Query FD01846349_04379 hypothetical protein
Match_columns 190
No_of_seqs 102 out of 277
Neff 7.49049
Searched_HMMs 86581
Date Tue Feb 27 19:48:25 2024
Command hhsearch -cpu 8 -i ../results/full.a3m -d /cluster/toolkit/production/databases/hh-suite/mmcif70/pdb70 -d /cluster/toolkit/production/databases/hh-suite/pfama/pfama -o ../results/7347228.hhr -oa3m ../results/7347228.a3m -p 20 -Z 250 -loc -z 1 -b 1 -B 250 -ssm 2 -sc 1 -seq 1 -dbstrlen 10000 -norealign -maxres 32000 -contxt /cluster/toolkit/production/bioprogs/tools/hh-suite-build-new/data/context_data.crf
No Hit Prob E-value P-value Score SS Cols Query HMM Template HMM
1 4YU6_A Immune inhibitor A, met 97.2 0.00017 2E-09 70.5 -0.1 38 130-171 326-363 (756)
2 PF05547.15 ; Peptidase_M6 ; Im 96.5 0.0024 2.8E-08 54.1 1.7 50 131-185 217-277 (283)
3 PF09471.14 ; Peptidase_M64 ; I 96.3 0.002 2.3E-08 56.2 0.2 17 131-147 145-161 (302)
4 3P1V_A Metallo-endopeptidase; 96.1 0.003 3.4E-08 57.7 0.2 16 131-147 290-306 (407)
5 PF05548.15 ; Peptidase_M11 ; G 95.9 0.006 6.9E-08 52.0 1.2 31 131-170 141-172 (302)
6 PF11350.12 ; DUF3152 ; Protein 95.9 0.0037 4.3E-08 52.4 -0.3 31 127-167 144-175 (211)
7 8K5Y_A Matrix metalloproteinas 94.8 0.019 2.2E-07 46.2 0.5 23 131-168 196-218 (242)
8 1SLM_A STROMELYSIN-1; HYDROLAS 94.6 0.019 2.2E-07 46.6 0.1 23 131-168 198-220 (255)
9 8JUG_A Matrilysin; Matrilysin, 94.5 0.023 2.7E-07 42.0 0.4 23 131-168 119-141 (175)
10 1HY7_A STROMELYSIN-1; mixed al 94.4 0.026 3E-07 41.7 0.4 23 131-168 116-138 (173)
11 3MA2_D Matrix metalloproteinas 94.4 0.027 3.1E-07 41.9 0.5 23 131-168 125-147 (181)
12 7XJO_A Matrix metalloproteinas 94.3 0.03 3.4E-07 41.0 0.5 23 131-168 118-140 (168)
13 1HFC_A FIBROBLAST COLLAGENASE; 94.0 0.034 3.9E-07 40.9 0.5 23 131-168 115-137 (169)
14 1L6J_A Matrix metalloproteinas 94.0 0.028 3.2E-07 51.2 -0.1 24 129-167 377-400 (425)
15 6ESM_A Matrix metalloproteinas 93.9 0.035 4E-07 40.1 0.4 23 131-168 114-136 (160)
16 6R7W_A Mirolysin; metallopepti 93.8 0.032 3.7E-07 47.0 0.1 13 131-144 167-179 (277)
17 6Z2O_A O-glycan protease; O-gl 93.8 0.042 4.9E-07 49.4 0.6 26 131-171 179-212 (371)
18 8B2Q_A Karilysin long form Kly 93.5 0.047 5.4E-07 39.5 0.3 23 131-168 118-140 (166)
19 3LUM_D Ulilysin; metallopeptid 93.4 0.049 5.6E-07 45.1 0.3 13 131-144 165-177 (262)
20 PF13582.10 ; Reprolysin_3 ; Me 93.3 0.067 7.7E-07 36.1 0.9 14 130-144 103-116 (118)
21 1HV5_F STROMELYSIN 3; stromely 93.3 0.052 6E-07 39.5 0.4 23 131-168 116-138 (165)
22 2MZH_A Matrilysin; zymogen, hy 93.3 0.053 6.1E-07 43.8 0.4 23 131-168 192-214 (248)
23 1RM8_A Matrix metalloproteinas 93.3 0.053 6.1E-07 39.6 0.4 23 131-168 120-142 (169)
24 PF00413.28 ; Peptidase_M10 ; M 93.3 0.047 5.4E-07 39.3 0.1 25 129-168 107-131 (156)
25 4QKZ_A Neutrophil collagenase; 93.1 0.058 6.7E-07 39.0 0.3 25 129-168 113-137 (163)
26 PF05572.17 ; Peptidase_M43 ; P 93.0 0.055 6.4E-07 42.0 0.1 12 131-143 71-82 (159)
27 6R7V_A Mirolysin; metallopepti 92.7 0.064 7.4E-07 46.5 0.1 13 131-144 204-216 (314)
28 1SU3_B Interstitial collagenas 92.7 0.072 8.3E-07 47.8 0.4 22 131-167 196-217 (450)
29 1EAK_B 72 KDA TYPE IV COLLAGEN 92.6 0.065 7.5E-07 49.1 0.1 24 129-167 367-390 (421)
30 2JSD_A Matrix metalloproteinas 92.4 0.087 1E-06 38.0 0.5 23 131-168 111-133 (160)
31 1FBL_A FIBROBLAST (INTERSTITIA 92.4 0.088 1E-06 45.3 0.6 26 131-171 116-141 (370)
32 1Y93_A Macrophage metalloelast 92.4 0.093 1.1E-06 38.0 0.6 25 131-170 111-135 (159)
33 5B5O_A Collagenase 3; MMP-13, 92.2 0.092 1.1E-06 38.5 0.4 22 131-167 117-138 (172)
34 1R55_A ADAM 33; metalloproteas 91.6 0.17 2E-06 38.8 1.4 35 131-170 139-173 (214)
35 8DF2_A NPCBM/NEW2 domain-conta 91.5 0.14 1.6E-06 48.3 0.8 26 131-171 220-252 (486)
36 PF01457.20 ; Peptidase_M8 ; Le 91.4 0.39 4.4E-06 45.7 3.6 109 23-144 105-230 (529)
37 2L0R_A Lethal factor; protein, 91.4 0.13 1.5E-06 36.9 0.4 21 102-140 2-22 (106)
38 PF13583.10 ; Reprolysin_4 ; Me 90.9 0.14 1.6E-06 38.9 0.1 13 131-144 136-148 (201)
39 PF02031.20 ; Peptidase_M7 ; St 90.9 0.22 2.5E-06 35.1 1.1 28 129-171 79-108 (133)
40 8CD8_A Ulilysin; Inhibitor, co 90.7 0.15 1.7E-06 45.7 0.2 13 131-144 244-256 (361)
41 PF01421.23 ; Reprolysin ; Repr 90.2 0.17 1.9E-06 38.0 0.1 13 131-144 134-146 (203)
42 1BUD_A PROTEIN (ACUTOLYSIN A); 90.2 0.26 3E-06 36.8 1.1 29 131-168 136-164 (197)
43 3BA0_A Macrophage metalloelast 90.1 0.19 2.2E-06 43.2 0.3 23 131-168 110-132 (365)
44 PF12388.12 ; Peptidase_M57 ; D 90.0 0.22 2.5E-06 38.2 0.5 25 131-170 128-184 (205)
45 PF13688.10 ; Reprolysin_5 ; Me 89.9 0.18 2.1E-06 38.9 0.0 13 131-144 147-159 (205)
46 1ATL_B Snake venom metalloprot 89.8 0.19 2.2E-06 38.0 0.1 13 131-144 139-151 (202)
47 PF10462.13 ; Peptidase_M66 ; P 89.8 0.24 2.8E-06 43.3 0.8 15 129-144 198-212 (310)
48 4DD8_D Disintegrin and metallo 89.7 0.2 2.3E-06 37.9 0.1 13 131-144 136-148 (208)
49 1QUA_A ACUTOLYSIN-C; METALLOPR 89.6 0.2 2.3E-06 37.7 0.1 13 131-144 138-150 (197)
50 6O38_B Acinetobacter secreted 89.4 0.29 3.4E-06 46.3 1.0 29 131-168 495-528 (578)
51 4FVL_A Collagenase 3; protein- 89.4 0.24 2.7E-06 42.8 0.4 23 131-168 116-138 (368)
52 4J4M_B zinc-dependent metallop 89.1 0.23 2.7E-06 37.4 0.1 13 131-144 140-152 (202)
53 2X7M_A ARCHAEMETZINCIN; METALL 88.9 0.35 4.1E-06 39.4 1.1 30 131-175 142-171 (195)
54 8H3X_C Fragilysin; Bacteroide 88.5 0.31 3.6E-06 42.8 0.5 23 131-168 345-367 (397)
55 PF12044.12 ; Metallopep ; Puta 88.4 0.35 4.1E-06 44.9 0.8 22 132-170 330-351 (431)
56 1LML_A LEISHMANOLYSIN; LEISHMA 88.1 2.4 2.8E-05 39.8 6.1 109 23-144 49-174 (478)
57 PF07998.15 ; Peptidase_M54 ; P 88.0 0.3 3.5E-06 39.5 0.1 13 131-144 148-160 (194)
58 1KUF_A metalloproteinase; alph 87.9 0.31 3.6E-06 36.8 0.1 13 131-144 141-153 (203)
59 PF11150.12 ; DUF2927 ; Protein 87.4 0.35 4E-06 38.1 0.2 13 131-144 137-149 (200)
60 1YP1_A FII; FII crystal struct 87.3 0.35 4.1E-06 36.4 0.1 13 131-144 138-150 (202)
61 3HYG_A A disintegrin and metal 86.9 0.39 4.5E-06 36.8 0.1 13 131-144 148-160 (221)
62 4ON1_B Putative metalloproteas 86.6 0.48 5.5E-06 41.7 0.5 23 131-168 331-353 (379)
63 2W15_A ZINC METALLOPROTEINASE 86.5 0.42 4.8E-06 36.2 0.1 13 131-144 139-151 (202)
64 3ZVS_A ARCHAEMETZINCIN; METALL 85.6 0.49 5.7E-06 36.3 0.1 13 131-144 114-126 (160)
65 1C7K_A ZINC ENDOPROTEASE; alph 85.2 0.6 6.9E-06 33.0 0.4 22 131-167 80-103 (132)
66 7UAC_H Meprin A subunit alpha; 84.9 2.1 2.5E-05 40.1 4.0 57 70-146 95-153 (587)
67 4L63_A ECXA; MATRIX METALLOPRO 84.6 0.69 7.9E-06 38.7 0.6 25 131-170 157-202 (266)
68 5ZJK_J Myroilysin; hydrolase; 84.1 0.62 7.1E-06 36.6 0.1 16 131-147 100-115 (213)
69 3LMC_A Peptidase, zinc-depende 83.4 1 1.2E-05 37.7 1.1 30 131-175 146-175 (210)
70 6BE6_D Disintegrin and metallo 82.8 1 1.2E-05 41.3 0.9 13 131-144 167-179 (449)
71 3L0V_A Disintegrin and metallo 82.5 0.79 9.1E-06 37.5 0.1 13 131-144 188-200 (270)
72 3K7L_A Atragin; SVMP, METALLOP 81.9 0.85 9.8E-06 40.9 0.1 13 131-144 147-159 (422)
73 PF13058.10 ; DUF3920 ; Protein 81.8 0.69 7.9E-06 34.0 -0.5 11 130-140 78-88 (126)
74 8A7D_Q Pappalysin-1; Metzincin 81.7 1.1 1.3E-05 47.8 0.9 13 130-143 477-489 (1536)
75 PF06262.15 ; Zincin_1 ; Zincin 81.4 0.76 8.7E-06 32.8 -0.3 15 131-146 66-80 (87)
76 PF08434.15 ; CLCA ; Calcium-ac 81.2 1.1 1.3E-05 38.7 0.6 21 126-147 124-145 (266)
77 2DDF_B ADAM 17; TACE ADAM17 ZN 81.2 0.94 1.1E-05 36.5 0.1 13 131-144 185-197 (257)
78 PF01447.22 ; Peptidase_M4 ; Th 81.1 0.92 1.1E-05 35.2 0.0 10 131-140 137-146 (148)
79 3K7N_A K-like; SVMP, HYDROLASE 80.9 0.98 1.1E-05 39.9 0.1 16 130-146 141-156 (397)
80 2DW0_A Catrocollastatin; apopt 80.9 0.98 1.1E-05 40.3 0.1 13 131-144 140-152 (419)
81 3B2Z_F ADAMTS-4; metalloprotea 79.5 1.1 1.3E-05 37.3 0.0 13 131-144 146-158 (316)
82 2ERO_A vascular apoptosis-indu 79.1 1.3 1.5E-05 39.5 0.3 15 131-146 149-163 (427)
83 3LQ0_A ProAstacin; metallopept 79.0 1.4 1.6E-05 35.3 0.5 26 131-171 123-185 (235)
84 2E3X_A Coagulation factor X-ac 78.9 1.3 1.5E-05 40.0 0.3 15 131-146 142-156 (427)
85 8SL1_A Pappalysin-2; Protease, 77.2 1.7 1.9E-05 46.8 0.5 12 131-143 496-507 (1570)
86 6R4Z_B Pro-Pro endopeptidase; 76.8 1.4 1.6E-05 35.4 -0.1 10 131-140 117-126 (198)
87 2V4B_A ADAMTS-1; ZYMOGEN, PROT 76.2 1.6 1.9E-05 35.6 0.1 13 131-144 146-158 (300)
88 3E11_A predicted zincin-like m 76.1 1.4 1.6E-05 33.0 -0.3 15 131-146 93-107 (114)
89 1K7I_A secreted protease C; me 75.8 1.6 1.8E-05 40.1 -0.1 13 131-144 185-197 (479)
90 PF13574.10 ; Reprolysin_2 ; Me 75.5 1.8 2E-05 34.4 0.1 13 131-144 128-140 (203)
91 PF16313.9 ; DUF4953 ; Met-zinc 75.5 1.8 2E-05 38.0 0.1 16 131-147 16-31 (313)
92 1IAB_A ASTACIN; ZINC ENDOPEPTI 75.4 2 2.3E-05 32.8 0.4 25 131-170 89-150 (200)
93 8ESV_A Disintegrin and metallo 74.7 1.9 2.2E-05 41.1 0.1 13 131-144 175-187 (543)
94 3G5C_B ADAM 22; alpha/beta fol 74.5 1.9 2.2E-05 40.2 0.1 13 131-144 137-149 (510)
95 PF12725.11 ; DUF3810 ; Protein 73.4 2.1 2.4E-05 38.1 0.0 15 131-146 196-210 (319)
96 PF07737.15 ; ATLF ; Anthrax to 72.5 2.1 2.4E-05 33.9 -0.1 10 131-140 109-118 (189)
97 4WK7_A A disintegrin and metal 72.2 2.4 2.7E-05 33.4 0.1 13 131-144 146-158 (235)
98 2EJQ_A Hypothetical protein TT 72.2 2.1 2.5E-05 33.0 -0.1 15 131-146 92-108 (130)
99 1KAP_P ALKALINE PROTEASE; CALC 72.0 2.9 3.3E-05 38.0 0.6 15 131-146 182-196 (479)
100 4GWM_A Meprin A subunit beta; 71.9 2.3 2.6E-05 39.9 -0.1 15 131-146 127-141 (592)
101 6FPC_C PRO-PRO endopeptidase; 71.9 2.2 2.5E-05 33.9 -0.1 10 131-140 108-117 (191)
102 3VTG_A High choriolytic enzyme 71.8 2.6 3E-05 31.9 0.3 22 125-147 90-111 (200)
103 7T5T_A CapP toxin; Zinc metall 71.3 2.1 2.4E-05 37.2 -0.4 11 130-140 94-104 (291)
104 1CK7_A PROTEIN (GELATINASE A); 71.0 3 3.5E-05 40.1 0.5 22 131-167 371-392 (631)
105 7SKL_C Zinc metalloproteinase 69.9 3.1 3.5E-05 36.0 0.3 10 131-140 141-150 (301)
106 6SAR_A Beta-barrel assembly-en 69.6 7.1 8.2E-05 35.7 2.6 46 78-140 91-142 (487)
107 PF14247.10 ; DUF4344 ; Putativ 68.8 2.5 2.9E-05 35.6 -0.5 11 130-140 98-108 (223)
108 PF06114.17 ; Peptidase_M78 ; I 67.7 2.8 3.2E-05 30.5 -0.3 11 130-140 43-53 (139)
109 PF01400.28 ; Astacin ; Astacin 67.2 4.3 5E-05 30.2 0.6 15 132-147 84-98 (194)
110 5D7W_A Serralysin; protease, m 66.8 4 4.6E-05 36.8 0.4 15 131-146 171-185 (469)
111 7Y5Q_B Maltose/maltodextrin-bi 66.1 4.4 5.1E-05 44.9 0.6 12 131-143 876-887 (1944)
112 5CZW_A Myroilysin; propeptide, 65.8 3.8 4.4E-05 32.8 0.0 15 131-146 134-148 (238)
113 4GER_A Gentlyase metalloprotea 65.8 4 4.6E-05 35.3 0.2 10 131-140 132-141 (304)
114 3LQB_A LOC792177 protein; hydr 65.1 3.9 4.5E-05 31.0 -0.0 16 131-147 96-111 (199)
115 3UJZ_A Metalloprotease stcE; m 64.9 5 5.8E-05 41.1 0.7 13 131-144 414-426 (869)
116 6F8B_A Elastase; LasB, inhibit 64.5 4.3 5E-05 35.2 0.2 10 131-140 137-146 (301)
117 2RJQ_A ADAMTS-5; metalloprotea 64.2 4.3 5E-05 34.4 0.1 13 131-144 146-158 (378)
118 3NQX_A Secreted metalloproteas 62.7 4.5 5.2E-05 35.2 -0.1 10 131-140 138-147 (306)
119 PF10463.13 ; Peptidase_U49 ; P 62.3 3.9 4.6E-05 33.1 -0.5 11 130-140 96-106 (198)
120 PF04228.17 ; Zn_peptidase ; Pu 62.2 4 4.6E-05 35.8 -0.5 11 130-140 170-180 (292)
121 6YA1_A Zinc metalloproteinase; 60.3 5.4 6.3E-05 35.2 0.0 10 131-140 167-176 (336)
122 3DTE_A IrrE protein; Deinococc 59.9 4.7 5.4E-05 35.4 -0.5 11 130-140 98-108 (301)
123 5JVI_E Thermolysin; HYDROLASE, 59.7 5.5 6.3E-05 34.9 -0.1 10 131-140 139-148 (316)
124 3KWV_C Lethal factor; Bacillus 59.0 5.6 6.4E-05 34.8 -0.1 10 131-140 146-155 (263)
125 PF04298.16 ; Zn_peptidase_2 ; 58.2 5.8 6.7E-05 33.3 -0.1 10 131-140 89-98 (215)
126 6QIG_A A disintegrin and metal 57.8 6.6 7.7E-05 36.9 0.1 13 131-144 143-155 (604)
127 1G9K_A SERRALYSIN; beta jelly 57.4 7 8.1E-05 35.3 0.2 15 131-146 166-180 (463)
128 PF06167.16 ; Peptidase_M90 ; G 56.6 15 0.00018 31.1 2.1 33 102-140 123-155 (241)
129 8CR4_A Pro-elastase; LasB, Pse 56.6 6.5 7.5E-05 36.5 -0.1 10 131-140 335-344 (514)
130 4QHJ_A Uncharacterized protein 56.0 5.3 6.1E-05 29.1 -0.7 12 129-140 64-75 (110)
131 3EDH_A Bone morphogenetic prot 52.2 10 0.00012 28.7 0.4 15 132-147 91-105 (201)
132 PF13398.10 ; Peptidase_M50B ; 51.9 8.5 9.8E-05 31.6 -0.1 10 131-140 25-34 (205)
133 2VQX_A METALLOPROTEINASE; THER 51.5 9 0.0001 34.4 -0.1 10 131-140 159-168 (341)
134 4DV8_A Lethal factor; endopept 50.1 9.8 0.00011 36.2 -0.1 10 131-140 433-442 (526)
135 5A3Y_A THERMOLYSIN; HYDROLASE, 49.6 10 0.00012 35.3 -0.0 10 131-140 371-380 (548)
136 3SKS_A Putative Oligoendopepti 48.8 10 0.00012 35.2 -0.1 10 131-140 356-365 (567)
137 6H5W_A Angiotensin-converting 47.5 11 0.00013 35.4 -0.2 10 131-140 344-353 (591)
138 PF02128.19 ; Peptidase_M36 ; F 46.2 13 0.00015 33.4 0.1 10 131-140 180-189 (371)
139 3CQB_B Probable protease htpX 46.0 13 0.00015 26.2 0.1 13 131-144 86-98 (107)
140 PF20573.2 ; DUF6782 ; Putative 45.8 12 0.00014 30.6 -0.1 10 131-140 87-96 (234)
141 8A28_B Metalloendopeptidase; m 45.7 15 0.00017 31.5 0.4 14 132-146 116-129 (382)
142 PF01435.22 ; Peptidase_M48 ; P 45.2 14 0.00016 28.5 0.2 8 132-139 65-72 (198)
143 6S1Y_A Angiotensin-converting 44.7 13 0.00015 35.5 -0.1 10 131-140 354-363 (621)
144 5GIV_E Carboxypeptidase 1; M32 44.5 13 0.00015 34.2 -0.2 10 131-140 263-272 (503)
145 3CE2_A Putative peptidase; str 44.2 13 0.00015 35.2 -0.1 10 131-140 399-408 (618)
146 2QR4_B Peptidase M3B, oligoend 44.1 13 0.00015 34.9 -0.1 10 131-140 366-375 (587)
147 PF19093.4 ; DUF5781 ; Family o 43.2 14 0.00016 32.5 -0.2 9 131-139 69-77 (246)
148 7QP3_A Extracellular metallopr 42.8 12 0.00014 34.1 -0.7 10 131-140 181-190 (391)
149 3HQ2_B Bacillus subtilis M32 c 42.7 15 0.00017 33.8 -0.1 10 131-140 262-271 (501)
150 3AHN_A Oligopeptidase; HYDROLA 42.4 15 0.00017 34.1 -0.1 10 131-140 353-362 (564)
151 4CA7_A ANGIOTENSIN-CONVERTING 42.3 15 0.00017 34.6 -0.1 10 131-140 348-357 (598)
152 PF20344.2 ; DUF6639 ; Family o 42.3 15 0.00017 31.1 -0.1 10 131-140 129-138 (231)
153 PF02074.19 ; Peptidase_M32 ; C 41.1 16 0.00018 33.7 -0.1 10 131-140 254-263 (495)
154 PF19527.3 ; DUF6055 ; Family o 41.1 20 0.00023 32.6 0.4 12 129-140 134-145 (431)
155 7W6Y_A Anti sigma-E protein, R 40.9 18 0.00021 33.0 0.2 9 132-140 20-28 (456)
156 7Z6T_AAA Extracellular metallo 40.8 13 0.00015 33.7 -0.7 10 131-140 181-190 (388)
157 5IQJ_B Uncharacterized protein 40.3 17 0.00019 27.4 -0.1 10 131-140 10-19 (134)
158 7A03_A M32 carboxypeptidase; C 40.1 17 0.00019 33.4 -0.1 10 131-140 264-273 (500)
159 PF01432.24 ; Peptidase_M3 ; Pe 39.6 17 0.0002 32.5 -0.1 10 131-140 239-248 (451)
160 7W6X_A Regulator of sigma-E pr 39.4 20 0.00023 32.9 0.2 9 132-140 20-28 (458)
161 PF01401.22 ; Peptidase_M2 ; An 39.3 18 0.0002 33.9 -0.1 10 131-140 345-354 (587)
162 8BYJ_A Processed angiotensin-c 38.5 18 0.00021 34.4 -0.2 10 131-140 354-363 (609)
163 5AMB_B ANGIOTENSIN-CONVERTING 38.5 18 0.00021 34.3 -0.1 10 131-140 358-367 (629)
164 PF10460.13 ; Peptidase_M30 ; P 38.4 19 0.00021 31.6 -0.1 10 131-140 144-153 (371)
165 7Q3Y_A Angiotensin-converting 38.4 19 0.00022 37.4 -0.1 10 131-140 358-367 (1211)
166 6D2S_A HTH-type transcriptiona 38.2 17 0.00019 31.4 -0.5 11 130-140 89-99 (289)
167 5KDS_A F5/8 type C domain prot 38.2 19 0.00022 34.2 -0.1 11 130-140 279-289 (530)
168 1KA2_A M32 carboxypeptidase; H 38.1 19 0.00022 33.1 -0.1 10 131-140 266-275 (499)
169 PF20352.2 ; DUF6647 ; Family o 37.0 20 0.00023 29.3 -0.1 10 131-140 113-122 (175)
170 5KDJ_B F5/8 type C domain prot 36.9 21 0.00024 34.7 -0.1 11 130-140 342-352 (674)
171 4KA7_A Oligopeptidase A; Prote 36.1 21 0.00025 34.5 -0.1 10 131-140 491-500 (714)
172 5KD5_A Metallopeptidase; O-gly 35.9 23 0.00027 34.0 0.1 15 126-140 268-282 (559)
173 PF07607.15 ; DUF1570 ; Protein 35.8 21 0.00025 25.0 -0.2 13 128-140 1-13 (132)
174 6EOM_A MutT/NUDIX family prote 35.0 20 0.00023 34.6 -0.5 12 130-141 375-386 (566)
175 3C37_B Peptidase, M48 family; 34.8 23 0.00026 29.6 -0.1 10 131-140 103-112 (253)
176 2O3E_A Neurolysin; thermolysin 34.8 23 0.00027 34.0 -0.1 10 131-140 471-480 (678)
177 PF02163.26 ; Peptidase_M50 ; P 34.7 26 0.0003 32.4 0.2 9 132-140 11-19 (403)
178 3HOA_B Thermostable carboxypep 34.5 23 0.00027 33.0 -0.1 10 131-140 273-282 (509)
179 1J7N_B Lethal Factor precursor 34.2 24 0.00028 35.9 -0.1 10 131-140 683-692 (776)
180 4IL3_A Ste24p; membrane protei 33.9 24 0.00028 32.4 -0.2 9 131-139 294-302 (461)
181 6SGO_A Secreted protein; Struc 33.5 48 0.00055 25.8 1.4 16 134-150 43-60 (157)
182 3DWC_C Metallocarboxypeptidase 33.5 21 0.00025 32.9 -0.6 10 131-140 264-273 (505)
183 PF19985.3 ; DUF6421 ; Family o 33.5 19 0.00022 33.8 -0.8 12 130-141 222-233 (446)
184 7BB8_B Neutral metalloprotease 33.0 26 0.0003 31.8 -0.1 10 131-140 211-220 (410)
185 5SYT_A CAAX prenyl protease 1 32.8 27 0.00032 32.8 0.0 9 131-139 332-340 (480)
186 7Q3Y_A Angiotensin-converting 32.8 26 0.0003 36.4 -0.1 10 131-140 956-965 (1211)
187 PF13402.10 ; Peptidase_M60 ; P 32.8 27 0.00031 29.0 -0.1 11 130-140 133-143 (262)
188 1Y79_1 Peptidyl-Dipeptidase Dc 32.7 26 0.0003 33.6 -0.1 10 131-140 466-475 (680)
189 5E3X_A Thermostable carboxypep 32.7 26 0.0003 32.1 -0.2 10 131-140 250-259 (489)
190 6CYY_B HTH-type transcriptiona 32.2 24 0.00027 32.6 -0.5 11 130-140 183-193 (429)
191 1XFX_A Calmodulin-sensitive ad 32.0 28 0.00032 35.6 -0.1 10 131-140 145-154 (777)
192 PF15887.9 ; Peptidase_Mx ; Put 30.6 42 0.00048 29.4 0.7 7 134-140 87-93 (236)
193 5ZUM_A dipeptidyl-peptidase II 30.5 29 0.00034 33.2 -0.2 11 131-141 354-364 (537)
194 PF05569.15 ; Peptidase_M56 ; B 30.5 29 0.00033 29.3 -0.2 9 131-139 191-199 (291)
195 PF18818.5 ; MPTase-PolyVal ; Z 29.7 32 0.00037 24.5 -0.1 11 131-141 47-57 (128)
196 3KHI_A Putative Metal-dependen 29.5 37 0.00043 29.4 0.3 15 126-140 142-156 (267)
197 4FCA_A Conserved domain protei 29.1 40 0.00046 32.3 0.4 13 128-140 246-258 (525)
198 PF10026.13 ; DUF2268 ; Predict 29.1 32 0.00037 27.2 -0.1 10 131-140 67-76 (192)
199 7JFS_A F5/8 type C domain prot 28.1 36 0.00042 34.5 -0.1 11 130-140 730-740 (981)
200 6XSX_A ZmpA Glycopeptidase; gl 27.9 39 0.00045 31.8 0.2 15 126-140 273-287 (529)
201 5L44_B K-26 dipeptidyl carboxy 27.0 37 0.00043 32.6 -0.1 10 131-140 472-481 (683)
202 4LGJ_A Uncharacterized protein 26.9 1.3E+02 0.0015 27.1 3.2 53 129-188 156-229 (271)
203 6PNJ_K photosystem I reaction 26.6 47 0.00054 20.8 0.3 6 136-141 22-27 (39)
204 PF04450.16 ; BSP ; Peptidase o 26.5 38 0.00044 27.5 -0.1 10 131-140 103-112 (217)
205 3B4R_A Putative zinc metallopr 26.2 45 0.00052 28.0 0.2 9 132-140 52-60 (224)
206 7XO6_D Angiotensin-converting 26.0 40 0.00046 34.2 -0.1 10 131-140 371-380 (805)
207 2LN3_A DE NOVO DESIGNED PROTEI 25.4 3.4E+02 0.004 19.2 4.2 40 7-54 27-75 (83)
208 PF14891.10 ; Peptidase_M91 ; E 24.9 43 0.0005 26.9 -0.1 10 131-140 81-90 (178)
209 6NCL_c4 P4; tape-measure prote 24.8 38 0.00043 28.5 -0.5 11 130-140 102-112 (181)
210 2O36_A Thimet oligopeptidase; 24.8 43 0.0005 32.1 -0.1 10 131-140 455-464 (674)
211 7WPC_D Angiotensin-converting 24.5 44 0.00051 33.9 -0.1 10 131-140 371-380 (805)
212 7LX0_k Photosystem I reaction 23.7 57 0.00066 21.5 0.3 6 136-141 31-36 (49)
213 4L7A_A Uncharacterized protein 23.7 47 0.00054 28.4 -0.1 10 131-140 141-150 (271)
214 PF03571.19 ; Peptidase_M49 ; P 22.1 69 0.00079 31.4 0.6 12 130-141 312-324 (568)
215 4JIX_B Projannalysin; Hydrolas 22.1 52 0.0006 23.8 -0.1 10 131-140 68-77 (112)
216 PF13485.10 ; Peptidase_MA_2 ; 21.7 56 0.00064 26.1 -0.1 10 131-140 69-78 (243)
217 PF13699.10 ; DUF4157 ; Domain 21.5 70 0.00081 19.5 0.4 10 131-140 63-72 (78)
218 7JS4_A F5/8 type C domain prot 21.4 61 0.0007 32.8 0.1 11 130-140 279-289 (980)
219 6GGR_B Bacteriophage virulence 21.2 51 0.00059 28.1 -0.4 18 127-145 159-177 (212)
220 PF01752.21 ; Peptidase_M9 ; Co 21.1 58 0.00067 27.1 -0.1 10 131-140 161-170 (286)
221 1G12_A PEPTIDYL-LYS METALLOEND 21.1 62 0.00072 24.8 0.1 16 131-147 114-133 (167)
222 PF21420.1 ; Tautomerase-like ; 20.8 4E+02 0.0047 17.4 3.7 24 19-42 9-32 (45)
223 7YX8_A Peptidase M60 domain-co 20.1 70 0.00081 29.5 0.2 15 126-140 252-266 (441)
No 1
>4YU6_A Immune inhibitor A, metalloprotease; hydrolase, metallopeptidase, metzincin; 2.6A {Bacillus cereus var. anthracis (strain CI)}
Probab=97.16 E-value=0.00017 Score=70.50 Aligned_cols=38 Identities=32% Similarity=0.448 Sum_probs=24.1 Template_Neff=7.900
Q ss_pred eecChhhHhhhcCCCcccccCcCCCCCcccccchhccccCCh
Q FD01846349_043 130 INVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMNIGM 171 (190)
Q Consensus 130 ~~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~~G~ 171 (190)
-++||||||.|| |+|+|...... ...+ ...=+||+.|.
T Consensus 326 Gv~aHE~GH~LG-LpDlYd~~~~~-~~~~--vg~wslMs~Gs 363 (756)
T 4YU6_A 326 GVFAHAFGHDLG-LPDEYDTKYTG-TGSP--VEAWSLMSGGS 363 (756)
T ss_dssp HHHHHHHHHHTT-CCCCSCTTCCS-SCCT--TGGGCTTTTTT
T ss_pred HHHHHHHHHhcC-CCccCCCCCCC-CCCc--ccceecccCCC
Confidence 479999999999 99999532000 0011 12339998763
No 2
>PF05547.15 ; Peptidase_M6 ; Immune inhibitor A peptidase M6, catalytic domain
Probab=96.50 E-value=0.0024 Score=54.10 Aligned_cols=50 Identities=24% Similarity=0.190 Sum_probs=0.0 Template_Neff=10.200
Q ss_pred ecChhhHhhhcCCCcccccC-cCCCCCcccccchhccccCChhh----------HHHHHHHHHHHH
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALD-KSGKATTAYRSDAAALMNIGMEL----------RSRYLEHVNTFL 185 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g-~~~~~~~~~~~d~~siM~~G~~v----------r~rh~~~~~~~l 185 (190)
+++|||||.|| |.|-|..+ .. .......-++|+.|.-- ..+|+..+.+|.
T Consensus 217 ~~~HE~gH~lG-l~d~y~~~~~~----~~~~~g~~~lM~~~~~~~~~~~~~~~~~~~~~~~~~~~~ 277 (283)
T Q97L20_CLOAB/1 217 VFCHEFGHDLG-LPDEYDTQYSG----KGEPVGYWSIMSSGSWSGTIPGTEPSGFSAYDKEYFQKR 277 (283)
T ss_pred HHHHHhHhhcC-ChhhcCCCCCC----CCCCccceeccccCCCCCCCCCCCCCCCCHHHHHHHHHH
No 3
>PF09471.14 ; Peptidase_M64 ; IgA Peptidase M64
Probab=96.33 E-value=0.002 Score=56.21 Aligned_cols=17 Identities=41% Similarity=0.565 Sum_probs=0.0 Template_Neff=8.700
Q ss_pred ecChhhHhhhcCCCccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEY 147 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY 147 (190)
+++|||||.+|.|.|||
T Consensus 145 v~~HElGHaf~~L~DEY 161 (302)
T Q08RZ3_STIAD/1 145 IFVHEFGHHFAGLADEY 161 (302)
T ss_pred HHHHHHHHHHhCCcccc
No 4
>3P1V_A Metallo-endopeptidase; STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-BIOLOGY, HYDROLASE; HET: PEG, PO4, MSE; 1.93A {Bacteroides ovatus ATCC 8483}
Probab=96.10 E-value=0.003 Score=57.72 Aligned_cols=16 Identities=56% Similarity=0.889 Sum_probs=0.0 Template_Neff=7.900
Q ss_pred ecChhhHhhh-cCCCccc
Q FD01846349_043 131 NVPHEIGHMI-GYHDDEY 147 (190)
Q Consensus 131 ~~aHEfGHml-G~l~DEY 147 (190)
+++|||||.+ | |.|||
T Consensus 290 v~~HE~GHsf~g-LaDEY 306 (407)
T 3P1V_A 290 VVVHEFGHSFGG-LADEY 306 (407)
T ss_dssp HHHHHHHHHTTC-CCCCC
T ss_pred HHHHHHHhHHhc-ccccc
No 5
>PF05548.15 ; Peptidase_M11 ; Gametolysin peptidase M11
Probab=95.91 E-value=0.006 Score=52.00 Aligned_cols=31 Identities=23% Similarity=0.165 Sum_probs=0.0 Template_Neff=10.500
Q ss_pred ecChhhHhhhcCCCcccccC-cCCCCCcccccchhccccCC
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALD-KSGKATTAYRSDAAALMNIG 170 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g-~~~~~~~~~~~d~~siM~~G 170 (190)
+++||+||.+| |.|.|..+ ... +.-++|+.|
T Consensus 141 ~~~HE~GH~~G-l~~~~~~~~~~~--------~~~~~Mg~~ 172 (302)
T Q948Y8_VOLCA/1 141 TVMQEAIHNYG-LWHSWRNGWEYE--------DYSTAMGRG 172 (302)
T ss_pred HHHHHHHHHcC-CccccCCCCCCC--------CCCCCCCCC
No 6
>PF11350.12 ; DUF3152 ; Protein of unknown function (DUF3152)
Probab=95.85 E-value=0.0037 Score=52.39 Aligned_cols=31 Identities=32% Similarity=0.440 Sum_probs=0.0 Template_Neff=6.900
Q ss_pred cceeecChhhHhhhcCC-CcccccCcCCCCCcccccchhccc
Q FD01846349_043 127 SNQINVPHEIGHMIGYH-DDEYALDKSGKATTAYRSDAAALM 167 (190)
Q Consensus 127 ~~q~~~aHEfGHmlG~l-~DEY~~g~~~~~~~~~~~d~~siM 167 (190)
+.++++.||+||+|| | .-+. .+......+||
T Consensus 144 YR~yvinHEvGHaLG-l~~H~~---------C~~~G~~apVM 175 (211)
T Q4JTR9_CORJK/1 144 YRQYMINHEVGHGIG-HKAHVP---------CSKDGALAPIM 175 (211)
T ss_pred HHHHHHHHHHHHHhc-ccCCCc---------CCCCCccCccc
No 7
>8K5Y_A Matrix metalloproteinase-9; MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, HYDROLASE; HET: VP6; 1.52A {Homo sapiens}
Probab=94.78 E-value=0.019 Score=46.17 Aligned_cols=23 Identities=39% Similarity=0.556 Sum_probs=0.0 Template_Neff=11.800
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
+++||+||.+| |..+. +..++|.
T Consensus 196 ~~~HE~GH~lG-l~h~~--------------~~~svm~ 218 (242)
T 8K5Y_A 196 VAAHEFGHALG-LDHSS--------------VPEALMY 218 (242)
T ss_dssp HHHHHHHHHTT-CCCCS--------------CTTSTTS
T ss_pred HHHHHHHHHhC-CCCCC--------------CCCcccc
No 8
>1SLM_A STROMELYSIN-1; HYDROLASE, METALLOPROTEASE, FIBROBLAST, COLLAGEN DEGRADATION; 1.9A {Homo sapiens} SCOP: a.20.1.2, d.92.1.11
Probab=94.56 E-value=0.019 Score=46.58 Aligned_cols=23 Identities=39% Similarity=0.530 Sum_probs=0.0 Template_Neff=11.700
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
+++||+||.|| |..++ +..++|.
T Consensus 198 ~~~HE~GH~lG-l~H~~--------------~~~~iM~ 220 (255)
T 1SLM_A 198 VAAHEIGHSLG-LFHSA--------------NTEALMY 220 (255)
T ss_dssp HHHHHHHHHTT-CCCCS--------------CTTSTTS
T ss_pred HHHHHhhhHhc-cCcCC--------------CCCCccc
No 9
>8JUG_A Matrilysin; Matrilysin, Matrin, Matrix metalloproteinase-7, Pump-1 protease, Uterine metalloproteinase, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex; HET: EOE, GGL, V1C, TBG, 7SF; 1.3A {Homo sapiens}
Probab=94.50 E-value=0.023 Score=41.97 Aligned_cols=23 Identities=30% Similarity=0.585 Sum_probs=0.0 Template_Neff=12.900
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
+++||+||.+| |..++ +..++|.
T Consensus 119 ~~~he~gh~lg-l~h~~--------------~~~~~m~ 141 (175)
T 8JUG_A 119 AATHQLGHSLG-MGHSS--------------DPNAVMY 141 (175)
T ss_dssp HHHHHHHHHHT-CCCCS--------------CTTSTTS
T ss_pred HHHHHHHHHhc-CCCCC--------------CCCcccc
No 10
>1HY7_A STROMELYSIN-1; mixed alpha beta structure, zinc protease, inhibited, HYDROLASE; HET: MBS; 1.5A {Homo sapiens} SCOP: d.92.1.11
Probab=94.38 E-value=0.026 Score=41.65 Aligned_cols=23 Identities=39% Similarity=0.530 Sum_probs=0.0 Template_Neff=12.900
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
+++||+||.+| |..++ +..++|.
T Consensus 116 ~~~he~gh~lg-l~h~~--------------~~~~~m~ 138 (173)
T 1HY7_A 116 VAAHEIGHSLG-LFHSA--------------NTEALMY 138 (173)
T ss_dssp HHHHHHHHHHT-BCCCS--------------CTTSTTS
T ss_pred HHHHHHHHHhc-cCCCC--------------CCCcccc
No 11
>3MA2_D Matrix metalloproteinase-14; Protein - protein complex, Cleavage on pair of basic residues, Disulfide bond, Membrane, Metal-binding, Metalloprotease, Protease; 2.05A {Homo sapiens} SCOP: d.92.1.11
Probab=94.36 E-value=0.027 Score=41.92 Aligned_cols=23 Identities=35% Similarity=0.647 Sum_probs=0.0 Template_Neff=12.900
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
++.||+||++| |..+. +..++|.
T Consensus 125 ~~~he~gh~lG-l~h~~--------------~~~~im~ 147 (181)
T 3MA2_D 125 VAVHELGHALG-LEHSS--------------DPSAIMA 147 (181)
T ss_dssp HHHHHHHHHTT-CCCCS--------------CTTSTTS
T ss_pred HHHHHHHHHhc-CCCCC--------------CCccccc
No 12
>7XJO_A Matrix metalloproteinase-2; Gelatinase A, Matrix metalloproteinase-2, 72 kDa type IV collagenase, HYDROLASE; HET: EME, DAB, RYH, EOE, B3P, KFB; 2.0A {Homo sapiens}
Probab=94.25 E-value=0.03 Score=40.99 Aligned_cols=23 Identities=35% Similarity=0.606 Sum_probs=0.0 Template_Neff=13.000
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
+++||+||.+| |..+. +..++|.
T Consensus 118 ~~~he~gh~lg-l~~~~--------------~~~~~m~ 140 (168)
T 7XJO_A 118 VAAHAFGHAMG-LEHSQ--------------DPGALMA 140 (168)
T ss_dssp HHHHHHHHHTT-BCCCC--------------CTTCTTS
T ss_pred HHHHHHHHHhc-CCCCC--------------CCCCccc
No 13
>1HFC_A FIBROBLAST COLLAGENASE; METALLOPROTEASE; HET: PLH; 1.5A {Homo sapiens} SCOP: d.92.1.11
Probab=94.04 E-value=0.034 Score=40.95 Aligned_cols=23 Identities=39% Similarity=0.612 Sum_probs=0.0 Template_Neff=12.800
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
++.||+||.+| |...+ +..++|.
T Consensus 115 ~~~he~gh~lg-l~h~~--------------~~~~~m~ 137 (169)
T 1HFC_A 115 VAAHELGHSLG-LSHST--------------DIGALMY 137 (169)
T ss_dssp HHHHHHHHHHT-CCCCS--------------CTTSTTC
T ss_pred HHHHHHHHHHc-cCCCC--------------CCCCccc
No 14
>1L6J_A Matrix metalloproteinase-9; Twisted beta sheet flanked by helices, HYDROLASE; 2.5A {Homo sapiens} SCOP: g.14.1.2, a.20.1.2, d.92.1.11
Probab=93.99 E-value=0.028 Score=51.17 Aligned_cols=24 Identities=38% Similarity=0.555 Sum_probs=0.0 Template_Neff=9.400
Q ss_pred eeecChhhHhhhcCCCcccccCcCCCCCcccccchhccc
Q FD01846349_043 129 QINVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALM 167 (190)
Q Consensus 129 q~~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM 167 (190)
+.+++||+||+|| |.... +..+||
T Consensus 377 ~~~~~he~gh~lg-l~h~~--------------~~~~~m 400 (425)
T 1L6J_A 377 FLVAAHEFGHALG-LDHSS--------------VPEALM 400 (425)
T ss_dssp HHHHHHHHHHHTT-CCCCC--------------CTTSTT
T ss_pred hHHHHHHhhHhhC-cccCC--------------Ccccee
No 15
>6ESM_A Matrix metalloproteinase-9,Matrix metalloproteinase-9; metzincin, carboxylate inhibitor alternative zinc-binding groups, HYDROLASE; HET: PZE, B9Z; 1.104A {Homo sapiens} SCOP: d.92.1.11
Probab=93.94 E-value=0.035 Score=40.13 Aligned_cols=23 Identities=35% Similarity=0.528 Sum_probs=0.0 Template_Neff=13.100
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
+++||+||.+| |..+. +..++|.
T Consensus 114 ~~~he~gh~lG-l~h~~--------------~~~~~~~ 136 (160)
T 6ESM_A 114 VAAHQFGHALG-LDHSS--------------VPEALMY 136 (160)
T ss_dssp HHHHHHHHHTT-CCCCS--------------CTTSTTS
T ss_pred HHHHHHHHHhc-CCCCC--------------CCcchhh
No 16
>6R7W_A Mirolysin; metallopeptidase zymogen, metzincin, pappalysin family, Tannerella forsythia, periodontopathogen, periodontal disease, HYDROLASE; HET: CIT; 1.5A {Tannerella forsythia}
Probab=93.84 E-value=0.032 Score=47.05 Aligned_cols=13 Identities=31% Similarity=0.659 Sum_probs=0.0 Template_Neff=10.400
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.|| |.
T Consensus 167 ~laHElGH~lG-L~ 179 (277)
T 6R7W_A 167 TATHEVGHWLD-LR 179 (277)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHhhhcC-Cc
No 17
>6Z2O_A O-glycan protease; O-glycan endopeptidase, mucins, OgpA. metalloprotease, HYDROLASE; HET: EDO; 1.649A {Akkermansia muciniphila ATCC BAA-835}
Probab=93.76 E-value=0.042 Score=49.37 Aligned_cols=26 Identities=35% Similarity=0.528 Sum_probs=0.0 Template_Neff=8.900
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchh--------ccccCCh
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAA--------ALMNIGM 171 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~--------siM~~G~ 171 (190)
.++||+||++| |+..+ +.. +||+.|.
T Consensus 179 ~~~HELGHafG-LpH~~--------------~~~~~~~~~g~~lM~~g~ 212 (371)
T 6Z2O_A 179 GMAHELGHGLN-LPHNH--------------QTASDGKKYGTALMGSGN 212 (371)
T ss_dssp HHHHHHHHHTT-CCCCB--------------CCHHHHHHHCEETTCSSS
T ss_pred HHHHHHHHhcC-CCCCC--------------CCcccccccccccccCCC
No 18
>8B2Q_A Karilysin long form Kly38; Metallopeptidase inhibitor, HYDROLASE INHIBITOR; HET: GOL, MES; 1.35A {Tannerella forsythia}
Probab=93.46 E-value=0.047 Score=39.49 Aligned_cols=23 Identities=39% Similarity=0.651 Sum_probs=0.0 Template_Neff=13.300
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
++.||+||++| |..+. +..++|.
T Consensus 118 ~~~he~gh~lg-l~~~~--------------~~~~~m~ 140 (166)
T 8B2Q_A 118 VAAHEIGHLLG-IEHSN--------------VSSALMY 140 (166)
T ss_dssp HHHHHHHHHHT-BCCCS--------------CTTSTTS
T ss_pred HHHHHHHHHhc-CCCCC--------------CCccccH
No 19
>3LUM_D Ulilysin; metallopeptidase, hydrolase, metal ion binding, calcium ion binding, Calcium, Disulfide bond, Metal-binding, Metalloprotease, Protease, Zinc, Zymogen; HET: ARG, VAL, CA, GOL; 1.7A {Methanosarcina acetivorans}
Probab=93.36 E-value=0.049 Score=45.09 Aligned_cols=13 Identities=38% Similarity=0.626 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||.+| |.
T Consensus 165 ~laHElGH~lG-L~ 177 (262)
T 3LUM_D 165 TATHEIGHWLN-LY 177 (262)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred hHHHHHhHHhc-cc
No 20
>PF13582.10 ; Reprolysin_3 ; Metallo-peptidase family M12B Reprolysin-like
Probab=93.34 E-value=0.067 Score=36.10 Aligned_cols=14 Identities=36% Similarity=0.643 Sum_probs=0.0 Template_Neff=13.400
Q ss_pred eecChhhHhhhcCCC
Q FD01846349_043 130 INVPHEIGHMIGYHD 144 (190)
Q Consensus 130 ~~~aHEfGHmlG~l~ 144 (190)
.+++||+||.+| +.
T Consensus 103 ~~~ahe~gh~lg-~~ 116 (118)
T ASPN_XANCP/225 103 YSFAHEIGHLQS-AR 116 (118)
T ss_pred eehhHHHHHHhh-cc
No 21
>1HV5_F STROMELYSIN 3; stromelysin-3, inhibition, phosphinic inhibitor, hydrolase; HET: CPS, RXP, ZN; 2.6A {Mus musculus} SCOP: d.92.1.11
Probab=93.34 E-value=0.052 Score=39.46 Aligned_cols=23 Identities=39% Similarity=0.625 Sum_probs=0.0 Template_Neff=13.100
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
++.||+||.+| |..+. +..++|.
T Consensus 116 ~~~he~gh~lg-l~h~~--------------~~~~~m~ 138 (165)
T 1HV5_F 116 VAAHEFGHVLG-LQHTT--------------AAKALMS 138 (165)
T ss_dssp HHHHHHHHHTT-CCCCS--------------STTCTTC
T ss_pred HHHHHHHHHHc-CCCCc--------------cCCceee
No 22
>2MZH_A Matrilysin; zymogen, hydrolase, zwitterionic membrane-bound form, metalloenzyme; HET: CA, PX4, ZN; NMR {Homo sapiens} SCOP: d.92.1.0, a.20.1.0
Probab=93.30 E-value=0.053 Score=43.75 Aligned_cols=23 Identities=30% Similarity=0.560 Sum_probs=0.0 Template_Neff=11.800
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
++.||+||.+| |..+. +..+||.
T Consensus 192 ~~~hE~Gh~lG-l~h~~--------------~~~sim~ 214 (248)
T 2MZH_A 192 AATHALGHSLG-MGHSS--------------DPNAVMY 214 (248)
T ss_dssp HHHHHHHHHTT-CCCCS--------------CTTCSSC
T ss_pred HHHHHHHHHcC-CCCCC--------------CCCCccc
No 23
>1RM8_A Matrix metalloproteinase-16; MMP-16, MT3-MMP, MT-MMP, Membrane Type - Matrix Metalloproteinase, Batimastat, Hydroxamate inhibitor, Protease, HYDROLASE; HET: BAT; 1.8A {Homo sapiens} SCOP: d.92.1.11
Probab=93.26 E-value=0.053 Score=39.57 Aligned_cols=23 Identities=35% Similarity=0.647 Sum_probs=0.0 Template_Neff=13.100
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
++.||+||.+| |..+. +..++|.
T Consensus 120 ~~~he~gh~lg-l~~~~--------------~~~~~m~ 142 (169)
T 1RM8_A 120 VAVHELGHALG-LEHSN--------------DPTAIMA 142 (169)
T ss_dssp HHHHHHHHHHT-CCCCS--------------CTTSTTS
T ss_pred HHHHHhhHHhC-cccCC--------------CCccccc
No 24
>PF00413.28 ; Peptidase_M10 ; Matrixin
Probab=93.25 E-value=0.047 Score=39.27 Aligned_cols=25 Identities=36% Similarity=0.545 Sum_probs=0.0 Template_Neff=13.100
Q ss_pred eeecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 129 QINVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 129 q~~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
+.++.||+||.+| |..++ +..++|.
T Consensus 107 ~~~~~he~gh~lg-l~~~~--------------~~~~~m~ 131 (156)
T Q8BG29_MOUSE/1 107 FVVLAHEIGHTLG-LTHSP--------------APRALMA 131 (156)
T ss_pred hHHHHHHHHHHhc-CCCCC--------------Ccccccc
No 25
>4QKZ_A Neutrophil collagenase; Hydrolase, HYDROLASE-HYDROLASE INHIBITOR complex; HET: MES, QZK; 1.2A {Homo sapiens} SCOP: d.92.1.11
Probab=93.09 E-value=0.058 Score=38.98 Aligned_cols=25 Identities=36% Similarity=0.546 Sum_probs=0.0 Template_Neff=13.200
Q ss_pred eeecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 129 QINVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 129 q~~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
+.+++||+||.+| |..+. +..++|.
T Consensus 113 ~~~~~he~gh~lg-l~h~~--------------~~~~~m~ 137 (163)
T 4QKZ_A 113 FLVAAHEFGHSLG-LAHSS--------------DPGALMY 137 (163)
T ss_dssp HHHHHHHHHHHHT-CCCCS--------------CTTSTTS
T ss_pred ehHHHHHHHHHHh-cCCCC--------------CCCCccc
No 26
>PF05572.17 ; Peptidase_M43 ; Pregnancy-associated plasma protein-A
Probab=92.96 E-value=0.055 Score=42.01 Aligned_cols=12 Identities=33% Similarity=0.708 Sum_probs=0.0 Template_Neff=10.000
Q ss_pred ecChhhHhhhcCC
Q FD01846349_043 131 NVPHEIGHMIGYH 143 (190)
Q Consensus 131 ~~aHEfGHmlG~l 143 (190)
+++||+||.+| |
T Consensus 71 ~~~HElGH~lG-L 82 (159)
T A8FWW8_SHESH/1 71 VLTHEFGHFLD-L 82 (159)
T ss_pred HHHHHHHHHcc-C
No 27
>6R7V_A Mirolysin; metallopeptidase zymogen, metzincin, pappalysin family, Tannerella forsythia, periodontopathogen, periodontal disease, HYDROLASE; HET: GOL; 1.4A {Tannerella forsythia}
Probab=92.70 E-value=0.064 Score=46.51 Aligned_cols=13 Identities=23% Similarity=0.567 Sum_probs=0.0 Template_Neff=9.900
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| |.
T Consensus 204 ~laHElGH~lG-L~ 216 (314)
T 6R7V_A 204 TATHAVGHWLD-LR 216 (314)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHhHhcC-Cc
No 28
>1SU3_B Interstitial collagenase; Prodomain, Hemopexin domain, exocite, Structural Proteomics in Europe, SPINE, Structural Genomics, HYDROLASE; HET: SO4, EPE; 2.2A {Homo sapiens} SCOP: b.66.1.1, a.20.1.2, d.92.1.11
Probab=92.68 E-value=0.072 Score=47.77 Aligned_cols=22 Identities=41% Similarity=0.661 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALM 167 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM 167 (190)
+++||+||.+| |...+ +..+||
T Consensus 196 v~~HE~GHalG-l~h~~--------------~~~siM 217 (450)
T 1SU3_B 196 VAAHELGHSLG-LSHST--------------DIGALM 217 (450)
T ss_dssp HHHHHHHHHHT-CCCCS--------------CTTSTT
T ss_pred HHHHHHHHHhC-CCcCC--------------CCCccc
No 29
>1EAK_B 72 KDA TYPE IV COLLAGENASE; HYDROLASE-HYDROLASE INHIBITOR COMPLEX, HYDROLYSE, MATRIX METALLOPROTEINASE, GELATINASE A, HYDROLASE- HYDROLASE INHIBITOR COMPLEX; HET: SO4; 2.66A {HOMO SAPIENS} SCOP: g.14.1.2, a.20.1.2, d.92.1.11
Probab=92.64 E-value=0.065 Score=49.07 Aligned_cols=24 Identities=33% Similarity=0.612 Sum_probs=0.0 Template_Neff=8.800
Q ss_pred eeecChhhHhhhcCCCcccccCcCCCCCcccccchhccc
Q FD01846349_043 129 QINVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALM 167 (190)
Q Consensus 129 q~~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM 167 (190)
..+++||+||+|| |..+. |..++|
T Consensus 367 ~~~~~h~~g~~~g-~~h~~--------------~~~~~~ 390 (421)
T 1EAK_B 367 FLVAAHQFGHAMG-LEHSQ--------------DPGALM 390 (421)
T ss_dssp HHHHHHHHHHHTT-CCCCS--------------CTTSTT
T ss_pred EEEEEccceeeec-CccCC--------------CCCCcc
No 30
>2JSD_A Matrix metalloproteinase-20; MMP-NNGH, Structural Genomics, Structural Proteomics in Europe, SPINE, SPINE-2, SPINE2-COMPLEXES, HYDROLASE; HET: ZN, NGH, CA; NMR {Homo sapiens} SCOP: d.92.1.11
Probab=92.44 E-value=0.087 Score=38.05 Aligned_cols=23 Identities=39% Similarity=0.609 Sum_probs=0.0 Template_Neff=13.100
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
++.||+||.+| |..+. +..++|.
T Consensus 111 ~~~he~gh~lg-l~~~~--------------~~~~~~~ 133 (160)
T 2JSD_A 111 VAAHEFGHALG-LAHST--------------DPSALMY 133 (160)
T ss_dssp HHHHHHHHHHT-CCCCC--------------CTTCSSC
T ss_pred HHHHHHHHHhc-CCCCC--------------CCCCccC
No 31
>1FBL_A FIBROBLAST (INTERSTITIAL) COLLAGENASE (MMP-1); METALLOPROTEASE; HET: HTA; 2.5A {Sus scrofa} SCOP: b.66.1.1, d.92.1.11
Probab=92.43 E-value=0.088 Score=45.29 Aligned_cols=26 Identities=35% Similarity=0.511 Sum_probs=0.0 Template_Neff=11.700
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhccccCCh
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMNIGM 171 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~~G~ 171 (190)
+++||+||++| |..++ +..++|....
T Consensus 116 ~~~HE~Gh~lG-l~h~~--------------~~~s~m~~~~ 141 (370)
T 1FBL_A 116 VAAHELGHSLG-LSHST--------------DIGALMYPNY 141 (370)
T ss_dssp HHHHHHHHHTT-EECCS--------------CTTSTTSSSC
T ss_pred HHHHHHHHHcC-CCcCC--------------CCCcccCccc
No 32
>1Y93_A Macrophage metalloelastase; MATRIX METALLOPROTEINASE, MMP12, ELASTASE, COMPLEX (ELASTASE-INHIBITOR), METALLO ELASTASE, ACETOHYDROXAMIC ACID, hydrolase; 1.03A {Homo sapiens} SCOP: d.92.1.11
Probab=92.39 E-value=0.093 Score=37.97 Aligned_cols=25 Identities=36% Similarity=0.484 Sum_probs=0.0 Template_Neff=13.000
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhccccCC
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMNIG 170 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~~G 170 (190)
++.||+||.+| |..+. +..++|..+
T Consensus 111 ~~~he~gh~lg-l~~~~--------------~~~~~~~~~ 135 (159)
T 1Y93_A 111 TAVHEIGHSLG-LGHSS--------------DPKAVMFPT 135 (159)
T ss_dssp HHHHHHHHHTT-CCCCS--------------CTTSTTSSS
T ss_pred HHHHHHHHHhC-CCCCC--------------CcchhhcCc
No 33
>5B5O_A Collagenase 3; MMP-13, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex; HET: WMM; 1.2A {Homo sapiens} SCOP: d.92.1.11
Probab=92.23 E-value=0.092 Score=38.54 Aligned_cols=22 Identities=45% Similarity=0.711 Sum_probs=0.0 Template_Neff=13.000
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALM 167 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM 167 (190)
++.||+||.+| |..+. +..++|
T Consensus 117 ~~~he~gh~lg-l~h~~--------------~~~~~~ 138 (172)
T 5B5O_A 117 VAAHEFGHSLG-LDHSK--------------DPGALM 138 (172)
T ss_dssp HHHHHHHHHHT-BCCCS--------------CTTSTT
T ss_pred HHHHHHHHHhc-CCcCC--------------CCcccc
No 34
>1R55_A ADAM 33; metalloprotease, inhibitor, asthma, adam, HYDROLASE; HET: 097, MAN, NAG; 1.58A {Homo sapiens} SCOP: d.92.1.9, l.1.1.1
Probab=91.62 E-value=0.17 Score=38.78 Aligned_cols=35 Identities=23% Similarity=0.294 Sum_probs=0.0 Template_Neff=12.800
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhccccCC
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMNIG 170 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~~G 170 (190)
++|||+||.+| +......... .....+...||+..
T Consensus 139 ~~ahElgH~lG-~~h~~~~~~~----~~~~~~~~~im~~~ 173 (214)
T 1R55_A 139 TMAHEIGHSLG-LSHDPDGCCV----EAAAESGGCVMAAA 173 (214)
T ss_dssp HHHHHHHHHTT-CCCCCTTCCC----SSCGGGTCBTTCSS
T ss_pred HHHHHHHHHcC-CCCCCCCCcc----cccccCCCccccCC
No 35
>8DF2_A NPCBM/NEW2 domain-containing protein; Glycopeptidase, Hydrolase; HET: NA; 2.35A {Akkermansia muciniphila}
Probab=91.46 E-value=0.14 Score=48.31 Aligned_cols=26 Identities=35% Similarity=0.504 Sum_probs=0.0 Template_Neff=7.600
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchh-------ccccCCh
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAA-------ALMNIGM 171 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~-------siM~~G~ 171 (190)
.++||+||.+| |+-.. +.. +||+.|+
T Consensus 220 ~~~HELGHafG-LpH~~--------------~~~~e~~~g~~LMg~Gn 252 (486)
T 8DF2_A 220 GTAHELGHSFG-LPHTG--------------DGWNYPDAGASLMGHGN 252 (486)
T ss_dssp HHHHHHHHHTT-CCCCC--------------CCTTCTTSCEETTTTGG
T ss_pred HHHHHHHHHcC-CCCCC--------------CCCCCCcCCCccccCCC
No 36
>PF01457.20 ; Peptidase_M8 ; Leishmanolysin
Probab=91.42 E-value=0.39 Score=45.68 Aligned_cols=109 Identities=10% Similarity=0.070 Sum_probs=0.0 Template_Neff=8.400
Q ss_pred CCHHHHHHHHHHHHHHHHHHcCCceEEEecCCch-----hhHHhCCCcccEEEEEEEcCCCCcEEEEEEECCCCCCCCce
Q FD01846349_043 23 WTFIEKSLFIINVYTTVCSEWNGKIFFSVSGSSD-----FARKFQGKPLPFDIQMIPVNHGEHWDVTALKVRPGDDVRTY 97 (190)
Q Consensus 23 Wt~~e~~~f~~~~~~~I~~~Ws~k~~l~~~~~~~-----~~~~~~~~~~~v~v~v~~v~~~~h~~V~V~k~~~g~~~rS~ 97 (190)
.|++.++.+++.+...+...|...+.+++..+.- ....|..-+++-...-.-+. +.+..|.|...+.. .+.
T Consensus 105 lt~~k~~~l~~~ilp~a~~~~~~~L~V~~~~~~~~~~~~~~~~C~~~~ip~~~~~~gv~-~~DlviyV~~~~~~---~~~ 180 (529)
T A4H627_LEIBR/4 105 LTEEKRHILINILLPLALQLHVERLKVRQVQGTWKVTGMEGDVCGEFKVPEEHVTVGFS-NIDFVLYVASVPIE---GNI 180 (529)
T ss_pred CCHHHHHHHHHhHHHHHHHHHHHhhceeccCCceEecCCccceeccccCCHHHcCCCCC-CccEEEEEEECccC---CCe
Q ss_pred EEeC------------CcEEEechhHhhceeecCCccccCCcceeecChhhHhhhcCCC
Q FD01846349_043 98 VIWG------------SRILHIDSEDVVAVRKCLDPAQTVCSNQINVPHEIGHMIGYHD 144 (190)
Q Consensus 98 v~~~------------~~~v~l~~~D~~~~~~~~~~~~~~~~~q~~~aHEfGHmlG~l~ 144 (190)
..|. .|.|.++...+.... ......+++||++|+|| +.
T Consensus 181 ~a~a~~c~~~~~~RP~~G~in~~p~~i~~~~--------~~~~~~~~~HEi~H~LG-F~ 230 (529)
T A4H627_LEIBR/4 181 LAWSAFCQVFPDGRPAVGVINIPAAYIRSPY--------DQIMVRTVAHEVAHALG-FN 230 (529)
T ss_pred eeEeeEEEECCCCCEEEEEEEcCHHHcCCCc--------chhHHHHHHHHHHHHhC-CC
No 37
>2L0R_A Lethal factor; protein, Anthrax Lethal Factor, catalytic domain, Zn metalloprotease, Bacillus Anthracis, HYDROLASE, TOXIN; NMR {Bacillus anthracis}
Probab=91.37 E-value=0.13 Score=36.94 Aligned_cols=21 Identities=24% Similarity=0.464 Sum_probs=0.0 Template_Neff=10.200
Q ss_pred CcEEEechhHhhceeecCCccccCCcceeecChhhHhhh
Q FD01846349_043 102 SRILHIDSEDVVAVRKCLDPAQTVCSNQINVPHEIGHMI 140 (190)
Q Consensus 102 ~~~v~l~~~D~~~~~~~~~~~~~~~~~q~~~aHEfGHml 140 (190)
.++|.|.+ .+.++.|||||++
T Consensus 2 ~~~i~~~~------------------~~~~v~HE~gH~i 22 (106)
T 2L0R_A 2 SKGVELRN------------------DSEGFIHEFGHAV 22 (106)
T ss_dssp CCSSTTTH------------------HHHHHHHHHHHHH
T ss_pred CCceeecC------------------cchHHHHHHHHHH
No 38
>PF13583.10 ; Reprolysin_4 ; Metallo-peptidase family M12B Reprolysin-like
Probab=90.89 E-value=0.14 Score=38.92 Aligned_cols=13 Identities=62% Similarity=1.176 Sum_probs=0.0 Template_Neff=12.800
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 136 ~~aHElgH~lG-~~ 148 (201)
T C2M7W3_CAPGI/1 136 TIAHEIGHMFG-AD 148 (201)
T ss_pred HHHHHHHHhhC-CC
No 39
>PF02031.20 ; Peptidase_M7 ; Streptomyces extracellular neutral proteinase (M7) family
Probab=90.86 E-value=0.22 Score=35.14 Aligned_cols=28 Identities=36% Similarity=0.578 Sum_probs=0.0 Template_Neff=12.700
Q ss_pred eeecChhhHhhhcCCCcccccCcCCCCCcccccch--hccccCCh
Q FD01846349_043 129 QINVPHEIGHMIGYHDDEYALDKSGKATTAYRSDA--AALMNIGM 171 (190)
Q Consensus 129 q~~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~--~siM~~G~ 171 (190)
+.+++||+||.+| |..++ +. .++|....
T Consensus 79 ~~~~~he~gh~lg-l~~~~--------------~~~~~~~m~~~~ 108 (133)
T SNPA_STRCO/80- 79 TRVTAHETGHVLG-LPDHY--------------SGPCSELMSGGG 108 (133)
T ss_pred chhhHHHHHHHhc-CCCCC--------------CCCccccccCCC
No 40
>8CD8_A Ulilysin; Inhibitor, complex, protease, serine protease, metalloprotease, metzincin, HYDROLASE; HET: GOL, AES; 1.65A {Escherichia coli}
Probab=90.70 E-value=0.15 Score=45.70 Aligned_cols=13 Identities=38% Similarity=0.626 Sum_probs=0.0 Template_Neff=9.100
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||.+| |.
T Consensus 244 tlaHEiGH~lG-L~ 256 (361)
T 8CD8_A 244 TATHEIGHWLN-LY 256 (361)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-CC
No 41
>PF01421.23 ; Reprolysin ; Reprolysin (M12B) family zinc metalloprotease
Probab=90.22 E-value=0.17 Score=38.05 Aligned_cols=13 Identities=38% Similarity=0.869 Sum_probs=0.0 Template_Neff=13.200
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||.+| +.
T Consensus 134 ~~aHE~gH~lG-~~ 146 (203)
T ADA12_HUMAN/21 134 TLAHELGHNFG-MN 146 (203)
T ss_pred HHHHHHHHhcC-CC
No 42
>1BUD_A PROTEIN (ACUTOLYSIN A); METALLOPROTEINASE, SNAKE VENOM, MMP, TOXIN; 1.9A {Deinagkistrodon acutus} SCOP: d.92.1.9
Probab=90.18 E-value=0.26 Score=36.83 Aligned_cols=29 Identities=21% Similarity=0.445 Sum_probs=0.0 Template_Neff=13.200
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
.+|||+||.+| +.......... +...||.
T Consensus 136 ~~ahelgh~lG-~~h~~~~~~c~--------~~~~im~ 164 (197)
T 1BUD_A 136 TLAHEMAHNLG-VSHDEGSCSCG--------GKSCIMS 164 (197)
T ss_dssp HHHHHHHHHTT-CCCCCTTCCSS--------SSCCTTC
T ss_pred HHHHHHHHHcC-CCCCCCCCCCC--------CCCcccC
No 43
>3BA0_A Macrophage metalloelastase; Full-length MMP-12, hemopexin domain, catalytic domain, domain interaction., Calcium, Extracellular matrix, Glycoprotein, Hydrolase, Metal-binding, Metalloprotease, Polymorphism; 3.0A {Homo sapiens} SCOP: d.92.1.11, b.66.1.0
Probab=90.11 E-value=0.19 Score=43.22 Aligned_cols=23 Identities=39% Similarity=0.579 Sum_probs=0.0 Template_Neff=11.700
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
++.||+||.+| |.++. +..++|.
T Consensus 110 ~~~hE~Gh~lG-l~h~~--------------~~~~~m~ 132 (365)
T 3BA0_A 110 TAVHEIGHSLG-LGHSS--------------DPKAVMF 132 (365)
T ss_dssp HHHHHHHHHHT-CCCCS--------------CTTTTTS
T ss_pred HHHHHhhHHcC-CCcCC--------------CCccccc
No 44
>PF12388.12 ; Peptidase_M57 ; Dual-action HEIGH metallo-peptidase
Probab=89.96 E-value=0.22 Score=38.15 Aligned_cols=25 Identities=32% Similarity=0.563 Sum_probs=0.0 Template_Neff=12.600
Q ss_pred ecChhhHhhhcCCCcc--------------------------------cccCcCCCCCcccccchhccccCC
Q FD01846349_043 131 NVPHEIGHMIGYHDDE--------------------------------YALDKSGKATTAYRSDAAALMNIG 170 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE--------------------------------Y~~g~~~~~~~~~~~d~~siM~~G 170 (190)
++.||+||++| |..+ | |..++|..+
T Consensus 128 ~~~he~gh~lg-l~h~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~--------------d~~sim~~~ 184 (205)
T H8N0W2_CORCM/5 128 VITHELGHTIG-FRHSDYYDRSISCGSGGNEGASNVGAIHIPGTPTTAT--------------RGGSVMNSC 184 (205)
T ss_pred HHHHHHHHHhc-CCCCccCCCccCCCCCCcccCCCCCceecCCCCCCcC--------------CCCceeecc
No 45
>PF13688.10 ; Reprolysin_5 ; Metallo-peptidase family M12
Probab=89.87 E-value=0.18 Score=38.93 Aligned_cols=13 Identities=38% Similarity=0.593 Sum_probs=0.0 Template_Neff=12.300
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 147 ~~aHElgH~lG-~~ 159 (205)
T B6QQC2_TALMQ/2 147 VFAHETGHTFG-AV 159 (205)
T ss_pred HHHHHHHhccC-CC
No 46
>1ATL_B Snake venom metalloproteinase atrolysin-D; METALLOENDOPEPTIDASE, HYDROLASE-HYDROLASE INHIBITOR complex; HET: 0QI; 1.8A {Crotalus atrox} SCOP: d.92.1.9
Probab=89.84 E-value=0.19 Score=37.96 Aligned_cols=13 Identities=38% Similarity=0.922 Sum_probs=0.0 Template_Neff=13.000
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 139 ~~ahelgh~lG-~~ 151 (202)
T 1ATL_B 139 TMAHELGHNLG-ME 151 (202)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHCC-CC
No 47
>PF10462.13 ; Peptidase_M66 ; Peptidase M66
Probab=89.78 E-value=0.24 Score=43.28 Aligned_cols=15 Identities=33% Similarity=0.532 Sum_probs=0.0 Template_Neff=9.300
Q ss_pred eeecChhhHhhhcCCC
Q FD01846349_043 129 QINVPHEIGHMIGYHD 144 (190)
Q Consensus 129 q~~~aHEfGHmlG~l~ 144 (190)
..++|||+||.+| |.
T Consensus 198 ~~~~aHElGHn~G-l~ 212 (310)
T DTML4_DICDI/98 198 TFTFFHEQGHAMG-LP 212 (310)
T ss_pred ccchhhhHHHhcC-CC
No 48
>4DD8_D Disintegrin and metalloproteinase domain-containing protein 8; batimastat, inflammation, alpha/beta motif, metalloproteinase, allergic asthma, tumorigenesis, arthritis, aberrant neural cell signaling, HYDROLASE-HYDROLASE INHIBITOR complex; HET: BAT; 2.1A {Homo sapiens} SCOP: d.92.1.0
Probab=89.67 E-value=0.2 Score=37.95 Aligned_cols=13 Identities=46% Similarity=0.966 Sum_probs=0.0 Template_Neff=13.100
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||.+| +.
T Consensus 136 ~~ahelgh~~G-~~ 148 (208)
T 4DD8_D 136 TMAHEMGHNLG-MD 148 (208)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHhCC-CC
No 49
>1QUA_A ACUTOLYSIN-C; METALLOPROTEASE, HEMORRHAGIC TOXIN, SNAKE VENOM PROTEINASE, AGKISTRODON ACUTUS, TOXIN; 2.2A {Deinagkistrodon acutus} SCOP: d.92.1.9
Probab=89.57 E-value=0.2 Score=37.65 Aligned_cols=13 Identities=38% Similarity=0.910 Sum_probs=0.0 Template_Neff=13.000
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 138 ~~ahelgh~~G-~~ 150 (197)
T 1QUA_A 138 TMAHELGHNLG-MN 150 (197)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcc-CC
No 50
>6O38_B Acinetobacter secreted protease CpaA; Metalloprotease, chaperone, complex, Type II secretion, SUGAR BINDING PROTEIN; HET: SO4, MSE; 2.595A {Acinetobacter nosocomialis M2}
Probab=89.40 E-value=0.29 Score=46.30 Aligned_cols=29 Identities=21% Similarity=0.310 Sum_probs=0.0 Template_Neff=9.800
Q ss_pred ecChhhHhhhcCCCc----ccccC-cCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDD----EYALD-KSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~D----EY~~g-~~~~~~~~~~~d~~siM~ 168 (190)
++|||+||.+| +.- .|..| ... +..+||+
T Consensus 495 ~~aHElGHnlG-~~Hd~~~~~~~g~~~~--------~~~~IM~ 528 (578)
T 6O38_B 495 AMRHEVGHNLG-LYHNGSTNIGSGFAHP--------LGSTAMG 528 (578)
T ss_dssp GHHHHHHHHHT-CBCTTCSSSSBCCCCT--------TCCCGGG
T ss_pred HHHHHHHHHcC-CCCCCCCCCcccccCC--------Ccccccc
No 51
>4FVL_A Collagenase 3; protein-peptide complex, collagenase, cleavage with mmp3, hydrolase, pro-peptide, metzincin, Zinc metalloprotease, collagen cleavage, collagen; HET: PEG, CA, PGO, GOL; 2.436A {Homo sapiens} SCOP: b.66.1.0, d.92.1.11
Probab=89.35 E-value=0.24 Score=42.83 Aligned_cols=23 Identities=39% Similarity=0.583 Sum_probs=0.0 Template_Neff=11.500
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
+++||+||.+| |..+. +..++|.
T Consensus 116 ~~~he~Gh~lg-l~h~~--------------~~~~~m~ 138 (368)
T 4FVL_A 116 VAAHAFGHSLG-LDHSK--------------DPGALMF 138 (368)
T ss_dssp HHHHHHHHHHT-EECCS--------------CTTSTTC
T ss_pred HHHHHHHHhcC-CCcCC--------------CCCcccc
No 52
>4J4M_B zinc-dependent metalloproteinase; alpha/beta-mixed fold, endopeptidase, HYDROLASE; 1.8A {Protobothrops mucrosquamatus} SCOP: d.92.1.0
Probab=89.13 E-value=0.23 Score=37.39 Aligned_cols=13 Identities=38% Similarity=0.841 Sum_probs=0.0 Template_Neff=13.100
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||.+| +.
T Consensus 140 ~~~helgh~lg-~~ 152 (202)
T 4J4M_B 140 TMTHELGHNLG-MA 152 (202)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-CC
No 53
>2X7M_A ARCHAEMETZINCIN; METALLOPROTEASE, PROTEASE, HYDROLASE, METZINCIN, METAL-BINDING; 1.5A {METHANOPYRUS KANDLERI}
Probab=88.91 E-value=0.35 Score=39.38 Aligned_cols=30 Identities=27% Similarity=0.454 Sum_probs=0.0 Template_Neff=9.200
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhccccCChhhHH
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMNIGMELRS 175 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~~G~~vr~ 175 (190)
+++||+||++| |.--- +...+|.....+..
T Consensus 142 ~~~HelGH~lG-l~hc~--------------~~~CvM~~~~~~~~ 171 (195)
T 2X7M_A 142 ELTHELGHTFG-LGHCP--------------DRNCVMSFSSSLLE 171 (195)
T ss_dssp HHHHHHHHHTT-CCCCS--------------CTTSTTSCCSSHHH
T ss_pred HHHHHHHHHcC-CCCCC--------------CCCCcccCCCCHHH
No 54
>8H3X_C Fragilysin; Bacteroide Fragilis Toxin, nanobody, TOXIN; 1.66A {Bacteroides fragilis}
Probab=88.49 E-value=0.31 Score=42.77 Aligned_cols=23 Identities=30% Similarity=0.660 Sum_probs=0.0 Template_Neff=11.300
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
++|||+||.+| +.... +...||.
T Consensus 345 ~~aHElGH~lG-~~H~~--------------~~~~iM~ 367 (397)
T 8H3X_C 345 VMAHELGHILG-AEHTD--------------NSKDLMY 367 (397)
T ss_dssp HHHHHHHHHTT-CCCBS--------------CTTSTTB
T ss_pred HHHHHHHHHcC-CCCCC--------------CCccccc
No 55
>PF12044.12 ; Metallopep ; Putative peptidase family
Probab=88.40 E-value=0.35 Score=44.92 Aligned_cols=22 Identities=27% Similarity=0.469 Sum_probs=0.0 Template_Neff=7.800
Q ss_pred cChhhHhhhcCCCcccccCcCCCCCcccccchhccccCC
Q FD01846349_043 132 VPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMNIG 170 (190)
Q Consensus 132 ~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~~G 170 (190)
++||+||++| -|+ +...||+.|
T Consensus 330 ~lHELGH~fg---------------LpH--~~~giM~rG 351 (431)
T A7F056_SCLS1/1 330 HLHEVGHLFG---------------CPH--QENGVMLRD 351 (431)
T ss_pred HHHHHHHHhC---------------CCC--CCCCccccc
No 56
>1LML_A LEISHMANOLYSIN; LEISHMANOLYSIN, METALLOPROTEASE, GLYCOPROTEIN; 1.86A {Leishmania major} SCOP: d.92.1.3
Probab=88.13 E-value=2.4 Score=39.82 Aligned_cols=109 Identities=11% Similarity=0.064 Sum_probs=0.0 Template_Neff=8.700
Q ss_pred CCHHHHHHHHHHHHHHHHHHcCCceEEEecCCch-----hhHHhCC------------CcccEEEEEEEcCCCCcEEEEE
Q FD01846349_043 23 WTFIEKSLFIINVYTTVCSEWNGKIFFSVSGSSD-----FARKFQG------------KPLPFDIQMIPVNHGEHWDVTA 85 (190)
Q Consensus 23 Wt~~e~~~f~~~~~~~I~~~Ws~k~~l~~~~~~~-----~~~~~~~------------~~~~v~v~v~~v~~~~h~~V~V 85 (190)
.|++.++.+++.+...+.+.|.....+++..+.- ....|.. ....+.|-|.............
T Consensus 49 lt~~~~~~l~~~il~~a~~~~~~~L~V~~~~~~~~~~~~~~~~c~~~~ip~~~~~~gi~~~Dl~i~v~~~~~~~~~~a~a 128 (478)
T 1LML_A 49 LTNEKRDILVKHLIPQAVQLHTERLKVQQVQGKWKVTDMVGDICGDFKVPQAHITEGFSNTDFVMYVASVPSEEGVLAWA 128 (478)
T ss_dssp CCHHHHHHCCCCCHHHHHHHHHTTEEECCEESEECCCCCCSTTGGGSCCCHHHHHTCEESCSEEEEEECCCCSTTCCCEE
T ss_pred CCHHHHHHHHHcHHHHHHHHHHHhhcccccCCceEEecccCCcccCCCCCHHHHcCCCCCCCEEEEEEeCCCCCCeeEEe
Q ss_pred EECCCCCCCCceEEeCCcEEEechhHhhceeecCCccccCCcceeecChhhHhhhcCCC
Q FD01846349_043 86 LKVRPGDDVRTYVIWGSRILHIDSEDVVAVRKCLDPAQTVCSNQINVPHEIGHMIGYHD 144 (190)
Q Consensus 86 ~k~~~g~~~rS~v~~~~~~v~l~~~D~~~~~~~~~~~~~~~~~q~~~aHEfGHmlG~l~ 144 (190)
..-......|.. .|.|.++...+.... ......++.||+||+|| +.
T Consensus 129 ~~c~~~~~~RP~----~G~i~~~~~~~~~~~--------~~~~~~~~lHEi~H~LG-f~ 174 (478)
T 1LML_A 129 TTCQTFSDGHPA----VGVINIPAANIASRY--------DQLVTRVVTHEMAHALG-FS 174 (478)
T ss_dssp EEEEECTTSCEE----EEEEECCGGGCCCSC--------CHHHHHHHHHHHHHHTT-CS
T ss_pred eeeeecCCCCeE----EEEEecCHHHHhhcc--------hhHhhHHHHHHHHHHhc-CC
No 57
>PF07998.15 ; Peptidase_M54 ; Peptidase family M54
Probab=88.01 E-value=0.3 Score=39.51 Aligned_cols=13 Identities=54% Similarity=0.897 Sum_probs=0.0 Template_Neff=9.600
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
.++||+||++| |.
T Consensus 148 ~~~helGh~lG-l~ 160 (194)
T O59448_PYRHO/1 148 GVLHEIGHLYG-LS 160 (194)
T ss_pred HHHHHHHHHcC-Cc
No 58
>1KUF_A metalloproteinase; alpha/beta protein, HYDROLASE; HET: CD; 1.35A {Protobothrops mucrosquamatus} SCOP: d.92.1.9
Probab=87.93 E-value=0.31 Score=36.83 Aligned_cols=13 Identities=38% Similarity=0.917 Sum_probs=0.0 Template_Neff=13.000
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||.+| +.
T Consensus 141 ~~ahelgh~lG-~~ 153 (203)
T 1KUF_A 141 TMTHELGHNLG-ME 153 (203)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-CC
No 59
>PF11150.12 ; DUF2927 ; Protein of unknown function (DUF2927)
Probab=87.45 E-value=0.35 Score=38.10 Aligned_cols=13 Identities=15% Similarity=0.194 Sum_probs=0.0 Template_Neff=11.300
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++.||+||++| |.
T Consensus 137 ~i~hElghalG-l~ 149 (200)
T D5ATR9_RHOCB/1 137 CLHEETSQALG-PL 149 (200)
T ss_pred HHHHHHHHHHC-CC
No 60
>1YP1_A FII; FII crystal structure, HYDROLASE; 1.9A {Deinagkistrodon acutus} SCOP: d.92.1.9
Probab=87.29 E-value=0.35 Score=36.36 Aligned_cols=13 Identities=38% Similarity=0.682 Sum_probs=0.0 Template_Neff=13.100
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||.+| +.
T Consensus 138 ~~ahelgh~~G-~~ 150 (202)
T 1YP1_A 138 VMAHELGHNLG-ML 150 (202)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-CC
No 61
>3HYG_A A disintegrin and metalloproteinase with thrombospondin motifs 5; alpha/beta structure, central five stranded beta-sheet, Cleavage on pair of basic residues, Disulfide bond, Extracellular matrix; HET: 099; 1.4A {Homo sapiens} SCOP: d.92.1.0
Probab=86.85 E-value=0.39 Score=36.85 Aligned_cols=13 Identities=54% Similarity=1.055 Sum_probs=0.0 Template_Neff=13.000
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 148 ~~ahelgh~lG-~~ 160 (221)
T 3HYG_A 148 TVAHEIGHLLG-LS 160 (221)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-CC
No 62
>4ON1_B Putative metalloprotease II; pathogenicity island, human pathogen, fragilysin, metalloproteinases, extracellular, hydrolase; 2.13A {Bacteroides fragilis}
Probab=86.55 E-value=0.48 Score=41.72 Aligned_cols=23 Identities=35% Similarity=0.684 Sum_probs=0.0 Template_Neff=10.800
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhcccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMN 168 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~ 168 (190)
++|||+||.+| +...- +...||.
T Consensus 331 ~~aHElGH~~G-~~Hd~--------------~~~~iM~ 353 (379)
T 4ON1_B 331 TLAHEIGHLLG-AEHVD--------------NEQDLMY 353 (379)
T ss_dssp HHHHHHHHHHT-CCCBS--------------CTTSTTB
T ss_pred HHHHHHHHHhC-CCCCC--------------CCCCccc
No 63
>2W15_A ZINC METALLOPROTEINASE BAP1; HYDROLASE INHIBITOR COMPLEX, METAL-BINDING, ZINC-DEPENDING, METALLOPROTEASE, METALLOPROTEINASE-INHIBITOR COMPLEX, ZINC, TOXIN, SECRETED, PROTEASE, HYDROLASE, P-I SNAKE VENOM; HET: WR2; 1.05A {BOTHROPS ASPER} SCOP: d.92.1.9
Probab=86.49 E-value=0.42 Score=36.20 Aligned_cols=13 Identities=38% Similarity=0.841 Sum_probs=0.0 Template_Neff=12.900
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||.+| +.
T Consensus 139 ~~~he~gh~lG-~~ 151 (202)
T 2W15_A 139 TMAHELGHNLG-IH 151 (202)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-CC
No 64
>3ZVS_A ARCHAEMETZINCIN; METALLOPROTEASE, PROTEASE, HYDROLASE, METZINCIN, METAL-BINDING; HET: MLI; 1.396A {ARCHAEOGLOBUS FULGIDUS}
Probab=85.56 E-value=0.49 Score=36.33 Aligned_cols=13 Identities=46% Similarity=0.897 Sum_probs=0.0 Template_Neff=10.600
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||++| +.
T Consensus 114 ~~~helGh~lG-l~ 126 (160)
T 3ZVS_A 114 EAVHEIGHVLG-LK 126 (160)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-CC
No 65
>1C7K_A ZINC ENDOPROTEASE; alpha and beta protein, METALLOPROTEINASE, HYDROLASE; 1.0A {Streptomyces caespitosus} SCOP: d.92.1.1
Probab=85.18 E-value=0.6 Score=33.00 Aligned_cols=22 Identities=41% Similarity=0.773 Sum_probs=0.0 Template_Neff=12.500
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchh--ccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAA--ALM 167 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~--siM 167 (190)
.+.||+||.+| |.++. +.. ++|
T Consensus 80 ~~~he~g~~lg-l~~~~--------------~~~~~~~~ 103 (132)
T 1C7K_A 80 VTAHETGHVLG-LPDHY--------------QGPCSELM 103 (132)
T ss_dssp HHHHHHHHHHT-CCCCT--------------TSCTTCGG
T ss_pred HHHHHHHHHhc-CCccC--------------CCCCcccc
No 66
>7UAC_H Meprin A subunit alpha; Metalloprotease, complex, helical, extracellular, ONCOPROTEIN; HET: BMA, FUC, NAG;{Homo sapiens}
Probab=84.94 E-value=2.1 Score=40.07 Aligned_cols=57 Identities=19% Similarity=0.189 Sum_probs=0.0 Template_Neff=10.900
Q ss_pred EEEEEcCCCCcEEEEEEECCCCCCCCceEEeCCcE--EEechhHhhceeecCCccccCCcceeecChhhHhhhcCCCcc
Q FD01846349_043 70 IQMIPVNHGEHWDVTALKVRPGDDVRTYVIWGSRI--LHIDSEDVVAVRKCLDPAQTVCSNQINVPHEIGHMIGYHDDE 146 (190)
Q Consensus 70 v~v~~v~~~~h~~V~V~k~~~g~~~rS~v~~~~~~--v~l~~~D~~~~~~~~~~~~~~~~~q~~~aHEfGHmlG~l~DE 146 (190)
+++........+....... | ..+++....+. +.|.. ......++.||+||+|| |.-|
T Consensus 95 i~F~~~~~~~~~i~~~~~~--~--~~s~~g~~~~~~~~~l~~---------------~~~~~~~i~HElgH~lG-l~He 153 (587)
T 7UAC_H 95 VDFKPYEGESSYIIFQQFD--G--CWSEVGDQHVGQNISIGQ---------------GCAYKAIIEHEILHALG-FYHE 153 (587)
T ss_dssp CCEEECSSCSSCEEEECCS--S--CBBCSSCCSSCEEEECCT---------------TCCCHHHHHHHHHHHTT-CCCG
T ss_pred eeeecCCCCCceEEEEccC--C--ceeeecccCCcceEEECC---------------CccccHHHHHHHHHHhc-CCcc
No 67
>4L63_A ECXA; MATRIX METALLOPROTEASE, AB5 TOXIN, OB FOLD, CHOLERA-LIKE TOXIN, PENTAMER, TOXIN, PROTEASE, GM1, TOXILYSIN, HYDROLASE; HET: EPE; 1.8A {Escherichia coli}
Probab=84.62 E-value=0.69 Score=38.67 Aligned_cols=25 Identities=32% Similarity=0.638 Sum_probs=0.0 Template_Neff=10.700
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchh---------------------ccccCC
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAA---------------------ALMNIG 170 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~---------------------siM~~G 170 (190)
++.||+||.+| |..+. +.. +||...
T Consensus 157 ~~~hE~GhalG-l~h~~--------------~~~~~~~~~~~~~~~~~~~~~~~~siM~~~ 202 (266)
T 4L63_A 157 TIKHEIGHILG-LLHNN--------------EGGSYFPHGVGLEVARCRLLNQAPSIMLNG 202 (266)
T ss_dssp HHHHHHHHHTT-BCCTT--------------CTTCEETTEEEEEESBCCSSCCCCCTTCCT
T ss_pred HHHHHHHHHhh-cCCCC--------------CCCCCCCCCceeeEEecCCCCCCCcccccC
No 68
>5ZJK_J Myroilysin; hydrolase; HET: PO4, ZN; 2.6A {Myroides sp. CSLB8}
Probab=84.11 E-value=0.62 Score=36.56 Aligned_cols=16 Identities=44% Similarity=0.623 Sum_probs=0.0 Template_Neff=11.900
Q ss_pred ecChhhHhhhcCCCccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEY 147 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY 147 (190)
+++||+||.+| |.+++
T Consensus 100 ~~~he~gh~lG-l~h~~ 115 (213)
T 5ZJK_J 100 TVIHEFGHALG-MIHEH 115 (213)
T ss_dssp HHHHHHHHHTT-BCCGG
T ss_pred HHHHHHHHHHh-cccCC
No 69
>3LMC_A Peptidase, zinc-dependent; Structural Genomics, PSI-2, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG, MuR16, A2SQK8, HYDROLASE; HET: MSE; 1.997A {Methanocorpusculum labreanum}
Probab=83.44 E-value=1 Score=37.72 Aligned_cols=30 Identities=27% Similarity=0.411 Sum_probs=0.0 Template_Neff=8.100
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhccccCChhhHH
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALMNIGMELRS 175 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM~~G~~vr~ 175 (190)
.++||+||++| |.--- +...+|.....+..
T Consensus 146 ~~~heiGhl~G-l~hc~--------------~~~CvM~~~~~~~~ 175 (210)
T 3LMC_A 146 EGAHEIGHLFG-LGHCD--------------NPGCIMYCPRNLDE 175 (210)
T ss_dssp HHHHHHHHHTT-CCCCS--------------CTTSTTSCCSSHHH
T ss_pred HHHHHHHHHcC-CCCCC--------------CCCCCccCCCCHHH
No 70
>6BE6_D Disintegrin and metalloproteinase domain-containing protein 10; ADAM10, MEMBRANE PROTEIN; HET: NAG, SO4, MAN; 2.8A {Homo sapiens}
Probab=82.77 E-value=1 Score=41.31 Aligned_cols=13 Identities=38% Similarity=0.787 Sum_probs=0.0 Template_Neff=9.800
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| ..
T Consensus 167 ~~AHElGH~lG-a~ 179 (449)
T 6BE6_D 167 TFAHEVGHNFG-SP 179 (449)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred eeehhhHhhcC-CC
No 71
>3L0V_A Disintegrin and metalloproteinase domain-containing protein 17; Metal-binding, Metalloprotease, Notch signaling pathway, Protease, HYDROLASE-HYDROLASE INHIBITOR complex; HET: 724; 1.75A {Homo sapiens} SCOP: d.92.1.10
Probab=82.51 E-value=0.79 Score=37.52 Aligned_cols=13 Identities=38% Similarity=0.774 Sum_probs=0.0 Template_Neff=11.800
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 188 ~~aHElgH~lG-~~ 200 (270)
T 3L0V_A 188 VTTHELGHNFG-AE 200 (270)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-Cc
No 72
>3K7L_A Atragin; SVMP, METALLOPROTEASE, HYDROLASE; HET: NAG; 2.5A {Naja Atra}
Probab=81.92 E-value=0.85 Score=40.89 Aligned_cols=13 Identities=38% Similarity=0.902 Sum_probs=0.0 Template_Neff=10.700
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 147 ~~AHElGH~lG-~~ 159 (422)
T 3K7L_A 147 TMAHEMGHNLG-MN 159 (422)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-CC
No 73
>PF13058.10 ; DUF3920 ; Protein of unknown function (DUF3920)
Probab=81.76 E-value=0.69 Score=34.01 Aligned_cols=11 Identities=27% Similarity=0.465 Sum_probs=0.0 Template_Neff=10.600
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
.+++||+||.+
T Consensus 78 ~~laHElgH~~ 88 (126)
T A0A6L8P3L9_BAC 78 KTLLHEFRHAM 88 (126)
T ss_pred HHHHHHHHHHH
No 74
>8A7D_Q Pappalysin-1; Metzincin metalloprotease Inhibitor complex, HYDROLASE; HET: NAG; 3.06A {Homo sapiens}
Probab=81.66 E-value=1.1 Score=47.81 Aligned_cols=13 Identities=38% Similarity=0.711 Sum_probs=0.0 Template_Neff=9.300
Q ss_pred eecChhhHhhhcCC
Q FD01846349_043 130 INVPHEIGHMIGYH 143 (190)
Q Consensus 130 ~~~aHEfGHmlG~l 143 (190)
.+++||+||.|| |
T Consensus 477 ~~l~HE~GH~lg-L 489 (1536)
T 8A7D_Q 477 HTMIHQIGHSLG-L 489 (1536)
T ss_dssp --------------
T ss_pred ceeHHHHHHHhC-C
No 75
>PF06262.15 ; Zincin_1 ; Zincin-like metallopeptidase
Probab=81.43 E-value=0.76 Score=32.79 Aligned_cols=15 Identities=53% Similarity=0.775 Sum_probs=0.0 Template_Neff=8.200
Q ss_pred ecChhhHhhhcCCCcc
Q FD01846349_043 131 NVPHEIGHMIGYHDDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE 146 (190)
++.||+||.+| +++|
T Consensus 66 ~l~hEl~h~~g-~~~~ 80 (87)
T D0LB94_GORB4/2 66 TVIHEIAHHFG-IDDA 80 (87)
T ss_pred HHHHHHHHHcC-CCHH
No 76
>PF08434.15 ; CLCA ; Calcium-activated chloride channel N terminal
Probab=81.25 E-value=1.1 Score=38.71 Aligned_cols=21 Identities=33% Similarity=0.360 Sum_probs=0.0 Template_Neff=8.500
Q ss_pred CcceeecChhhHh-hhcCCCccc
Q FD01846349_043 126 CSNQINVPHEIGH-MIGYHDDEY 147 (190)
Q Consensus 126 ~~~q~~~aHEfGH-mlG~l~DEY 147 (190)
+....+++||+|| ..| +.|||
T Consensus 124 ~~~~~~l~hEwahyryG-vfdE~ 145 (266)
T G3TD43_LOXAF/2 124 GPSGRALVHEWAHLRWG-VFDEY 145 (266)
T ss_pred cccchhhHHHHHhhccc-cCCCC
No 77
>2DDF_B ADAM 17; TACE ADAM17 ZN-Endopeptidase, Hydrolase; HET: CIT, INN, IPA; 1.7A {Homo sapiens} SCOP: d.92.1.10
Probab=81.16 E-value=0.94 Score=36.50 Aligned_cols=13 Identities=38% Similarity=0.774 Sum_probs=0.0 Template_Neff=12.100
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 185 ~~ahelgh~lG-~~ 197 (257)
T 2DDF_B 185 VTTHELGHNFG-AE 197 (257)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-Cc
No 78
>PF01447.22 ; Peptidase_M4 ; Thermolysin metallopeptidase, catalytic domain
Probab=81.08 E-value=0.92 Score=35.24 Aligned_cols=10 Identities=30% Similarity=0.544 Sum_probs=0.0 Template_Neff=9.200
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 137 vv~HE~~H~v 146 (148)
T Q82P96_STRAW/2 137 VAAHEMSHGV 146 (148)
T ss_pred hHhHHhHccc
No 79
>3K7N_A K-like; SVMP, HYDROLASE; HET: FUC, FUL, NAG; 2.3A {Naja Atra}
Probab=80.92 E-value=0.98 Score=39.93 Aligned_cols=16 Identities=31% Similarity=0.738 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred eecChhhHhhhcCCCcc
Q FD01846349_043 130 INVPHEIGHMIGYHDDE 146 (190)
Q Consensus 130 ~~~aHEfGHmlG~l~DE 146 (190)
.++|||+||++| +...
T Consensus 141 ~~~ahelGH~lG-~~hd 156 (397)
T 3K7N_A 141 STITHELGHNLG-IHHD 156 (397)
T ss_dssp HHHHHHHHHHTT-CCCC
T ss_pred hHHHHHHHHHcC-CCCC
No 80
>2DW0_A Catrocollastatin; apoptotic toxin, SVMP, metalloproteinase, APOPTOSIS, TOXIN; HET: NAG, BMA, MAN, GM6; 2.15A {Crotalus atrox}
Probab=80.89 E-value=0.98 Score=40.31 Aligned_cols=13 Identities=38% Similarity=0.795 Sum_probs=0.0 Template_Neff=10.900
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 140 ~~aHElGH~lG-~~ 152 (419)
T 2DW0_A 140 IMAHEMGHNLG-IN 152 (419)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-CC
No 81
>3B2Z_F ADAMTS-4; metalloprotease, aggrecanase, Cleavage on pair of basic residues, Extracellular matrix, Glycoprotein, Hydrolase, Metal-binding, Secreted, Zymogen; HET: CA; 2.8A {Homo sapiens}
Probab=79.46 E-value=1.1 Score=37.28 Aligned_cols=13 Identities=23% Similarity=0.557 Sum_probs=0.0 Template_Neff=12.100
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 146 ~~ahelgh~lG-~~ 158 (316)
T 3B2Z_F 146 TAAHQLGHVFN-ML 158 (316)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcc-Cc
No 82
>2ERO_A vascular apoptosis-inducing protein 1; metalloprotease, disintegrin, calcium-binding, ADAM, SVMP, MDC protein, TOXIN; HET: NAG; 2.5A {Crotalus atrox}
Probab=79.09 E-value=1.3 Score=39.51 Aligned_cols=15 Identities=40% Similarity=0.888 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhhcCCCcc
Q FD01846349_043 131 NVPHEIGHMIGYHDDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE 146 (190)
++|||+||.+| +...
T Consensus 149 ~~aHElgH~lG-~~hd 163 (427)
T 2ERO_A 149 AMAHEMGHNLG-MDHD 163 (427)
T ss_dssp HHHHHHHHHTT-CCCC
T ss_pred HHHHHHHHHcC-CCCC
No 83
>3LQ0_A ProAstacin; metallopeptidase, zymogen activation, proenzyme, protease, Disulfide bond, Hydrolase, Metal-binding, Metalloprotease, Zymogen; HET: GOL; 1.45A {Astacus astacus}
Probab=78.98 E-value=1.4 Score=35.30 Aligned_cols=26 Identities=27% Similarity=0.525 Sum_probs=0.0 Template_Neff=11.700
Q ss_pred ecChhhHhhhcCCCc-------------------------------------ccccCcCCCCCcccccchhccccCCh
Q FD01846349_043 131 NVPHEIGHMIGYHDD-------------------------------------EYALDKSGKATTAYRSDAAALMNIGM 171 (190)
Q Consensus 131 ~~aHEfGHmlG~l~D-------------------------------------EY~~g~~~~~~~~~~~d~~siM~~G~ 171 (190)
.++||+||.+| |.. .| |..++|..+.
T Consensus 123 ~~~~e~gh~lG-l~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~--------------d~~sim~~~~ 185 (235)
T 3LQ0_A 123 TILHALMHAIG-FYHEHTRMDRDNYVTINYQNVDPSMTSNFDIDTYSRYVGEDY--------------QYYSIMHYGK 185 (235)
T ss_dssp HHHHHHHHHHH-BCCGGGSTTGGGTEEECGGGBCTTSGGGGCCCTTSCCCCSCC--------------CTTCTTCCCT
T ss_pred HHHHHHHHHHh-cccHhhCCCccccEEEcHHhcChhhhcccCCCccccccCCCC--------------CCcccccCCC
No 84
>2E3X_A Coagulation factor X-activating enzyme heavy chain; disintegrin, metalloproteinase, C-type lectin, HYDROLASE, BLOOD CLOTTING, TOXIN; HET: GM6, MAN, NAG; 2.91A {Daboia russellii siamensis}
Probab=78.93 E-value=1.3 Score=39.96 Aligned_cols=15 Identities=27% Similarity=0.536 Sum_probs=0.0 Template_Neff=10.400
Q ss_pred ecChhhHhhhcCCCcc
Q FD01846349_043 131 NVPHEIGHMIGYHDDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE 146 (190)
++|||+||.+| +...
T Consensus 142 ~~aHElGH~lG-~~HD 156 (427)
T 2E3X_A 142 IMAHELSHNLG-MYHD 156 (427)
T ss_dssp HHHHHHHHTTT-CCCC
T ss_pred HHHHHHHHHcC-CCCC
No 85
>8SL1_A Pappalysin-2; Protease, zinc binding, growth factor signaling, peptide binding, HYDROLASE, PEPTIDE BINDING PROTEIN; HET: NAG;{Homo sapiens}
Probab=77.25 E-value=1.7 Score=46.80 Aligned_cols=12 Identities=33% Similarity=0.888 Sum_probs=0.0 Template_Neff=9.100
Q ss_pred ecChhhHhhhcCC
Q FD01846349_043 131 NVPHEIGHMIGYH 143 (190)
Q Consensus 131 ~~aHEfGHmlG~l 143 (190)
+++||+||.|| |
T Consensus 496 tl~HEiGH~lG-L 507 (1570)
T 8SL1_A 496 TMIHQVGHVLG-L 507 (1570)
T ss_dssp HHHHHHHHHTT-C
T ss_pred hhHHHHHHHhC-C
No 86
>6R4Z_B Pro-Pro endopeptidase; Pro-Pro endopeptidase 1, zinc metallopeptidase, Clostridium difficile, virulence factor, HYDROLASE; 1.052A {Peptoclostridium difficile}
Probab=76.80 E-value=1.4 Score=35.42 Aligned_cols=10 Identities=30% Similarity=0.268 Sum_probs=0.0 Template_Neff=10.200
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||++
T Consensus 117 ~~~HE~gH~i 126 (198)
T 6R4Z_B 117 LELHATAHAI 126 (198)
T ss_dssp HHHHHHHHHC
T ss_pred HHHHHHHHHH
No 87
>2V4B_A ADAMTS-1; ZYMOGEN, PROTEASE, ADAMTS-1, HYDROLASE, METALLOPROTEASE, HEPARIN-BINDING, METALLOPROTEINASE, METZINCIN, GLYCOPROTEIN, METAL-BINDING, EXTRACELLULAR MATRIX, CLEAVAGE ON PAIR OF; HET: NI; 2.0A {HOMO SAPIENS}
Probab=76.16 E-value=1.6 Score=35.56 Aligned_cols=13 Identities=31% Similarity=0.687 Sum_probs=0.0 Template_Neff=12.600
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
.+|||+||.+| +.
T Consensus 146 ~~ahelgh~lG-~~ 158 (300)
T 2V4B_A 146 TTAHELGHVFN-MP 158 (300)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-Cc
No 88
>3E11_A predicted zincin-like metalloprotease; Duf1025 family protein, zincin-like fold, conserved matrix metalloprotease motif, structural genomics, Joint Center for Structural Genomics; HET: MSE; 1.8A {Acidothermus cellulolyticus 11B} SCOP: l.1.1.1, d.92.1.17
Probab=76.15 E-value=1.4 Score=32.97 Aligned_cols=15 Identities=60% Similarity=0.873 Sum_probs=0.0 Template_Neff=8.600
Q ss_pred ecChhhHhhhcCCCcc
Q FD01846349_043 131 NVPHEIGHMIGYHDDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE 146 (190)
++.||+||.+| +++|
T Consensus 93 ~l~~El~~~lg-~~~e 107 (114)
T 3E11_A 93 TVVHEIAHHFG-IDDE 107 (114)
T ss_dssp HHHHHHHHHTT-CCHH
T ss_pred HHHHHHHHHcC-CCHH
No 89
>1K7I_A secreted protease C; metalloprotease, hydrolase, protease; 1.59A {Erwinia chrysanthemi} SCOP: d.92.1.6, b.80.7.1
Probab=75.83 E-value=1.6 Score=40.08 Aligned_cols=13 Identities=46% Similarity=0.856 Sum_probs=0.0 Template_Neff=10.500
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++.||+||.|| |.
T Consensus 185 ~~~HEiGHaLG-L~ 197 (479)
T 1K7I_A 185 TFTHEIGHALG-LA 197 (479)
T ss_dssp HHHHHHHHHHT-CC
T ss_pred HHHHHHhHHhc-cC
No 90
>PF13574.10 ; Reprolysin_2 ; Metallo-peptidase family M12B Reprolysin-like
Probab=75.53 E-value=1.8 Score=34.36 Aligned_cols=13 Identities=38% Similarity=0.733 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||.+| +.
T Consensus 128 ~~ahelgh~lg-~~ 140 (203)
T A9VCC2_MONBE/2 128 VFAHEVGHNFG-AS 140 (203)
T ss_pred HHHHHHHHhcC-CC
No 91
>PF16313.9 ; DUF4953 ; Met-zincin
Probab=75.52 E-value=1.8 Score=37.96 Aligned_cols=16 Identities=31% Similarity=0.630 Sum_probs=0.0 Template_Neff=9.500
Q ss_pred ecChhhHhhhcCCCccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEY 147 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY 147 (190)
+++||+||++| |...+
T Consensus 16 ~~~hevGh~lG-l~hn~ 31 (313)
T G8TEJ0_NIAKG/4 16 VSSHEVGHTLG-LRHNM 31 (313)
T ss_pred HHHHHHHHHhc-Ccccc
No 92
>1IAB_A ASTACIN; ZINC ENDOPEPTIDASE; 1.79A {Astacus astacus} SCOP: d.92.1.8
Probab=75.39 E-value=2 Score=32.76 Aligned_cols=25 Identities=32% Similarity=0.608 Sum_probs=0.0 Template_Neff=12.500
Q ss_pred ecChhhHhhhcCCCc-------------------------------------ccccCcCCCCCcccccchhccccCC
Q FD01846349_043 131 NVPHEIGHMIGYHDD-------------------------------------EYALDKSGKATTAYRSDAAALMNIG 170 (190)
Q Consensus 131 ~~aHEfGHmlG~l~D-------------------------------------EY~~g~~~~~~~~~~~d~~siM~~G 170 (190)
.++||+||.+| |.. .| |..+||..+
T Consensus 89 ~~~~~~g~~lg-l~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~--------------d~~si~~~~ 150 (200)
T 1IAB_A 89 TIIHELMHAIG-FYHEHTRMDRDNYVTINYQNVDPSMTSNFDIDTYSRYVGEDY--------------QYYSIMHYG 150 (200)
T ss_dssp HHHHHHHHHHT-BCCGGGSTTGGGTEEECGGGBCGGGGGGGCCCSSEECCSCCC--------------CTTCTTCCC
T ss_pred HHHHHHHHHHc-hhchhhCCCccccEEEehhhCChHHHhcCCccccccccCCCC--------------CCcccccCC
No 93
>8ESV_A Disintegrin and metalloproteinase domain-containing protein 10; Protease, Metalloprotease, Tetraspanin, Sheddase, Adhesion, MEMBRANE PROTEIN; HET: Y01, MAN, NAG, BAT; 3.3A {Homo sapiens}
Probab=74.67 E-value=1.9 Score=41.11 Aligned_cols=13 Identities=38% Similarity=0.787 Sum_probs=0.0 Template_Neff=8.900
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| ..
T Consensus 175 t~AHEiGH~fG-a~ 187 (543)
T 8ESV_A 175 TFAHEVGHNFG-SP 187 (543)
T ss_pred HHHHHHHHhcC-CC
No 94
>3G5C_B ADAM 22; alpha/beta fold, cross-linked domain, Cell adhesion, Cleavage on pair of basic residues, EGF-like domain, Glycoprotein, Membrane; HET: NAG; 2.36A {Homo sapiens}
Probab=74.51 E-value=1.9 Score=40.24 Aligned_cols=13 Identities=23% Similarity=0.404 Sum_probs=0.0 Template_Neff=9.900
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.|| +.
T Consensus 137 ~~AHElGH~lG-~~ 149 (510)
T 3G5C_B 137 TLAQSLAHNIG-II 149 (510)
T ss_dssp HHHHHHHHHHT-CC
T ss_pred HHHHHHHHHcC-Cc
No 95
>PF12725.11 ; DUF3810 ; Protein of unknown function (DUF3810)
Probab=73.39 E-value=2.1 Score=38.14 Aligned_cols=15 Identities=33% Similarity=0.565 Sum_probs=0.0 Template_Neff=8.400
Q ss_pred ecChhhHhhhcCCCcc
Q FD01846349_043 131 NVPHEIGHMIGYHDDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE 146 (190)
++|||++|..| ..+|
T Consensus 196 t~aHE~AH~~G-~a~E 210 (319)
T R7INP0_9FIRM/3 196 DTCHELAHLHG-FMRE 210 (319)
T ss_pred HHHHHHHHHhc-ccCH
No 96
>PF07737.15 ; ATLF ; Anthrax toxin lethal factor, N- and C-terminal domain
Probab=72.48 E-value=2.1 Score=33.94 Aligned_cols=10 Identities=30% Similarity=0.411 Sum_probs=0.0 Template_Neff=10.500
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||++
T Consensus 109 ~~~HE~gH~i 118 (189)
T A0A443IT43_9BA 109 LEYHELAHSL 118 (189)
T ss_pred HHHHHHHHHH
No 97
>4WK7_A A disintegrin and metalloproteinase with thrombospondin motifs 4; Metalloprotease, Osteoarthritis, Inhibitor, hydrolase-hydrolase inhibitor complex; HET: 3PQ; 1.24A {Homo sapiens} SCOP: d.92.1.0
Probab=72.22 E-value=2.4 Score=33.42 Aligned_cols=13 Identities=31% Similarity=0.606 Sum_probs=0.0 Template_Neff=12.400
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 146 ~~ahelgh~lG-~~ 158 (235)
T 4WK7_A 146 TAAHELGHVFN-ML 158 (235)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcc-CC
No 98
>2EJQ_A Hypothetical protein TTHA0227; hypothetical protein, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI; 2.08A {Thermus thermophilus} SCOP: d.92.1.17
Probab=72.17 E-value=2.1 Score=32.96 Aligned_cols=15 Identities=20% Similarity=0.450 Sum_probs=0.0 Template_Neff=8.100
Q ss_pred ecChhhHhhhcCC--Ccc
Q FD01846349_043 131 NVPHEIGHMIGYH--DDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l--~DE 146 (190)
++.||+||.+| + +++
T Consensus 92 tl~hEl~h~lg-~~~~~~ 108 (130)
T 2EJQ_A 92 TMLHELRHHLE-SLAGRD 108 (130)
T ss_dssp HHHHHHHHHHH-HHHTTC
T ss_pred HHHHHHHHHhh-hcCCch
No 99
>1KAP_P ALKALINE PROTEASE; CALCIUM BINDING PROTEIN, ZINC METALLOPROTEASE; 1.64A {Pseudomonas aeruginosa} SCOP: d.92.1.6, b.80.7.1
Probab=72.01 E-value=2.9 Score=38.05 Aligned_cols=15 Identities=40% Similarity=0.798 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred ecChhhHhhhcCCCcc
Q FD01846349_043 131 NVPHEIGHMIGYHDDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE 146 (190)
++.||+||+|| |..+
T Consensus 182 ~~~hEiGhalG-l~h~ 196 (479)
T 1KAP_P 182 TLTHEIGHTLG-LSHP 196 (479)
T ss_dssp HHHHHHHHHHT-CCCS
T ss_pred hHHhHHHHHhc-CCCC
No 100
>4GWM_A Meprin A subunit beta; Mulidomain structure, Hydrolase; HET: NAG, BMA, MAN, FUC; 1.85A {Homo sapiens}
Probab=71.92 E-value=2.3 Score=39.86 Aligned_cols=15 Identities=40% Similarity=0.519 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred ecChhhHhhhcCCCcc
Q FD01846349_043 131 NVPHEIGHMIGYHDDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE 146 (190)
+++||+||+|| |..|
T Consensus 127 ~i~helgh~lG-l~he 141 (592)
T 4GWM_A 127 TVQHEFLHALG-FWHE 141 (592)
T ss_dssp HHHHHHHHHHT-CCCS
T ss_pred HHHHHHHHHhc-Chhh
No 101
>6FPC_C PRO-PRO endopeptidase; Endopeptidase, Metalloprotease, Zinc, HYDROLASE; HET: SO4, CD; 1.75A {Paenibacillus alvei}
Probab=71.89 E-value=2.2 Score=33.88 Aligned_cols=10 Identities=30% Similarity=0.185 Sum_probs=0.0 Template_Neff=10.500
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||.+
T Consensus 108 ~~~HE~gH~i 117 (191)
T 6FPC_C 108 LEIHETLHAV 117 (191)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 102
>3VTG_A High choriolytic enzyme 1; hatching enzyme, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, astacin family, zinc; 1.34A {Oryzias latipes}
Probab=71.77 E-value=2.6 Score=31.94 Aligned_cols=22 Identities=27% Similarity=0.483 Sum_probs=0.0 Template_Neff=12.700
Q ss_pred CCcceeecChhhHhhhcCCCccc
Q FD01846349_043 125 VCSNQINVPHEIGHMIGYHDDEY 147 (190)
Q Consensus 125 ~~~~q~~~aHEfGHmlG~l~DEY 147 (190)
.......+.||+||.+| |..++
T Consensus 90 ~~~~~~~~~~e~g~~~g-l~~~~ 111 (200)
T 3VTG_A 90 GCMYSGIIQHELNHALG-FQHEQ 111 (200)
T ss_dssp TCCSHHHHHHHHHHHHT-BCCGG
T ss_pred CCCcchHHHHHHHHHhc-cccHh
No 103
>7T5T_A CapP toxin; Zinc metallopeptidase, IrrE, cysteine switch, HYDROLASE; HET: SO4, NHE; 1.35A {Thauera sp. K11}
Probab=71.30 E-value=2.1 Score=37.17 Aligned_cols=11 Identities=45% Similarity=0.881 Sum_probs=0.0 Template_Neff=9.300
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+++|||+||.+
T Consensus 94 ftiaHElgH~~ 104 (291)
T 7T5T_A 94 FTQAHELGHYI 104 (291)
T ss_dssp HHHHHHHHHHH
T ss_pred HHHHHHHHHHH
No 104
>1CK7_A PROTEIN (GELATINASE A); HYDROLASE (METALLOPROTEASE), FULL-LENGTH, METALLOPROTEINASE, GELATINASE A, HYDROLASE; HET: SO4; 2.8A {Homo sapiens} SCOP: b.66.1.1, g.14.1.2, a.20.1.2, d.92.1.11
Probab=71.02 E-value=3 Score=40.06 Aligned_cols=22 Identities=36% Similarity=0.638 Sum_probs=0.0 Template_Neff=10.000
Q ss_pred ecChhhHhhhcCCCcccccCcCCCCCcccccchhccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEYALDKSGKATTAYRSDAAALM 167 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY~~g~~~~~~~~~~~d~~siM 167 (190)
+++||+||.+| |..-- +..+||
T Consensus 371 ~~~~~~~~~~~-~~~~~--------------~~~~~~ 392 (631)
T 1CK7_A 371 VAAHAFGHAMG-LEHSQ--------------DPGALM 392 (631)
T ss_dssp HHHHHHHHHHT-CCCCC--------------CTTSTT
T ss_pred EehhhcccccC-CCcCC--------------Cccccc
No 105
>7SKL_C Zinc metalloproteinase aureolysin; Metallopeptidase, inhibitor complex, point mutant, HYDROLASE; HET: EDO; 1.6A {Staphylococcus aureus}
Probab=69.87 E-value=3.1 Score=36.03 Aligned_cols=10 Identities=40% Similarity=0.614 Sum_probs=0.0 Template_Neff=9.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 141 Vv~HE~gH~v 150 (301)
T 7SKL_C 141 VVAHELTHGV 150 (301)
T ss_dssp HHHHHHHHHH
T ss_pred hhhHhHHhhH
No 106
>6SAR_A Beta-barrel assembly-enhancing protease; outer membrane bam complex chaperone protease, CHAPERONE; 2.18A {Escherichia coli (strain K12)}
Probab=69.60 E-value=7.1 Score=35.72 Aligned_cols=46 Identities=13% Similarity=0.192 Sum_probs=0.0 Template_Neff=10.900
Q ss_pred CCcEEEEEEECCC-CCCCCceEEeCCcEEEech---hHhhceeecCCccccCCcce--eecChhhHhhh
Q FD01846349_043 78 GEHWDVTALKVRP-GDDVRTYVIWGSRILHIDS---EDVVAVRKCLDPAQTVCSNQ--INVPHEIGHMI 140 (190)
Q Consensus 78 ~~h~~V~V~k~~~-g~~~rS~v~~~~~~v~l~~---~D~~~~~~~~~~~~~~~~~q--~~~aHEfGHml 140 (190)
...|.|.|.+.+. + .++.+ .|.|.+.+ ..+ .+..+ -++|||+||..
T Consensus 91 ~~~~~~~~~~~~~~n----Afa~p-gg~i~v~~gll~~~------------~~~~ela~vlaHE~~H~~ 142 (487)
T 6SAR_A 91 KTPFHFFLINNDEIN----AFAFF-GGNVVLHSALFRYS------------DNESQLASVMAHEISHVT 142 (487)
T ss_dssp CSCCEEEEECCSSCC----EEEET-TTEEEEETHHHHHC------------SSHHHHHHHHHHHHHHHH
T ss_pred CCCeEEEEecCCCCc----eEeec-CCEEEEechhHHhC------------CCHHHHHHHHHHHHHHHH
No 107
>PF14247.10 ; DUF4344 ; Putative metallopeptidase
Probab=68.84 E-value=2.5 Score=35.64 Aligned_cols=11 Identities=45% Similarity=0.558 Sum_probs=0.0 Template_Neff=8.400
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
++++||+||++
T Consensus 98 ~~l~HElgHal 108 (223)
T G8AGR9_9PROT/4 98 EVVLHELAHAI 108 (223)
T ss_pred HHHHHHHHHHH
No 108
>PF06114.17 ; Peptidase_M78 ; IrrE N-terminal-like domain
Probab=67.74 E-value=2.8 Score=30.50 Aligned_cols=11 Identities=27% Similarity=0.697 Sum_probs=0.0 Template_Neff=11.700
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
.+++||+||++
T Consensus 43 ~~l~hEl~H~~ 53 (139)
T Q89Y86_BRADU/3 43 FSAAHELAHHV 53 (139)
T ss_pred hHHHHHHHHHH
No 109
>PF01400.28 ; Astacin ; Astacin (Peptidase family M12A)
Probab=67.16 E-value=4.3 Score=30.23 Aligned_cols=15 Identities=47% Similarity=0.764 Sum_probs=0.0 Template_Neff=13.100
Q ss_pred cChhhHhhhcCCCccc
Q FD01846349_043 132 VPHEIGHMIGYHDDEY 147 (190)
Q Consensus 132 ~aHEfGHmlG~l~DEY 147 (190)
+.||+||++| +..+.
T Consensus 84 ~~~~~g~~lg-~~~~~ 98 (194)
T BMP1_HUMAN/128 84 VVHELGHVVG-FWHEH 98 (194)
T ss_pred HHHHHHHHHc-ccCcC
No 110
>5D7W_A Serralysin; protease, metalloprotease, HYDROLASE; HET: GOL; 1.1A {Serratia marcescens} SCOP: l.1.1.1, b.80.7.0, d.92.1.0
Probab=66.80 E-value=4 Score=36.85 Aligned_cols=15 Identities=40% Similarity=0.758 Sum_probs=0.0 Template_Neff=11.300
Q ss_pred ecChhhHhhhcCCCcc
Q FD01846349_043 131 NVPHEIGHMIGYHDDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE 146 (190)
++.||+||.+| |..+
T Consensus 171 ~~~hE~Gh~lG-l~h~ 185 (469)
T 5D7W_A 171 TFTHEIGHALG-LSHP 185 (469)
T ss_dssp HHHHHHHHHHT-CCCS
T ss_pred HHHHhhhHHhc-CCCC
No 111
>7Y5Q_B Maltose/maltodextrin-binding periplasmic protein,Pappalysin-1; Hydrolase, METAL BINDING PROTEIN; 3.8A {Homo sapiens}
Probab=66.14 E-value=4.4 Score=44.95 Aligned_cols=12 Identities=50% Similarity=0.883 Sum_probs=0.0 Template_Neff=8.300
Q ss_pred ecChhhHhhhcCC
Q FD01846349_043 131 NVPHEIGHMIGYH 143 (190)
Q Consensus 131 ~~aHEfGHmlG~l 143 (190)
+++||+||-|| |
T Consensus 876 t~~HEvGH~LG-L 887 (1944)
T 7Y5Q_B 876 TMIHEIGHSLG-L 887 (1944)
T ss_dssp HHHHHHHHHTT-C
T ss_pred hhHHHHHHHhC-C
No 112
>5CZW_A Myroilysin; propeptide, Inhibition, protease, HYDROLASE; HET: MLY; 1.6A {Myroides profundi}
Probab=65.84 E-value=3.8 Score=32.83 Aligned_cols=15 Identities=47% Similarity=0.713 Sum_probs=0.0 Template_Neff=11.800
Q ss_pred ecChhhHhhhcCCCcc
Q FD01846349_043 131 NVPHEIGHMIGYHDDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE 146 (190)
++.||+||.+| |..+
T Consensus 134 ~~~he~gh~lg-l~h~ 148 (238)
T 5CZW_A 134 TVIHEFGHALG-MIHE 148 (238)
T ss_dssp HHHHHHHHHHT-CCCB
T ss_pred HHHHHHHHHHh-cccc
No 113
>4GER_A Gentlyase metalloprotease; protease, metalloproteinase, tissue disaggregation, thermolysin-like protease, HYDROLASE; HET: LYS, THR; 1.59A {Paenibacillus polymyxa} SCOP: d.92.1.2
Probab=65.81 E-value=4 Score=35.30 Aligned_cols=10 Identities=40% Similarity=0.551 Sum_probs=0.0 Template_Neff=10.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 132 Vv~HE~~H~v 141 (304)
T 4GER_A 132 VVGHELTHGV 141 (304)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 114
>3LQB_A LOC792177 protein; hydrolase, metalloprotease, hatching enzyme, astacin, Metal-binding, Protease; 1.1A {Danio rerio}
Probab=65.11 E-value=3.9 Score=30.98 Aligned_cols=16 Identities=31% Similarity=0.501 Sum_probs=0.0 Template_Neff=12.700
Q ss_pred ecChhhHhhhcCCCccc
Q FD01846349_043 131 NVPHEIGHMIGYHDDEY 147 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DEY 147 (190)
.+.||+||.+| |..++
T Consensus 96 ~~~~e~g~~lg-l~~~~ 111 (199)
T 3LQB_A 96 IAQHELNHALG-FYHEQ 111 (199)
T ss_dssp HHHHHHHHHHT-CCCGG
T ss_pred HHHHHHHHHhc-ccchh
No 115
>3UJZ_A Metalloprotease stcE; metalloprotease, mucin-type glycoprotein, HYDROLASE; HET: MSE; 2.5A {Escherichia coli}
Probab=64.89 E-value=5 Score=41.13 Aligned_cols=13 Identities=31% Similarity=0.711 Sum_probs=0.0 Template_Neff=7.200
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
+++||+||.+| |.
T Consensus 414 ~faHElGHn~G-L~ 426 (869)
T 3UJZ_A 414 EFSHDVGHNYG-LG 426 (869)
T ss_dssp HHHHHHHHTTT-CC
T ss_pred cchhhhhhccC-CC
No 116
>6F8B_A Elastase; LasB, inhibitor, hydrolase; HET: CXH; 1.3A {Pseudomonas aeruginosa} SCOP: d.92.1.2
Probab=64.52 E-value=4.3 Score=35.18 Aligned_cols=10 Identities=30% Similarity=0.494 Sum_probs=0.0 Template_Neff=9.800
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 137 Vi~HE~~H~v 146 (301)
T 6F8B_A 137 VAAHEVSHGF 146 (301)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHhhHHHH
No 117
>2RJQ_A ADAMTS-5; metalloprotease domain, aggrecanase, Cleavage on pair of basic residues, Extracellular matrix, Glycoprotein, Hydrolase, Metal-binding, Secreted, Zymogen; HET: NAG, BAT; 2.6A {Homo sapiens}
Probab=64.16 E-value=4.3 Score=34.40 Aligned_cols=13 Identities=54% Similarity=1.055 Sum_probs=0.0 Template_Neff=12.600
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| ..
T Consensus 146 ~~ahelgh~lG-~~ 158 (378)
T 2RJQ_A 146 TVAHEIGHLLG-LS 158 (378)
T ss_dssp HHHHHHHHHTT-CC
T ss_pred HHHHHHHHHcC-Cc
No 118
>3NQX_A Secreted metalloprotease Mcp02; Zinc metalloprotease, alpha/beta protein, HYDROLASE; 1.7A {Pseudoalteromonas sp.}
Probab=62.67 E-value=4.5 Score=35.18 Aligned_cols=10 Identities=30% Similarity=0.458 Sum_probs=0.0 Template_Neff=9.800
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 138 Vi~HE~gH~v 147 (306)
T 3NQX_A 138 VSAHEVSHGF 147 (306)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 119
>PF10463.13 ; Peptidase_U49 ; Peptidase U49
Probab=62.31 E-value=3.9 Score=33.15 Aligned_cols=11 Identities=36% Similarity=0.631 Sum_probs=0.0 Template_Neff=9.700
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
.+++||+||.+
T Consensus 96 ~vl~HE~~H~~ 106 (198)
T LIT_ECOLI/61-2 96 WILHHEISHVV 106 (198)
T ss_pred HHHHHHHHHHH
No 120
>PF04228.17 ; Zn_peptidase ; Putative neutral zinc metallopeptidase
Probab=62.19 E-value=4 Score=35.82 Aligned_cols=11 Identities=36% Similarity=0.836 Sum_probs=0.0 Template_Neff=8.600
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+++|||+||.+
T Consensus 170 ~vlAHE~GHhv 180 (292)
T Q9HV81_PSEAE/1 170 YVIAHEVGHHV 180 (292)
T ss_pred HHHHHHHHHHH
No 121
>6YA1_A Zinc metalloproteinase; ProA, M4 protease, TLP-like, Metalloprotease, zinc, METAL BINDING PROTEIN; HET: ACT; 1.48A {Legionella pneumophila} SCOP: d.92.1.0
Probab=60.27 E-value=5.4 Score=35.23 Aligned_cols=10 Identities=30% Similarity=0.318 Sum_probs=0.0 Template_Neff=9.700
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 167 Vv~HE~gH~v 176 (336)
T 6YA1_A 167 VGGHEVSHGF 176 (336)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 122
>3DTE_A IrrE protein; Deinococcus, Radiotolerance, Gene regulation, Metallopeptidase, IrrE; HET: MSE; 2.6A {Deinococcus deserti}
Probab=59.94 E-value=4.7 Score=35.41 Aligned_cols=11 Identities=36% Similarity=0.779 Sum_probs=0.0 Template_Neff=9.000
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+++|||+||.+
T Consensus 98 FtlaHELgH~l 108 (301)
T 3DTE_A 98 FTLAHEISHAL 108 (301)
T ss_dssp HHHHHHHHHHH
T ss_pred HHHHHHHHHHH
No 123
>5JVI_E Thermolysin; HYDROLASE, METALLOPROTEASE, HYDROLASE INHIBITOR COMPLEX; HET: 6QC, DMS, GOL; 1.12A {Bacillus thermoproteolyticus} SCOP: d.92.1.2
Probab=59.66 E-value=5.5 Score=34.94 Aligned_cols=10 Identities=40% Similarity=0.707 Sum_probs=0.0 Template_Neff=9.600
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 139 Vi~HE~~Hgv 148 (316)
T 5JVI_E 139 VVAHELTHAV 148 (316)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 124
>3KWV_C Lethal factor; Bacillus anthracis, protective antigen, lethal factor, lethal toxin, octamer, protein transport, toxin, protein unfolding, protein translocation; 3.101A {Bacillus anthracis}
Probab=58.96 E-value=5.6 Score=34.82 Aligned_cols=10 Identities=50% Similarity=0.733 Sum_probs=0.0 Template_Neff=7.400
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||++
T Consensus 146 ~vlHE~GHai 155 (263)
T 3KWV_C 146 NVYYEIGKIL 155 (263)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 125
>PF04298.16 ; Zn_peptidase_2 ; Putative neutral zinc metallopeptidase
Probab=58.18 E-value=5.8 Score=33.26 Aligned_cols=10 Identities=50% Similarity=0.893 Sum_probs=0.0 Template_Neff=8.400
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++|||+||.+
T Consensus 89 ~aAHE~GHal 98 (215)
T K0AZJ2_GOTA9/1 89 VAAHEVGHAI 98 (215)
T ss_pred HHHHHHHHHH
No 126
>6QIG_A A disintegrin and metalloproteinase with thrombospondin motifs 13; Metalloproteinase, BLOOD CLOTTING; HET: FUC, NAG, GOL, MAN, BMA, PEG; 2.8A {Rattus norvegicus}
Probab=57.75 E-value=6.6 Score=36.90 Aligned_cols=13 Identities=38% Similarity=0.902 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
++|||+||.+| +.
T Consensus 143 ~~aheigh~lG-~~ 155 (604)
T 6QIG_A 143 TIAHQIGHSFG-LE 155 (604)
T ss_dssp HHHHHHHHHHT-CC
T ss_pred HHHHHHHHhCC-CC
No 127
>1G9K_A SERRALYSIN; beta jelly roll, HYDROLASE; 1.96A {Pseudomonas} SCOP: d.92.1.6, b.80.7.1
Probab=57.43 E-value=7 Score=35.30 Aligned_cols=15 Identities=40% Similarity=0.798 Sum_probs=0.0 Template_Neff=11.200
Q ss_pred ecChhhHhhhcCCCcc
Q FD01846349_043 131 NVPHEIGHMIGYHDDE 146 (190)
Q Consensus 131 ~~aHEfGHmlG~l~DE 146 (190)
++.||+||.+| |..+
T Consensus 166 ~~~he~Gh~lG-l~h~ 180 (463)
T 1G9K_A 166 TLTHEIGHTLG-LSHP 180 (463)
T ss_dssp HHHHHHHHHHT-CCCS
T ss_pred HHHHHHHHHhh-cCCC
No 128
>PF06167.16 ; Peptidase_M90 ; Glucose-regulated metallo-peptidase M90
Probab=56.58 E-value=15 Score=31.05 Aligned_cols=33 Identities=15% Similarity=0.122 Sum_probs=0.0 Template_Neff=9.200
Q ss_pred CcEEEechhHhhceeecCCccccCCcceeecChhhHhhh
Q FD01846349_043 102 SRILHIDSEDVVAVRKCLDPAQTVCSNQINVPHEIGHMI 140 (190)
Q Consensus 102 ~~~v~l~~~D~~~~~~~~~~~~~~~~~q~~~aHEfGHml 140 (190)
.|.|.|.-.++...... ......++.|||+|.+
T Consensus 123 ~g~i~ls~~~~~~~~~~------~~~~~nv~lHE~aH~l 155 (241)
T Q2ND92_ERYLH/2 123 RGPVVLSWDDALQGGLD------ATDGHNVVIHEFAHQL 155 (241)
T ss_pred CccEEEeHHHHHhcCCC------CCCCccchHHHHHHHH
No 129
>8CR4_A Pro-elastase; LasB, Pseudomonas aeruginosa, recombinant, HYDROLASE; 0.91A {Pseudomonas aeruginosa}
Probab=56.56 E-value=6.5 Score=36.46 Aligned_cols=10 Identities=30% Similarity=0.494 Sum_probs=0.0 Template_Neff=10.600
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 335 Vv~HE~gH~v 344 (514)
T 8CR4_A 335 VAAHEVSHGF 344 (514)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 130
>4QHJ_A Uncharacterized protein MJ1213; Minigluzincin, Proteolytic enzyme, HYDROLASE; HET: ACT; 1.75A {Methanocaldococcus jannaschii}
Probab=56.01 E-value=5.3 Score=29.09 Aligned_cols=12 Identities=25% Similarity=0.459 Sum_probs=0.0 Template_Neff=9.700
Q ss_pred eeecChhhHhhh
Q FD01846349_043 129 QINVPHEIGHMI 140 (190)
Q Consensus 129 q~~~aHEfGHml 140 (190)
+.+++||++|..
T Consensus 64 ~~vl~HEl~H~~ 75 (110)
T 4QHJ_A 64 RFILAHELLHLK 75 (110)
T ss_dssp HHHHHHHHHHHH
T ss_pred HHHHHHHHHHHH
No 131
>3EDH_A Bone morphogenetic protein 1; vicinal disulfide, Alternative splicing, Calcium, Chondrogenesis, Cleavage on pair of basic residues, Cytokine, Developmental protein, Differentiation; HET: DMS; 1.25A {Homo sapiens} SCOP: d.92.1.0
Probab=52.20 E-value=10 Score=28.70 Aligned_cols=15 Identities=47% Similarity=0.764 Sum_probs=0.0 Template_Neff=12.700
Q ss_pred cChhhHhhhcCCCccc
Q FD01846349_043 132 VPHEIGHMIGYHDDEY 147 (190)
Q Consensus 132 ~aHEfGHmlG~l~DEY 147 (190)
+.||+||.+| +..++
T Consensus 91 ~~~~~g~~lg-~~~~~ 105 (201)
T 3EDH_A 91 VVHELGHVVG-FWHEH 105 (201)
T ss_dssp HHHHHHHHHT-BCCGG
T ss_pred HHHHHHHHHc-ccchh
No 132
>PF13398.10 ; Peptidase_M50B ; Peptidase M50B-like
Probab=51.89 E-value=8.5 Score=31.63 Aligned_cols=10 Identities=40% Similarity=0.800 Sum_probs=0.0 Template_Neff=9.300
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+..||+||.+
T Consensus 25 ~~~HE~gH~l 34 (205)
T C7QD62_CATAD/3 25 TIAHEGGHAV 34 (205)
T ss_pred HHHHHHHHHH
No 133
>2VQX_A METALLOPROTEINASE; THERMOLYSIN-LIKE STRUCTURE, ZINC, PROTEASE, HYDROLASE, METALLOPROTEASE; 1.821A {SERRATIA PROTEAMACULANS}
Probab=51.53 E-value=9 Score=34.41 Aligned_cols=10 Identities=30% Similarity=0.484 Sum_probs=0.0 Template_Neff=8.800
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 159 ViaHE~~Hgv 168 (341)
T 2VQX_A 159 VVGHALAHGV 168 (341)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 134
>4DV8_A Lethal factor; endopeptidase, Zinc dependent, HYDROLASE; HET: 0LX; 1.632A {Bacillus anthracis} SCOP: d.166.1.1, d.92.1.14
Probab=50.05 E-value=9.8 Score=36.21 Aligned_cols=10 Identities=40% Similarity=0.783 Sum_probs=0.0 Template_Neff=9.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||++
T Consensus 433 ~~lHE~gHav 442 (526)
T 4DV8_A 433 GFIHEFGHAV 442 (526)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 135
>5A3Y_A THERMOLYSIN; HYDROLASE, MULTI CRYSTAL DATA COLLECTION, SYNCHROTRON SERIAL CRYSTALLOGRAPHY, SSX, SAD; HET: LYS, TMO; 1.27A {BACILLUS THERMOPROTEOLYTICUS}
Probab=49.58 E-value=10 Score=35.33 Aligned_cols=10 Identities=40% Similarity=0.707 Sum_probs=0.0 Template_Neff=10.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+||.+
T Consensus 371 Vi~HE~gH~i 380 (548)
T 5A3Y_A 371 VVAHELTHAV 380 (548)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 136
>3SKS_A Putative Oligoendopeptidase F; Structural Genomics, Center for Structural Genomics of Infectious Diseases, CSGID, oligoendopeptidase, protease, HYDROLASE; HET: PO4; 2.05A {Bacillus anthracis}
Probab=48.76 E-value=10 Score=35.16 Aligned_cols=10 Identities=40% Similarity=0.713 Sum_probs=0.0 Template_Neff=11.400
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 356 ~l~HE~GHa~ 365 (567)
T 3SKS_A 356 VLTHEAGHAF 365 (567)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 137
>6H5W_A Angiotensin-converting enzyme; Angiotensin-1 converting enzyme, ACE inhibitor, Omapatrilat, Vasopeptidase inhibitor, HYDROLASE; HET: FUC, FT8, NAG, P6G, CSO, EDO, BMA, IMD, BO3; 1.37A {Homo sapiens} SCOP: d.92.1.5
Probab=47.54 E-value=11 Score=35.41 Aligned_cols=10 Identities=40% Similarity=0.737 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 344 tl~HE~GHa~ 353 (591)
T 6H5W_A 344 VAHHEMGHIQ 353 (591)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 138
>PF02128.19 ; Peptidase_M36 ; Fungalysin metallopeptidase (M36)
Probab=46.22 E-value=13 Score=33.35 Aligned_cols=10 Identities=40% Similarity=0.371 Sum_probs=0.0 Template_Neff=9.800
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 180 Vv~HE~~Hgv 189 (371)
T G9NXA4_HYPAI/2 180 IVIHEYTHGL 189 (371)
T ss_pred eEeEehHhhh
No 139
>3CQB_B Probable protease htpX homolog; Heat shock protein HtpX domain, PSI-2, Protein Structure Initiative, Structural Genomics, Midwest Center for Structural Genomics; HET: EDO, MSE; 1.86A {Vibrio parahaemolyticus RIMD 2210633}
Probab=46.00 E-value=13 Score=26.23 Aligned_cols=13 Identities=31% Similarity=0.626 Sum_probs=0.0 Template_Neff=10.700
Q ss_pred ecChhhHhhhcCCC
Q FD01846349_043 131 NVPHEIGHMIGYHD 144 (190)
Q Consensus 131 ~~aHEfGHmlG~l~ 144 (190)
.++||++|... .+
T Consensus 86 vl~HEl~H~~~-~~ 98 (107)
T 3CQB_B 86 VLAHEVSHIAN-GD 98 (107)
T ss_dssp HHHHHHHHHHT-TC
T ss_pred HHHHHHHHHHc-CC
No 140
>PF20573.2 ; DUF6782 ; Putative metallopeptidase family (DUF6782)
Probab=45.84 E-value=12 Score=30.57 Aligned_cols=10 Identities=30% Similarity=0.438 Sum_probs=0.0 Template_Neff=10.800
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+||.+
T Consensus 87 ~laHEl~H~~ 96 (234)
T A0A4S3MQF4_9RH 87 ILLHELRHLD 96 (234)
T ss_pred HHHHHHHHHH
No 141
>8A28_B Metalloendopeptidase; metallopeptidase zymogen, HYDROLASE; HET: GOL, PGE; 2.4A {Limulus polyphemus}
Probab=45.69 E-value=15 Score=31.48 Aligned_cols=14 Identities=43% Similarity=0.731 Sum_probs=0.0 Template_Neff=12.300
Q ss_pred cChhhHhhhcCCCcc
Q FD01846349_043 132 VPHEIGHMIGYHDDE 146 (190)
Q Consensus 132 ~aHEfGHmlG~l~DE 146 (190)
+.||+||+|| +..|
T Consensus 116 ~~~~~~~~lg-~~~~ 129 (382)
T 8A28_B 116 VVHALGHAVG-FWHE 129 (382)
T ss_dssp HHHHHHHHTT-CCCG
T ss_pred HHHHHHHHhC-Ccch
No 142
>PF01435.22 ; Peptidase_M48 ; Peptidase family M48
Probab=45.17 E-value=14 Score=28.50 Aligned_cols=8 Identities=50% Similarity=1.012 Sum_probs=0.0 Template_Neff=11.900
Q ss_pred cChhhHhh
Q FD01846349_043 132 VPHEIGHM 139 (190)
Q Consensus 132 ~aHEfGHm 139 (190)
+|||+||+
T Consensus 65 laHEl~H~ 72 (198)
T O53978_MYCTU/6 65 MGHELGHA 72 (198)
T ss_pred HHHHHHHH
No 143
>6S1Y_A Angiotensin-converting enzyme; metalloprotease, mosquito control, insecticide design, HYDROLASE; HET: PEG, BMA, KSN, NAG, EDO; 2.2A {Anopheles gambiae} SCOP: d.92.1.5
Probab=44.65 E-value=13 Score=35.45 Aligned_cols=10 Identities=50% Similarity=0.856 Sum_probs=0.0 Template_Neff=10.600
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 354 tl~HE~GHal 363 (621)
T 6S1Y_A 354 VVHHELGHIQ 363 (621)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 144
>5GIV_E Carboxypeptidase 1; M32 carboxypeptidase, Cobalt, Metallopeptidase, HYDROLASE; 2.4A {Deinococcus radiodurans str. R1} SCOP: d.92.1.0
Probab=44.46 E-value=13 Score=34.22 Aligned_cols=10 Identities=40% Similarity=0.737 Sum_probs=0.0 Template_Neff=10.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||.+
T Consensus 263 ~l~HE~GHa~ 272 (503)
T 5GIV_E 263 STLHEAGHAL 272 (503)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 145
>3CE2_A Putative peptidase; structural genomics, UNKNOWN FUNCTION, putative peptidase, PSI-2, Protein Structure Initiative, New York SGX Research Center for; 2.6A {Chlamydophila abortus}
Probab=44.15 E-value=13 Score=35.23 Aligned_cols=10 Identities=40% Similarity=0.667 Sum_probs=0.0 Template_Neff=10.800
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+||.+
T Consensus 399 ~l~HE~GHa~ 408 (618)
T 3CE2_A 399 VIAHEGGHSM 408 (618)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 146
>2QR4_B Peptidase M3B, oligoendopeptidase F; structural genomics, oligoendopeptidase F, PSI-2, Protein Structure Initiative, New York SGX Research Center for Structural Genomics; HET: MSE; 2.5A {Enterococcus faecium}
Probab=44.14 E-value=13 Score=34.85 Aligned_cols=10 Identities=40% Similarity=0.896 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 366 ~l~HE~GHa~ 375 (587)
T 2QR4_B 366 TLVHEMGHSV 375 (587)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 147
>PF19093.4 ; DUF5781 ; Family of unknown function (DUF5781)
Probab=43.24 E-value=14 Score=32.48 Aligned_cols=9 Identities=44% Similarity=0.667 Sum_probs=0.0 Template_Neff=4.500
Q ss_pred ecChhhHhh
Q FD01846349_043 131 NVPHEIGHM 139 (190)
Q Consensus 131 ~~aHEfGHm 139 (190)
+++||+.||
T Consensus 69 lllHEM~Hm 77 (246)
T V4XWU0_9ARCH/1 69 LALHELAHM 77 (246)
T ss_pred HHHHHHHHH
No 148
>7QP3_A Extracellular metalloproteinase; Keratinase, Protease, Metalloprotein, RECOMBINATION; HET: A2G, EPE; 1.85A {Pseudogymnoascus pannorum}
Probab=42.82 E-value=12 Score=34.09 Aligned_cols=10 Identities=30% Similarity=0.391 Sum_probs=0.0 Template_Neff=9.300
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 181 Vv~HE~~Hgv 190 (391)
T 7QP3_A 181 VIIHEYTHGV 190 (391)
T ss_dssp HHHHHHHHHH
T ss_pred eEEEccceeh
No 149
>3HQ2_B Bacillus subtilis M32 carboxypeptidase; Hydrolase, Metal-binding, Metalloprotease, Protease, Zinc; HET: PO4; 2.9A {Bacillus subtilis} SCOP: d.92.1.0
Probab=42.68 E-value=15 Score=33.78 Aligned_cols=10 Identities=50% Similarity=0.740 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||.+
T Consensus 262 ~l~HE~GHa~ 271 (501)
T 3HQ2_B 262 GTIHECGHAI 271 (501)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 150
>3AHN_A Oligopeptidase; HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex; HET: 3A1, ACT; 1.8A {Geobacillus sp. MO-1}
Probab=42.39 E-value=15 Score=34.05 Aligned_cols=10 Identities=40% Similarity=0.713 Sum_probs=0.0 Template_Neff=11.500
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 353 ~l~HE~GHa~ 362 (564)
T 3AHN_A 353 VLTHEAGHAF 362 (564)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 151
>4CA7_A ANGIOTENSIN-CONVERTING ENZYME; HYDROLASE, ZINC METALLOPEPTIDASE, INHIBITOR BINDING; HET: BMA, MAN, NAG, 3EF; 1.82A {DROSOPHILA MELANOGASTER} SCOP: d.92.1.5
Probab=42.26 E-value=15 Score=34.58 Aligned_cols=10 Identities=50% Similarity=0.946 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||.+
T Consensus 348 ~l~HE~GHal 357 (598)
T 4CA7_A 348 TVHHELGHIQ 357 (598)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 152
>PF20344.2 ; DUF6639 ; Family of unknown function (DUF6639)
Probab=42.26 E-value=15 Score=31.08 Aligned_cols=10 Identities=50% Similarity=0.763 Sum_probs=0.0 Template_Neff=8.800
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||++|.+
T Consensus 129 vlaHEl~Hal 138 (231)
T A0A011M873_9PR 129 LVAHEIAHAL 138 (231)
T ss_pred HHHHHHHHHH
No 153
>PF02074.19 ; Peptidase_M32 ; Carboxypeptidase Taq (M32) metallopeptidase
Probab=41.14 E-value=16 Score=33.67 Aligned_cols=10 Identities=50% Similarity=0.617 Sum_probs=0.0 Template_Neff=10.800
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||.+
T Consensus 254 ~l~HE~GHal 263 (495)
T A0A095XNW5_9HY 254 AVWHEAGHGM 263 (495)
T ss_pred HHHHHHHHHH
No 154
>PF19527.3 ; DUF6055 ; Family of unknown function (DUF6055)
Probab=41.12 E-value=20 Score=32.60 Aligned_cols=12 Identities=42% Similarity=0.747 Sum_probs=0.0 Template_Neff=10.500
Q ss_pred eeecChhhHhhh
Q FD01846349_043 129 QINVPHEIGHMI 140 (190)
Q Consensus 129 q~~~aHEfGHml 140 (190)
..+++|||.|++
T Consensus 134 ~~~l~HE~~H~i 145 (431)
T A0A1I7IU67_9FL 134 GSTIAHEIGHSF 145 (431)
T ss_pred CcchHHHHHHhe
No 155
>7W6Y_A Anti sigma-E protein, RseA; Intramembrane protease, HYDROLASE; HET: MSE, BAT; 3.1A {Kangiella koreensis DSM 16069}
Probab=40.86 E-value=18 Score=33.00 Aligned_cols=9 Identities=44% Similarity=0.542 Sum_probs=0.0 Template_Neff=10.600
Q ss_pred cChhhHhhh
Q FD01846349_043 132 VPHEIGHMI 140 (190)
Q Consensus 132 ~aHEfGHml 140 (190)
++||+||.+
T Consensus 20 ~vHE~gH~~ 28 (456)
T 7W6Y_A 20 TFHEWGHYW 28 (456)
T ss_dssp HHHHHHHHH
T ss_pred HHHHHHHHH
No 156
>7Z6T_AAA Extracellular metalloproteinase mep; Keratinase, Protease, Metalloprotein, RECOMBINATION, PEPTIDE BINDING PROTEIN; HET: SO4, NAG, DNO, MAN, EDO, BMA; 1.51A {Aspergillus clavatus}
Probab=40.80 E-value=13 Score=33.73 Aligned_cols=10 Identities=40% Similarity=0.381 Sum_probs=0.0 Template_Neff=9.500
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+||.+
T Consensus 181 Vv~HE~~Hgv 190 (388)
T 7Z6T_AAA 181 IVIHEYTHGV 190 (388)
T ss_pred EEEEecceeh
No 157
>5IQJ_B Uncharacterized protein; Unknown Function, CSGID, Vibrio cholerae, Structural Genomics, Center for Structural Genomics of Infectious Diseases; HET: SO4, TTN, PGE; 1.9A {Vibrio cholerae O1 biovar El Tor}
Probab=40.29 E-value=17 Score=27.41 Aligned_cols=10 Identities=30% Similarity=0.478 Sum_probs=0.0 Template_Neff=9.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.||.||.+
T Consensus 10 ~a~HEaGHav 19 (134)
T 5IQJ_B 10 AALHESAHTV 19 (134)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 158
>7A03_A M32 carboxypeptidase; Carboxypeptidase, Metalloenzyme, HYDROLASE; HET: GOL; 1.39A {Chitinophagaceae bacterium} SCOP: d.92.1.0
Probab=40.09 E-value=17 Score=33.36 Aligned_cols=10 Identities=40% Similarity=0.604 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.||+||.+
T Consensus 264 ~l~HE~GHal 273 (500)
T 7A03_A 264 SCIHEGGHAL 273 (500)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 159
>PF01432.24 ; Peptidase_M3 ; Peptidase family M3
Probab=39.57 E-value=17 Score=32.50 Aligned_cols=10 Identities=40% Similarity=0.796 Sum_probs=0.0 Template_Neff=11.500
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||++
T Consensus 239 ~l~hE~Ghal 248 (451)
T DCP_ECOLI/229- 239 TLFHEFGHTL 248 (451)
T ss_pred HHHHHHHHHH
No 160
>7W6X_A Regulator of sigma-E protease RseP; Intramembrane protease, HYDROLASE; HET: FME, BAT; 3.2A {Escherichia coli}
Probab=39.41 E-value=20 Score=32.91 Aligned_cols=9 Identities=44% Similarity=0.785 Sum_probs=0.0 Template_Neff=10.400
Q ss_pred cChhhHhhh
Q FD01846349_043 132 VPHEIGHMI 140 (190)
Q Consensus 132 ~aHEfGHml 140 (190)
+.||+||.+
T Consensus 20 ~vHE~GH~~ 28 (458)
T 7W6X_A 20 TVHEFGHFW 28 (458)
T ss_dssp HHHHHHHHH
T ss_pred HHHHHHHHH
No 161
>PF01401.22 ; Peptidase_M2 ; Angiotensin-converting enzyme
Probab=39.29 E-value=18 Score=33.95 Aligned_cols=10 Identities=50% Similarity=0.856 Sum_probs=0.0 Template_Neff=11.200
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||.+
T Consensus 345 ~l~HElGHa~ 354 (587)
T B4GKQ4_DROPE/3 345 VVHHELGHIQ 354 (587)
T ss_pred HHHHHHHHHH
No 162
>8BYJ_A Processed angiotensin-converting enzyme 2; Cov-2-sars bind proteins, MEMBRANE PROTEIN; HET: LFI; 2.07A {Homo sapiens}
Probab=38.54 E-value=18 Score=34.39 Aligned_cols=10 Identities=40% Similarity=0.826 Sum_probs=0.0 Template_Neff=10.600
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 354 tl~HE~GHa~ 363 (609)
T 8BYJ_A 354 TAHHEMGHIQ 363 (609)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 163
>5AMB_B ANGIOTENSIN-CONVERTING ENZYME; HYDROLASE, ANGIOTENSIN-CONVERTING ENZYME, METALLOPROTEASE, AMYLOID-BETA; HET: NAG, FUC, PEG, P6G, PG4, BMA; 1.55A {HOMO SAPIENS}
Probab=38.54 E-value=18 Score=34.35 Aligned_cols=10 Identities=50% Similarity=0.936 Sum_probs=0.0 Template_Neff=10.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||++
T Consensus 358 ~l~HE~GHa~ 367 (629)
T 5AMB_B 358 TVHHEMGHIQ 367 (629)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 164
>PF10460.13 ; Peptidase_M30 ; Peptidase M30
Probab=38.42 E-value=19 Score=31.63 Aligned_cols=10 Identities=40% Similarity=0.504 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||.|++
T Consensus 144 tlaHE~~H~i 153 (371)
T B2JNA9_PARP8/2 144 TMAHESMHMQ 153 (371)
T ss_pred HHHHHHHHHH
No 165
>7Q3Y_A Angiotensin-converting enzyme; Zinc metalloprotease Dicarboxypeptidase Glycoprotein, HYDROLASE; HET: BMA, MAN, FUC, NAG;{Homo sapiens}
Probab=38.37 E-value=19 Score=37.37 Aligned_cols=10 Identities=50% Similarity=0.936 Sum_probs=0.0 Template_Neff=10.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 358 ~l~HE~GHal 367 (1211)
T 7Q3Y_A 358 TVHHEMGHIQ 367 (1211)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 166
>6D2S_A HTH-type transcriptional regulator PrpR; Transcriptional regulator, TRANSCRIPTION; HET: EDO; 1.819A {Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)}
Probab=38.25 E-value=17 Score=31.44 Aligned_cols=11 Identities=0% Similarity=0.154 Sum_probs=0.0 Template_Neff=9.800
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+++|||+||.+
T Consensus 89 F~laHElgh~~ 99 (289)
T 6D2S_A 89 FQIATQLALVG 99 (289)
T ss_dssp HHHHHHHHHHH
T ss_pred HHHHHHHHHHh
No 167
>5KDS_A F5/8 type C domain protein; O-glycopeptidase, PF13402/M60-like, Bovine submaxillary mucin, O-glycan, HYDROLASE; HET: NAG, EPE, TLA, A2G, SIA, EDO; 1.6A {Bos taurus}
Probab=38.16 E-value=19 Score=34.20 Aligned_cols=11 Identities=45% Similarity=0.791 Sum_probs=0.0 Template_Neff=9.500
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+.++||+||..
T Consensus 279 WG~~HE~GH~~ 289 (530)
T 5KDS_A 279 WGVAHELGHNF 289 (530)
T ss_pred hHHHHHHHHHh
No 168
>1KA2_A M32 carboxypeptidase; HEXXH motif, M32 family, metallopeptidase, carboxypeptidase; 2.2A {Pyrococcus furiosus} SCOP: d.92.1.5
Probab=38.09 E-value=19 Score=33.10 Aligned_cols=10 Identities=40% Similarity=0.813 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||.+
T Consensus 266 ~l~HE~GHal 275 (499)
T 1KA2_A 266 STVHEFGHAL 275 (499)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 169
>PF20352.2 ; DUF6647 ; Family of unknown function (DUF6647)
Probab=37.00 E-value=20 Score=29.27 Aligned_cols=10 Identities=30% Similarity=0.291 Sum_probs=0.0 Template_Neff=7.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+.|.+
T Consensus 113 vLaHElvHal 122 (175)
T A0A0T5NWM3_9RH 113 VLLHELVHHR 122 (175)
T ss_pred HHHHHHHHHH
No 170
>5KDJ_B F5/8 type C domain protein; O-glycopeptidase, PF13402/M60-like, HYDROLASE; HET: GOL; 2.15A {Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)}
Probab=36.89 E-value=21 Score=34.72 Aligned_cols=11 Identities=45% Similarity=0.791 Sum_probs=0.0 Template_Neff=10.200
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+.++||+||+.
T Consensus 342 Wg~~HE~GH~~ 352 (674)
T 5KDJ_B 342 WGVAHELGHNF 352 (674)
T ss_dssp HHHHHHHHHHH
T ss_pred hhHHHHHHHhh
No 171
>4KA7_A Oligopeptidase A; Protease, Mitochondria, chloroplast, HYDROLASE-HYDROLASE SUBSTRATE complex; HET: GOL; 1.8A {Arabidopsis thaliana}
Probab=36.09 E-value=21 Score=34.48 Aligned_cols=10 Identities=40% Similarity=0.783 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 491 ~l~HE~GHal 500 (714)
T 4KA7_A 491 TVFHQFGHAL 500 (714)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 172
>5KD5_A Metallopeptidase; O-glycopeptidase, PF13402/M60-like, Hydrolase; HET: EDO; 1.65A {Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)}
Probab=35.86 E-value=23 Score=34.03 Aligned_cols=15 Identities=40% Similarity=0.530 Sum_probs=0.0 Template_Neff=9.100
Q ss_pred CcceeecChhhHhhh
Q FD01846349_043 126 CSNQINVPHEIGHMI 140 (190)
Q Consensus 126 ~~~q~~~aHEfGHml 140 (190)
....+.++||+||..
T Consensus 268 ~~~~WG~~HEiGH~~ 282 (559)
T 5KD5_A 268 EDNAWGPAHEIGHVH 282 (559)
T ss_dssp HHHHHHHHHHHHHHH
T ss_pred CCCCcHHHHHHHhhc
No 173
>PF07607.15 ; DUF1570 ; Protein of unknown function (DUF1570)
Probab=35.78 E-value=21 Score=25.03 Aligned_cols=13 Identities=31% Similarity=0.302 Sum_probs=0.0 Template_Neff=12.400
Q ss_pred ceeecChhhHhhh
Q FD01846349_043 128 NQINVPHEIGHMI 140 (190)
Q Consensus 128 ~q~~~aHEfGHml 140 (190)
...+++||+.|.+
T Consensus 1 ~~~~~~hE~~H~~ 13 (132)
T Q7UU86_RHOBA/2 1 IAATVRHEAAHQS 13 (132)
T ss_pred CchHHHHHHHHHH
No 174
>6EOM_A MutT/NUDIX family protein; Caldithrix abyssi, Metallopeptidase, Dipeptidyl peptidase III, DPP III, Zinc-Hydrolase, HYDROLASE; HET: LYS; 2.103A {Caldithrix abyssi DSM 13497}
Probab=34.98 E-value=20 Score=34.59 Aligned_cols=12 Identities=42% Similarity=0.656 Sum_probs=0.0 Template_Neff=8.900
Q ss_pred eecChhhHhhhc
Q FD01846349_043 130 INVPHEIGHMIG 141 (190)
Q Consensus 130 ~~~aHEfGHmlG 141 (190)
.++.||+||.+|
T Consensus 375 ~v~~HElgH~~g 386 (566)
T 6EOM_A 375 HTLMHEISHGLG 386 (566)
T ss_dssp HHHHHHHHHTSS
T ss_pred HHHHHHHHhhcC
No 175
>3C37_B Peptidase, M48 family; Q74D82, GsR143A, Peptidase, M48 family, Structural Genomics, PSI-2, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG; HET: PEG, MSE; 1.7A {Geobacter sulfurreducens PCA}
Probab=34.79 E-value=23 Score=29.60 Aligned_cols=10 Identities=40% Similarity=0.743 Sum_probs=0.0 Template_Neff=10.400
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++|||+||..
T Consensus 103 vLAHEl~H~~ 112 (253)
T 3C37_B 103 VLAHEINHAV 112 (253)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 176
>2O3E_A Neurolysin; thermolysin-like domain, substrate-binding channel, HYDROLASE; 2.2A {Rattus norvegicus} SCOP: d.92.1.5
Probab=34.77 E-value=23 Score=34.01 Aligned_cols=10 Identities=40% Similarity=0.763 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 471 ~l~HE~Ghal 480 (678)
T 2O3E_A 471 TYFHEFGHVM 480 (678)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 177
>PF02163.26 ; Peptidase_M50 ; Peptidase family M50
Probab=34.68 E-value=26 Score=32.43 Aligned_cols=9 Identities=44% Similarity=0.892 Sum_probs=0.0 Template_Neff=8.500
Q ss_pred cChhhHhhh
Q FD01846349_043 132 VPHEIGHMI 140 (190)
Q Consensus 132 ~aHEfGHml 140 (190)
+.|||||.+
T Consensus 11 ~~he~~h~~ 19 (403)
T EEP_ENTFA/6-40 11 LVHEFGHFY 19 (403)
T ss_pred HHHHHHHHH
No 178
>3HOA_B Thermostable carboxypeptidase 1; proline-rich loop, Carboxypeptidase, Hydrolase; 2.1A {Thermus thermophilus HB27} SCOP: d.92.1.0
Probab=34.52 E-value=23 Score=33.02 Aligned_cols=10 Identities=40% Similarity=0.830 Sum_probs=0.0 Template_Neff=10.300
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.||+||.+
T Consensus 273 ~l~HE~GHal 282 (509)
T 3HOA_B 273 GTLHEMGHAL 282 (509)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 179
>1J7N_B Lethal Factor precursor; Anthrax, Lethal Toxin, Lethal Factor, Zinc Metalloprotease, MAPKK, MEK, TOXIN; HET: SO4; 2.3A {Bacillus anthracis} SCOP: d.166.1.1, d.92.1.14
Probab=34.20 E-value=24 Score=35.95 Aligned_cols=10 Identities=40% Similarity=0.783 Sum_probs=0.0 Template_Neff=7.200
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||++
T Consensus 683 ~llHEfgHai 692 (776)
T 1J7N_B 683 GFIHEFGHAV 692 (776)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 180
>4IL3_A Ste24p; membrane protein, alpha helical, CaaX Protease, a-factor, structural genomics, MPSBC, PSI-Biology, Membrane Protein Structural Biology Consortium; 3.102A {Saccharomyces mikatae}
Probab=33.87 E-value=24 Score=32.36 Aligned_cols=9 Identities=56% Similarity=0.929 Sum_probs=0.0 Template_Neff=10.500
Q ss_pred ecChhhHhh
Q FD01846349_043 131 NVPHEIGHM 139 (190)
Q Consensus 131 ~~aHEfGHm 139 (190)
.+|||+||.
T Consensus 294 vlaHElgH~ 302 (461)
T 4IL3_A 294 VLAHEIGHW 302 (461)
T ss_dssp HHHHHHHHH
T ss_pred HHHHHHHHH
No 181
>6SGO_A Secreted protein; Structure from MOLMOL, UNKNOWN FUNCTION; NMR {Melampsora larici-populina}
Probab=33.54 E-value=48 Score=25.76 Aligned_cols=16 Identities=38% Similarity=0.800 Sum_probs=0.0 Template_Neff=1.000
Q ss_pred hhhHhhhcCCCcc--cccC
Q FD01846349_043 134 HEIGHMIGYHDDE--YALD 150 (190)
Q Consensus 134 HEfGHmlG~l~DE--Y~~g 150 (190)
||+.|.+| -.|. |..|
T Consensus 43 helahflg-phdpeiyvng 60 (157)
T 6SGO_A 43 HELAHFLG-PHDPEIYVNG 60 (157)
T ss_dssp HHHHHHSS-TTCCEEEETT
T ss_pred HHHHHHhC-CCCcceEEcC
No 182
>3DWC_C Metallocarboxypeptidase; metallocarboxypeptidase, cowrin family of metallocarboxypeptidases, Carboxypeptidase, Hydrolase; HET: SO4, GOL, CSX; 2.1A {Trypanosoma cruzi}
Probab=33.49 E-value=21 Score=32.93 Aligned_cols=10 Identities=50% Similarity=0.667 Sum_probs=0.0 Template_Neff=10.800
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.||+||.+
T Consensus 264 tl~HE~GHal 273 (505)
T 3DWC_C 264 GVIHETGHAK 273 (505)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHcHhh
No 183
>PF19985.3 ; DUF6421 ; Family of unknown function (DUF6421)
Probab=33.47 E-value=19 Score=33.78 Aligned_cols=12 Identities=33% Similarity=0.614 Sum_probs=0.0 Template_Neff=8.400
Q ss_pred eecChhhHhhhc
Q FD01846349_043 130 INVPHEIGHMIG 141 (190)
Q Consensus 130 ~~~aHEfGHmlG 141 (190)
+++.||+||.+|
T Consensus 222 ~~~lHE~~H~~G 233 (446)
T A0A0Q4UJ45_9MI 222 WDIIHDRSHMRG 233 (446)
T ss_pred HHHHHhcccccC
No 184
>7BB8_B Neutral metalloprotease; Protease, Virulence factor, peptidase, HYDROLASE; HET: CAC; 1.506A {Staphylococcus lugdunensis}
Probab=32.96 E-value=26 Score=31.78 Aligned_cols=10 Identities=40% Similarity=0.796 Sum_probs=0.0 Template_Neff=10.200
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||-|++
T Consensus 211 tlaHE~~H~i 220 (410)
T 7BB8_B 211 TLAHEYQHMV 220 (410)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 185
>5SYT_A CAAX prenyl protease 1 homolog; Hydrolase, Membrane Protein, CaaX protease, zinc metalloprotease, STE24, isoprenylation, Structural Genomics, PSI-2, Protein Structure Initiative, Membrane; HET: PC1, SO4, C8E, DMS, CXE, GOL, PEG; 2.0A {Homo sapiens}
Probab=32.82 E-value=27 Score=32.79 Aligned_cols=9 Identities=44% Similarity=0.815 Sum_probs=0.0 Template_Neff=9.300
Q ss_pred ecChhhHhh
Q FD01846349_043 131 NVPHEIGHM 139 (190)
Q Consensus 131 ~~aHEfGHm 139 (190)
.+|||+||.
T Consensus 332 vlAHElgH~ 340 (480)
T 5SYT_A 332 VLGHELGHW 340 (480)
T ss_dssp HHHHHHHHH
T ss_pred HHHHHHHHH
No 186
>7Q3Y_A Angiotensin-converting enzyme; Zinc metalloprotease Dicarboxypeptidase Glycoprotein, HYDROLASE; HET: BMA, MAN, FUC, NAG;{Homo sapiens}
Probab=32.80 E-value=26 Score=36.38 Aligned_cols=10 Identities=40% Similarity=0.737 Sum_probs=0.0 Template_Neff=10.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 956 tl~HE~GHal 965 (1211)
T 7Q3Y_A 956 VAHHEMGHIQ 965 (1211)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 187
>PF13402.10 ; Peptidase_M60 ; Peptidase M60, enhancin and enhancin-like
Probab=32.77 E-value=27 Score=29.01 Aligned_cols=11 Identities=36% Similarity=0.537 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+.+.||+||..
T Consensus 133 w~~~HE~gH~~ 143 (262)
T Q815S7_BACCR/9 133 WGPWHEVGHLH 143 (262)
T ss_pred CchhHHhcccc
No 188
>1Y79_1 Peptidyl-Dipeptidase Dcp; hinge bending peptidyl dipeptidase carboxypeptidase Dcp neurolysin ACE, HYDROLASE; HET: TRP; 2.0A {Escherichia coli}
Probab=32.74 E-value=26 Score=33.62 Aligned_cols=10 Identities=40% Similarity=0.796 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 466 ~l~hE~GHa~ 475 (680)
T 1Y79_1 466 TLFHEFGHTL 475 (680)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 189
>5E3X_A Thermostable carboxypeptidase 1; Carboxypeptidase, Fervidobacterium, FisCP, HYDROLASE; 2.197A {Fervidobacterium islandicum} SCOP: d.92.1.0
Probab=32.66 E-value=26 Score=32.12 Aligned_cols=10 Identities=40% Similarity=0.787 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||.+
T Consensus 250 ~l~HE~GHa~ 259 (489)
T 5E3X_A 250 STIHEFGHAL 259 (489)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 190
>6CYY_B HTH-type transcriptional regulator PrpR; Transcription, regulator, DNA BINDING PROTEIN; HET: COA, SF4; 2.506A {Mycobacterium tuberculosis}
Probab=32.23 E-value=24 Score=32.64 Aligned_cols=11 Identities=0% Similarity=0.154 Sum_probs=0.0 Template_Neff=9.400
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+++|||+||.+
T Consensus 183 FtlaHELgH~~ 193 (429)
T 6CYY_B 183 FQIATQLALVG 193 (429)
T ss_dssp HHHHHHHHHHH
T ss_pred HHHHHHHHHHc
No 191
>1XFX_A Calmodulin-sensitive adenylate cyclase; protein-protein interaction, LYASE-METAL BINDING PROTEIN COMPLEX; HET: CA, MSE; 3.2A {Bacillus anthracis}
Probab=31.97 E-value=28 Score=35.58 Aligned_cols=10 Identities=50% Similarity=0.477 Sum_probs=0.0 Template_Neff=7.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.|||||++
T Consensus 145 ~vlHE~GHAi 154 (777)
T 1XFX_A 145 EVYYEIGKGI 154 (777)
T ss_dssp THHHHHHHHT
T ss_pred HHHHHHHHHH
No 192
>PF15887.9 ; Peptidase_Mx ; Putative zinc-binding metallo-peptidase
Probab=30.63 E-value=42 Score=29.36 Aligned_cols=7 Identities=71% Similarity=1.293 Sum_probs=0.0 Template_Neff=6.100
Q ss_pred hhhHhhh
Q FD01846349_043 134 HEIGHMI 140 (190)
Q Consensus 134 HEfGHml 140 (190)
|||||.+
T Consensus 87 HE~GH~~ 93 (236)
T A1WU06_HALHL/7 87 HEIAHML 93 (236)
T ss_pred HHHHHHH
No 193
>5ZUM_A dipeptidyl-peptidase III; metallopeptidase, HYDROLASE; HET: MSE; 1.9A {Corallococcus sp. EGB}
Probab=30.52 E-value=29 Score=33.24 Aligned_cols=11 Identities=36% Similarity=0.528 Sum_probs=0.0 Template_Neff=9.000
Q ss_pred ecChhhHhhhc
Q FD01846349_043 131 NVPHEIGHMIG 141 (190)
Q Consensus 131 ~~aHEfGHmlG 141 (190)
++.||+||.+|
T Consensus 354 v~~HElgH~~g 364 (537)
T 5ZUM_A 354 ILMHELMHGLG 364 (537)
T ss_dssp HHHHHHHHTSS
T ss_pred HHHHHHHhhcC
No 194
>PF05569.15 ; Peptidase_M56 ; BlaR1 peptidase M56
Probab=30.48 E-value=29 Score=29.32 Aligned_cols=9 Identities=33% Similarity=0.405 Sum_probs=0.0 Template_Neff=11.000
Q ss_pred ecChhhHhh
Q FD01846349_043 131 NVPHEIGHM 139 (190)
Q Consensus 131 ~~aHEfGHm 139 (190)
.++||+||.
T Consensus 191 il~HEl~Hi 199 (291)
T Q8YAA1_LISMO/6 191 IFKHELVHC 199 (291)
T ss_pred HHHHHHHHH
No 195
>PF18818.5 ; MPTase-PolyVal ; Zincin-like metallopeptidase
Probab=29.66 E-value=32 Score=24.50 Aligned_cols=11 Identities=27% Similarity=0.531 Sum_probs=0.0 Template_Neff=11.700
Q ss_pred ecChhhHhhhc
Q FD01846349_043 131 NVPHEIGHMIG 141 (190)
Q Consensus 131 ~~aHEfGHmlG 141 (190)
+++||++|..+
T Consensus 47 ~~~hel~h~~~ 57 (128)
T B8EPP9_METSB/1 47 TLAHEVTHWTK 57 (128)
T ss_pred HHHHHHHHhcC
No 196
>3KHI_A Putative Metal-dependent Hydrolase; A Putative Metal-dependent Hydrolase, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2; HET: MSE, EDO; 1.95A {Klebsiella pneumoniae subsp. pneumoniae MGH 78578}
Probab=29.54 E-value=37 Score=29.44 Aligned_cols=15 Identities=33% Similarity=0.377 Sum_probs=0.0 Template_Neff=8.700
Q ss_pred CcceeecChhhHhhh
Q FD01846349_043 126 CSNQINVPHEIGHMI 140 (190)
Q Consensus 126 ~~~q~~~aHEfGHml 140 (190)
.....++.|||+|.+
T Consensus 142 ~~~~nv~lHE~AHal 156 (267)
T 3KHI_A 142 ASGFNLVVHEVAHKL 156 (267)
T ss_dssp SSSCCHHHHHHHHHH
T ss_pred cCCCchHHHHHHHHH
No 197
>4FCA_A Conserved domain protein; structural genomics, The Center for Structural Genomics of Infectious Diseases, CSGID, NIAID, National Institute of Allergy; HET: MSE; 2.055A {Bacillus anthracis}
Probab=29.12 E-value=40 Score=32.25 Aligned_cols=13 Identities=31% Similarity=0.388 Sum_probs=0.0 Template_Neff=9.000
Q ss_pred ceeecChhhHhhh
Q FD01846349_043 128 NQINVPHEIGHMI 140 (190)
Q Consensus 128 ~q~~~aHEfGHml 140 (190)
.++.+.||+||..
T Consensus 246 ~~WG~~HEiGH~~ 258 (525)
T 4FCA_A 246 DGWGPWHEVGHQH 258 (525)
T ss_dssp HCHHHHHHHHHHH
T ss_pred CccchHHHHHHHh
No 198
>PF10026.13 ; DUF2268 ; Predicted Zn-dependent protease (DUF2268)
Probab=29.09 E-value=32 Score=27.22 Aligned_cols=10 Identities=40% Similarity=0.551 Sum_probs=0.0 Template_Neff=10.600
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+.|++
T Consensus 67 ~i~HE~~H~~ 76 (192)
T Q5L1T9_GEOKA/6 67 LVAHEYNHVC 76 (192)
T ss_pred HHHHHHHHHH
No 199
>7JFS_A F5/8 type C domain protein; glycopeptidase, HYDROLASE; 4.6A {Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)}
Probab=28.06 E-value=36 Score=34.52 Aligned_cols=11 Identities=45% Similarity=0.791 Sum_probs=0.0 Template_Neff=10.800
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+.++||+||..
T Consensus 730 Wg~~HE~GH~~ 740 (981)
T 7JFS_A 730 WGVAHELGHNF 740 (981)
T ss_dssp HHHHHHHHHHT
T ss_pred hhHHHHHHHHH
No 200
>6XSX_A ZmpA Glycopeptidase; glycopeptidase, HYDROLASE; HET: MES, EDO; 2.1A {Clostridium perfringens}
Probab=27.93 E-value=39 Score=31.80 Aligned_cols=15 Identities=27% Similarity=0.441 Sum_probs=0.0 Template_Neff=10.200
Q ss_pred CcceeecChhhHhhh
Q FD01846349_043 126 CSNQINVPHEIGHMI 140 (190)
Q Consensus 126 ~~~q~~~aHEfGHml 140 (190)
....+.+.||+||..
T Consensus 273 ~~~~Wg~~HE~GH~~ 287 (529)
T 6XSX_A 273 VDTGWGFMHEMGHNF 287 (529)
T ss_dssp TCCSHHHHHHHHHHT
T ss_pred CCCCcHHHHHHHhhc
No 201
>5L44_B K-26 dipeptidyl carboxypeptidase; dipeptidyl carboxypeptidase, metalloprotease, K-26 tripeptide, angiotensin-1 converting enzyme, hydrolase; HET: SO4, K26; 1.75A {Astrosporangium hypotensionis K-26}
Probab=26.99 E-value=37 Score=32.60 Aligned_cols=10 Identities=40% Similarity=0.787 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++|||||.+
T Consensus 472 ~l~HE~Gha~ 481 (683)
T 5L44_B 472 TMFHEFGHAL 481 (683)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 202
>4LGJ_A Uncharacterized protein; Metallopeptidase, a type III secretion protease, HYDROLASE; 1.55A {Escherichia coli O157:H7}
Probab=26.91 E-value=1.3e+02 Score=27.06 Aligned_cols=53 Identities=21% Similarity=0.142 Sum_probs=0.0 Template_Neff=5.000
Q ss_pred eeecChhhHh-hhcCCCcccccCcCCCCCccccc---------------chhccccCChh-----hHHHHHHHHHHHHHh
Q FD01846349_043 129 QINVPHEIGH-MIGYHDDEYALDKSGKATTAYRS---------------DAAALMNIGME-----LRSRYLEHVNTFLNV 187 (190)
Q Consensus 129 q~~~aHEfGH-mlG~l~DEY~~g~~~~~~~~~~~---------------d~~siM~~G~~-----vr~rh~~~~~~~l~~ 187 (190)
|..+.||+-| +-| +.|.-..+ .+... ....-++.... ++.|.+..+++.+.+
T Consensus 156 q~~LIHEiIH~LTg-~~DP~~~~------~~~rGPtE~La~rI~~Emg~~~P~~~~Y~~p~R~~~~~~r~~~~l~~~~~R 228 (271)
T 4LGJ_A 156 QEGLIHEIIHHVTG-SSDPSGDS------NIELGPTEILARRVAQELGWSVPDFKGYAEPEREAHLRLRNLNALRQAAMR 228 (271)
T ss_dssp HHHHHHHHHHHHHC-CCCCSSCC------SSCCCHHHHHHHHHHHHHTCCCCCCCCTTCHHHHHHHHHHHHHHHHHHHHH
T ss_pred HHHHHHHHHHHHHC-CCCCCCCC------CCCCCHHHHHHHHHHHHhCCCCCCcccCCCHHHHHHHHHHHHHHHHHHHHh
Q ss_pred h
Q FD01846349_043 188 I 188 (190)
Q Consensus 188 ~ 188 (190)
+
T Consensus 229 h 229 (271)
T 4LGJ_A 229 H 229 (271)
T ss_dssp T
T ss_pred C
No 203
>6PNJ_K photosystem I reaction center subunit PsaK; trimeric alpha helical complex, PHOTOSYNTHESIS; HET: BCR, LMT, LHG, LMG, PQN, CLA, SF4, CL0, F6C; 3.2A {Fischerella thermalis PCC 7521}
Probab=26.65 E-value=47 Score=20.84 Aligned_cols=6 Identities=67% Similarity=1.431 Sum_probs=0.0 Template_Neff=3.400
Q ss_pred hHhhhc
Q FD01846349_043 136 IGHMIG 141 (190)
Q Consensus 136 fGHmlG 141 (190)
|||++|
T Consensus 22 ~GHIiG 27 (39)
T 6PNJ_K 22 FGHVIG 27 (39)
T ss_dssp HHHHHH
T ss_pred HHHHHH
No 204
>PF04450.16 ; BSP ; Peptidase of plants and bacteria
Probab=26.51 E-value=38 Score=27.47 Aligned_cols=10 Identities=30% Similarity=0.441 Sum_probs=0.0 Template_Neff=10.500
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+.|++
T Consensus 103 vl~HE~~H~~ 112 (217)
T Q8A0Q7_BACTN/3 103 VLLHELTHAY 112 (217)
T ss_pred HHHHHHHHHH
No 205
>3B4R_A Putative zinc metalloprotease MJ0392; Intramembrane protease, metalloprotease, CBS domain, Hydrolase, Metal-binding, Transmembrane, Zinc; 3.3A {Methanocaldococcus jannaschii}
Probab=26.19 E-value=45 Score=27.96 Aligned_cols=9 Identities=56% Similarity=0.888 Sum_probs=0.0 Template_Neff=9.100
Q ss_pred cChhhHhhh
Q FD01846349_043 132 VPHEIGHMI 140 (190)
Q Consensus 132 ~aHEfGHml 140 (190)
+.||+||.+
T Consensus 52 ~~HE~gH~~ 60 (224)
T 3B4R_A 52 VLHELGHSY 60 (224)
T ss_dssp HHHHHHHHH
T ss_pred HHHHHHHHH
No 206
>7XO6_D Angiotensin-converting enzyme 2; VIRAL PROTEIN; HET: NAG; 2.6A {Mus musculus}
Probab=26.02 E-value=40 Score=34.19 Aligned_cols=10 Identities=40% Similarity=0.826 Sum_probs=0.0 Template_Neff=8.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+||++
T Consensus 371 tl~HE~GHa~ 380 (805)
T 7XO6_D 371 TAHHEMGHIQ 380 (805)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 207
>2LN3_A DE NOVO DESIGNED PROTEIN OR135; Structural Genomics, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG), PSI-Biology, Protein Structure Initiative, DE NOVO PROTEIN; NMR {artificial gene}
Probab=25.38 E-value=3.4e+02 Score=19.16 Aligned_cols=40 Identities=25% Similarity=0.369 Sum_probs=0.0 Template_Neff=1.000
Q ss_pred EEEEEEeeeCCCCCCCCC-HHHHHHHHHHHHH-------HHHHHcCC-ceEEEecCC
Q FD01846349_043 7 LKCKYTWVKNSDVKDDWT-FIEKSLFIINVYT-------TVCSEWNG-KIFFSVSGS 54 (190)
Q Consensus 7 ~r~~f~f~~~~~~~~~Wt-~~e~~~f~~~~~~-------~I~~~Ws~-k~~l~~~~~ 54 (190)
+.+...| +=| +.+++.|.+.++. +|+..|.+ +.+|+..++
T Consensus 27 ldlevef--------dstddkeieeferdmedlakktgvqiqkqwqgnklrirlkgs 75 (83)
T 2LN3_A 27 LDLEVEF--------DSTDDKEIEEFERDMEDLAKKTGVQIQKQWQGNKLRIRLKGS 75 (83)
T ss_dssp CEEEEEE--------CCCCHHHHHHHHHHHHHHHHHHTCCEEEEEETTEEEEEEESS
T ss_pred CCeEEEe--------cCCCHHHHHHHHHhHHHHHHHHCcchhhhhcCCeeEEEEeec
No 208
>PF14891.10 ; Peptidase_M91 ; Effector protein
Probab=24.87 E-value=43 Score=26.87 Aligned_cols=10 Identities=30% Similarity=0.434 Sum_probs=0.0 Template_Neff=9.300
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||++|..
T Consensus 81 ~L~HEL~Ha~ 90 (178)
T D3Q9W2_STANL/5 81 VLYHEMAHSY 90 (178)
T ss_pred HHHHHHHHHH
No 209
>6NCL_c4 P4; tape-measure protein, minor capsid proteins, zip protein, giant virus, VIRUS; 3.5A {Paramecium bursaria Chlorella virus 1}
Probab=24.84 E-value=38 Score=28.52 Aligned_cols=11 Identities=27% Similarity=0.413 Sum_probs=0.0 Template_Neff=4.900
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+++.||+.|++
T Consensus 102 yV~iHELAH~~ 112 (181)
T 6NCL_c4 102 KSICHELAHGT 112 (181)
T ss_pred HHHHHHHHHHh
No 210
>2O36_A Thimet oligopeptidase; thermolysin-like domain, substrate-binding channel, HYDROLASE; 1.95A {Homo sapiens} SCOP: d.92.1.5
Probab=24.83 E-value=43 Score=32.12 Aligned_cols=10 Identities=40% Similarity=0.763 Sum_probs=0.0 Template_Neff=11.100
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+||.+
T Consensus 455 ~l~HE~Gha~ 464 (674)
T 2O36_A 455 TYFHEFGHVM 464 (674)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 211
>7WPC_D Angiotensin-converting enzyme 2; VIRAL PROTEIN; HET: NAG; 2.57A {Severe acute respiratory syndrome coronavirus 2}
Probab=24.54 E-value=44 Score=33.89 Aligned_cols=10 Identities=40% Similarity=0.826 Sum_probs=0.0 Template_Neff=8.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+||.+
T Consensus 371 tl~HE~GHa~ 380 (805)
T 7WPC_D 371 TAHHEMGHIQ 380 (805)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 212
>7LX0_k Photosystem I reaction center subunit PsaK; Photosystem I, Photosynthesis, Far-red light, Chlorophyll f; HET: CLA, CL0, PQN, SF4, LMG, BCR, LHG, LMT, F6C; 2.96A {Fischerella thermalis PCC 7521}
Probab=23.71 E-value=57 Score=21.52 Aligned_cols=6 Identities=67% Similarity=1.431 Sum_probs=0.0 Template_Neff=3.100
Q ss_pred hHhhhc
Q FD01846349_043 136 IGHMIG 141 (190)
Q Consensus 136 fGHmlG 141 (190)
|||++|
T Consensus 31 fGHIlG 36 (49)
T 7LX0_k 31 FGHVIG 36 (49)
T ss_dssp HHHHHH
T ss_pred HHHHHH
No 213
>4L7A_A Uncharacterized protein; Putative zinc-binding metallo-peptidase, PF15890 family protein, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure; HET: MSE; 2.09A {Bacteroides caccae}
Probab=23.69 E-value=47 Score=28.42 Aligned_cols=10 Identities=30% Similarity=0.690 Sum_probs=0.0 Template_Neff=9.800
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++-|||+|++
T Consensus 141 ~i~HEf~h~l 150 (271)
T 4L7A_A 141 VMHHEFAHIL 150 (271)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 214
>PF03571.19 ; Peptidase_M49 ; Peptidase family M49
Probab=22.15 E-value=69 Score=31.40 Aligned_cols=12 Identities=42% Similarity=0.584 Sum_probs=0.0 Template_Neff=8.100
Q ss_pred eecChhh-Hhhhc
Q FD01846349_043 130 INVPHEI-GHMIG 141 (190)
Q Consensus 130 ~~~aHEf-GHmlG 141 (190)
.++.||+ ||.+|
T Consensus 312 ~v~lHEllgHg~G 324 (568)
T Q0CEW8_ASPTN/8 312 KVALHELFGHGTG 324 (568)
T ss_pred EeehHHHHhcccc
No 215
>4JIX_B Projannalysin; Hydrolase, Metallopeptidase Zymogen, Minigluzincin; HET: GOL, SO4; 2.0A {Methanocaldococcus jannaschii}
Probab=22.13 E-value=52 Score=23.83 Aligned_cols=10 Identities=30% Similarity=0.381 Sum_probs=0.0 Template_Neff=9.900
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
++.||+.|+.
T Consensus 68 vi~HEl~H~~ 77 (112)
T 4JIX_B 68 IILHELIHFK 77 (112)
T ss_dssp HHHHHHHHHH
T ss_pred HHHHHHHHHH
No 216
>PF13485.10 ; Peptidase_MA_2 ; Peptidase MA superfamily
Probab=21.71 E-value=56 Score=26.12 Aligned_cols=10 Identities=30% Similarity=0.783 Sum_probs=0.0 Template_Neff=12.000
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+.|++
T Consensus 69 ~l~HEl~H~~ 78 (243)
T Q3Z8Y5_DEHM1/1 69 AITHELAHKV 78 (243)
T ss_pred HHHHHHHHHH
No 217
>PF13699.10 ; DUF4157 ; Domain of unknown function (DUF4157)
Probab=21.46 E-value=70 Score=19.54 Aligned_cols=10 Identities=30% Similarity=0.411 Sum_probs=0.0 Template_Neff=12.700
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
.++||++|.+
T Consensus 63 ~~~~e~~h~~ 72 (78)
T B1Y034_LEPCP/1 63 LLRHELTHVG 72 (78)
T ss_pred eHHHHHHHHH
No 218
>7JS4_A F5/8 type C domain protein; glycopeptidase, HYDROLASE; 4.6A {Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)}
Probab=21.45 E-value=61 Score=32.77 Aligned_cols=11 Identities=45% Similarity=0.791 Sum_probs=0.0 Template_Neff=11.200
Q ss_pred eecChhhHhhh
Q FD01846349_043 130 INVPHEIGHMI 140 (190)
Q Consensus 130 ~~~aHEfGHml 140 (190)
+.+.||+||+.
T Consensus 279 Wg~~HE~GH~~ 289 (980)
T 7JS4_A 279 WGVAHELGHNF 289 (980)
T ss_dssp HHHHHHHHHHH
T ss_pred chHHHHHHHcc
No 219
>6GGR_B Bacteriophage virulence determinant; Protease, Metalloprotease, zinc, METAL BINDING PROTEIN; 2.097A {Mus musculus}
Probab=21.23 E-value=51 Score=28.07 Aligned_cols=18 Identities=17% Similarity=0.279 Sum_probs=0.0 Template_Neff=7.200
Q ss_pred cceeecChhhHh-hhcCCCc
Q FD01846349_043 127 SNQINVPHEIGH-MIGYHDD 145 (190)
Q Consensus 127 ~~q~~~aHEfGH-mlG~l~D 145 (190)
..+..+.||+-| +.| +.|
T Consensus 159 s~~r~liHEivHaLTg-~~D 177 (212)
T 6GGR_B 159 DTTRSFIHQVVHALTH-LQD 177 (212)
T ss_dssp CHHHHHHHHHHHHHHC-CCS
T ss_pred cHHHHHHHHHHHHHhC-CCC
No 220
>PF01752.21 ; Peptidase_M9 ; Collagenase
Probab=21.14 E-value=58 Score=27.12 Aligned_cols=10 Identities=40% Similarity=0.644 Sum_probs=0.0 Template_Neff=11.500
Q ss_pred ecChhhHhhh
Q FD01846349_043 131 NVPHEIGHMI 140 (190)
Q Consensus 131 ~~aHEfGHml 140 (190)
+++||+.|++
T Consensus 161 ~l~HE~~H~~ 170 (286)
T Q2SA85_HAHCH/3 161 NLEHEYVHYL 170 (286)
T ss_pred HHHHHHHHHH
No 221
>1G12_A PEPTIDYL-LYS METALLOENDOPEPTIDASE; zinc cordinate, METALLOPROTEASE, HYDROLASE; HET: MAN; 1.6A {Grifola frondosa} SCOP: d.92.1.12
Probab=21.06 E-value=62 Score=24.76 Aligned_cols=16 Identities=38% Similarity=0.673 Sum_probs=0.0 Template_Neff=10.900
Q ss_pred ecChhhHhhh---cCCCcc-c
Q FD01846349_043 131 NVPHEIGHMI---GYHDDE-Y 147 (190)
Q Consensus 131 ~~aHEfGHml---G~l~DE-Y 147 (190)
++.||+-|+. + ..|. |
T Consensus 114 ~llHE~~H~~~~~~-~~d~~y 133 (167)
T 1G12_A 114 TLVHESSHFTRNGG-TKDYAY 133 (167)
T ss_dssp HHHHHHHHSGGGTC-CBCSCC
T ss_pred HHHHHHHhccccCC-CCcccc
No 222
>PF21420.1 ; Tautomerase-like ; Tautomerase-like
Probab=20.75 E-value=4e+02 Score=17.40 Aligned_cols=24 Identities=8% Similarity=-0.135 Sum_probs=0.0 Template_Neff=2.700
Q ss_pred CCCCCCHHHHHHHHHHHHHHHHHH
Q FD01846349_043 19 VKDDWTFIEKSLFIINVYTTVCSE 42 (190)
Q Consensus 19 ~~~~Wt~~e~~~f~~~~~~~I~~~ 42 (190)
...+.+.+++++|.+......+++
T Consensus 9 ~e~pl~~e~krAfa~eA~~IFqeV 32 (45)
T A9W9V0_CHLAA/2 9 GDRPPDRTRKQAFAAEASAIFQRV 32 (45)
T ss_pred CCCCCCHHHHHHHHHHHHHHHHHH
No 223
>7YX8_A Peptidase M60 domain-containing protein; Glycoprotease, mucinase, T antigen, Tn antigen, AM0627, HYDROLASE; HET: A2G, GOL, GAL; 1.5A {Akkermansia muciniphila}
Probab=20.08 E-value=70 Score=29.53 Aligned_cols=15 Identities=20% Similarity=0.461 Sum_probs=0.0 Template_Neff=9.900
Q ss_pred CcceeecChhhHhhh
Q FD01846349_043 126 CSNQINVPHEIGHMI 140 (190)
Q Consensus 126 ~~~q~~~aHEfGHml 140 (190)
+...+...||+||..
T Consensus 252 ~~~~Wg~~HEiGH~~ 266 (441)
T 7YX8_A 252 GDACWGFSHAVGHVM 266 (441)
T ss_dssp HHHHHHHHHHHHHHH
T ss_pred CCcccHHHHHHHHHH