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Conserved domains on  [gi|15220874|ref|NP_173228|]
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Kunitz family trypsin and protease inhibitor protein [Arabidopsis thaliana]

Protein Classification

Kunitz-type protease inhibitor( domain architecture ID 11087211)

Kunitz-type protease inhibitor similar to Solanum tuberosum aspartic protease inhibitor 8 (also called cathepsin D inhibitor) that may protect the plant by inhibiting proteases of invading organisms

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_STI_VvMLP-like cd23375
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Vitis vinifera ...
 25-194 8.19e-102

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: 291.05  E-value: 8.19e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  25 AVEPVKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYD-KSRTIPVSTDVNIK 103
Cdd:cd23375   1 APEPVLDTAGKILRTGVNYYILPVNRGRGGGLTLASTGNETCPLDVVQEQNEVNNGLPLTFSPVNpKKGVIRVSTDLNIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 104 FSPTSI------WELANFDETTKQWFISTCGVEGNPGQKTVDNWFKIDKFEKDYKIRFCPTVCNFCKVICRDVGVFVQDG 177
Cdd:cd23375  81 FSASTScpestvWKLDDYDESTGQYFVTTGGVEGNPGRETIRNWFKIEKYEDGYKLVYCPSVCNYCKVICKDVGIYIDNG 160

                       170
                ....*....|....*..
gi 15220874 178 KRRLALSDVPLKVMFKR 194
Cdd:cd23375 161 VRRLALSDKPLKVKFKK 177
 
Name Accession Description Interval E-value
beta-trefoil_STI_VvMLP-like cd23375
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Vitis vinifera ...
 25-194 8.19e-102

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: 291.05  E-value: 8.19e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  25 AVEPVKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYD-KSRTIPVSTDVNIK 103
Cdd:cd23375   1 APEPVLDTAGKILRTGVNYYILPVNRGRGGGLTLASTGNETCPLDVVQEQNEVNNGLPLTFSPVNpKKGVIRVSTDLNIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 104 FSPTSI------WELANFDETTKQWFISTCGVEGNPGQKTVDNWFKIDKFEKDYKIRFCPTVCNFCKVICRDVGVFVQDG 177
Cdd:cd23375  81 FSASTScpestvWKLDDYDESTGQYFVTTGGVEGNPGRETIRNWFKIEKYEDGYKLVYCPSVCNYCKVICKDVGIYIDNG 160

                       170
                ....*....|....*..
gi 15220874 178 KRRLALSDVPLKVMFKR 194
Cdd:cd23375 161 VRRLALSDKPLKVKFKK 177
Kunitz_legume pfam00197
Trypsin and protease inhibitor;
29-194 5.04e-79

Trypsin and protease inhibitor;


Pssm-ID: 395144  Cd Length: 174  Bit Score: 233.35  E-value: 5.04e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874    29 VKDINGKSLLTGVNYYILPVIR-GRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYD-KSRTIPVSTDVNIKF-- 104
Cdd:pfam00197   1 VLDTDGNPLRAGVEYYILPAIGgGSGGGLTLASRGNGTCPLDVVQEPSEVSKGLPVKFSPSNsKKGVIRESTDLNIEFfs 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874   105 -----SPTSIWELANFDETTKQWFISTCGVEGNPGQKTVDNWFKIDKFEKDYKIRFCPTVCnfCKVICRDVGVFV-QDGK 178
Cdd:pfam00197  81 apticVQSTVWKVGDGDPETGRRFVVTGGVVGNPGPDTVSNWFKIEKTGGGYKLVFCPSVC--CKVKCGDVGIFVdDNGN 158

                         170
                  ....*....|....*.
gi 15220874   179 RRLALSDVPLKVMFKR 194
Cdd:pfam00197 159 RRLALSDEPFPVVFKK 174
STI smart00452
Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;
29-195 5.24e-52

Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;


Pssm-ID: 214670  Cd Length: 172  Bit Score: 164.81  E-value: 5.24e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874     29 VKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYDKSRTIP-VSTDVNIKFS-- 105
Cdd:smart00452   1 VLDTDGNPLRNGGTYYILPAIRGHGGGLTLAATGNEICPLTVVQSPNEVDNGLPVKFSPPNPSDFIIrESTDLNIEFDap 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874    106 ----PTSIWELANfDETTKQWFISTCGVEGnpgqkTVDNWFKIDKFEKD---YKIRFCPtvCNFCKVICRDVGVF-VQDG 177
Cdd:smart00452  81 plcaQSTVWTVDE-DSTPGGLAVKTGGYPG-----VNDSWFKIEKYSGEsngYKLVYCP--NGSDDDKCGDVGIFiDPNG 152

                          170
                   ....*....|....*....
gi 15220874    178 KRRLALSDV-PLKVMFKRA 195
Cdd:smart00452 153 GRRLVLSNEnPLVVVFKKA 171
 
Name Accession Description Interval E-value
beta-trefoil_STI_VvMLP-like cd23375
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Vitis vinifera ...
 25-194 8.19e-102

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: 291.05  E-value: 8.19e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  25 AVEPVKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYD-KSRTIPVSTDVNIK 103
Cdd:cd23375   1 APEPVLDTAGKILRTGVNYYILPVNRGRGGGLTLASTGNETCPLDVVQEQNEVNNGLPLTFSPVNpKKGVIRVSTDLNIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 104 FSPTSI------WELANFDETTKQWFISTCGVEGNPGQKTVDNWFKIDKFEKDYKIRFCPTVCNFCKVICRDVGVFVQDG 177
Cdd:cd23375  81 FSASTScpestvWKLDDYDESTGQYFVTTGGVEGNPGRETIRNWFKIEKYEDGYKLVYCPSVCNYCKVICKDVGIYIDNG 160

                       170
                ....*....|....*..
gi 15220874 178 KRRLALSDVPLKVMFKR 194
Cdd:cd23375 161 VRRLALSDKPLKVKFKK 177
Kunitz_legume pfam00197
Trypsin and protease inhibitor;
29-194 5.04e-79

Trypsin and protease inhibitor;


Pssm-ID: 395144  Cd Length: 174  Bit Score: 233.35  E-value: 5.04e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874    29 VKDINGKSLLTGVNYYILPVIR-GRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYD-KSRTIPVSTDVNIKF-- 104
Cdd:pfam00197   1 VLDTDGNPLRAGVEYYILPAIGgGSGGGLTLASRGNGTCPLDVVQEPSEVSKGLPVKFSPSNsKKGVIRESTDLNIEFfs 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874   105 -----SPTSIWELANFDETTKQWFISTCGVEGNPGQKTVDNWFKIDKFEKDYKIRFCPTVCnfCKVICRDVGVFV-QDGK 178
Cdd:pfam00197  81 apticVQSTVWKVGDGDPETGRRFVVTGGVVGNPGPDTVSNWFKIEKTGGGYKLVFCPSVC--CKVKCGDVGIFVdDNGN 158

                         170
                  ....*....|....*.
gi 15220874   179 RRLALSDVPLKVMFKR 194
Cdd:pfam00197 159 RRLALSDEPFPVVFKK 174
beta-trefoil_STI_MkMLP-like cd23370
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Murraya koenigii ...
 28-193 1.99e-65

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: 199.08  E-value: 1.99e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  28 PVKDINGKSLLTGVNYYILPVIRGRG-GGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYDKSRTI-PVSTDVNIKFS 105
Cdd:cd23370   1 PVLDINGNKVRTGTEYYIVSAIWGAGgGGLSLFRGRNGTCPLDVIQLRSDLDRGLPLTFSPADYNDGVvYESTDLNIKFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 106 P-------TSIWELANFDETTKQWFISTCGVEGNPGQKTVDNWFKIDKFEKD--YKIRFCPTVCNFCKVICRDVGVFVQD 176
Cdd:cd23370  81 AadalcneSTVWKVDNYDESTGKWFITTGGVEGNPGAQTLLNWFKIEKVGTGntYKIVHCPSVCDSCVTLCNDVGRSSDD 160

                       170
                ....*....|....*...
gi 15220874 177 GKRRLALS-DVPLKVMFK 193
Cdd:cd23370 161 GVRRLALSdDPPFPVVFI 178
beta-trefoil_STI cd00178
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold; The STI-like domain is found ...
 40-194 3.46e-59

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: 182.56  E-value: 3.46e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  40 GVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYD-KSRTIPVSTDVNIKFSPTS-------IWE 111
Cdd:cd00178   1 GVPYYILPAIWGGGGGLTLAKTGNETCPLDVVQSPSDTDNGLPVTFSPANpKDGVIRESTDLNIKFSADTtccaestVWK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 112 LANFDEtTKQWFISTCGVEGNpgqKTVDNWFKIDKFEK--DYKIRFCPTVCNfCKVICRDVGVFVQDGKRRLALS-DVPL 188
Cdd:cd00178  81 VVGDDS-TGGRFVTTGGVKGN---ETLNSWFKIEKAGNgnGYKLVFCPSVCG-CKVVCGDVGIVVDNGNRRLALTeGEPL 155


                ....*.
gi 15220874 189 KVMFKR 194
Cdd:cd00178 156 EVVFKK 161
STI smart00452
Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;
29-195 5.24e-52

Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;


Pssm-ID: 214670  Cd Length: 172  Bit Score: 164.81  E-value: 5.24e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874     29 VKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYDKSRTIP-VSTDVNIKFS-- 105
Cdd:smart00452   1 VLDTDGNPLRNGGTYYILPAIRGHGGGLTLAATGNEICPLTVVQSPNEVDNGLPVKFSPPNPSDFIIrESTDLNIEFDap 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874    106 ----PTSIWELANfDETTKQWFISTCGVEGnpgqkTVDNWFKIDKFEKD---YKIRFCPtvCNFCKVICRDVGVF-VQDG 177
Cdd:smart00452  81 plcaQSTVWTVDE-DSTPGGLAVKTGGYPG-----VNDSWFKIEKYSGEsngYKLVYCP--NGSDDDKCGDVGIFiDPNG 152

                          170
                   ....*....|....*....
gi 15220874    178 KRRLALSDV-PLKVMFKRA 195
Cdd:smart00452 153 GRRLVLSNEnPLVVVFKKA 171
beta-trefoil_STI_AtTPI-like cd23366
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana ...
 5-195 2.89e-42

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: 140.65  E-value: 2.89e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874   5 LYIFLLLAVFIShrgvTTEAAVEPVKDINGKsLLTGVNYYILPVIRG-RGGGLTMSNLKTETCPTSVIQDQFEVSQGLPV 83
Cdd:cd23366   3 FYFLLALTAVLA----ATANAGGAVLDSDGD-IIFNGSYYVLPVIRGtGGGGLTLSGLGSEPCPLYVGQESSEVNEGIPV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  84 KFSPYdKSRT--IPVSTDVNIKFS-------PTSIWELANFDETTKQWFISTcGVEGNPGQKTVDNWFKIDKFEK---DY 151
Cdd:cd23366  78 KFSNW-KSKVgfVPESENLNIEMDvgaticiQSTYWWLGEFDKERKALFVAA-GPKPEGFKDSLKSFFQIKKSEDllgGY 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15220874 152 KIRFCPTvcnfcKVICRDVGVFV-QDGKRRLALSDVPLKVMFKRA 195
Cdd:cd23366 156 KIVFCPS-----DPSCTDVGIFVdENGVRRLALSDKPFEVVFVKA 195
beta-trefoil_STI_KPI104-like cd23367
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Medicago truncatula ...
 27-194 1.35e-41

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: 138.25  E-value: 1.35e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  27 EPVKDINGKSLLTGVNYYILPVIRGRGGGLTMSNlKTETCPTSVIQDQFEVSQGLPVKFSPYDKSRT-IPVSTDVNIKFS 105
Cdd:cd23367   1 PPVLDTNGKPLESGVEYYIKPAITDVGGALTLVN-RNNSCPLYVGQENVTPSSGLPVKFTPFVDGETvVREGRDFTITFQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 106 PTSI------WELANFDETTKQWFISTCGVEGNpgqktvDNWFKIDKF-EKDYKIRFCPT-VCNFCKVICRDVGVFVQDG 177
Cdd:cd23367  80 ASTTcgqsteWRVGERDPVSGRRLITTGGENGY------GNYFRIVRSnRGGYNLRWCPTeVCPNCRFRCGTVGILTENG 153

                       170
                ....*....|....*..
gi 15220874 178 KRRLALSDVPLKVMFKR 194
Cdd:cd23367 154 KRLLALDGPALPVVFER 170
beta-trefoil_STI_WCI3-like cd23362
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus ...
 28-195 3.38e-34

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: 119.26  E-value: 3.38e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  28 PVKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYDKSRTIPVSTDVNIKF--- 104
Cdd:cd23362   1 DVVDTDGNPVENGGTYYILPVIWGKGGGIELAATGNETCPLTVVQSPNEVSKGLPIRISSPLRIAFIPEGLLLRIGFtav 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 105 ---SPTSIWelanfdettkqWFIstcgVEGNPGQK---------TVDNWFKIDK---FEKDYKIRFCPTVcnfcKVICRD 169
Cdd:cd23362  81 ppcAPTPSW-----------WTV----VKGLPEGPavkltgyknTVDGWFKIEKvssDLNSYKLLFCPED----DDSCGD 141

                       170       180
                ....*....|....*....|....*...
gi 15220874 170 VGVFV-QDGKRRLALS-DVPLKVMFKRA 195
Cdd:cd23362 142 IGIHRdDKGNRRLVVTeENPLVVVFQKA 169
beta-trefoil_STI_DrTI cd23376
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Delonix regia ...
 27-192 2.12e-32

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: 114.73  E-value: 2.12e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  27 EPVKDINGKSLLTGVNYYILPVIRG-RGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYD-KSRTIPVSTDVNIKF 104
Cdd:cd23376   1 EKVKDTNGNPLSPGAEYYILPANSGpGGGGLRLGKTGNSTCPLTVLQEYSELFLGLPVKFNVQGsSDGIILTGTPLDIEF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 105 ------SPTSIWELANFDETTKQWfISTCGVEGNPGQKTVDNWFKIDKFEKDYKIRFCPTVCNFckvICRDVGVFVQDGK 178
Cdd:cd23376  81 vekpdcAESSKWVVVKDDFYPTKW-VGIGGGEDHPGKEIVDGVFKIEKYGEGYKLVFCPKGSSG---TCFDIGRYDDVNG 156

                       170
                ....*....|....*.
gi 15220874 179 RRLALSD--VPLKVMF 192
Cdd:cd23376 157 RRLVLENsgTPFEVVF 172
beta-trefoil_STI_LSPI cd23371
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Carica papaya latex ...
 28-196 1.39e-31

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: 112.72  E-value: 1.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  28 PVKDINGKSLLTGVNYYILPVIRGR-GGGLTMSNLKTET-CPTSVIQDQFEVSQGLPVKFSPYD--KSRTIPVSTDVNIK 103
Cdd:cd23371   2 PIVDIDGKPLRYGVDYFVVSAIWGAgGGGLSLYGPGNKKkCPLSVVQDPFDSDNGIPVKFSAVKnvKDNIVRESTDLNVK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 104 FS------PTSIWELaNFDETTKQWFISTCGVEGNPGQKTVDNWFKIDK---FEKDYKIRFCPTVCNFCKVICRDVGVFV 174
Cdd:cd23371  82 FNitincnETTVWKV-DRFPGVIGWTVTLGGVKGYHGFESTHSMFKIKRaglVSFSYKFRFCPSYPRTRLIPCNNVGVFS 160

                       170       180
                ....*....|....*....|...
gi 15220874 175 -QDGKRRLALSDVPLKVMFKRAY 196
Cdd:cd23371 161 dKYRIRRLVLTDDAKEFVFVKAN 183
beta-trefoil_STI_CrataBL-like cd23374
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Crateva tapia bark ...
 37-194 1.94e-31

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: 111.81  E-value: 1.94e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  37 LLTGVNYYILPVIRGRGGGLTMSNLKTET---CPTSVIQDQFEVSQGLPVKFSPYD-KSRTIPVSTDVNIKFSPTS---- 108
Cdd:cd23374   2 VLAGVPYYILPAKIGTGGGLIPSNRRKNTqqlCPLDIVQSQFPFVLGVPVTFTPLNsKLKVVPLSTNLNIEFDSDVwlcp 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 109 ---IWELANFdettkQW----FISTCGVEGNPgqktvDNWFKIDKFEKDYKIRFCPTvcnfcKVICRDVGVFVQD-GKRR 180
Cdd:cd23374  82 eskVWTVDSS-----QWlrgsYVSTGGEKGSG-----GSWFRIERDGDSYKLVHCPR-----GTSCRDVGIETDGgGVRR 146

                       170
                ....*....|....
gi 15220874 181 LALSDVPLKVMFKR 194
Cdd:cd23374 147 LVLGDRPLAVKFQK 160
beta-trefoil_STI_MP4-like cd23377
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Mucuna pruriens MP-4 ...
 26-195 3.60e-31

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: 111.60  E-value: 3.60e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  26 VEPVKDINGKSLLTGVNYYILPVIRG-RGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFS-PYDKSRTIPVSTDVNIK 103
Cdd:cd23377   1 VEQVRDTNGNPIFPGGRYYIMPAIFGpAGGGVKLGKTGNSTCPVTVLQDYSEVVNGLPVKFTiPGISPGIIFTGTPLDIE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 104 FS------PTSIWELANFDETTKQWfISTCGVEGNPGQKTVDNWFKIDKFEKD--YKIRFCPTVCNfcKVICRDVGVFVQ 175
Cdd:cd23377  81 FTkkpncaESSKWLVFVDDFIPKAC-VGIGGPEDHPGKQILSGKFNIQKYGSGngYKLVFCPDGSA--PGNCSDIGRYDN 157

                       170       180
                ....*....|....*....|..
gi 15220874 176 DGK-RRLALS-DVPLKVMFKRA 195
Cdd:cd23377 158 EEGgRRLVLTeDEPFEVVFVDA 179
beta-trefoil_STI_ASI cd23373
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in alpha-amylase ...
 25-194 1.20e-30

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: 110.15  E-value: 1.20e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  25 AVEPVKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPY----DKSRTIPVSTDV 100
Cdd:cd23373   1 APQPVYDTDGHELSSDASYYVLPANRGHGGGLTMAPGWLRRCPLFVSQEPDEALVGFPVRFTPLgnssSSDAAIRLSTDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 101 NIKFSPTSI------WELANFDETTKQwFISTCGVEG--NPGQKTVdnwFKIDKF---EKDYKIRFCPTVCNfckviCRD 169
Cdd:cd23373  81 RIEFRAITTcvqsleWHVSSEPSTGRR-HVAAGPVEGpsPPGREFV---FRVERYsgaEKGYKLVSCGDKDP-----CRD 151

                       170       180
                ....*....|....*....|....*
gi 15220874 170 VGVFVQDGKRRLALSDVPLKVMFKR 194
Cdd:cd23373 152 LGLYRDKKKWWLTVSDPPHVVVFKK 176
beta-trefoil_STI_LlTI-like cd23365
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Leucaena leucocephala ...
 29-195 5.27e-30

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: 108.36  E-value: 5.27e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  29 VKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYDKSRTIPVSTDVNIKFSP-- 106
Cdd:cd23365   2 LLDTDGDPLNNGGQYYILPALRGKGGGLELARTGDETCPLTVVQARSETSRGLPVRISSPPRIAIITTAFYLNIEFQPap 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 107 -----TSIWELANFDETTKQwfistcgVEGNPGQKTVDNWFKIDKFEKDYKIRFCPTVCNFCKviCRDVGVFVQD-GKRR 180
Cdd:cd23365  82 aclpkPLRWRIEQESSSEGE-------VKIAPDEERLFGPFQIKPYREDYKLVYCESSSDDDS--CRDLGISIDDeNNRR 152

                       170
                ....*....|....*.
gi 15220874 181 LALSD-VPLKVMFKRA 195
Cdd:cd23365 153 LVVKDgDPLAVRFKKA 168
beta-trefoil_STI_GWIN3 cd23380
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Populus sp. ...
 29-193 5.69e-29

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: 105.67  E-value: 5.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  29 VKDINGKSLLTGVNYYILPVIRGRGGGltMSNLKTETCPTSVIQDQFevSQGLPVKFSPYDKSR--TIPVSTDVNIKFSP 106
Cdd:cd23380   4 VLDFNGNEVLAGAYYYIAPEDSLPFLV--VAAIRPGTCWSDVILERF--LDGLPIKFSPVAPSNdsVIRESTYLNIEFNA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 107 --------TSIWElANFDETTKQWFISTCGVEGNpgqktvdNWFKIDKFEKD---YKIRFCPTVCNFCKviCRDVGVFVQ 175
Cdd:cd23380  80 elckvcgvTTMWK-VEFNATMQQPFVTTGGVDRL-------NWFKITKAEEDnrfYQLSYCPVSGIQCP--CVTVGISNR 149

                       170
                ....*....|....*...
gi 15220874 176 DGKRRLALSDVPLKVMFK 193
Cdd:cd23380 150 NGTERLALNDEPLPFVFR 167
beta-trefoil_STI_API-A-like cd23381
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Sagittaria ...
 31-194 2.57e-27

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Sagittaria sagittifolia proteinase inhibitor A (API-A) and similar proteins; API-A, also called double-headed proteinase inhibitor A, inhibits an equimolar amount of trypsin and chymotrypsin simultaneously, and inhibits kallikrein weakly. It possesses two distinct reactive sites, unlike other members of their family. API-A contains 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: 467406  Cd Length: 188  Bit Score: 101.96  E-value: 2.57e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  31 DINGKSLLTGVNYYILPV----IRGRGGGLTMSnlKTETCPTSVIQDQFEVSQGLPVKFSPYDKSRT-IPVSTDVNIKFS 105
Cdd:cd23381   1 DIDGNQLNAGSNYYLVTIqsaaIGFRGGLSTLR--LDGTCPSYVGQAPSDVDRGLPVSFSPAATSQPvVQLSSRLNISFS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 106 PT------SIWELANFDETTKQWFisTCGVEGNPGQKTVDNWFKIDKFEKD--YKIRFCPTV---------------CNF 162
Cdd:cd23381  79 MSvpcinsTVWSLGKSETNGGIST--QNITIGDYGYLNFFSWFEIESTEETgvYKLVACSCEqaigpfdvsdmgasrSGF 156

                       170       180       190
                ....*....|....*....|....*....|..
gi 15220874 163 CKVICRDVGVFVQDGKRRLALSDVPLKVMFKR 194
Cdd:cd23381 157 CKIGCPEVGSFNVGGQTLLGLSPEHFLVVFKK 188
beta-trefoil_STI_CPI-like cd23372
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Solanum tuberosum ...
 40-195 6.32e-25

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: 95.18  E-value: 6.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  40 GVNYYILPVIRGRGGG---LTMSNLKTETCPTSVIQDQFEVSQ-GLPVKFSPYDK-SRTIPVSTDVNIKFS-PTS----- 108
Cdd:cd23372   1 GESYRIISILWGALGGdvyLGKIPNSDAPCPNGVFQYNSDVGPsGTPVRFIPLSEySGVIFENQDLNIQFSiPTSklcvn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 109 --IWELANFDETTKQWFISTCGVEGNPgqktVDNWFKIDKFEKD---YKIRFCP--TVCNFCKVICRDVGVFVQDGKRRL 181
Cdd:cd23372  81 ytVWKVGDENASLGTMLLETGGTIGQA----DSSWFKIVKSSLMkfgYKLLYCPstSICPRDDLFCADVGVVFQNGYRRL 156

                       170
                ....*....|....*
gi 15220874 182 AL-SDVPLKVMFKRA 195
Cdd:cd23372 157 ALvNDNPLDVVFQKV 171
beta-trefoil_STI_SKTI cd23363
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in the soybean Kunitz ...
 29-194 2.46e-23

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: 91.38  E-value: 2.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  29 VKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYDKSRTIPVSTDVNIKFSPTS 108
Cdd:cd23363   3 VLDTDGNPLQNGGTYYVLPVIRGAGGGIRVAPTGNERCPLTVVQSRNELDKGIGTIISSPYRIRFIAEGHPLSIKFDSFA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 109 IWELANfdETTKQWFIstcgVEGNPG---------QKTVDNWFKIDKFEKD----YKIRFCPTVCNFCKviCRDVGVFVQ 175
Cdd:cd23363  83 VIPLCV--PIPTEWSV----VEDLPEgpavkigenKNAVDGWFRIERVSDDefngYKLVFCPQQAEDDK--CGDIGISID 154

                       170       180
                ....*....|....*....|.
gi 15220874 176 D-GKRRLALS-DVPLKVMFKR 194
Cdd:cd23363 155 DdGIRRLVVSkNKPLVVQFQK 175
beta-trefoil_STI_SPOR cd23368
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Ipomoea batatas ...
 28-194 2.49e-20

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: 83.56  E-value: 2.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  28 PVKDINGKSLLTGVNYYILPVIRG-RGGGLTMSNLK-TETCPTSVIQDQFEvSQGLPVKFSPYDKSRT-IPVSTDVNIKF 104
Cdd:cd23368   2 PVLDTDGDELRAGGTYYITSATWGaGGGGVRLVRLDsTTKCPSDVIISRSL-DDGDPITITPADPNATvVLPSTFQSFKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 105 S-PTSI-------WElANFDETTKQWFISTcG--VEGNPGQktvdnwFKIDKFEKD---YKIRFCPtvcnFCKVICRDVG 171
Cdd:cd23368  81 NiPTNPlcvnnvyWG-IQYDPESGQYFVKA-GefVSNNSNQ------FKIEVVPDNlnaYKITYCP----FGSDKCYNVG 148

                       170       180
                ....*....|....*....|....*.
gi 15220874 172 VFV--QDGKRRLALSDV-PLKVMFKR 194
Cdd:cd23368 149 TYYdpLLRATRLALSDDsPFVVVFKK 174
beta-trefoil_STI_WSCP_II cd23360
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in class II ...
 27-153 3.33e-17

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: 75.18  E-value: 3.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  27 EPVKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTET-CPTSVIQDQFEVSQGLPVKFS-PYDK-SRTIPVSTDVNIK 103
Cdd:cd23360   1 EPVKDTAGNPLKTGAQYFIQPVKTNNGGGLVPAAIDLLPlCPLGITQTLLPYQPGLPVSFSlPLSSvGNTVRTSTDVNIE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220874 104 FSPtSIWELANfdETTKQWFI---STCGVE------GNPGQKTvdNWFKIDKFEK---DYKI 153
Cdd:cd23360  81 FKS-PIWPVCK--EFSKLWAVdssSSAPKEpaiiigGKPGSRN--SLFKIEKAGGganTYKL 137
beta-trefoil_STI_AtKTI6-like cd23369
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana ...
 27-155 1.76e-08

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: 51.62  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  27 EPVKDINGKSLLTGVNYYILPV-IRGRGGGLTMSNLKTE-TCPTSVI-QDQFEVSQGLPVKFSPYDKSRT-IPVSTDVNI 102
Cdd:cd23369   4 EVVLDTNGNPVKPGAPYYILDAtNYGRGISRSQVGPDDPnPCPQTVVlGSDPLISAPPPVAFVLESSSDDvVRVSTELSI 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220874 103 KFSPTS------IWELANFDETTKQWFIStcgvegnpGQK-TVDNWFKIDKF-EKDYKIRF 155
Cdd:cd23369  84 RFAEPShcaesgYWRVANSSSPKKEVVLT--------GSKsSNDSTFTIKKSdDGYYKFAF 136
beta-trefoil_STI_BbKI-like cd23364
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides ...
 29-157 2.04e-07

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: 48.47  E-value: 2.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  29 VKDINGKSLLTGVN-YYILPVIRGRGGgLTMSNLKTETCPTSVIQDQFEvSQGLPVKFSPYDKSRTIPVSTDVNIKFSPT 107
Cdd:cd23364   3 VVDTNGQPVSNGADaYYLVPVSHGHAG-LALAKIGNEAEPRAVVLDPHH-RPGLPVRFESPLRINIIKESYFLNIKFGPS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15220874 108 S----IWELanfdetTKQWFISTCGVEGNpgQKTVDNWFKIDKFEKDYKIRFCP 157
Cdd:cd23364  81 SsdsgVWDV------IQQDPIGLAVKVTD--TKSLLGPFKVEKEGEGYKIVYYP 126
beta-trefoil_STI_AMTIN cd23378
Alocasia macrorrhizos trypsin/chymotrypsin inhibitor (AMTIN) and similar proteins; AMTIN, also ...
 27-168 2.75e-05

Alocasia macrorrhizos trypsin/chymotrypsin inhibitor (AMTIN) and similar proteins; AMTIN, also called alocasin, is a multi-functional inhibitor that shows inhibition against proteases, amylases, and subtilisin. It inhibits the proteases, trypsin and chymotrypsin, and alpha-amylase. It also has antifungal activity against midgut proteases of Aedes aegypti. 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: 467403  Cd Length: 182  Bit Score: 43.01  E-value: 2.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  27 EPVKDINGKSLLTGVNYYILPVIRgRGGGLTMSNLKTeTCPTSVIQDQFEVSQGLPVKFSPYD-KSRTIPVSTDVNIKF- 104
Cdd:cd23378   1 NPVLDVDGNELQRGQLYYATSVMR-PGSGLTLAAPSG-SCPLNVAQAPFNDYSGRPLAFFPENaDDDTVQEGSTLYIMFp 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220874 105 SPTSIWELANFDETTKQWFISTcgveGNPGQKTV---DNWFKIDK------FEKDYKIRFCPTVCNFCKVICR 168
Cdd:cd23378  79 EPTECPQSTVWTLDREAGFVTT----GGTSSKAIgphNSRFAIRRagdassQPRDYQIEVCPCSTGVERPSCR 147
beta-trefoil_STI_COTI cd23379
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Senna obtusifolia ...
 29-192 6.81e-05

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: 41.69  E-value: 6.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  29 VKDINGKSLLTGVNYYILPVirGRGGGLTMSNLK---TETCPTSVIQDqfEVSQGLPVKFSPYDKSRTIPVSTDVNIKFS 105
Cdd:cd23379   2 VYDSDGDILRNGGKYFISPP--NGGGAILAAAIShgsDRSCSLAVIQA--LSYIGWPVTISTPFPPTFITTSFPLNISFA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 106 PTSiwelANFDETTKQWFISTCGVEGNP---GQKT-----VDNWFKIDKFEKD---YKIRFCPTVCNFckviCRDVGV-F 173
Cdd:cd23379  78 YLP----PNVCTKSPDWVVVKSNPLGEPvmvGDFEefdnpVSGYFYIKSYDSSkgyYKLVFCYGGDDS----CGNIGVdK 149

                       170       180
                ....*....|....*....|.
gi 15220874 174 VQDGKRRLALSD--VPLKVMF 192
Cdd:cd23379 150 DSNGFRRLVVTDdrEPLVFKF 170
beta-trefoil_STI_WBA1 cd23361
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus ...
 25-194 1.93e-04

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: 40.55  E-value: 1.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874  25 AVEPVKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEvsqglpVKFSPYDKSR-TIPVSTDV--- 100
Cdd:cd23361   1 ADDPVYDAEGNKLVNRGKYTIVSFSDGAGIDVVATGNENPEDPLSIVKSTRN------IMYATSISSEdKTPPQPRNile 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220874 101 NIKFSptsiWELANFDETTKQWFISTCGVEG---------NPGQKTVDNWFKIDKFEKDYKIRFCPTVCNfckviCRDVG 171
Cdd:cd23361  75 NMRLK----INFATDPHKGDVWSVVDFQPDGqqlklagryPNQVKGAFTIQKGSNTPRTYKLLFCPVGSP-----CKNIG 145

                       170       180
                ....*....|....*....|....*.
gi 15220874 172 -VFVQDGKRRLALSDV--PLKVMFKR 194
Cdd:cd23361 146 iSTDPEGKKRLVVSYQsdPLVVKFHR 171
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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