GREMLIN Database
Tox-REase-5 - Restriction endonuclease fold toxin 5
PFAM: PF15648 Sequences:
Download Alignment
We filter this alignment to remove sites that have many gaps before running GREMLIN.

Date: 2015_10
Length: 95 (90)
Sequences: 908 (757)
Seq/√Len: 79.8
META: 0.7

GREMLIN Results:

Legend: The darker and larger the blue dots, the higher coevolution strength.

Residue pairs sorted by coevolution strength:
i j Sco Prob
43_E71_Q3.1981.00
42_L91_H3.1901.00
46_P93_A3.1171.00
35_D38_D3.0561.00
49_D94_E2.8621.00
70_D74_R2.6051.00
6_E13_R2.3771.00
4_Y8_I2.3311.00
51_F64_G2.3071.00
75_Q90_W2.2531.00
29_V78_A1.9691.00
27_N78_A1.9331.00
34_F84_P1.8101.00
35_D42_L1.7181.00
52_F58_F1.6051.00
53_D56_G1.5801.00
29_V74_R1.5641.00
40_V89_E1.5520.99
11_A14_G1.5460.99
8_I91_H1.4350.99
11_A15_T1.4310.99
65_A68_L1.4140.99
73_R77_A1.4030.99
59_K62_F1.3740.99
47_G94_E1.3390.98
6_E11_A1.3080.98
21_I24_W1.2720.98
17_Y34_F1.2680.98
33_G42_L1.2630.98
13_R16_E1.2390.97
70_D73_R1.2350.97
43_E88_I1.2120.97
46_P50_Q1.1630.96
69_L72_A1.1500.96
34_F41_L1.1260.96
53_D57_E1.1160.95
34_F39_G1.0870.95
7_Q93_A1.0860.95
4_Y91_H1.0400.93
2_R15_T1.0350.93
9_T33_G1.0350.93
9_T42_L1.0270.93
38_D89_E1.0230.93
2_R6_E1.0200.92
54_K57_E1.0180.92
58_F62_F0.9900.91
58_F64_G0.9530.90
6_E12_P0.9520.90
68_L92_F0.9510.90
2_R13_R0.9500.90
33_G44_A0.9460.89
82_G85_P0.9440.89
41_L79_A0.9210.88
47_G93_A0.9190.88
89_E92_F0.9190.88
47_G50_Q0.9140.88
66_D70_D0.9120.88
74_R78_A0.8940.86
35_D39_G0.8810.86
2_R11_A0.8770.85
2_R12_P0.8330.82
26_V31_F0.8100.81
51_F62_F0.8020.80
52_F65_A0.8010.80
52_F56_G0.7950.79
64_G68_L0.7840.78
48_Y51_F0.7800.78
12_P15_T0.7740.77
11_A34_F0.7740.77
19_V22_P0.7690.77
49_D68_L0.7510.75
41_L68_L0.7420.74
60_P64_G0.7390.74
4_Y33_G0.7260.73
63_K67_K0.7180.72
63_K66_D0.7170.72
4_Y15_T0.7160.72
70_D77_A0.7140.72
79_A88_I0.7120.71
76_L88_I0.7020.70
8_I42_L0.6970.70
12_P34_F0.6890.69
34_F76_L0.6880.69
69_L77_A0.6830.68
3_A6_E0.6770.68
75_Q88_I0.6700.67
31_F75_Q0.6630.66
8_I44_A0.6620.66
4_Y7_Q0.6610.66
46_P94_E0.6560.65
82_G88_I0.6410.63
59_K63_K0.6360.63
7_Q33_G0.6340.62
75_Q78_A0.6270.62
69_L73_R0.6250.61
61_W76_L0.6190.61
44_A91_H0.6180.60
26_V41_L0.6150.60
35_D40_V0.6120.60
49_D54_K0.6070.59
20_W24_W0.6020.58
73_R76_L0.6010.58
16_E71_Q0.5960.58
45_K75_Q0.5940.57
50_Q62_F0.5870.57
65_A69_L0.5870.57
25_K30_K0.5860.56
41_L85_P0.5850.56
24_W28_G0.5850.56
48_Y68_L0.5830.56
39_G43_E0.5700.54
50_Q64_G0.5690.54
44_A89_E0.5640.54
76_L89_E0.5610.53
20_W23_E0.5590.53
7_Q31_F0.5520.52
77_A80_R0.5520.52
23_E28_G0.5480.52
3_A13_R0.5430.51
66_D82_G0.5370.50
60_P63_K0.5370.50
39_G84_P0.5340.50
19_V29_V0.5330.50
54_K61_W0.5280.49
58_F61_W0.5270.49
57_E61_W0.5270.49
14_G17_Y0.5230.48
31_F56_G0.5220.48
61_W65_A0.5160.47
17_Y41_L0.5130.47
48_Y64_G0.5120.47
35_D91_H0.5060.46
51_F65_A0.5060.46
7_Q43_E0.5000.45
3_A14_G0.5000.45
Legend: The i and j are positions as given in the UniProt sequence. Only predictions with Prob ≥ 0.7 are listed. For all 3L/2 predictions, click on one of the links below.

Sco = ((raw_sco - min_sco)/(avg_sco - min_sco))/2 + 0.5
Prob = P(contact | Sco, seq80/√len)
seq80 = effective number of sequences, after reducing redundancy to 80% identity

HHsearch Results:
Legend: GREMLIN results (Prob ≥ 0.7) overlaid on top PDB hits. The grey/red filled circles underneath are pdb residue contacts (min distance < 5 Angstroms). The shade of the circles is based on the top 10 (or top 20 if e-value < 1E-20) HHsearch results which uses the overall probability and per-site alignment prob. Inter oligomeric contacts in the pdb are in shades of red.
PDB Chains Cov % HHΔ  
3wnoA 2 0.9368 13 0.91 Contact Map
3syyA 3 0.9158 10 0.914 Contact Map
2w45A 1 0.9053 9.6 0.915 Contact Map
3sm4A 3 0.9158 9.4 0.915 Contact Map
3k93A 3 0.8947 7.3 0.919 Contact Map
4d3tA 2 0.5684 6.3 0.922 Contact Map
3ljwA 1 0.4 4.7 0.926 Contact Map
2qnkA 1 0.5368 3.9 0.929 Contact Map
1mjtA 2 0.5474 3.6 0.93 Contact Map
3q2uA 1 0.4632 2.4 0.937 Contact Map

Sequence Conservation (Image Generated using WebLogo v3)
Legend: Color is used to show Hydrophobicity (Blue: Hydrophilic, Green: Neutral and Black: Hydrophobic). Amount of gaps is represented by width.

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