blastp_kegg |
lcl|csv:101208839
|
7 |
154 |
+ |
148 |
Gaps:2 |
84.88 |
172 |
46.58 |
2e-38 |
pectinesterase inhibitor-like
|
blastp_kegg |
lcl|csv:101203438
|
7 |
154 |
+ |
148 |
Gaps:2 |
84.88 |
172 |
46.58 |
2e-38 |
pectinesterase inhibitor-like
|
blastp_kegg |
lcl|csv:101215721
|
7 |
154 |
+ |
148 |
Gaps:2 |
84.88 |
172 |
46.58 |
2e-38 |
pectinesterase inhibitor-like
|
blastp_kegg |
lcl|cmo:103496650
|
9 |
154 |
+ |
146 |
Gaps:2 |
83.72 |
172 |
46.53 |
2e-38 |
pectinesterase inhibitor-like
|
blastp_kegg |
lcl|csv:101216343
|
7 |
154 |
+ |
148 |
Gaps:2 |
84.88 |
172 |
45.89 |
9e-38 |
pectinesterase inhibitor-like
|
blastp_kegg |
lcl|cmo:103502096
|
9 |
154 |
+ |
146 |
Gaps:2 |
80.90 |
178 |
47.22 |
1e-37 |
pectinesterase inhibitor-like
|
blastp_kegg |
lcl|csv:101218656
|
7 |
154 |
+ |
148 |
Gaps:2 |
84.88 |
172 |
46.58 |
6e-37 |
pectinesterase inhibitor-like
|
blastp_kegg |
lcl|cmo:103487678
|
7 |
154 |
+ |
148 |
Gaps:2 |
84.88 |
172 |
45.21 |
1e-36 |
pectinesterase inhibitor-like
|
blastp_kegg |
lcl|cmo:103498012
|
9 |
154 |
+ |
146 |
Gaps:2 |
84.71 |
170 |
46.53 |
2e-36 |
pectinesterase inhibitor
|
blastp_kegg |
lcl|cmo:103501963
|
7 |
154 |
+ |
148 |
Gaps:2 |
84.88 |
172 |
45.21 |
2e-36 |
pectinesterase inhibitor-like
|
blastp_pdb |
1xg2_B
|
10 |
154 |
+ |
145 |
Gaps:1 |
95.42 |
153 |
43.84 |
5e-36 |
mol:protein length:153 Pectinesterase inhibitor
|
blastp_pdb |
1x8z_C
|
14 |
154 |
+ |
141 |
Gaps:1 |
91.50 |
153 |
33.57 |
3e-18 |
mol:protein length:153 invertase/pectin methylesterase inhibitor fam
|
blastp_pdb |
1x8z_B
|
14 |
154 |
+ |
141 |
Gaps:1 |
91.50 |
153 |
33.57 |
3e-18 |
mol:protein length:153 invertase/pectin methylesterase inhibitor fam
|
blastp_pdb |
1x8z_A
|
14 |
154 |
+ |
141 |
Gaps:1 |
91.50 |
153 |
33.57 |
3e-18 |
mol:protein length:153 invertase/pectin methylesterase inhibitor fam
|
blastp_pdb |
1x91_A
|
14 |
154 |
+ |
141 |
Gaps:1 |
91.50 |
153 |
32.86 |
2e-17 |
mol:protein length:153 invertase/pectin methylesterase inhibitor fam
|
blastp_pdb |
1x90_B
|
14 |
154 |
+ |
141 |
Gaps:1 |
92.11 |
152 |
32.86 |
2e-17 |
mol:protein length:152 invertase/pectin methylesterase inhibitor fam
|
blastp_pdb |
1x90_A
|
14 |
154 |
+ |
141 |
Gaps:1 |
92.11 |
152 |
32.86 |
2e-17 |
mol:protein length:152 invertase/pectin methylesterase inhibitor fam
|
blastp_uniprot_sprot |
sp|P83326|PMEI_ACTDE
|
2 |
154 |
+ |
153 |
Gaps:1 |
83.24 |
185 |
42.86 |
4e-36 |
Pectinesterase inhibitor OS Actinidia deliciosa GN PMEI PE 1 SV 2
|
blastp_uniprot_sprot |
sp|Q9LUV1|PMEI2_ARATH
|
11 |
154 |
+ |
144 |
Gaps:2 |
83.24 |
173 |
37.50 |
5e-26 |
Pectinesterase inhibitor 2 OS Arabidopsis thaliana GN PMEI2 PE 1 SV 1
|
blastp_uniprot_sprot |
sp|Q9LNF2|PMEI1_ARATH
|
3 |
154 |
+ |
152 |
Gaps:1 |
85.80 |
176 |
32.45 |
4e-18 |
Pectinesterase inhibitor 1 OS Arabidopsis thaliana GN PMEI1 PE 1 SV 1
|
blastp_uniprot_sprot |
sp|Q8GT41|PLA1_PLAAC
|
4 |
155 |
+ |
152 |
Gaps:13 |
88.83 |
179 |
26.42 |
1e-09 |
Putative invertase inhibitor OS Platanus acerifolia PE 1 SV 1
|
rpsblast_cdd |
gnl|CDD|162447
|
2 |
155 |
+ |
154 |
Gaps:2 |
87.64 |
178 |
28.85 |
1e-25 |
TIGR01614 PME_inhib pectinesterase inhibitor domain. This model describes a plant domain of about 200 amino acids characterized by four conserved Cys residues shown in a pectinesterase inhibitor from Kiwi to form two disulfide bonds: first to second and third to fourth. Roughly half the members of this family have the region described by this HMM followed immediately by a pectinesterase domain pfam01095. This suggests that the pairing of the enzymatic domain and its inhibitor reflects a conserved regulatory mechanism for this enzyme family.
|
rpsblast_cdd |
gnl|CDD|202862
|
9 |
150 |
+ |
142 |
Gaps:2 |
99.31 |
145 |
35.42 |
2e-24 |
pfam04043 PMEI Plant invertase/pectin methylesterase inhibitor. This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences (personal obs:C Yeats) suggesting that both PMEs and their inhibitor are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.
|
rpsblast_cdd |
gnl|CDD|197924
|
6 |
150 |
+ |
145 |
Gaps:2 |
99.32 |
148 |
31.97 |
1e-22 |
smart00856 PMEI Plant invertase/pectin methylesterase inhibitor. This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences suggesting that both PMEs and their inhibitors are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.
|