Chain J, Kunitz-type inihibitor
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
beta-trefoil_STI_BbKI-like | cd23364 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides ... |
3-164 | 1.23e-123 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides Kunitz-type serine protease inhibitor BbKI and similar proteins; This subfamily includes Bauhinia bauhinioides BbKI, BbCI, Bauhinia rufa BrTI, and similar proteins. BbKI inhibits bovine trypsin, human plasma kallikrein and plasmin, and weakly inhibits bovine chymotrypsin. BbCI inhibits cruzipain, a cysteine proteinase from Trypanosoma cruzi. It also inhibits cathepsin L, a cysteine proteinase with high homology to cruzipain, but not cathepsin B, papain, bromelain, or ficin. BrTI acts as an inhibitor of trypsin and human plasma kallikrein. It does not inhibit chymotrypsin, porcine pancreatic elastase, human neutrophil elastase, coagulation factor Xa, human thrombin, porcine pancreatic kallikrein or plasmin. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. : Pssm-ID: 467389 Cd Length: 162 Bit Score: 344.31 E-value: 1.23e-123
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Name | Accession | Description | Interval | E-value | ||||
beta-trefoil_STI_BbKI-like | cd23364 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides ... |
3-164 | 1.23e-123 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides Kunitz-type serine protease inhibitor BbKI and similar proteins; This subfamily includes Bauhinia bauhinioides BbKI, BbCI, Bauhinia rufa BrTI, and similar proteins. BbKI inhibits bovine trypsin, human plasma kallikrein and plasmin, and weakly inhibits bovine chymotrypsin. BbCI inhibits cruzipain, a cysteine proteinase from Trypanosoma cruzi. It also inhibits cathepsin L, a cysteine proteinase with high homology to cruzipain, but not cathepsin B, papain, bromelain, or ficin. BrTI acts as an inhibitor of trypsin and human plasma kallikrein. It does not inhibit chymotrypsin, porcine pancreatic elastase, human neutrophil elastase, coagulation factor Xa, human thrombin, porcine pancreatic kallikrein or plasmin. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467389 Cd Length: 162 Bit Score: 344.31 E-value: 1.23e-123
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STI | smart00452 | Soybean trypsin inhibitor (Kunitz) family of protease inhibitors; |
5-164 | 1.68e-25 | ||||
Soybean trypsin inhibitor (Kunitz) family of protease inhibitors; Pssm-ID: 214670 Cd Length: 172 Bit Score: 95.86 E-value: 1.68e-25
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Kunitz_legume | pfam00197 | Trypsin and protease inhibitor; |
5-162 | 8.53e-25 | ||||
Trypsin and protease inhibitor; Pssm-ID: 395144 Cd Length: 174 Bit Score: 93.91 E-value: 8.53e-25
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Name | Accession | Description | Interval | E-value | ||||
beta-trefoil_STI_BbKI-like | cd23364 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides ... |
3-164 | 1.23e-123 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides Kunitz-type serine protease inhibitor BbKI and similar proteins; This subfamily includes Bauhinia bauhinioides BbKI, BbCI, Bauhinia rufa BrTI, and similar proteins. BbKI inhibits bovine trypsin, human plasma kallikrein and plasmin, and weakly inhibits bovine chymotrypsin. BbCI inhibits cruzipain, a cysteine proteinase from Trypanosoma cruzi. It also inhibits cathepsin L, a cysteine proteinase with high homology to cruzipain, but not cathepsin B, papain, bromelain, or ficin. BrTI acts as an inhibitor of trypsin and human plasma kallikrein. It does not inhibit chymotrypsin, porcine pancreatic elastase, human neutrophil elastase, coagulation factor Xa, human thrombin, porcine pancreatic kallikrein or plasmin. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467389 Cd Length: 162 Bit Score: 344.31 E-value: 1.23e-123
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beta-trefoil_STI | cd00178 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold; The STI-like domain is found ... |
20-162 | 1.37e-29 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold; The STI-like domain is found in the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. They inhibit proteases by binding with high affinity to their active sites. Plant Kunitz-type inhibitors are thought to be important in defense, especially against insect pests. The STI-like domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467384 Cd Length: 161 Bit Score: 105.90 E-value: 1.37e-29
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beta-trefoil_STI_WCI3-like | cd23362 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus ... |
5-164 | 2.38e-29 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus tetragonolobus chymotrypsin inhibitor 3 (WCI-3) and similar proteins; This subfamily includes Psophocarpus tetragonolobus WCI-3, trypsin inhibitor 1 (WTI-1), and trypsin inhibitor DE-3 from Erythrina caffra (ETI). WTI-1 is a Kunitz type protease inhibitor that inhibits bovine trypsin stoichiometrically, but not bovine alpha-chymotrypsin. WCI-3 is a Kunitz-type winged bean chymotrypsin inhibitor (WbCI) that inhibits alpha-chymotrypsin at the molar ratio of 1:2 instead of 1:1, the usual ratio of 1:1 common to other members of the family. ETI is a trypsin inhibitor that shows high homology to other Kunitz trypsin protease inhibitors, but has the unique ability to bind and inhibit tissue plasminogen activator. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467387 Cd Length: 170 Bit Score: 105.39 E-value: 2.38e-29
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beta-trefoil_STI_LlTI-like | cd23365 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Leucaena leucocephala ... |
4-163 | 5.61e-26 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Leucaena leucocephala trypsin inhibitor (LlTI) and similar proteins; LlTI is a Kunitz-type trypsin inhibitor that inhibits trypsin, plasmin, human plasma kallikrein, chymotrypsin, and factor XIIa activity. This subfamily also includes tamarind Kunitz inhibitor (TKI), Enterolobium contortisiliquum trypsin inhibitor (EcTI), Acacia confusa trypsin inhibitor (AcTI), Bauhinia ungulata factor Xa inhibitor BuXI, and Phanera variegata trypsin inhibitor BvTI. TKI is a Kunitz-type dual inhibitor (TKI) of factor Xa (FXa) and trypsin. It shows prolongation of blood coagulation time. EcTI also belongs to the Kunitz family of plant inhibitors, common in plant seeds. It inhibits trypsin, chymotrypsin, plasma kallikrein, plasmin, human neutrophil elastase, and Factor XIIa in the stoichiometric ratio 1:1, but not thrombin, bovine pancreatic elastase, or Factor Xa. It is involved in the inhibition of the invasion of gastric cancer cells through alterations in integrin-dependent cell signaling pathway. AcTI inhibits trypsin and alpha-chymotrypsin stoichiometrically at the molar ratio of 1:1 and 2:1 respectively. BuXI inhibits bovine trypsin and chymotrypsin, and human plasmin, plasma kallikrein, factor XIIa, and factor Xa. BvTI inhibits bovine trypsin and chymotrypsin, and human plasmin, plasma kallikrein and factor XIIa. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467390 Cd Length: 170 Bit Score: 96.80 E-value: 5.61e-26
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STI | smart00452 | Soybean trypsin inhibitor (Kunitz) family of protease inhibitors; |
5-164 | 1.68e-25 | ||||
Soybean trypsin inhibitor (Kunitz) family of protease inhibitors; Pssm-ID: 214670 Cd Length: 172 Bit Score: 95.86 E-value: 1.68e-25
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Kunitz_legume | pfam00197 | Trypsin and protease inhibitor; |
5-162 | 8.53e-25 | ||||
Trypsin and protease inhibitor; Pssm-ID: 395144 Cd Length: 174 Bit Score: 93.91 E-value: 8.53e-25
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beta-trefoil_STI_SKTI | cd23363 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in the soybean Kunitz ... |
4-162 | 1.70e-20 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in the soybean Kunitz trypsin inhibitor (SKTI) subfamily; SKTI is extracted from soybean (Glycine max L.) seeds. It shows inhibition of trypsin and possesses insect resistance and anti-tumor properties. This subfamily includes KTI1-3. KTI1 and KTI2 probably do not possess trypsin inhibitor activity. KTI3, also called trypsin inhibitor A, is responsible for most of the Kunitz trypsin inhibitor activity and protein found in soybean seeds. Members of this subfamily contain a soybean trypsin inhibitor (STI)-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467388 Cd Length: 175 Bit Score: 82.90 E-value: 1.70e-20
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beta-trefoil_STI_VvMLP-like | cd23375 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Vitis vinifera ... |
5-162 | 4.16e-16 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Vitis vinifera miraculin-like protein (VvMLP) and similar proteins; This subfamily includes VvMLP, Synsepalum dulcificum miraculin (SdMIR), and Arabidopsis thaliana Kunitz trypsin inhibitor 5 (AtKTI5, also known as AtKTI2). VvMLP exhibits significant homology to miraculin. However, it exists as a monomer in solution with no detectable taste-modifying activity. It can act as a moderate trypsin inhibitor. SdMIR has the property of modifying a sour taste into a sweet taste. This alteration of taste perception persists for many minutes. AtKTI5 can inhibit both serine proteases and cysteine proteases. It may be involved in the modulation of the proteases that participate in the hydrolysis of dietary proteins in the gut of spider mites. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467400 Cd Length: 177 Bit Score: 71.48 E-value: 4.16e-16
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beta-trefoil_STI_MkMLP-like | cd23370 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Murraya koenigii ... |
5-162 | 9.94e-13 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Murraya koenigii miraculin-like protein (MkMLP) and similar proteins; This subfamily includes Theobroma cacao 21 kDa seed protein (TcASP) and Murraya koenigii miraculin-like protein (MkMLP). TcASP shows homology to the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. MkMLP is closer to miraculin, a taste modifying protein, rather than classical Kunitz family members like soybean Kunitz-type trypsin inhibitor (STI). MkMLP is functionally unstable at higher temperatures. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467395 Cd Length: 179 Bit Score: 62.72 E-value: 9.94e-13
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beta-trefoil_STI_DrTI | cd23376 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Delonix regia ... |
5-138 | 2.73e-12 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Delonix regia Kunitz-type serine protease inhibitor DrTI and similar proteins; DrTI is a Kunitz-type trypsin inhibitor that inhibits bovine trypsin and human plasma kallikrein, but not chymotrypsin and tissue kallikrein. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467401 Cd Length: 174 Bit Score: 61.19 E-value: 2.73e-12
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beta-trefoil_STI_AtKTI6-like | cd23369 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana ... |
4-151 | 2.75e-11 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana Kunitz trypsin inhibitor 6 (AtKTI6) and similar proteins; This subfamily includes AtKTI6 and AtKTI7, which exhibit Kunitz trypsin protease inhibitor activity. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467394 Cd Length: 170 Bit Score: 58.55 E-value: 2.75e-11
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beta-trefoil_STI_COTI | cd23379 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Senna obtusifolia ... |
4-162 | 2.04e-10 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Senna obtusifolia trypsin inhibitor 1 (COTI) and similar proteins; COTI is a specific inhibitor of bovine trypsin. It also exhibits strong inhibitory effect on midgut trypsin from Pieris rapae, Helicoverpa armigera, Spodoptera exigua, and Spodoptera litura. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467404 Cd Length: 172 Bit Score: 56.33 E-value: 2.04e-10
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beta-trefoil_STI_KPI104-like | cd23367 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Medicago truncatula ... |
5-159 | 6.86e-10 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Medicago truncatula Kunitz type trypsin inhibitor 104 (KPI104) and similar proteins; This subfamily includes Medicago truncatula KPI104, KPI106, and KPI111. They are protease inhibitors involved in the control of mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis). KPI104 interacts with cysteine protease (CP). It shows a stronger affinity for serine carboxypeptidase (SCP1) than for CP. KPI111 only interacts with SCP1. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467392 Cd Length: 170 Bit Score: 54.66 E-value: 6.86e-10
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beta-trefoil_STI_WSCP_II | cd23360 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in class II ... |
4-127 | 2.48e-08 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in class II water-soluble chlorophyll proteins (WSCPs) and similar proteins; There are two kinds of water-soluble chlorophyll (Chl) proteins (WSCPs): Chenopodium-type (Class I, a WSCP from Chenopodium, Atriplex, Polygonum, and Amaranthus species) and Brassica-type (Class II, a WSCP from Brassica, Raphanus, and Lepidium species). Classes I and II WSCPs differ mainly in their photoconvertiblity. Class I WSCPs show a light-induced absorption change, whereas Class II WSCPs do not. This family includes Class II WSCPs. They possess the complete motif of the Kunitz-type proteinase inhibitor but may not inhibit trypsin, whose activity is inhibited strongly by one Kunitz-proteinase inhibitor, the soybean trypsin inhibitor (STI). Members of this subfamily contain a STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467385 Cd Length: 176 Bit Score: 50.53 E-value: 2.48e-08
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beta-trefoil_STI_WBA1 | cd23361 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus ... |
5-132 | 1.12e-07 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus tetragonolobus albumin-1 and similar proteins; Albumin-1, also called WBA-1, or winged bean albumin 1, acts as a 2S seed storage protein that is homologous with Kunitz-type seed trypsin inhibitors. It contains a soybean trypsin inhibitor (STI)-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467386 Cd Length: 174 Bit Score: 49.02 E-value: 1.12e-07
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beta-trefoil_STI_AtTPI-like | cd23366 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana ... |
5-163 | 1.18e-07 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana trypsin protease inhibitor (AtTPI) and similar proteins; AtTPI, also called kunitz trypsin inhibitor 4 (AtKTI4), or Kunitz trypsin inhibitor 1 (AtKTI1), exhibits Kunitz trypsin protease inhibitor activity. It is involved in modulating programmed cell death (PCD) in plant-pathogen interactions. It can also inhibit both serine proteases and cysteine proteases. It may be involved in the modulation of proteases that participate in the hydrolysis of dietary proteins in the gut of spider mites. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467391 Cd Length: 195 Bit Score: 48.97 E-value: 1.18e-07
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beta-trefoil_STI_CrataBL-like | cd23374 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Crateva tapia bark ... |
12-139 | 1.28e-07 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Crateva tapia bark lectin (CrataBL) and similar proteins; CrataBL is both a Kunitz-type plant protease inhibitor and a glucose- and N-acetylglucosamine-binding lectin. It has hemagglutinating activity against human and rabbit erythrocytes which does not require divalent cations. It inhibits factor Xa and, to a lesser extent, trypsin. It does not inhibit neutrophil elastase, human plasma kallikrein, papain, human plasmin, porcine pancreatic kallikrein and bovine chymotrypsin. CrataBL has insecticidal activity against the termite species Nasutitermes corniger. It induces apoptosis in prostate cancer cell lines DU145 and PC3. The family includes CrataBL-form I and CrataBL-form II. This subfamily also includes Arabidopsis thaliana Kunitz trypsin inhibitor 3 (AtKTI3) that exhibits Kunitz trypsin protease inhibitor activity. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467399 Cd Length: 160 Bit Score: 48.63 E-value: 1.28e-07
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beta-trefoil_STI_MP4-like | cd23377 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Mucuna pruriens MP-4 ... |
5-138 | 4.74e-07 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Mucuna pruriens MP-4 and similar proteins; This subfamily includes Mucuna pruriens MP-4, Canavalia lineata subtilisin inhibitor CLSI-II, Cicer arietinum trypsin protein inhibitor 2 (CaTI2), Pisum sativum Kunitz-type trypsin inhibitor-like 1 protein (PIP20-1) and Kunitz-type trypsin inhibitor-like 2 protein (PIP20-2). MP-4 contributes significantly to the snake venom neutralization activity of Mucuna pruriens seeds through an indirect antibody-mediated mechanism and not through direct inhibition of venom proteases. CLSI-II inhibits subtilisin-type microbial serine proteases including proteinase K, subtilisin BPN', subtilisin Carlsberg and subtilisin E in a non-stoichiometric manner. It weakly inhibits Aspergillus oryzae protease and some metalloproteases including pronase E. It does not inhibit trypsin, chymotrypsin, Streptomyces griseus alkaline protease or Achromobacter lyticus lysyl endopeptidase. CLSI-II has a wider inhibitory specificity than CLSI-III. CaTI2 is a Kunitz trypsin inhibitor (KTI) with antifungal effect on Fusarium oxysporum f. sp. ciceris, a fungal pathogen known to cause severe damage to chickpea crop. It may be binding to the trypsin active pocket in a non-substrate like manner. PIP20-1 (also called protease inhibitor from pea 1 or FUC1) and PIP20-2 (also called protease inhibitor from pea 2 or FUC2) may act as protease inhibitors involved in plant defense responses. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467402 Cd Length: 179 Bit Score: 47.27 E-value: 4.74e-07
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beta-trefoil_STI_GWIN3 | cd23380 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Populus sp. ... |
5-161 | 4.05e-06 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Populus sp. wound-responsive protein GWIN3 and similar proteins; GWIN3 may play a role in wound response. It shows high sequence similarity with sweet potato sporamins and legume Kunitz trypsin inhibitors. It remains unclear if GWIN3 is a trypsin inhibitor, but proteinase inhibitor function would be consistent with its wound-regulated behavior. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467405 Cd Length: 168 Bit Score: 44.43 E-value: 4.05e-06
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beta-trefoil_STI_LSPI | cd23371 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Carica papaya latex ... |
5-119 | 1.34e-05 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Carica papaya latex serine proteinase inhibitor (LSPI) and similar proteins; LSPI, also called papaya protease inhibitor (PPI), is a double-headed Kunitz-type serine protease inhibitor. A single LSPI molecule can bind two trypsin units at the same time. LSPI may serve as a defense protein as it is induced by wounding and is inactive against endogenous proteases from C. papaya. LSPI belongs to the miraculin family of taste-modifying proteins, which are active against serine proteases. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467396 Cd Length: 183 Bit Score: 43.38 E-value: 1.34e-05
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beta-trefoil_STI_SPOR | cd23368 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Ipomoea batatas ... |
5-128 | 1.63e-05 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Ipomoea batatas sporamin and similar proteins; This subfamily includes Ipomoea batatas sporamin A and sporamin B. They are major tuberous root proteins that belong to the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. They exhibit antitumor activity in a number of types of tumor cells. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467393 Cd Length: 174 Bit Score: 42.73 E-value: 1.63e-05
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beta-trefoil_STI_ASI | cd23373 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in alpha-amylase ... |
5-162 | 1.98e-04 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in alpha-amylase/subtilisin inhibitor (ASI) and similar proteins; This subfamily includes rice ASI (RASI) and barley ASI (BASI). RASI can inhibit alpha-amylase from larvae of the red flour beetle (Tribolium castaneum) and subtilisin from Bacillus subtilis. BASI is a bifunctional protein that can simultaneously inhibit alpha-amylase isozyme (AMY2) and serine proteases of the subtilisin family. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467398 Cd Length: 176 Bit Score: 39.66 E-value: 1.98e-04
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beta-trefoil_STI_CPI-like | cd23372 | soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Solanum tuberosum ... |
34-163 | 1.64e-03 | ||||
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Solanum tuberosum cysteine protease inhibitor (CPI), serine protease inhibitor (SPI), aspartic protease inhibitor (API) and similar proteins; This subfamily includes Solanum tuberosum CPI, SPI, API, and similar proteins. CPI is a Kunitz-type potato cathepsin D inhibitor. It acts as a potent inhibitor of cathepsin l (cysteine protease) but does not inhibit trypsin or chymotrypsin (serine proteases). SPI is a potent inhibitor of serine proteases (chymotrypsin and trypsin). It inhibits tightly human leukocyte elastase (HLE). It does not inhibit papain, pepsin nor cathepsin D (cysteine and aspartic proteases). API functions as the inhibitor of cathepsin D (aspartic protease). It may also inhibit trypsin and chymotrypsin (serine proteases). CPI, SPI, and API protect plants by inhibiting proteases of invading organisms. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467397 Cd Length: 171 Bit Score: 37.01 E-value: 1.64e-03
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Blast search parameters | ||||
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