blastp_kegg |
lcl|rcu:RCOM_0790520
|
3 |
137 |
+ |
135 |
Gaps:12 |
30.83 |
399 |
42.28 |
3e-20 |
Protein Z putative
|
blastp_kegg |
lcl|vvi:100266122
|
33 |
134 |
+ |
102 |
Gaps:12 |
22.02 |
445 |
48.98 |
9e-18 |
serpin-ZX-like
|
blastp_kegg |
lcl|sot:102585963
|
33 |
137 |
+ |
105 |
Gaps:12 |
24.28 |
416 |
46.53 |
2e-17 |
serpin-ZX-like
|
blastp_kegg |
lcl|sot:102585630
|
35 |
137 |
+ |
103 |
Gaps:12 |
25.38 |
390 |
46.46 |
2e-17 |
serpin-ZX-like
|
blastp_kegg |
lcl|sot:102586305
|
3 |
138 |
+ |
136 |
Gaps:20 |
30.24 |
410 |
42.74 |
3e-17 |
serpin-ZX-like
|
blastp_kegg |
lcl|sly:101266216
|
33 |
137 |
+ |
105 |
Gaps:4 |
24.28 |
416 |
42.57 |
6e-17 |
serpin-ZX-like
|
blastp_kegg |
lcl|mdm:103440470
|
35 |
134 |
+ |
100 |
Gaps:12 |
24.74 |
388 |
47.92 |
1e-16 |
serpin-ZX-like
|
blastp_kegg |
lcl|mdm:103420936
|
35 |
134 |
+ |
100 |
Gaps:12 |
24.74 |
388 |
47.92 |
1e-16 |
serpin-ZX-like
|
blastp_kegg |
lcl|mtr:MTR_3g015620
|
32 |
137 |
+ |
106 |
Gaps:4 |
26.84 |
380 |
46.08 |
3e-16 |
Serpin-ZX
|
blastp_kegg |
lcl|pper:PRUPE_ppa006990mg
|
35 |
134 |
+ |
100 |
Gaps:12 |
24.81 |
387 |
45.83 |
7e-16 |
hypothetical protein
|
blastp_pdb |
3le2_A
|
35 |
134 |
+ |
100 |
Gaps:4 |
24.43 |
393 |
42.71 |
9e-14 |
mol:protein length:393 Serpin-ZX
|
blastp_pdb |
3ozq_A
|
34 |
134 |
+ |
101 |
Gaps:14 |
24.73 |
376 |
33.33 |
5e-06 |
mol:protein length:376 Serpin48
|
blastp_pdb |
1jmo_A
|
31 |
134 |
+ |
104 |
Gaps:2 |
22.08 |
480 |
24.53 |
8e-06 |
mol:protein length:480 HEPARIN COFACTOR II
|
blastp_pdb |
1jmj_B
|
31 |
134 |
+ |
104 |
Gaps:2 |
22.08 |
480 |
24.53 |
8e-06 |
mol:protein length:480 HEPARIN COFACTOR II
|
blastp_pdb |
1jmj_A
|
31 |
134 |
+ |
104 |
Gaps:2 |
22.08 |
480 |
24.53 |
8e-06 |
mol:protein length:480 HEPARIN COFACTOR II
|
blastp_uniprot_sprot |
sp|Q9S7T8|SPZX_ARATH
|
35 |
134 |
+ |
100 |
Gaps:4 |
24.55 |
391 |
42.71 |
4e-13 |
Serpin-ZX OS Arabidopsis thaliana GN At1g47710 PE 1 SV 1
|
blastp_uniprot_sprot |
sp|O48706|SPZ3_ARATH
|
29 |
137 |
+ |
109 |
Gaps:8 |
25.96 |
389 |
40.59 |
2e-12 |
Serpin-Z3 OS Arabidopsis thaliana GN At2g26390 PE 3 SV 1
|
blastp_uniprot_sprot |
sp|Q9SIR9|SPZ10_ARATH
|
29 |
137 |
+ |
109 |
Gaps:8 |
26.23 |
385 |
39.60 |
2e-10 |
Serpin-Z10 OS Arabidopsis thaliana GN At2g25240 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q9M1T7|SPZ4_ARATH
|
29 |
137 |
+ |
109 |
Gaps:4 |
26.72 |
393 |
38.10 |
2e-10 |
Serpin-Z4 OS Arabidopsis thaliana GN At3g45220 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q9ST58|SPZ1C_WHEAT
|
35 |
134 |
+ |
100 |
Gaps:4 |
24.12 |
398 |
35.42 |
4e-09 |
Serpin-Z1C OS Triticum aestivum PE 1 SV 1
|
blastp_uniprot_sprot |
sp|Q53KS9|SPZ2B_ORYSJ
|
4 |
118 |
+ |
115 |
Gaps:16 |
24.50 |
404 |
37.37 |
6e-09 |
Serpin-Z2B OS Oryza sativa subsp. japonica GN Os11g0239200 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q9SH52|SPZ1_ARATH
|
35 |
137 |
+ |
103 |
Gaps:5 |
25.97 |
385 |
35.00 |
9e-09 |
Serpin-Z1 OS Arabidopsis thaliana GN At1g64030 PE 2 SV 2
|
blastp_uniprot_sprot |
sp|Q9ST57|SPZ2A_WHEAT
|
36 |
134 |
+ |
99 |
Gaps:10 |
23.87 |
398 |
37.89 |
4e-08 |
Serpin-Z2A OS Triticum aestivum PE 1 SV 1
|
blastp_uniprot_sprot |
sp|Q53Q32|SPZ6B_ORYSJ
|
4 |
135 |
+ |
132 |
Gaps:13 |
29.90 |
398 |
38.66 |
5e-08 |
Serpin-Z6B OS Oryza sativa subsp. japonica GN Os11g0230700 PE 3 SV 2
|
blastp_uniprot_sprot |
sp|Q7XMK1|SPZ10_ORYSJ
|
1 |
134 |
+ |
134 |
Gaps:22 |
28.57 |
392 |
38.39 |
3e-07 |
Putative non-inhibitory serpin-10 OS Oryza sativa subsp. japonica GN Os04g0533700 PE 3 SV 1
|
rpsblast_cdd |
gnl|CDD|29118
|
32 |
137 |
+ |
106 |
Gaps:4 |
26.77 |
381 |
42.16 |
2e-18 |
cd02043 plant_SERPIN SERine Proteinase INhibitors (serpins) plant specific subgroup. It has been suggested that plant serpins play a role in defense against insect predators. This subgroup corresponds to clade P of the serpin superfamily. In general serpins exhibit conformational polymorphism shifting from native to cleaved latent delta or polymorphic forms. Many serpins such as antitrypsin and antichymotrypsin function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones..
|
rpsblast_cdd |
gnl|CDD|200983
|
32 |
137 |
+ |
106 |
Gaps:5 |
27.37 |
369 |
31.68 |
4e-15 |
pfam00079 Serpin Serpin (serine protease inhibitor). Structure is a multi-domain fold containing a bundle of helices and a beta sandwich.
|
rpsblast_cdd |
gnl|CDD|29117
|
32 |
137 |
+ |
106 |
Gaps:5 |
27.75 |
364 |
28.71 |
3e-14 |
cd00172 SERPIN SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved latent delta or polymorphic forms. Many serpins such as antitrypsin and antichymotrypsin function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders emphysema cirrhosis and dementia..
|
rpsblast_cdd |
gnl|CDD|197513
|
32 |
136 |
+ |
105 |
Gaps:3 |
28.41 |
359 |
28.43 |
3e-12 |
smart00093 SERPIN SERine Proteinase INhibitors.
|
rpsblast_cdd |
gnl|CDD|29124
|
2 |
134 |
+ |
133 |
Gaps:19 |
32.42 |
364 |
28.81 |
2e-07 |
cd02049 bacterial_SERPIN SERine Proteinase INhibitors (serpins) prokaryotic subgroup. Little information about specific functions is available for this subgroup most likely they are inhibitory members of the serpin superfamily. In general serpins exhibit conformational polymorphism shifting from native to cleaved latent delta or polymorphic forms. Many serpins such as antitrypsin and antichymotrypsin function as serine protease inhibitors..
|