.
64. Sokolov, N.N., Anikeitcheva, N.V., Eldarov, M.A., Rtsner, A.B.,
Karpichev, I.V., Kalugin, A.A., Samko, O.T., Choroshoutina, E.B.
unpublished observations.
65. Sokolov, N.N., Anikeitcheva, N.V., Rtsner, A.B., Choroshoutina, E.B.,
Kalugin, A.A. unpublished observations.
66. Sokolov, N.N., Anikeitcheva, N.V., Kalugin, A.A., Choroshoutina, E.B.,
Berlin, Y.A., Plutalov, O.V., Gnedoi, S.N., Votrin, I.I. unpublished
observations.
67. Sokolov, N.N., Anikeitcheva, N.V., Kalugin, A.A., Samko, O.T.,
Choroshoutina, E.B., Fitsner, A.B. unpublished observations.
68. Sokolov, N.N., Anikeitcheva, N.V., Samko, O.T., Kalugin, A.A., Rtsner,
A.B. unpublished observations.
69. Sokolov, N.N., Eldarov, M.A., Anikeitcheva, N.V., Karpichev, I.V., Samko,
O.T., Rtsner, A.B., Kalugin, A.A. unpublished observations.
70. Sokolov, N.N., Eldarov, M.A., Fitsner, A.B., Anikeitcheva, N.V.,
Karpichev, I.V., Kalugin, A.A., Samko, O.T., Choroshoutina, E.B.
unpublished observations.
71. Sokolov, N.N., Fitsner, A.B., Anikeitcheva, N.V., Kalugin, A.A.
unpublished observations.
72. Sokolov, N.N., Fitsner, A.B., Anikeitcheva, N.V., Kalugin, A.A., Samko,
O.T. unpublished observations.
73. Sokolov, N.N., Fitsner, A.B., Anikeitcheva, N.V., Samko, O.T.,
Choroshoutina, E.B., Kalugin, A.A. unpublished observations.
74. Sokolov, N.N., Fitsner, A.B., Anikeitcheva, N.V., Samko, O.T., Kalugin,
A.A. unpublished observations.
75. Solaiman, D.K.Y., Somkuti, G.A. (1990) FEMS Microbiol. Lett 67:
261-266
76. Stefan, C , Xia, Y. and Van Etten, J.L. unpublished observations.
77. Steponaviciene D., Petrusyte M., Janulaitis A. unpublished observations.
78. Traykjv, E., Xia, Y., Zhang, Y., Roy, P.H. and Van Etten, J.L. unpublished
observations.
79. Wemette, C M . , SakJahna, R., Periman, P.S., Butow, R.A. (1990) J. Bid.
Chem. 265: 18976-18982
80. White, D. and Simcox, T.G. unpublished observations.
81. Wijdenbosch, M.M. unpublished observations.
82. Yamamoto, K., Sagawa, H., Kotani, H., Hiraoka, N., Nakamura, T.
unpublished observations.
83. Yau, E.K., Coward, J.K. (1989) Abstr. Am. Chem. Soc. 198: 100
84. Zernov, Y.P., Lebedev, L.R., Babtrin, I.V., duzhikov, V.E. (1990) Bioorg.
Khim. 16: 603-604
85. Zhou, B., Morgan, R. unpublished observations.
Acidiphilium species 32H
Acidiphilium species 29H
Acidiphilium species 27H
Acidiphilium species 26H
Acidiphilium species 21H
Acidiphilium species 18H
Acidiphilium species 17H
Acidiphilium species 16H
Acidiphilium species 14H
Acidiphilium species 8H
Acidiphilium species 6H
Acidiphilium species 5H
Acidiphilium species 2H
Acidiphilium species 1H
Acidiphilium species 22
Acidiphilium species 17
Acidiphilium species 15
Acetobaaer pasteurianus D
Acetobacter pasteurianus C
Acetobacter pasteurianus B
Acetobacter pasteurianus
Microorganism
IC Inagaki
K.Inagaki
K.Inagaki
K.Inagaki
K.Inagaki
K.Inagaki
K.Inagaki
K.Inagaki
K.Inagaki
K. Inagaki
IC Inagaki
K.Inagaki
K. Inagaki
K.Inagaki
K. Inagaki
K. Inagaki
K. Inagaki
K. Inagaki
J. Grones
J. Grones
J. Grones
IFO 13752
Source
Asp36HI (Bsml)
Asp35HI (Bsml)
AspttHI (Sacll)
Asp29Hl (Rsal)
AspllHl (BsmT)
Asp26W (Bsml)
Asp2\m (Xholl)
Aspl8Hl(RsaT)
Asplim (Rsal)
Aspl6HI (Rsal)
AspUHl (Xholl)
Asp8HI (Xholl)
Asp6Hl (Xholl)
Asp5HI (Sphl)
AspliU. (EcoRH)
Aspim (XhoE)
Asp22l (Xholl)
Asplll (Xholl)
Asp\5l(Xhol)
ApaDl
ApaCl (BarriHl)
ApaBI
ApaORl (EcoRIl)
Enzyme1
(Bsml)
GAATGC (1/-1)
GAATGC (1/-1)
GAATGC (1/-1)
CCGCGG
GTAC
GAATGC (1/-1)
GAATGC (1/-1)
RGATCY
GTAC
GTAC
GTAC
RGATCY
RGATCY
RGATCY
GCATGC
CCWGG
RGATCY
RGATCY
RGATCY
CTCGAG
?
GGATCC
GCANNNNNtTGC
CCtWGG
Sequence2
46
46
46
46
4
113
46
46
21
113
113
113
21
21
21
6
71
21
21
21
1
>20
5
34
71
10
10
10
10
33
83
10
10
22
83
83
83
22
22
22
8
136
22
22
6
22
?
3
20
136
4
4
4
4
0
12
4
4
3
12
12
12
3
3
3
2
17
3
3
3
0
?
1
5
17
4
4
4
4
1
11
4
4
0
11
11
11
0
0
0
0
2
0
0
0
1
?
0
2
2
1
1
1
1
0
3
1
1
8
3
3
3
8
8
8
1
6
8
8
8
0
?
1
2
6
22
22
22
23
21
21
22
22
21
21
21
21
21
21
21
21
21
21
21
21
19
18
19
26
:ids
<v
TABLE 1
Acidiphilium species 3SH
IC Inagaki
AJ/>40HI
GAATGC (1/-1)
Number of Cleavage Sites3
X Ad2 SV40 <X>X pBR References
Acidiphilium species 36H
IC Inagaki
AipSOHI (Bsml)
'ucle
21
Acidiphilium species 40H
K. Inagaki
50
X
>
Acidiphilium species 50H
•arch
&
ipple
3
t 2079
Microorganism
K. Inagaki
Source
Afal6W {Pvul)
Afa22Ml {Pvul)
Enzyme1
CGAtTCG
CGAtTCG
Sequence2
3
3
7
7
0
0
X Ad2SV40
0
0
1
1
20
20
Number of Cleavage Sites3
Acidiphilium species 22M
K. Inagaki
References
Acidiphilium species 16R
K. Inagaki
Arthrobacter citreus
Agrobactenum tumefaciens RFLl
NEB #688
NEB 577
A.A. Janulaitis
Ascl
Acil
AtulU {BamHI)
GGtCGCGCC
CCGC (-2/-2)
GGATCC
GCCGGC
2
516
5
1
2
582
3
13
0
11
1
1
0
36
0
0
0
67
1
4
45
54
28
21
<DX pBR
Acidiphilium facilis 24R
Arthrobacter species
65
74
15
71
1
2
1
0
11
0
3
164
0
24
74
2
15
GtGNCC
15
CAGtCTG
BavBU {Asul)
ATCGAT
BavBl {Pvull)
BavCl {Clal)
N.N. Sokolov
N.N. Sokolov
64
Bacillus alvei B
Bacillus alvei C
9
69
3
?
73
1
?
1
70
57
?
0
>5
7
25
?
0
?
1
59
GtGYRCC
>18
2
?
1
7
9,10
BbvBl {HgiCl)
15
?
2
0
0
9
N.N. Sokolov
>20
30
1
2
1
9
Bacillus brevis B
?
28
40
0
0
15
?
BciBU
CTGCAG
61
4
0
2
BciM
BmeBl {Pstl)
RtCCGGY
1
2
11
N.N. Sokolov
Z. Chen
BssM {CfrlOl)
CtGTACG
15
164
Bacillus circulars A
Bacillus megaterium B78
V. Bouriotis
BsiWl {SpH)
ATtCGAT
74
11
ATCGAT
Bacillus species
D. Clark
BsiXl {Clal)
GtGNCC
20
BciBl {Clal)
Bacillus species
D. Clark
BsiZl {Asul)
19
N.N. Sokolov
Bacillus species
D. Clark
10
Bacillus circulans B
Bacillus species
216
66
CCNNNNNtNNGG 176
22
72
Bsll {BsiYl)
0
22
68
NEB 606
0
1
14
Bacillus species
0
42
12
87
87
0
31
0
9
116
116
2
24
0
1
BspFl {Mbol)
15
411
1
4
N.N. Sokolov
380
8
4
Bacillus species
BspJU {Clal)
GCNGC
6
10
8
8
BssXl {FnuAHI)
GCtTNAGC
46
BspJl {Mbol)
G. Elgar
Bspl720l {Espl)
GAATGC
N.N. Sokolov
Bacillus species
S.K. Degtyarev
BscCl {Bsml)
Bacillus species
Bacillus species 1720
D.Clark
tGATC
tGATC
ATtCGAT
Bacillus species 2G
i
O'
8
I
Bacillus species RFL143
Bacillus species RFL142
Bacillus species RFL141
Bacillus species RFrL140
Bacillus species RFL139
Bacillus species RFL138
Bacillus species RFL137
Bacillus species RFL136
Bacillus species RFL135
Bacillus species RFL133
Bacillus species RFL132
Bacillus species RFL131
Bacillus species RFL130
Bacillus species RFL129
Bacillus species RFL128
Bacillus species RFL127
Bacillus species RFL126
Bacillus species RJ5L125
Bacillus species RFL71
Bacillus species E l 3
Bacillus species Cl
Microorganism
Z.Chen
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
D.Qaric
T.G. Simcox
Source
Bsp¥\05l (Caiill)
Bsp¥53l (Avail)
Bsp\43l (MboT)
Bsp\42l (Xhol)
Bsp\4\\(Xho\)
BsplAQX (Xhol)
Bsp\39\(Xhol)
Bspmi(MboT)
Bsp\31l(HaeUT)
Bsp\36l (MboT)
Bsp\35l (Mbol)
Bspl33l (Avail)
Bsp\32l (Avail)
Bspl3U(BamHl)
Bsp\3Ol (BamYO)
Bspl29l (Xhol)
Bspl2&l (Avail)
Bsp\21\ (CldT)
Bspl26I (CldT)
Bsp\25l (CldT)
BsplU (Avail)
BscDl (Pstl)
BspCl (PvuT)
Enzyme1
ATCGAT
CCSGG
GGWCC
GATC
CTCGAG
CTCGAG
CTCGAG
CTCGAG
GATC
GGCC
GATC
GATC
GGWCC
GGWCC
GGATCC
GGATCC
CTCGAG
GGWCC
ATCGAT
ATCGAT
ATCGAT
GGWCC
CTGCAG
CGATtCG
Sequence2
28
15
114
35
116
1
1
1
1
116
149
116
116
35
35
5
5
1
35
15
15
15
35
28
3
30
2
97
73
87
6
6
6
6
87
216
87
87
73
73
3
3
6
73
2
2
2
73
30
7
2
0
0
6
8
0
0
0
0
8
18
8
8
6
6
1
1
0
6
0
0
0
6
2
0
X Ad2SV40
1
0
1
1
0
1
1
1
1
0
11
0
0
1
1
0
0
1
1
0
0
0
1
1
0
1
1
10
8
22
0
0
0
0
22
22
22
22
8
8
1
1
0
8
1
1
1
8
1
1
7
7
7
7
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
9
63
§.
1
Acic
?>•
Number of Cleavage Sites3
Bacillus species cy53
Z.Chen
Bspl45l (Cldt)
CTGCAG
References
Bacillus species cylO5
Z.Chen
Bsp26Zl (Psd)
<X>X pBR
Bacillus species cyl45
Z.Chen
S"
Bacillus species cy268
Vol. 19,
f
f
a
I
Bacillus stearothermophilus 77
Bacillus stearothermophilus 30
Bacillus stearothermophilus 29
Bacillus stearothermophilus 28
Bacillus stearothermophilus 1274
Bacillus stearothermophilus 1
Bacillus sphaericus DC3
Bacillus sphaericus DC2
Bacillus sphaericus DC1
Bacillus sphaericus 1894
Bacillus sphaericus
Bacillus sphaericus
Bacillus species cy317
Microorganism
Z.Chen
V.E. Repin
V.E. Repin
V.E. Repin
S.K. Degtyarev
Z.Chen
V.E. Repin
D.Clark
D.Clark
D.Clark
KCTC1188
P.C. Shaw
NEB 659
Z.Chen
Source
BsaCl (ScrFT)
BsrCl (ClaT)
Bsflll (Bell)
BsGOl (Said)
Bst29l (Said)
Bstm (ClaT)
Bst\274l (Mbol)
Bstll (EcoEll)
BshMl (HpaE)
BshU. (EcoKV)
Bspimi(Asul)
Bshm (Seal)
Bspl (Mbol)
Bad
Bsp3ni(EcoRO)
Enzyme 1
CCWGG
CCNGG
ATCGAT
TGATCA
CCTNAGG
CCTNAGG
ATCGAT
GATC
CCWGG
CCGG
GATATC
AGTACT
GtGNCC
GATC
ACNNNNGTAYC
CCWGG
Sequence2
35
71
185
15
8
2
2
15
116
71
328
21
5
74
116
10
71
216
73
136
233
2
5
7
7
2
87
136
171
9
5
164
87
5
136
18
6
17
17
0
1
0
0
0
8
17
1
1
0
11
8
0
17
11
1
2
3
0
0
0
0
0
0
2
5
0
0
2
0
1
2
22
8
6
16
1
0
0
0
1
22
6
26
1
1
15
22
0
6
6
6
6
7
7
56
62
62
57,83
7
58
9
9
9
61
41
85
7
Bacillus stearothermophilus CPW9
Z.Chen
Z.Chen
BsrMl (Mbol)
BsaHl (Acyl)
BsrEl (Ksp632T)
BsaWl
RCCGGY
GATC
GRCGYC
CTCTTC
?
110
61
116
40
34
?
30
86
40
87
44
29
?
2
11
1
8
0
1
?
1
9
0
0
7
2
?
1
19
7
22
6
2
?
6
7
6
6
6
6
6
*
S
i.
•**
*men
Bacillus stearothermophilus CPW11
Z.Chen
BsrFl (CfrlOT)
ACTGG
28
cleic Acids Rest
Bacillus stearothermophilus CPW13
Z.Chen
BsrSl (Bsrl)
CTGCAG
208
Bacillus stearothermophilus C1825
Z. Chen
BsaNl (EcoKU)
GGWCC
149
Number of Cleavage SitesJ
Bacillus stearothermophilus C34
Z.Chen
BsrM (Avail)
GGCC
References
Bacillus stearothermophilus CPW1
Z. Chen
BsaRl (HaelU)
Bacillus stearothermophilus CPW16
Z.Chen
BsaQl (Pstt)
OX pBR
Bacillus stearothermophilus CPW7
Z.Chen
Bacillus stearothermophilus CPW19
Z.Chen
X Ad2 SV40
Bacillus stearothermophilus CPW8
Bacillus stearothermophilus CPW59
Brevibacterium acetyliticum
Bacteroides fragilis
Bacteroides fragilis
Bacteroides caccae
Bacillus stearothermophilus V018
Bacillus stearothermophilus 022
Bacillus stearothermophilus M293
Bacillus stearothermophilus L170
Bacillus stearothermophilus K524
Bacillus stearothermophilus G426
Bacillus stearothermophilus F272
Bacillus stearothermophilus EJO4
Bacillus stearothermophilus D144
Bacillus stearothermophilus D47
Bacillus stearothermophilus CPWI
Microorganism
G.G. Prikhodko
NEB 678
NCTC 11155
NEB 668
NEB 669
ZLChen
Z.Chen
Z.Chen
Z. Chen
Z.Chen
Z.Chen
Z.Chen
Z. Chen
Z.Chen
Z.Chen
Z.Chen
Source
Bln\ (Avrll)
Biml (AsuU)
Bed
BfrAd (Clal)
Bfal (MaeT)
Bed
BsaVl (Bbvll)
BsaOl (Mcri)
BsaMl (BsmI)
BsdLl (Alul)
BsaKl (//pal)
BsaGl (HgiAT)
BsaFl (AflU)
BsaEl (NlalV)
BsaDl (flamHI)
BsaSl (Asul)
BsaNU (Pstl)
Enzyme1
CtCTAGG
TTtCGAA
WtCCGGW
ATCGAT
CtTAG
CCATC
GAAGAC
CGRYCG
GAATGC
AGCT
GTTAAC
GWGCWC
CTTAAG
GGNNCC
GGATCC
GGNCC
CTGCAG
Sequence2
2
7
81
15
13
145
24
22
46
143
14
28
3
82
5
74
28
2
1
28
2
54
27
62
50
10
158
6
38
4
178
3
164
30
2
0
0
0
12
10
3
0
4
34
4
0
1
16
1
11
2
X Ad2SV40
0
0
3
0
3
12
3
1
4
24
3
3
2
6
0
2
1
0
0
5
1
5
9
3
7
1
16
0
8
0
24
1
15
1
82
45,55
85
9
46
46
7
7
7
7
7
7
7
7
7
7
6
Number of Cleavage Sites3
Brevibacterium immotum
IAM1902
Cas2I
A.A. Janulaitis
Cfr56l (EcoSIT)
Cfr55l (CfrT)
CvifW (Rsal)
TCCGGA
GGTCTC
YGGCCR
GTTAC
TGtCA
CGATCG
71
24
2
39
113
273
3
4
136
8
18
70
83
206
7
1
17
0
0
0
12
36
0
2
2
0
0
2
11
18
0
0
6
1
1
6
3
21
1
32
27
27
27
27
78
27
al
tr
%
•leic
Citrobacter freundii RFL55
A.A. Janulaitis
CfrSTl (BspMO)
CCWGG
3
76,78
Gtrobacter freundii RFL56
A.A. Janulaitis
Cfr5%\ (EcoRK)
CTTAAG
References
Brevibacterium linens
A.A. Janulaitis
CviRI
Citrobacter freundii RFL57
A.A. Janulaitis
Cfi92l(A/ni)
<X>X pBR
Caulobacter species RFL2
JX. Van Etten
Citrobacter freundii RFL58
A.A. Janulaitis
(PVMI)
Chlorella strain NC64A (XZ-6E)
Citrobacter freundii RFL92
search, 1
g
f
f
•nt 2083
rv
Erwinia species RFL16
Enterobacter species RFL3
Enterobacter cloacae RFLl
Enterobacter aerogenes RFL2
Comamonas testosteroni RFLl
Microorganism
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Source
Esp24l (EcoKtt)
Esp23l (Espll)
Esp2\l (HgiCi)
Esp\6l (Esp3l)
Ese3l (SaclT)
Eclll (Sacll)
Eaell QChoY)
Crcll (SacE)
Enzyme1
GGYRCC
CCWGG
CGTCTC
GGYRCC
CGTCTC
CCGCGG
CCGCGG
CTCGAG
CCGCGG
Sequence2
25
114
71
14
25
14
4
4
4
1
97
10
57
136
21
57
21
33
33
6
33
1
17
0
1
0
0
0
0
0
3
1
2
0
3
0
1
1
1
1
6
9
1
0
1
0
0
0
X Ad2 SV40 <DX pBR
27
27
27
27
27
27
Number of Cleavage Sites3
Erwinia species RFL21
A.A. Janulaitis
Esp2Sl (HgiO)
CCSGtG
13
0
0
3
References
Erwinia species RFL23
Erwinia species RFL24
A.A. Janulaitis
Ecom (CauU)
GtGTNACC
33
52
2084 Nuc:leic Acids
2
§.
^.
So
27
1
27
17
£?
^°
9
10
uppk
Escherichiacoli HI
H. Matsumoto
0
Escherichia coli 0128
Ecoll2l(Eco51T)
CCGCGG
43
27
A.A. Janulaitis
Ecol5U (Sacll)
GCGCGC
0
2
Escherichia coli RFLl 12
A.A. Janulaitis
Eco\52l (BsePT)
GRGCYC
23
Escherichia coli RFL151
A.A. Janulaitis
Eco249l (HgiJU)
CCWGG
17
0
2
7
1
0
2
0
1
27
84
57
136
5
0
17
7
7
0
0
6
2
136
29
11
0
1
27
52
13
7
0
67
0
1
1
Escherichia coli RFL152
A.A. Janulaitis
Eco254l (EcoRll)
AGTtACT
5
71
27
Erwinia species RFL25
L.I. Glatman
£coO128I (BsfEU)
CTGAAG
40
4
6
Escherichia coli RFL249
A.A. Janulaitis
Eco255l (Seal)
CCWGG
27
27
27
Escherichia coli RFL254
A.A. Janulaitis
Eco256l (EcoRll)
RtAATTY
58
6
0
0
2
Escherichia coli RFL255
A.A. Janulaitis
Fsil
AGGCCT
33
1
0
4
1
0
0
2
Escherichia coli RFL256
NEB 685
GobAl (Stul)
CGATCG
3
4
7
71
Frankia species
Glaxo 2323C
KpH9l (Pvul)
CCGCtGG
0
6
1
Geodermatophilus obscurus
A.A. Janulaitis
Kpn378I (SaclT)
33
27
29
27
45
Klebsiella planticola RFL79
Y.P. Zemov
4
Klebsiella pneumoniae 378
CCGCGG
A.A. Janulaitis
Kpn\9l (Sactt)
Klebsiella pneumoniae RFLl9
2
Kasl (NarT)
0
NEB 593
GtGCGCC
Kluyvera ascorbata
?
?
?
Leal
20
?
N.N. Sokolov
1
>12
Lactobacillus casei
Source
MOKAI {NaeV)
Enzyme1
GGCGCC
GCCGGC
Sequence2
1
1
20
13
0
1
X Ad2SV40
2
0
4
4
13
39
Number of Cleavage Sites3
Microorganism
NRRLB16091
McaAd (Narl)
NRRL3097
Msal (Narl)
Mhal (Xhol)
ATCC 21561
CTCGAG
GGCGCC
CTCGAG
Mizl (PsA)
1
1
1
CTGCAG
6
20
6
28
0
0
0
30
1
2
1
2
0
0
4
0
1
42
39
39
39
139
References
Micromonospora aurantiaca
NRRL2997
Micromonospora halophytica
NRRLB16084
MscAl (Xhol)
0
4>X pBR
Micromonospora carbonacea
Micromonospora saitamica
NRRLB16O86
0
Micromonospora chalcea sp. izumensis
Micromonospora scalabitana sp
sporogenes
11
47,79
6
1
50
AtGATCT
0
22
50
Ncrl (Bglil)
1
11
0
12
Y.Li
3
18
0
1
12
Nocardia carnea C-212
5
0
0
1
13
47
GGATCC
149 216
1
0
0
1
27
0
Mp29132II (BamHT)
GGtCC
7
7
3
0
0
27
0
Plal (HaeUl)
TTtCGAA
3
24
2
1
1
27
2
0
PlalL (AsuS)
CGATCG
15
8
0
1
1
27
3.
1
Pv«84I (PvuT)
CAGtCTG
6
33
2
1
1
27
7
PvuMU
GCATGC
4
30
2
1
1
27
TTCGAA
PaeCl (Sphl)
CCGCGG
28
30
1
0
27
Nsp29l32I (AmU)
NRC5OO3
Paeil (SacU)
CTGCAG
28
30
2
2
1
1
27
ATCC 29132
Pseudomonas aeruginosa
A.A. Janulaitis
PaeZl (Pstl)
CTGCAG
28
30
0
1
1
27
Nostoc species
Pseudomonas aeruginosa RFL7
A.A. Janulaitis
Pae9l (Pstl)
CTGCAG
28
33
2
1
1
H. Ochiai
Pseudomonas aeruginosa RFL8
A.A. Janulaitis
PaeUI (Pstl)
CTGCAG
4
30
2
1
1
27
27
Phormidium lapideum
Pseudomonas aeruginosa RFL9
A.A. Janulaitis
Pae\5\ (Pstl)
CCGCGG
28
30
2
0
Pseudomonas aeruginosa RFL26
Pseudomonas aeruginosa RFL25
Pseudomonas aeruginosa RFL24
A.A. Janulaitis
A.A. Janulaitis
Pae26l (Pstl)
S.K. Degtyarev
Pseudomonas aeruginosa RFL14
A.A. Janulaitis
PaeMl (SacU)
CTGCAG
28
30
1
1
CCGCGG
Proteus vulgaris 84
Pseudomonas aeruginosa RFL15
A.A. Janulaitis
Pae22l (Pstl)
CTGCAG
28
2
0
Pae36l (SacE)
(PVUU)
Pseudomonas aeruginosa RFL17
A.A. Janulaitis
PaelAl (Pstl)
CTGCAG
30
33
A.A. Janulaitis
I
I
I
<•>•
I
Pseudomonas aeruginosa RFL22
A.A. Janulaitis
PaelSl (Pstl)
CTGCAG
28
4
Pseudomonas aeruginosa RFL36
Pseudoraonas aeruginosa RFL41
Pseudomonas aeruginosa RFL40
Pseudomonas aeruginosa RFL39
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Pae43l (SaclT)
Pae42l (SacTT)
Pae4U (PstT)
Pae40l (PstT)
Pae391 (PstT)
CCGCGG
CCGCGG
CCGCGG
CTGCAG
CTGCAG
CTGCAG
0
4
4
4
28
28
28
216
1
33
33
33
30
30
18
0
0
0
0
2
2
2
11
0
1
1
1
1
1
1
22
0
0
0
0
1
1
1
48
51
27
27
27
27
27
References
Pseudomonas aeruginosa RFL42
A.A. Janulaitis
Pae44l (SaclT)
TTAATtTAA
149
<1>X pBR
Number of Cleavage Sites3
X Ad2SV40
Pseudomonas aeruginosa RFL43
A.A. Janulaitis
Pacl
GGtCC
2
Sequence2
Pseudoraonas aeruginosa RFL44
NEB 585
PfKl (HaellT)
GAGCTC
16
73
Enzyme l
Pseudomonas alcaligenes
CAMB 2619
GGWCC
35
4
Source
Pseudomonas fluorescens
A.A. Janulaitis
Pfim(SacT)
Pfl\91 (Avail)
GTGCAC
Microorganism
Pseudoraonas fluorescens RFL18
A.A. Janulaitis
P/1231 (ApaLT)
30
Pseudomonas fluorescens RFL19
A.A. Janulaitis
Pseudomonas putidaRFL6
Pseudomonas putida Al
Pseudomonas medicaginis RFL35
Pseudomonas indigofera
Pseudomonas lindbergii
Pseudomonas glathei RFL34
Pseudomonas fragiRFL12
Pseudoraonas fluorescens RFL37
A.A. Janulaitis
P. Adams
A.A. Janulaitis
ATCC 31099
ATCC 14036
A.A. Janulaitis
A.A. Janulaitis
Pseudomonas fluoroviolaceus RFL16 A.A. Janulaitis
Pseudomonas fluorescens RFL67
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Ppulll (BsaAT)
PpulOl (AvaUT)
Ppu6l (BsaAT)
PpuAl (SplT)
Pme'iSl (HpaTT)
Phi (ApaLT)
Pinl (ScaT)
Pgt34l (Pmad)
PfrUl (ApaLl)
P/716I (EcoRV)
Pfl61\ (XhoT)
Pftm (PstT)
/7723II (SplT)
AGGCCT
YACGTR
ATGCAT
YACGTR
CtGTACG
CCGG
GTGCAC
AGTACT
CACGTG
GTGCAC
GATATC
CTCGAG
CTGCAG
CGTACG
6
14
14
14
1
328
4
5
3
4
21
1
28
1
11
9
22
22
171
4
7
5
10
7
30
6
9
7
4
7
0
3
0
0
0
0
0
0
1
0
2
0
0
6
0
1
0
2
2
5
2
0
0
1
1
0
1
1
2
1
1
0
0
0
1
0
1
26
3
1
0
3
1
0
1
0
3
8
0
49
27
27
39
39
27
27
27
27
27
30
27
27
27
27
Pseudomonas fluorescens RFL23
Pseudomonas putida RFL10
A.A. Janulaitis
Ppul31 (StuI)
1
Pseudomonas putida RFL11
A.A. Janulaitis
27
27
27
Pseudomonas putida RFL13
I
o
!
5=
I
Pseudomonas species
Pseudomonas species
Pseudomonas putidaRFL21
Pseudomonas putida RFL20
Microorganism
A.A. Janulaitis
D.Claric
D. White
A.A. Janulaitis
A.A. Janulaitis
Source
Psp4l (XhoT)
Psp3l (PvuU)
PspBl (PmaCX)
PspAl (Smal)
PpulU (BsaAI)
PpulOl (HgUU)
Enzyme1
CAGCTG
CTCX3AG
CAGCTG
CACGTG
CtCCGGG
GRGCYC
YACGTR
Sequence2
15
1
15
3
3
7
14
24
6
24
10
12
57
22
3
0
3
0
0
0
2
X Ad2SV40
0
1
0
0
0
2
0
1
0
1
0
0
2
1
37
27
27
9
80
35
Number of Cleavage Sites3
Pseudomonas species RFL3
A.A. Janulaitis
Psp5l (PvuJJ)
Pseudomonas species RFL46
Pseudomonas species RFL38
Pseudomonas species RFL33
Pseudomonas species RFL32
Pseudomonas species RFL31
Pseudomonas species RFL30
Pseudomonas species RFL29
Pseudomonas species RFL28
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Psp%9l (Son)
Psp56l (BamHT)
Psp461 (PsA)
Psp3%l (PmaO)
Psp33l (Sail)
Psp32l (SaO)
Psp3U(Hgini)
Psp30l (ApaY)
Psp29l (HaeUT)
Psp2&l (PsA)
PspSU (PpuMT)
GGATCC
CTGCAG
CACGTG
GTCGAC
GTCGAC
GRGCYC
GGGCCC
GGCC
CTGCAG
RGGWCCY
5
28
3
2
2
7
1
149
28
3
3
30
10
3
3
57
12
216
30
23
1
2
0
0
0
2
1
18
2
1
0
1
0
0
0
0
0
11
1
0
1
1
1
0
1
1
2
0
22
1
2
34
27
27
27
27
27
27
27
27
37
27
References
Pseudomonas species RFL4
A.A. Janulaitis
Pseudomonas species RFL56
A.A. Janulaitis
OX pBR
Pseudomonas species RFL5
Pseudomonas species RFL89
27
5"
SO
1
0
81
i.
0
4
5
3
1
60
2
0
5
45
GTCGAC
0
3
1
27
3
3
12
1
15
27
2
2
54
0
2
15
36
3
GTCGAC
13
7
11
2
15
8
RrMim
CTTAG
10
164
11
2
TtCATGA
Rmal (MaeT)
GCTCTTC(l/4)
74
164
11
M M . Wijdenbosch Real (BspHY)
T. Tenkanen
Sapl
GGNCC
74
164
Rhodococcus capsulatum
Rhodothermus marinus
NEB 597
Scum (AsuT)
GGNCC
74
(Sail)
Saccharopolyspora species
A.A. Janulaitis
SauSl (AsuT)
GGNCC
ATCC4273
Staphylococcus aureus RFL2
A.A. Janulaitis
Sau\3l(Asu[)
Rhodococcus rtiodochrous
Staphylococcus aureus RFL5
A.A. Janulaitis
!
5=
Staphylococcus auieus RFL13
Streptomyces tanashiensis
Streptomyces takatoensis
Streptomyces species 8387
Streptomyces olivochromogenes
Streptomyces moderatus
Streptomyces corchorusii
Streptomyces bikiniensis JAM68
Staphylococcus wameri
Staphylococcus aurcus RFL17
Staphylococcus aurcus RFL16
Staphylococcus aureus RFL15
Staphylococcus aurcus RFL14
Microorganism
ATCC 33159
ATCC 27649
Takara#8387
S.K. Degtyarev
DSM 40529
ATCC 25444
S.K. Degtyarcv
Streptococcus themiophilus strain 134 D.K.Y. Solaiman
Streptococcus faecium
MM. Wijdenbosch SunI (SpO)
NEB 674
B. Frcy
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Source
StaAlQChoT)
Stal (SacE)
S*e8387I
So/101791 (Xhol)
Smo40529l (Noel)
ScoAl (Psff)
SW68I (Xhol)
Sth\34l(HpdH)
Sfcl
Swal
SauYR (Ami)
Saul6l (EcoRE)
Sau\5l(MboT)
Sau\4l (Ami)
Enzyme1
CtGTACG
CTCGAG
CCGCGG
CCTGCAtGG
CtTCGAG
GCCGGC
CTGCAG
CtTCGAG
CtOGG
CTYRAG
ATTTTAAAT
GGNCC
CCWGG
GATC
GGNCC
Sequence2
1
1
4
5
1
1
28
1
328
17
0
74
71
116
74
6
4
33
3
6
13
30
6
171
29
1
164
136
87
164
0
0
0
1
2
0
1
4
1
11
17
8
11
1
0
1
0
1
1
5
5
0
2
2
0
2
0
0
0
4
1
0
26
6
0
15
6
22
15
X Ad2 SV40 <DX pBR
39
40
12
12
13
12
75
53
16
27
27
27
36
Number of Cleavage Sites3
Synechococcus uniformis
PCC6308
Thermococcus litoralis
Z.Chen
NEB 521
Tspll (Bsrl)
TspAl (EcoRll)
TUT. (Xhol)
SynU (XmrX)
Synl (Avail)
?
ACTGG(1/-1)
CCWGG
CTCGAG
GAANNNNTTC
GGWCC
2
2
110
71
1
24
35
?
?
86
136
6
5
73
?
?
11
17
0
0
6
0
0
0
0
9
2
1
3
1
2
1
0
0
0
19
6
0
2
8
0
0
25
24
25
25
38
8
45
15
15
81
13
1
I
Resttarci
Thermophilic species
V.E. Repin
Tfel
?
1
0
cleic A
Thermus species strain 1
ICInagaki
Tnol
4
0
References
Synechocystis species
Thiobacillus ferrooxidans AP19-3
IFO 12443
CCGCGG
0
?
Thiobacillus novellus
Ttol (SacH)
33
?
ICInagaki
1
Thiobacillus thiooxidans ON106
?
Tvel
27
IFO 14567
22
Thiobacillus versutus
0
GATC
8
UbaAl (Mbol)
87
A.A. Janulaitis
116
Unidentified bacterium RFL4
Unidentified bacterium RFL59
Unidentified bacterium RFLS8
Unidentified bacterium RFL57
Unidentified bacterium RFL54
Unidentified bacterium RFL51
Unidentified bacterium RFL48
Unidentified bacterium RFL46
Unidentified bacterium RFL43
Unidentified bacterium RFL42
Unidentified bacterium RFL41
Unidentified bacterium RFL40
Unidentified bacterium RFL39
Unidentified bacterium RFL38
Unidentified bacterium RFL36
Unidentified bacterium RFL34
Unidentified bacterium RFL31
Unidentified bacterium RFL30
Unidentified bacterium RFL24
Unidentified bacterium RFL22
Unidentified bacterium RFL20
Unidentified bacterium RFL19
Unidentified bacterium RFL17
Unidentified bacterium RFL13
Unidentified bacterium RFL11
Unidentified bacterium RFL9
Microorganism
A.A. Janulaitis
A. A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Source
Uba59l (Mbol)
UbaSSl (EcdRI)
UbaSll (Hgim)
Uba54l (HaelU)
Uba5ll(BamHI)
Uba4Sl (Avail)
Uba46l (Pstl)
Uba43l (CM)
UbaAll (CaulT)
Uba4U(Caull)
UbaMl (StuT)
Uba39\ (HgOlT)
Uba3Sl (BamHT)
Uba361 (CfrT)
Uba34l (CM)
Uba3U (flamffl)
Uba30l (CM)
Uba24l (CM)
UbcCm (CM)
Ulxi20l (£coRU)
Uba\9l (BamHT)
Uballl (ScrFI)
Ubal3l (EcoRJJ)
UbalUiEcoKO)
Uba9l (HaeUT)
Enzyme1
GGCC
CCWGG
CCWGG
CCNGG
GGATCC
CCWGG
ATCGAT
ATCGAT
ATCGAT
GGATCC
ATCGAT
YGGCCR
GGATCC
GRGCYC
AGGCCT
CCSGG
CCSGG
ATCGAT
CTGCAG
GGWCC
GGATCC
GGCC
GRGCYC
GAATTC
GATC
Sequence2
97
22
6
References
11
2
6 31
36
36
2
31
1 31
6 31
1
1 31
1 36
1 77
11
8 27
1 27
22 27
2 27
1 27
1 77
6 77
1 36
2 77
0 34
10 34
10 34
1 34
1 27
18
0
0
22
114
31
16
0
0
1
2
0
0
0
0
0
3
0
2
<DX pBR
Number of Cleavage Sites3
18
17
X Ad2SV40
149 216
71 136
17
17
1
0
0
0
1
0
71 136
185 233
5
3
2
2
71 136
15
2
17
0
15
15
5
15
3
2
70
39
7
1
3
0
0
0
1
1
2
97
2
0
2
1
5
7
30
6
0
57
11
15
73
1
2
1
0
1
28
3
6
114
35
5
57
5
8
149 216
7
5
87
27
116
I
I
a
VO
Unidentified bacterium RFL71
Unidentified bacterium RFL69
Unidentified bacterium RFL66
Unidentified bacterium RFL65
Unidentified bacterium RFL62
Unidentified bacterium RFL61
Microorganism
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Source
Ubal6l (KpnT)
Uballl (PstT)
UbaJll (PstY)
Uba69l (BsePl)
Uba66l (SacU)
Uba65l (Eco3\T)
Uba6\l (HaelU)
Uba62l (Avail)
Enzyme1
CCWGG
CCGCGG
GGTACC
CTGCAG
CTGCAG
GCGCGC
CCGCGG
GGTCTC
GGWCC
Sequence2
71
71
4
2
28
28
6
4
12
136
136
30
8
33
30
52
33
18
149 216
35 73
0
6
17
17
0
1
2
2
0
0
0
18
6
0
0
0
2
2
1
0
1
1
1
1
0
11
1
0
0
0
1
1
6
6
0
0
1
1
0
0
1
22
8
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
Number of Cleavage Sites3
Unidentified bacterium RFL72
A.A. Janulaitis
Uballl (SacU)
CCWGG
6
18
1
0
1
27
References
Unidentified bacterium RFL76
A.A. Janulaitis
UbaZU (EcdRE)
AAGCTT
2
8
1
0
1
27
Unidentified bacterium RFL90
Unidentified bacterium RFL89
Unidentified bacterium RFL88
Unidentified bacterium RFL87
Unidentified bacterium RFL86
Unidentified bacterium RFL85
Unidentified bacterium RFL84
Unidentified bacterium RFL83
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
UbalO94l (Seal)
Uba\093l (SacU)
Uba90l (SacU)
Uba&9l (Salt)
Ubam (BamHJ)
Uba%ll (Kpnl)
Uba&6l (KpnY)
AGTACT
CCGCGG
CCGCGG
GTCGAC
GGATCC
GGTACC
5
4
4
4
2
5
5
33
33
3
0
0
0
2
Unidentified bacterium RFL1093
A.A. Janulaitis
CCGCGG
0
1
1
Unidentified bacterium RFL1094
UbalQ951(SacU)
0
0
A.A. Janulaitis
33
2
Unidentified bacterium RFL1095
15
4>X pBR
Unidentified bacterium RFL77
A.A. Janulaitis
UbaXll (EcoKU)
GGTCTC
2
8
1
0
0
0
1
27
X Ad2SV40
Unidentified bacterium RFL81
A.A. Janulaitis
Ubam (//mdUI)
UbaMl (EcollI)
GGTACC
8
1
0
0
27
ATCGAT
A.A. Janulaitis
UbalQ96l (ClaT)
Unidentified bacterium RFL1096
0
11
UbalQ91l (HaeUT)
18
A.A. Janulaitis
149 216
Unidentified bacterium RFL1097
GGCC
GGCC
Unidentified bacterium RFL82
A.A. Janulaitis
Uba.%51 (KpnT)
GGTACC
2
2
3
0
1
27
5
27
27
1
22
1
GGATCC
0
Ubal(mi (BamHT)
1
A.A. Janulaitis
3
Unidentified bacterium RFL1098
1
I
s
I
Unidentified bacterium RFLl 121
Unidentified bacterium RFLl 120
Unidentified bacterium RFLl 119
Unidentified bacterium RFLl 118
Unidentified bacterium RFLl 117
Unidentified bacterium RFLl 116
Unidentified bacterium RFLl 115
Unidentified bacterium RFLl 114
Unidentified bacterium RFLl 113
Unidentified bacterium RFLl 112
Unidentified bacterium RFLl 111
Unidentified bacterium RFLl 110
Unidentified bacterium RFLl 109
Unidentified bacterium RFLl 108
Unidentified bacterium RFLl 101
Unidentified bacterium RFLl 100
Unidentified bacterium RFLl099
Microorganism
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Source
Uball23l(PsA)
Uba\\22\(NaeV)
Ubainil (EcoRU)
Uba\\20l (EcoRU)
Uba\U9l(PsA)
Ubalim (EcoRU)
Uba\m\(NruV)
UbalU6l(PsA)
UbalU5l(PsA)
Uba\U4l (EcoRU)
UbalU3I(SacU)
UbalU2I(PsA)
UbaUUl(Sacn)
UbalUOU(EcoR\)
UbaU09U(MboT)
UballOm(SacU)
UbanOU(MboI)
Uba\099l (Asul)
UbaUO0l(Clal)
Enzyme 1
GRGCYC
CTGCAG
GCCGGC
CCWGG
CCWGG
CTGCAG
CCWGG
TCGCGA
CTGCAG
CTGCAG
CCWGG
CCGCGG
CTGCAG
CCGCGG
GGATCC
GATC
CCGCGG
GATC
GGNCC
ATCGAT
Sequence2
71
7
28
1
71
71
28
71
5
28
28
71
4
28
4
5
116
4
116
15
74
33
136
57
30
13
136
136
30
136
5
30
30
136
33
30
33
3
87
33
87
2
164
0
17
2
2
1
17
17
2
17
0
2
2
17
0
2
0
1
8
0
8
0
11
3
1
2
0
1
0
2
2
1
2
2
1
1
2
1
1
1
0
0
1
0
0
2
9
0
6
2
1
4
6
6
1
6
1
1
1
6
0
1
0
1
22
0
22
15
1
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
33
27
27
27
27
I"
^°
Vol.
§.
I
Number of Cleavage Sites3
Unidentified bacterium RFLl 122
A.A. Janulaitis
UbaU24l(Hgmi)
CCWGG
4
1
26
ft
:leic
Unidentified bacterium RFLl 127
References
Unidentified bacterium RFLl 123
A.A. Janulaitis
UbaU25l (EcoRU)
CCGCGG
57
5
<X>X pBR
Unidentified bacterium RFLl 124
A.A. Janulaitis
Uba\\26\(SacU)
25
1
Unidentified bacterium RFLl 128
X Ad2SV40
Unidentified bacterium RFLl 125
A.A. Janulaitis
GGYRCC
171
Unidentified bacterium RFLl 126
UbainiKHgiO)
328
27
A.A. Janulaitis
CCGG
1
Uba\mi(HpaU)
0
A.A. Janulaitis
0
CGATCG
7
UbaU29I(Pvub
3
A.A. Janulaitis
Unidentified bacterium RFLl 129
°nt 209
Unidentified bacterium RFLl 134
Unidentified bacterium RFLl 133
Unidentified bacterium RFLl 131
Unidentified bacterium RFLl 130
Microorganism
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Source
Ubal\53l(HaeUY)
Uba\\52l(HaeY\T)
Uba\l50l(Haem)
Uba 11491 (PsA)
UbalU&l (Xhol)
UbaU41l(HaeUT)
Uball46l (HaelU)
Uball45l(Clal)
Uba\\44l(Cla\)
UbaU42l(HgiJll)
UbaU4ll(HpalT)
UbaU40l(HaeHV)
Uball39l (PvuT)
Ubaimi(Clal)
Uball31\(Clal)
Uball36l(BspMIl)
UbaU34l(Asul)
Uba\\33l(Clal)
Ubainil (Avail)
Uball30l(XhoI)
Enzyme1
CTCGAG
GGCC
GGCC
GGCC
CTGCAG
CTCGAG
GGCC
GGCC
ATCGAT
ATCGAT
GRGCYC
CCGG
GGCC
CGATCG
ATCGAT
ATCGAT
TCCGGA
GGNCC
ATCGAT
GGWCC
CTCGAG
Sequence2
149
1
149
149
149
28
1
149
149
15
15
7
328
149
3
15
15
24
74
15
35
1
12
216
6
216
216
216
30
6
216
216
2
2
57
171
216
7
2
2
8
164
2
73
6
1
1
18
0
18
18
18
2
0
18
18
0
0
2
1
18
0
0
0
0
11
0
6
0
X Ad2SV40
0
0
0
11
1
11
11
11
1
1
11
11
0
0
0
5
11
0
0
0
0
2
0
1
1
1
0
0
22
0
22
22
22
1
0
22
22
1
1
2
26
22
1
1
1
1
15
1
8
0
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
cids
o
1
Unidentified bacterium RFLl 136
A.A. Janulaitis
Uball54lQthoV)
GGCC
1
12
0
Number of Cleavage Sites3
Unidentified bacterium RFLl 137
A.A. Janulaitis
Uba\l55l(Haem)
GGGCCC
1
5
References
Unidentified bacterium RFLl 138
A.A. Janulaitis
UbaU56l(ApaT)
GGGCCC
5
8
§.
1
imen
Unidentified bacterium RFLl 142
Unidentified bacterium RFLl 144
Unidentified bacterium RFLl 145
Unidentified bacterium RFLl 146
Unidentified bacterium RFLl 147
Unidentified bacterium RFLl 148
Unidentified bacterium RFLl 149
Unidentified bacterium RFLl 150
Unidentified bacterium RFLl 152
Unidentified bacterium RFLl 153
Unidentified bacterium RFLl 154
Unidentified bacterium RFLl 155
Unidentified bacterium RFLl 156
Unidentified bacterium RFLl 157
<X>X pBR
Unidentified bacterium RFLl 139
A.A. Janulaitis
Uban5Tl(ApaT)
AGTACT
So
Unidentified bacterium RFLl 140
A.A. Janulaitis
Uball5Sl(ScaT)
Unidentified bacterium RFLl 141
A.A. Janulaitis
Unidentified bacterium RFLl 158
Unidentified bacterium RFL1164
Unidentified bacterium RFL1163
Unidentified bacterium RFLl 162
Unidentified bacterium RFL1161
Unidentified bacterium RFL1160
Unidentified bacterium RFLl 159
Microorganism
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Source
UbaU64l(AsuY)
UbaU63l (BamHT)
UbaU62l (SphT)
UbaU6U(ClaI)
Ubal\60l (Asul)
UbaU591(HgiJlY)
Enzyme1
Sequence 2
Unidentified bacterium RFLl 180
Unidentified bacterium RFLl 179
Unidentified bacterium RFLl 178
Unidentified bacterium RFLl 177
Unidentified bacterium RFLl 176
Unidentified bacterium RFLl 175
Unidentified bacterium RFLl 174
Unidentified bacterium RFLl 173
Unidentified bacterium RFLl 172
Unidentified bacterium RFLl 171
Unidentified bacterium RFLl 170
Unidentified bacterium RFLl 169
Unidentified bacterium RFLl 168
Unidentified bacterium RFLl 167
Unidentified bacterium RFLl 166
Unidentified bacterium RFLl 165
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
UbaUWltftuT)
UbaW9l (HaeUT)
Ubalim (HaeUT)
Uba\\ll\(MboT)
UbaU16l (HaeUl)
UballlSl (HaeUT)
Ubam4l(HaeUl)
UbaW3l (BamHT)
Uballlll
Ubam\l(EcoRil)
UbaWOKStul)
UbaU69l (HaeUT)
UbaU6Sl(Clal)
Uball61l (BamHT)
UbaU661(XhoI)
UbaU65l(ApaT)
UbamiHtfboI)
(BamlU)
Unidentified bacterium RFLl 181
A.A. Janulaitis
UbaU64TL(HindlU)
GRGCYC
GGNCC
ATCGAT
GCATGC
GGATCC
GGNCC
AAGCTT
GGGCCC
CTCGAG
GGATCC
ATCGAT
GGCC
AGGCCT
CCWGG
GGATCC
GGATCC
GGCC
GGCC
GGCC
GATC
GGCC
GGCC
AGGCCT
CCWGG
GATC
Unidentified bacterium RFLl 182
Number of Cleavage Sites3
2
7 57
74 164
1
0
2
2
11
0
0
2
References
8
11
k Ad2SV40 tfX pBR
3
6
1
0
0
11
1
0
6
1
1
3
3
71 136
5
5
0
15 27
1 27
22
27
27
27
27
1 27
1 27
27
0 27
0 27
2
0
1
0
2
2 27
15 27
1 27
15
6
12
74 164
5
12
0
0
22 27
149 216
18
18
22 27
0 27
22 27
27
27
18
1
6
27
149 216
149 216
0
6
1
6
0
22
27
1 27
1 27
1
0
18
7
11
22
27
1
5
3
15
2
149 216
11
17
1
11
11
22
6
1
0
11
2
22
116 87
149 216
8
18
18
7
17
0
11
6 11
71 136
8
149 216
87
116
5"
<•>•
I
I
i.
!
i
Number of Cleavage Sites 3
Unidentified bacterium RFLl 188
Unidentified bacterium RFLl 187
Unidentified bacterium RFLl 186
Unidentified bacterium RFLl 185
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Uba\ 1901 (Eaml 1051)
t/6all89I(£coRII)
GACNNNNNGTC
GACNNNNNGTC
CCWGG
YGGCCR
CCGCGG
CTGCAG
CCWGG
CCTNAGG
CTGCAG
34
9
9
71
39
4
28
71
2
28
116
136
29
9
9
136
70
33
30
136
7
87
30
0
17
1
0
0
17
0
0
2
17
0
8
2
0
0
2
2
1
1
2
2
1
1
2
0
0
1
1
1
1
6
2
1
1
6
6
0
1
6
0
1
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
References
Unidentified bacterium RFLl 189
A.A. Janulaitis
Ubal 1911 (Ea/nl 1051)
CTCTTC
71
2
0
0
1
27
*X pBR
Unidentified bacterium RFLl 190
A.A. Janulaitis
CCWGG
15
2
0
0
1
27
X Ad2SV40
Unidentified bacterium RFLl 191
A.A. Janulaitis
ATCGAT
15
2
0
0
1
27
Sequence2
Unidentified bacterium RFLl 192
A.A. Janulaitis
ATCGAT
15
2
0
0
0
27
Enzyme 1
Unidentified bacterium RFLl 193
A.A. Janulaitis
{/&ill92I(ttp632I)
(/6all93I(£coRH)
f/6all95I(C/aI)
Mwll96I(C/aI)
ATCGAT
15
2
0
0
0
27
Source
Unidentified bacterium RFLl 195
A.A. Janulaitis
Uba\\91\ (ClaT)
ATCGAT
15
2
1
0
3
27
Microorganism
Unidentified bacterium RFLl 196
A.A. Janulaitis
UbaU9Sl(Clal)
ATCGAT
15
8
1
22
27
22
Unidentified bacterium RFLl 197
A.A. Janulaitis
UbaU99l(Clal)
ATCGAT
2
12
1
1
GATC
Unidentified bacterium RFLl 198
A.A. Janulaitis
Uba\200l (Clal)
GGTACC
1
7
0
8
0
0
27
Uball&ll (MboT)
Unidentified bacterium RFLl 199
A.A. Janulaitis
Uba\20U (KpnT)
GGGCCC
4
87
1
1
27
A.A. Janulaitis
Unidentified bacterium RFLl200
A.A. Janulaitis
Uba\2V2I (ApaT)
GTGCAC
116
3
1
2
Unidentified bacterium RFLl 183
Unidentified bacterium RFL1201
A.A. Janulaitis
Ubal2O3l (ApaLT)
GATC
5
0
0
A.A. Janulaitis
Unidentified bacterium RFLl202
A.A. Janulaitis
UbaUMl (MboT)
GGATCC
40
2
Unidentified bacterium RFLl 184
Unidentified bacterium RFLl203
A.A. Janulaitis
Uba\205l (flamffl)
8
57
UbaUMliPsA)
UbalWm(SauI)
Ubam5l(EcoRH)
UballMKJPsiQ
UbaUVJliSacU)
Ubaimi(CfrI)
Unidentified bacterium RFL1204
A.A. Janulaitis
CYCGRG
7
Unidentified bacterium RFL1205
UbaUOSU (Aval)
GRGCYC
A.A. Janulaitis
Ubal206l (HgiJlI)
Unidentified bacterium RFLl206
X
2.
8-
8
i
Unidentified bacterium RFL1219
Unidentified bacterium RFL1218
Unidentified bacterium RFL1217
Unidentified bacterium RFL1216
Unidentified bacterium RFL1215
Unidentified bacterium RFL1214
Unidentified bacterium RFL1213
Unidentified bacterium RFL1212
Unidentified bacterium RFL1211
Unidentified bacterium RFL1210
Unidentified bacterium RFL1209
Unidentified bacterium RFL1208
Unidentified bacterium RFL1207
Microorganism
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Source
Uba\22U (EspT)
Uba\220l (SmaY)
Ubal2\9l (HindUT)
Ubal2m (EcoRST)
Uba\2\l\ (Sad)
Ubal2161(PsA)
Uba\2l5l (PsA)
Ubal2l4l (HaeUT)
Ubal2\3l (PsA)
UbaYim (PsA)
Ubal2Ul(PstT)
UbalUOl (HaeUT)
Ubal2Q91 (HaeUT)
UbaUO&l (HaeUT)
UballQin (HaeUT)
Enzyme1
GCTNAGC
GCTNAGC
CCCGGG
AAGCTT
CCWGG
AGGCCT
CTGCAG
CTGCAG
GGCC
CTGCAG
CTGCAG
CTGCAG
GGCC
GGCC
GGCC
GGCC
Sequence2
5
149
6
6
3
6
71
6
28
28
149
28
28
28
149
149
149
149
30
3
216
8
8
12
12
136
11
30
30
216
30
30
30
216
216
216
216
2
2
1
18
1
1
0
6
17
7
2
2
18
2
2
2
18
18
18
18
0
0
1
0
11
0
0
0
0
2
1
1
1
11
1
1
1
11
11
11
11
22
1
1
1
1
22
0
0
0
1
6
0
1
1
22
1
1
1
22
22
22
22
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
27
3-
2
a
Number of Cleavage Sites3
Unidentified bacterium RFL1220
A.A. Janulaitis
Uba\222l (Espl)
GGCC
28
8
3
11
27
f Rei
Unidentified bacterium RFL1226
Unidentified bacterium RFL1225
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
Ubal2301 (HaeUT)
Ubal229l (SacU)
Uba\22%\ (HaeUT)
Uba\221\ (PvuII)
GGCC
CCGCGG
GGCC
149
Unidentified bacterium RFL1230
Unidentified bacterium RFL1229
Unidentified bacterium RFL1228
Unidentified bacterium RFL1227
A.A. Janulaitis
216
References
Unidentified bacterium RFL1221
A.A. Janulaitis
Uba 12231 (HaeUl)
GGATCC
6
24
18
1
0
22
27
149
<DX pBR
Unidentified bacterium RFL1222
A.A. Janulaitis
Uba\224l (BamYU)
CTGCAG
15
216
0
11
22
GGCC
X Ad2SV40
Unidentified bacterium RFL1223
A.A. Janulaitis
Uba\225l (PsA)
GCATGC
149
33
11
Uba\23U(HaeET)
f
^ M
X
n
&
o'
1
Unidentified bacterium RFL1224
A.A. Janulaitis
Ubal226l (SphT)
CAGCTG
4
216
18
18
A.A. Janulaitis
Unidentified bacterium RFL1231
lement 2095
Source
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
A.A. Janulaitis
T. Shimada
T. Shimada
T. Shimada
Microorganism
Unidentified bacterium RFL1232
Unidentified bacterium RFL1233
Unidentified bacterium RFL1234
Unidentified bacterium RFL1235
Unidentified bacterium RFL1236
Unidentified bacterium RFL1237
Unidentified bacterium RFL1238
Unidentified bacterium RFL1239
Unidentified bacterium RFL1240
Unidentified bacterium RFL1241
Unidentified bacterium RFL1242
Vibrio anguillarum RFL91
Vibrio parahaemolyticus K25
Vibrio parahaemolyticus K57
Vibrio parahaemolyticus K65
TACGTA
GGGCCC
GGATCC
GAATTC
GGCC
?
Ubal24OI (S/wBI)
Ubal24U {ApaT)
Uba\2A2\ {BamHl)
Var&m {EcoRI)
VartilW. {HaeUI)
Van9lW
VpaK65l (Avail)
VpaKSll
VpaK25l {Asul)
GGWCC
?
GGNCC
35
73
?
164
74
?
?
216
149
?
5
3
5
5
12
1
0
1
AGGCCT
Uba\239l {Sttd)
6
?
11
?
?
8
1
15
2
?
?
?
22
11
18
1
0
44
44
44
27
27
27
27
1
1
27
0
27
27
0
0
27
27
27
1
0
0
0
0
1
0
1
1
0
7
0
2
11
1
15
6
ATCGAT
CTCGAG
23
27
8-
o
o
g-
11"
Vol.
Uba\23M {Clal)
Ubal237l (XhoT)
0
14
0
22
11
27
27
1
0
27
References
1
1
157 303
6
CGCG
0
33
0
1
18
0
2
2
30
OX pBR
216
149
4
15
28
X Ad2 SV40
1
Uba\236l (FnuDlT)
GGCC
CCGCGG
ATCGAT
CTGCAG
Sequence2
eseai
Uba\2351 (HaellT)
Uba\234l(SacU)
Uba\233l (Clal)
Uba\232\ (Psil)
Enzyme1
Number of Cleavage Sites3
2096 Nuclei
FOOTNOTES
1. When two enzymes recognize the same sequence, i.e., are isoschizomers, the prototype (i.e., the first example isolated) is indicated in
parentheses.
2. Recognition sequences are written from 5 ' -> 3 ' , only one strand being given, and the point of cleavage is indicated by an arrow (T). When no
arrow appears, the precise cleavage site has not been determined. For example, CTGATCG is an abbreviation for
5' CTGATCG3'
3' GCTAGTC5'
For enzymes such as Sapl and AcH, which cleave away from their recognition sequences, the sites of cleavage are indicated in parentheses.
For example Sapl GCTCTTC(l/4) indicates cleavage as shown below
5'GCTCTTCNT'3'
3 ' CGAGAAGNNNNt' 5 '
Acfl CCGC(-2/-2) indicates cleavage as shown below
A is N6-methyladenosine.
In all cases the recognition sequences are oriented so that the cleavage sites lie on their 3 ' side.
^
2
§
x
|_
5'CCTGC'3'
3'GGTCG'5'
3. These columns indicate the frequency of cleavage by the various specific endonucleases on bacteriophage lambda DNA (X), adenovirus-2 DNA
(Ad2), simian virus 40 DNA (SV40), 9X174 Rf DNA and pBR322 DNA (pBR). In all cases the sites were derived by computer search of
the complete sequences obtained from GENBANK.
I
2098 Nucleic Acids Research, Vol. 19, Supplement
TABLE 2
Type I enzymes
Enzyme
Recognition sequence 2
C/rAI
EcoAI
EcoBl
EcoDI
GCANNNNNNNNGTGG
GAGNNNNNNNGTCA
TGANNNNNNNNTGCT
TTANNNNNNNGTCY
EcoDXXI
EcdEI
EcoKI
£coR124I
TCANNNNNNNATTC
GAGNNNNNNNATGC
AACNNNNNNGTGC
GAANNNNNNRTCG
GAANNNNNNNRTCG
GAGNNNNNNRTAYG
GAGNNNNNNGTRC
AACNNNNNNGTRC
AACNNNNNNRTAYG
EcoR124/3I
StySBl
StySJI
StySPI
StySQI
Me site 3
2(6),-3(6)
3(6),-4(6)
2(6),-3(6)
-3(6)
2(6),-4(6)
2(6),-3(6)
Type HI enzymes
Enzyme
EcoPl
EcoP15l
StyhTI
Recognition sequence 2
AGACC
CAGCAG
CGAAT
CAGAG
Me site 3
3(6)
4(6)
Nucleic Acids Research, Vol. 19, Supplement 2099
Tjrpe II enzymes
Enzyme1
Isoschizomers
Recognition2
Sequence
Me 3
site
EGJLMNOPRSUVX
ABDEGIJKLMNOPQRSUVX
GACGTtC
Aatll
Accl
Acil
Acyl
GTtMKAC
CCGC(-2/-2)
Ahall
Bbill
BsaHl
Hinll
Aflll
Bfrl
Aflin
Agel
AhaUI
Dral
Alul
AlwNI
Apal
Bspl20l
ApaBI
ApaLl
AlwUl
Snol
Vnel
Ascl
Asul
C/rl3I
NspIV
Sau96l
Asull
BpuUl
BspU9I
BstBI
Csp45I
Lspl
NspV
N
EMRV
GRTCGYC
GRTCGYC
GRTCGYC
GRCGYC
GRTCGYC
CTTTAAG
CTTTAAG
ATCRYGT
AtCCGGT
TTTTAAA
TTTTAAA
GN
AK
N
FOU
ABGJKNU
M
BGJMNU
N
ABDEFGUKLMNOPQRSUVX
AGTCT
CAGNNNTCTG
3(5)
GGGCCTC
GTGGCCC
GCANNNNNtTGC
GTTGCAC
GTTGCAC
GTTGCAC
4(5)
ABDEFGHUKLMNOPQRSUVX
N
BDEGIJKLMNOPRUVX
F
EGJKNX
FRU
JLMV
D
N
GTTGCAC
GGTCGCGCC
GTGNCC
GTGNCC
GTGNCC
Commercial4
source
4(5)
R
FKOU
JP
BEGJLMNRVX
GTGNCC
TTTCGAA
TTTCGAA
TTTCGAA
TTTCGAA
TTTCGAA
J
D
F
N
TTTCGAA
JL
TTCGAA
ABGKPU
RV
2100
Nucleic Acids Research, Vol. 19, Supplement
Enzyme 1
Isoschizomers
Recognition2
Sequence
Sful
TTtCGAA
Aval
Eco88l
Nsplll
Avail
Bmel8I
Eco47I
NspHU
SinI
Avalll
£coT22I
Nsil
Avrll
Blnl
Bael
Baa
MscI
BamHl
BstI
Bbvl
BbvU
Bbsl
CTYCGRG
CtYCGRG
CTYCGRG
GTGWCC
GTGWCC
GTGWCC
GGWCC
GTGWCC
ATGCAT
ATGCATT
ATGCATT
CTCTAGG
CTCTAGG
ACNNNNGTAYC
TGGTCCA
TGGTCCA
GTGATCC
GTGATCC
GCAGC(8/12)
GAAGAC(2/6)
GAAGAC
Me 3
site
M
ABEGIJKLMNOPRSUVX
F
JP
ABEGLJKMNPRSX
4(5)
4(5)
ABEGIJKRSVX
5(4)
N
ABDEFGHUKLMNOPQRSUVX
GJP
2(5),-2(5) EGIJNX
CCATC
ACGGCU2/13)
Bcgl*
BcH
GCANNNNNNTCG< 12/10)
TTGATCA
TGATCA
Betl
Bgtll
WTCCGGW
GCCNNNNTNGGC
ATGATCT
Binl
GGATCX4/5)
Bga
Alwl
BpulOI
BsaAI
BsaBl
Maml
D
FOU
J
JLRSV
GJ
KOU
BELMNRVX
N
K
Bed
Bcefl
Fbal
Commercial4
source
N
N
BEGIJLMNOPRSUVX
K
ABDEFGHULMNOPQRSUVX
ABDEFGHUKLMNOPQRSUVX
N
GGATCX4/5)
CCTNAGa-5/-2)
YACTGTR
GATNNTNNATC
N
GATNNTNNATC
M
N
Nucleic Acids Research, Vol. 19, Supplement 2101
Enzyme 1
Isoschizomers
Recognition2
Sequence
BssHll
GCGCGC
GTCGCGC
GTGCAG(16/14)
SscPI
Bsgl
Bsil
BsiYI
Bstl
BsmI
BsmAI
Alw26I
BspGI
BspHl
RspXI
BspMI
BspMll
AcclII
BspEI
Kpn2l
Mrol
BsrI
BstEU
BstPl
Eco91I
EcoO65I
BstXl
Caull
Bcnl
Neil
Cfrl
Eael
C/rlOI
Clal
BanUI
Bscl
BsplOei
BspDl
Bsul5l
Me3
site
DEGJLMNQRUVX
CTCGTG(-5/-l)
CCNNNNNTNNGG
CCNNNNNTNNGG
N
EGJLNUVX
N
F
GAATGC(1/-1)
GTCTC(iy5)
GTCTC(l/5)
CTGGAC
TTCATGA
TTCATGA
ACCTGC(4/8)
TTCCGGA
TTCCGGA
TTCCGGA
TTCCGGA
TTCCGGA
ACTGGdAl)
GTGTNACC
N
G
N
DEGJKQRV
N
F
MOU
N
BEGJLMNOPRSUVX
K
F
GTGTNACC
GTGTNACC
GTGTNACC
CCANNNNNTNTGG
CCTSGG
CCTSGG
CCTSGG
YTGGCCR
YTGGCCR
RTCCGGY
ATTCGAT
ATCGAT
ATTCGAT
ATTCGAT
Commercial*
source
GK
EGJKLMNOQRUVX
2(4)
4(5)
4(5)
2(5)
5(6)
FK
BEGJLMNOUVX
F
EGJKLMNVX
AFKMNOU
ABDJKMNPQRSVX
OU
JL
E
ATTCGAT
N
ATTCGAT
DF
2102
Nucleic Acids Research, Vol. 19, Supplement
Enzyme*
Isoschizomers
CviJl
CviRl
Ddel
Dpril*
Droll
£COO109I
Pssl
DroIII
Drdl
Drdll
Dual
EamllO5I
Ecil
EcoSlI
Bsal
Eco47lll
Eco571
EcdNl
EcoRI
EcoRlI6
+
+
+
Apyl
BsiNl
Mval
TspAI
EcoRV
Recognition2
Sequence
Me 3
site
RGTCY
3(5)
4(6)
1(5)
TGTCA
CTTNAG
GAtTC
RGTGNCCY
RGTGNCCY
RGGNCtCY
CACNNNtGTG
GACNNNNtNNGTC
GAACCA
CTCRYGG
GACNNNtNNGTC
TCCGCC
GGTCTCd/5)
GGTCTC(l/5)
AGCTGCT
CTGAAG(16/14)
CCTNNTNNNAGG
GTAATTC
TCCWGG
CCTWGG
CCTWGG
CCTWGG
CCWGG
AccII
GATTATC
GATTATC
GCtTNAGC
GCTTNAGC
GCtTNAGC
CGTCTC(l/5)
CCCGC(4/6)
GTCCC
GCTNGC
CGTCG
CGTCG
Bsp50l
CGTCG
Eco32I
Espl
BpullO2l
Ce/II
Esp3I
Faul
Finl
Fnu4Hl
FnuDIl
Commercial4
source
BEGULMNOPRUVX
ABEGIJLMNRSVX
EGJM
FGJKLNOUVX
I
EMNX
N
M
FN
F
N
FKMNORU
5(6),-5(6) N
N
ABDEFGHUKLMNOPQRSUVX
3(6)
BDEGJUV
2(5)
M
EJNX
2(4)
2(4)
AFKMOU
L
ABDEGIJKLMNOPQRSUVX
2(6)
F
EGJU
FN
M
FN
N
DEGJKQVX
F
Nucleic Acids Research, Vol. 19, Supplement 2103
Enzyme 1
Isoschizomers
Recognition2
Sequence
BstUl
Mvnl
Thai
CGTCG
CGTCG
CGTCG
GGATGO/13)
Fokl
Fsel
Fail
Gdill
Gsul
Hoel
Hoell
Me 3
site
N
M
BI
3(6),-2(6) DEGIKMNRUVX
GGCCGGTCC
RTAATTY
YGGCCGK-5/-1)
CTGGAG(16/14)
WGGTCCW
RGCGCTY
HoelU
BssCl
BsuRl
Pall
Hgdl
HgiAI
Alw21I
AspHI
HgiCl
BanI
Eco64I
HgiElI
Hgun
BanU
Eco2Al
Hhal
GGTCC
GGCC
GGTCC
GGTCC
GACGC(5710)
GWGCWTC
GWGCWTC
Commercial*
source
FN
3(5)
3(5)
GWGCWTC
GTGYRCC
GTGYRCC
GTGYRCC
ACCNNNNNNGGT
BDEGIJKLMNOPRSUVX
ABDGHUKLMNOPQRSUVX
G
DFGJ
EJPV
DNX
NX
F
M
EGIJMNOPUVX
F
GRGCYTC
GRGCYTC
GRGCYTC
EGIJKLMNOPRSUVX
F
Hindlll
GCGTC
GCGTC
GTCGC
GTCGC
GTYTRAC
GTYTRAC
ATAGCTT
Hinfl
Hpal
GTANTC
GTTTAAC
5(6)
ABDEFGUKLMNOPQRSUVX
ABDEGUKLMNOPQRSUVX
ABDEGUKLMNOPQRSUVX
Hpall
CTCGG
2(5)
ABDEFGJLMNOPQRSUVX
Cfol
Hin6l
HinPlI
Hindll
Hindi
Hapll
CTCGG
2(5)
BDEGJKNOPRSUX
BIJLMRV
F
NX
5(6)
M
ABEFGIJKLNOPQRSUVX
1(6)
GIK
2104
Nucleic Adds Research, Vol. 19, Supplement
Enzyme 1
Isoschizomers
Recognition2
Sequence
Me3
site
Commercial4
source
Mspl
CtCGG
1(5)
-2(5)
ABDEFGUKLMNOPQRSUVX
NVX
ABDEFGUKLMNOPQRSUVX
Hphl
Kpnl
GGTGA(8/7)
GGTACTC
Asp718I
Ksp632l
EamllOAl
Earl
Mael
Rmal
Maell
Maem
MboV
+
BspAl
Dpnll
Kzo9I
Ndell
+
Sau3Al
MboU
Mcrl
Mfel
Mlul
Mlyl
Mmel
Mnll
Msel
Mstl
AosI
AviH
Fdill
Fspl
Mwol
Noel
Narl
Bbel
Ehel
KasI
NunJI
ms
——.
GtGTACC
CTCTTC(l/4)
CTCTTC(V4)
CTCTTC(l/4)
CtTAG
CtTAG
ATCGT
TGTNAC
TGATC
TGATC
GATC
TGATC
TGATC
tGATC
GAAGA(8/7)
CGRYTCG
CTAATTG
AtCGCGT
GACTa575)
TCCRAC(20/18)
CCTC{7/7)
TtTAA
TGCTGCA
TGCTGCA
TGCTGCA
TGCTGCA
TGCTGCA
GCNNNNNTNNGC
GCCTGGC
GGTCGCC
GGCGCTC
GGCTGCC
GTGCGCC
GGTCGCC
2(6)
4(5)
5(6)
M
M
F
N
M
N
M
M
BEGLJKNPQRSVX
JL
N
D
BGM
ABDEGUKLMNOPQRSUVX
BGUKNOPQRSUVX
ABDEFGUKLMNOPQRSUVX
L
EGJNX
N
X
GJ
M
U
NS
EGKLMNOUVX
BEGJMNPUVX
K
FOU
N
GJ
Nucleic Acids Research, Vol. 19, Supplement 2105
Enzyme 1
Isoschizomers
Recognition2
Sequence
Ncol
Ndel
CTCATGG
CAtTATG
Nhel
NlalTI
NlaJV
NotI
Nrul
GTCTAGC
CATGT
GGNTNCC
GCTGGCCGC
TCGTCGA
TCGTCGA
TCGTCGA
RCATGtY
RCATGtY
CMGTCKG
TTAATtTAA
TCGTAG
CCANNNNTNTGG
CCANNNNTNTGG
GAGTC(4/5)
CACTGTG
CACtGTG
Bsp68I
Spol
Nspl
NspHl
NspBII
Part
P/Z1108I
P/ZMI
Van911
Plel
PmaCI
BbrPl
Eco72l
Pma
PpuML
PshAI
Me 3
site
4(6)
Commercial4
source
ABDEFGIJKLMNOPQRSUVX
BEFGKLMNPSVX
BEGJKLMNOPRUVX
N
N
ABDEFGIJKLMNOPQRSUVX
BDEGIJKLMNOPQUVX
F
R
AKMU
GJ
J
N
N
F
N
AK
M
F
N
N
CACTGTG
CACTGTG
RGTGWCCY
GACNNTNNGTC
Pstl
CTGCATG
Pvul
CGATTCG
CGATTCG
BspCI
Xorll
5(6)
ABDEFGHUKLMNOPQRSUVX
ABDEFGJKLMNOPQRSUVX
E
B
CGATTCG
ABDEFGIJKLMNOPQRSUVX
PvuU
CAGTCTG
RleAl
CCCACAU2/9)
Rsal
GTTAC
ABDEGLJLMNOPQRSUVX
GTTAC
GTTAC
K
F
CGTGWCCG
BEGJNX
CGGWCCG
CGTGWCCG
K
RV
GAGCTTC
ADEGIJKLMNOPQRSUVX
Afal
Csp6I
Rsrll
Cpol
Cspl
Sad
4(4)
2106 Nucleic Acids Research, Vol. 19, Supplement
Enzyme 1
Isoschizomers
Recognition2
Sequence
£c/136II
Sstl
GAGTCTC
GAGCTTC
CCGCTGG
CCGCTGG
CCGCTGG
Sacll
C/r42I
KpnVm
Kspl
Mral
S/r303I
Sstll
Sail
Sapl
Saul
Aocl
Axyl
Bse2\l
BsuZQl
Cvnl
Eco81l
Mstll
Seal
ScrFl
DsaV
Sdul
Bmyl
Bap12861
Nspll
Seel
BsaJl
SfaNl
Sfcl
Sfel
Sfil
Me 3
site
Commercial4
source
F
B
EIJLNOPRUVX
F
D
M
CCGCTGG
CCGCGG
GJ
D
B
ABDEFGHUKLMNOPQRSUVX
CCGCTGG
CCGCTGG
GTTCGAC
GCTCTTC(l/4)
CCTTNAGG
CCTTNAGG
CCTTNAGG
CCTTNAGG
M
E
GJV
D
NR
B
AFKOU
EX
ABEFGIJKLMNOPRSUVX
EGMNSUVX
M
FJ
M
EGKNRUX
CCTTNAGG
CCTTNAGG
CCTTNAGG
CCTTNAGG
AGTTACT
CCTNGG
TCCNGG
GDGCHTC
GDGCHTC
GDGCHTC
GDGCHTC
CTCNNGG
CTCNNGG
GCATCX5/9)
CTYRAG
CTTRYAG
GGCCNNNNTNGGCC
J
N
DNX
ABDEGULMNOPQRSUVX
CRTCCGGYG
CCCTGGG
2(4)
M
ABDEFGUKLMNOPQRSUVX
Cfr9l
CTCCGGG
2(4)
FU
Xmal
CTCCGGG
SgrAI
Smal
EINRVX
Nucleic Acids Research, Vol. 19, Supplement 2107
Enzyme
Isoschizomers
Snal
SnaBI
Ecol05I
Spel
SphI
Bbul
Pael
Spa
BsiWI
Sse838TL
Sspl
Stul
AatI
EcoUTL
Pme55I
Styl
BssTlI
Ecol30I
EcoTUI
Sival
Taql
TthBB8I
Recognition2
Sequence
GTATAC
TACTGTA
TACTGTA
AtCTAGT
GCATGTC
GCATGtC
GCATGTC
CTGTACG
CTGTACG
CCTGCATGG
AATTATT
AGGTCCT
AGGTCCT
AGGTCCT
AGGTCCT
CTCWWGG
CTCWWGG
CTCWWGG
CTCWWGG
ATTTTAAAT
TTCGA
TTCGA
Tfil
GACCGA(ll/9)
CACCCAU1/9)
GAWTC
Tsp45I
TspEI
GTSAC
AATT
Tthllll
GACNTNNGTC
GACNTNNGTC
CAARCA(ll/9)
ATTTAAT
ATTTAAT
ATTTAAT
Taqll*
Aspl
Tthlllll
Vspl
Asel
Asnl
Me3
site
Commercial4
source
EGJKMNVX
FOU
BEGKLMNORSUVX
ABDEGIJKLMNOPQRSUX
RV
F
AK
N
AK
BEGKLMNRUVX
ABEGIJKLMNPRVX
OU
F
D
BEGJMNRVX
D
FU
AK
4(6)
4(6)
ABDEFGULMNOPQRSUVX
K
N
EGIJKNPVX
M
Xbal
TTCTAGA
Xcml
CCANNNNNTNNNNTGG
N
Xhol
CTTCGAG
ABDEFGHUKLMNOPQRSUVX
BstVL
CTTCGAG
6(6)
DFK
N
M
ABDEFGHUKLMNOPQRSUVX
5(6)
G
2108 Nucleic Acids Research, Vol. 19, Supplement
Enzyme*
Isoschizomers
Recognition2
Sequence
Ccrl
PaeRTL
Slal
CTTCGAG
CTTCGAG
CTTCGAG
RTGATCY
RtGATCY
RTGATCY
Xholl
BstYl
Mfll
Xmalll
EagI
EclXI
Eco52l
Xmnl
Asp700I
CTGGCCG
CtGGCCG
CTGGCCG
CTGGCCG
GAANNTNNTTC
GAANNTNNTTC
Me3
site
5(6)
4(5)
Commercial4
source
X
NX
D
EGMVX
N
AK
B
N
M
EFKOU
DEGJNX
M
FOOTNOTES
1.
2.
3.
4.
* signifies that Dpnl and its isoschizomers require the presence of 6-methyladenosine
within the recognition sequence GATC.
Recognition sequences are given using the standard abbreviations (Eur. J. Biochem. 150:
1-5, 1985) to represent ambiguity:
R = G or A
Y = CorT
M = AorC
K = G or T
S = G or C
W = AorT
H = A or C or T
B = G or T or C
V = G or C or A
D = G or A or T
N = A or C or G or T
The site of methylation by the cognate methylase when known is indicated as follows.
The first number shows the base within the recognition sequence that is modified. A negative
number indicates the complementary strand, numbered from the 5' base of that strand. The
number in parentheses indicates the specific methylation involved. (6) = N6-methyladenosine;
(5) = 5-methylcytosine; (4) = N4-methylcytosine.
Commercial sources of restriction enzymes are abbreviated as follows:
A Amersham (2/91)
B BRL(2/91)
D Palliard Chemical (11/90)
E Stratagene (2/91)
F ESP Fermentas (9/90)
G BioExcellence (formerly Anglian) (11/90)
H American Allied (12/90)
I IBI (2/91)
J Janssen Biochimica (2/91)
Nucleic Acids Research, Vol. 19, Supplement 2109
5.
6.
7.
8.
K Takara (1/91)
L Northumbria Biologicals Ltd. (9/90)
M Boehringer Mannheim (2/91)
N New England Biolabs (2/91)
0 Toyobo (2/91)
P PL-Pharmacia-LKB (2/91)
Q Molecular Biology Resources (1/91)
R Promega Biotec (12/90)
S Sigma (2/91)
U USB (9/90)
V Serva (2/91)
X New York Biolabs (2/91)
Bcgl5 cleaves on both sides of the recognition sequence: 10 bases 5' to the recognition
sequence and 12 bases 3' to it on both strands. Thus the recognition site is excised in a
fragment, 34 base pairs long, with 2-base 3'-extensions at each end
-EcoRII isoschizomers fall into two classes based upon their sensitivity to methylation.
2?coRII will not cleave when the second cytosine in the recognition sequence is methylated to 5methylcytosine whereas Mval will cleave such a sequence. Isoschizomers of EcoiRH that are
like Mval are indicated by +.
Mbol isoschizomers fall into two classes based upon their sensitivity to methylation.
Mbol will not cleave when the recognition sequence contains 6-methyladenosine whereas
Sau3AI will not cleave when its recognition sequence contains 5-methylcytosine. Isoschizomers
of Mbol that are like Sau3AI are indicated by +.
Taqll differs from other restriction enzymes in recognizing two distinct sequences:
GACCG and CACCCA.