NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|254616|gb|AAB23101|]
View 

bifunctional subtilisin/alpha-amylase inhibitor, RASI [Oryza sativa=rice, seeds, bran, Peptide, 176 aa]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_STI_ASI cd23373
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in alpha-amylase ...
 1-171 5.74e-94

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: 270.40  E-value: 5.74e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     1 APPPVYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWGGAAS-PRTLRVSTDV 79
Cdd:cd23373   1 APQPVYDTDGHELSSDASYYVLPANRGHGGGLTMAPGWLRRCPLFVSQEPDEALVGFPVRFTPLGNSSSsDAAIRLSTDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    80 RIRFNAATLCVQSTEWHVGDEPLTGARRVVTGPLIGPSPSGRENAFRVEKYGG---GYKLVSCRD--SCQDLGVSRDgAG 154
Cdd:cd23373  81 RIEFRAITTCVQSLEWHVSSEPSTGRRHVAAGPVEGPSPPGREFVFRVERYSGaekGYKLVSCGDkdPCRDLGLYRD-KK 159

                       170
                ....*....|....*..
gi 254616   155 AAWIGASQPPHVVVFKK 171
Cdd:cd23373 160 KWWLTVSDPPHVVVFKK 176
 
Name Accession Description Interval E-value
beta-trefoil_STI_ASI cd23373
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in alpha-amylase ...
 1-171 5.74e-94

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: 270.40  E-value: 5.74e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     1 APPPVYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWGGAAS-PRTLRVSTDV 79
Cdd:cd23373   1 APQPVYDTDGHELSSDASYYVLPANRGHGGGLTMAPGWLRRCPLFVSQEPDEALVGFPVRFTPLGNSSSsDAAIRLSTDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    80 RIRFNAATLCVQSTEWHVGDEPLTGARRVVTGPLIGPSPSGRENAFRVEKYGG---GYKLVSCRD--SCQDLGVSRDgAG 154
Cdd:cd23373  81 RIEFRAITTCVQSLEWHVSSEPSTGRRHVAAGPVEGPSPPGREFVFRVERYSGaekGYKLVSCGDkdPCRDLGLYRD-KK 159

                       170
                ....*....|....*..
gi 254616   155 AAWIGASQPPHVVVFKK 171
Cdd:cd23373 160 KWWLTVSDPPHVVVFKK 176
Kunitz_legume pfam00197
Trypsin and protease inhibitor;
5-171 5.51e-66

Trypsin and protease inhibitor;


Pssm-ID: 395144  Cd Length: 174  Bit Score: 199.45  E-value: 5.51e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616       5 VYDTEGHELSADGSYYVLPA-SPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWGgaASPRTLRVSTDVRIRF 83
Cdd:pfam00197   1 VLDTDGNPLRAGVEYYILPAiGGGSGGGLTLASRGNGTCPLDVVQEPSEVSKGLPVKFSPSN--SKKGVIRESTDLNIEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616      84 N-AATLCVQSTEWHVGD-EPLTGARRVVTGPLIG-PSPSGRENAFRVEKYGGGYKLVSC-----RDSCQDLGVSRDGAGA 155
Cdd:pfam00197  79 FsAPTICVQSTVWKVGDgDPETGRRFVVTGGVVGnPGPDTVSNWFKIEKTGGGYKLVFCpsvccKVKCGDVGIFVDDNGN 158

                         170
                  ....*....|....*.
gi 254616     156 AWIGASQPPHVVVFKK 171
Cdd:pfam00197 159 RRLALSDEPFPVVFKK 174
STI smart00452
Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;
5-173 2.12e-63

Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;


Pssm-ID: 214670  Cd Length: 172  Bit Score: 192.93  E-value: 2.12e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616        5 VYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWggAASPRTLRVSTDVRIRFN 84
Cdd:smart00452   1 VLDTDGNPLRNGGTYYILPAIRGHGGGLTLAATGNEICPLTVVQSPNEVDNGLPVKFSPP--NPSDFIIRESTDLNIEFD 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616       85 AATLCVQSTEWHVGDEPLTGARRVVTgpliGPSPSGRENAFRVEKYGG---GYKLVSC-----RDSCQDLGVSRDGAGAA 156
Cdd:smart00452  79 APPLCAQSTVWTVDEDSTPGGLAVKT----GGYPGVNDSWFKIEKYSGesnGYKLVYCpngsdDDKCGDVGIFIDPNGGR 154

                          170
                   ....*....|....*...
gi 254616      157 WIGAS-QPPHVVVFKKAR 173
Cdd:smart00452 155 RLVLSnENPLVVVFKKAD 172
 
Name Accession Description Interval E-value
beta-trefoil_STI_ASI cd23373
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in alpha-amylase ...
 1-171 5.74e-94

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: 270.40  E-value: 5.74e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     1 APPPVYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWGGAAS-PRTLRVSTDV 79
Cdd:cd23373   1 APQPVYDTDGHELSSDASYYVLPANRGHGGGLTMAPGWLRRCPLFVSQEPDEALVGFPVRFTPLGNSSSsDAAIRLSTDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    80 RIRFNAATLCVQSTEWHVGDEPLTGARRVVTGPLIGPSPSGRENAFRVEKYGG---GYKLVSCRD--SCQDLGVSRDgAG 154
Cdd:cd23373  81 RIEFRAITTCVQSLEWHVSSEPSTGRRHVAAGPVEGPSPPGREFVFRVERYSGaekGYKLVSCGDkdPCRDLGLYRD-KK 159

                       170
                ....*....|....*..
gi 254616   155 AAWIGASQPPHVVVFKK 171
Cdd:cd23373 160 KWWLTVSDPPHVVVFKK 176
Kunitz_legume pfam00197
Trypsin and protease inhibitor;
5-171 5.51e-66

Trypsin and protease inhibitor;


Pssm-ID: 395144  Cd Length: 174  Bit Score: 199.45  E-value: 5.51e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616       5 VYDTEGHELSADGSYYVLPA-SPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWGgaASPRTLRVSTDVRIRF 83
Cdd:pfam00197   1 VLDTDGNPLRAGVEYYILPAiGGGSGGGLTLASRGNGTCPLDVVQEPSEVSKGLPVKFSPSN--SKKGVIRESTDLNIEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616      84 N-AATLCVQSTEWHVGD-EPLTGARRVVTGPLIG-PSPSGRENAFRVEKYGGGYKLVSC-----RDSCQDLGVSRDGAGA 155
Cdd:pfam00197  79 FsAPTICVQSTVWKVGDgDPETGRRFVVTGGVVGnPGPDTVSNWFKIEKTGGGYKLVFCpsvccKVKCGDVGIFVDDNGN 158

                         170
                  ....*....|....*.
gi 254616     156 AWIGASQPPHVVVFKK 171
Cdd:pfam00197 159 RRLALSDEPFPVVFKK 174
STI smart00452
Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;
5-173 2.12e-63

Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;


Pssm-ID: 214670  Cd Length: 172  Bit Score: 192.93  E-value: 2.12e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616        5 VYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWggAASPRTLRVSTDVRIRFN 84
Cdd:smart00452   1 VLDTDGNPLRNGGTYYILPAIRGHGGGLTLAATGNEICPLTVVQSPNEVDNGLPVKFSPP--NPSDFIIRESTDLNIEFD 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616       85 AATLCVQSTEWHVGDEPLTGARRVVTgpliGPSPSGRENAFRVEKYGG---GYKLVSC-----RDSCQDLGVSRDGAGAA 156
Cdd:smart00452  79 APPLCAQSTVWTVDEDSTPGGLAVKT----GGYPGVNDSWFKIEKYSGesnGYKLVYCpngsdDDKCGDVGIFIDPNGGR 154

                          170
                   ....*....|....*...
gi 254616      157 WIGAS-QPPHVVVFKKAR 173
Cdd:smart00452 155 RLVLSnENPLVVVFKKAD 172
beta-trefoil_STI_VvMLP-like cd23375
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Vitis vinifera ...
 1-171 1.63e-48

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: 155.07  E-value: 1.63e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     1 APPPVYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPwggaASPR--TLRVSTD 78
Cdd:cd23375   1 APEPVLDTAGKILRTGVNYYILPVNRGRGGGLTLASTGNETCPLDVVQEQNEVNNGLPLTFSP----VNPKkgVIRVSTD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    79 VRIRFNAATLCVQSTEWHVGD-EPLTGARRVVTGPLIGpSPsGRE---NAFRVEKYGGGYKLV-------SCRDSCQDLG 147
Cdd:cd23375  77 LNIKFSASTSCPESTVWKLDDyDESTGQYFVTTGGVEG-NP-GREtirNWFKIEKYEDGYKLVycpsvcnYCKVICKDVG 154

                       170       180
                ....*....|....*....|....
gi 254616   148 VSRDGaGAAWIGASQPPHVVVFKK 171
Cdd:cd23375 155 IYIDN-GVRRLALSDKPLKVKFKK 177
beta-trefoil_STI cd00178
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold; The STI-like domain is found ...
 16-171 3.25e-44

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: 143.65  E-value: 3.25e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    16 DGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWggAASPRTLRVSTDVRIRFNAAT-LCVQSTE 94
Cdd:cd00178   1 GVPYYILPAIWGGGGGLTLAKTGNETCPLDVVQSPSDTDNGLPVTFSPA--NPKDGVIRESTDLNIKFSADTtCCAESTV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    95 WHVGDEPLTGARRVVTGPLIGPSPsgRENAFRVEKYG--GGYKLV------SCRDSCQDLGVSRDGaGAAWIGASQ-PPH 165
Cdd:cd00178  79 WKVVGDDSTGGRFVTTGGVKGNET--LNSWFKIEKAGngNGYKLVfcpsvcGCKVVCGDVGIVVDN-GNRRLALTEgEPL 155


                ....*.
gi 254616   166 VVVFKK 171
Cdd:cd00178 156 EVVFKK 161
beta-trefoil_STI_AtTPI-like cd23366
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana ...
 4-172 8.41e-36

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: 123.31  E-value: 8.41e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     4 PVYDTEGHELSaDGSYYVLPASPGH-GGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWGGAAS--PRT--LRVSTD 78
Cdd:cd23366  22 AVLDSDGDIIF-NGSYYVLPVIRGTgGGGLTLSGLGSEPCPLYVGQESSEVNEGIPVKFSNWKSKVGfvPESenLNIEMD 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    79 VrirfnAATLCVQSTEWHVG-DEPLTGARRVVTGPLIGPSPSGRENAFRVEK---YGGGYKLVSC--RDSCQDLGVSRDG 152
Cdd:cd23366 101 V-----GATICIQSTYWWLGeFDKERKALFVAAGPKPEGFKDSLKSFFQIKKsedLLGGYKIVFCpsDPSCTDVGIFVDE 175

                       170       180
                ....*....|....*....|
gi 254616   153 AGAAWIGASQPPHVVVFKKA 172
Cdd:cd23366 176 NGVRRLALSDKPFEVVFVKA 195
beta-trefoil_STI_MkMLP-like cd23370
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Murraya koenigii ...
 4-171 1.96e-31

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: 111.64  E-value: 1.96e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     4 PVYDTEGHELSADGSYYVLPASPGHG-GGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWGgaASPRTLRVSTDVRIR 82
Cdd:cd23370   1 PVLDINGNKVRTGTEYYIVSAIWGAGgGGLSLFRGRNGTCPLDVIQLRSDLDRGLPLTFSPAD--YNDGVVYESTDLNIK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    83 FNAAT-LCVQSTEWHVGD-EPLTGARRVVTGPLIG-PSPSGRENAFRVEKYGGG--YKLV-------SCRDSCQDLGVSR 150
Cdd:cd23370  79 FSAADaLCNESTVWKVDNyDESTGKWFITTGGVEGnPGAQTLLNWFKIEKVGTGntYKIVhcpsvcdSCVTLCNDVGRSS 158

                       170       180
                ....*....|....*....|.
gi 254616   151 DGAGAAWIGASQPPHVVVFKK 171
Cdd:cd23370 159 DDGVRRLALSDDPPFPVVFIK 179
beta-trefoil_STI_KPI104-like cd23367
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Medicago truncatula ...
 3-150 6.59e-31

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: 110.13  E-value: 6.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     3 PPVYDTEGHELSADGSYYVLPASPGHGGGLTMApRRVIPCPLLVAQETDERRKGFPVRFTPWggAASPRTLRVSTDVRIR 82
Cdd:cd23367   1 PPVLDTNGKPLESGVEYYIKPAITDVGGALTLV-NRNNSCPLYVGQENVTPSSGLPVKFTPF--VDGETVVREGRDFTIT 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254616    83 FNAATLCVQSTEWHVGD-EPLTGARRVVTGpligpSPSGRENAFRVEK-YGGGYKLV--------SCRDSCQDLGVSR 150
Cdd:cd23367  78 FQASTTCGQSTEWRVGErDPVSGRRLITTG-----GENGYGNYFRIVRsNRGGYNLRwcptevcpNCRFRCGTVGILT 150
beta-trefoil_STI_DrTI cd23376
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Delonix regia ...
 4-154 1.43e-26

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: 98.94  E-value: 1.43e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     4 PVYDTEGHELSADGSYYVLPASPG-HGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTPWGGaaSPRTLRVSTDVRIR 82
Cdd:cd23376   2 KVKDTNGNPLSPGAEYYILPANSGpGGGGLRLGKTGNSTCPLTVLQEYSELFLGLPVKFNVQGS--SDGIILTGTPLDIE 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254616    83 FNAATLCVQSTEWH-VGDEPLTGARRVVTGPLIGPSPSGRENAFRVEKYGGGYKLVSCRDS----CQDLGVSRDGAG 154
Cdd:cd23376  80 FVEKPDCAESSKWVvVKDDFYPTKWVGIGGGEDHPGKEIVDGVFKIEKYGEGYKLVFCPKGssgtCFDIGRYDDVNG 156
beta-trefoil_STI_WCI3-like cd23362
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus ...
 4-172 1.97e-23

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: 90.75  E-value: 1.97e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     4 PVYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFtpwggaASP-RTLRVSTD--VR 80
Cdd:cd23362   1 DVVDTDGNPVENGGTYYILPVIWGKGGGIELAATGNETCPLTVVQSPNEVSKGLPIRI------SSPlRIAFIPEGllLR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    81 IRFNAATLCV-QSTEWH-VGDEP------LTGARRVVTGPligpspsgrenaFRVEKYGG---GYKLVSC---RDSCQDL 146
Cdd:cd23362  75 IGFTAVPPCApTPSWWTvVKGLPegpavkLTGYKNTVDGW------------FKIEKVSSdlnSYKLLFCpedDDSCGDI 142

                       170       180
                ....*....|....*....|....*..
gi 254616   147 GVSRDGAGAAWIGASQP-PHVVVFKKA 172
Cdd:cd23362 143 GIHRDDKGNRRLVVTEEnPLVVVFQKA 169
beta-trefoil_STI_LlTI-like cd23365
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Leucaena leucocephala ...
 5-172 2.56e-22

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: 87.94  E-value: 2.56e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     5 VYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFtpwggAASPRTLRVSTDVR--IR 82
Cdd:cd23365   2 LLDTDGDPLNNGGQYYILPALRGKGGGLELARTGDETCPLTVVQARSETSRGLPVRI-----SSPPRIAIITTAFYlnIE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    83 FNAATLCVQST-EWHV-GDEPLTGARRvvtgplIGPSPSGRENAFRVEKYGGGYKLVSC-----RDSCQDLGVSRDGAG- 154
Cdd:cd23365  77 FQPAPACLPKPlRWRIeQESSSEGEVK------IAPDEERLFGPFQIKPYREDYKLVYCesssdDDSCRDLGISIDDENn 150

                       170
                ....*....|....*...
gi 254616   155 AAWIGASQPPHVVVFKKA 172
Cdd:cd23365 151 RRLVVKDGDPLAVRFKKA 168
beta-trefoil_STI_API-A-like cd23381
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Sagittaria ...
 7-171 6.41e-22

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: 87.33  E-value: 6.41e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     7 DTEGHELSADGSYYVLP---ASPGHGGGLTMAPRRVIpCPLLVAQETDERRKGFPVRFTPwgGAASPRTLRVSTDVRIRF 83
Cdd:cd23381   1 DIDGNQLNAGSNYYLVTiqsAAIGFRGGLSTLRLDGT-CPSYVGQAPSDVDRGLPVSFSP--AATSQPVVQLSSRLNISF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    84 NAATLCVQSTEWHVGDEPLTGARRVVTGPLIGPSPSGRENAFRVEKYG--GGYKLVSC---------------------- 139
Cdd:cd23381  78 SMSVPCINSTVWSLGKSETNGGISTQNITIGDYGYLNFFSWFEIESTEetGVYKLVACsceqaigpfdvsdmgasrsgfc 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 254616   140 RDSCQDLGVSRDGaGAAWIGASQPPHVVVFKK 171
Cdd:cd23381 158 KIGCPEVGSFNVG-GQTLLGLSPEHFLVVFKK 188
beta-trefoil_STI_CrataBL-like cd23374
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Crateva tapia bark ...
 19-171 3.25e-19

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: 79.45  E-value: 3.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    19 YYVLPASPGHGGGLTMAPRRVI---PCPLLVAQETDERRKGFPVRFTPWGGAAspRTLRVSTDVRIRFNAAT-LCVQSTE 94
Cdd:cd23374   8 YYILPAKIGTGGGLIPSNRRKNtqqLCPLDIVQSQFPFVLGVPVTFTPLNSKL--KVVPLSTNLNIEFDSDVwLCPESKV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    95 WHVGDEPLTGARRVVTGPLIGpspsgRENA-FRVEKYGGGYKLVSCRD--SCQDLGVSRDGAGAAWIGASQPPHVVVFKK 171
Cdd:cd23374  86 WTVDSSQWLRGSYVSTGGEKG-----SGGSwFRIERDGDSYKLVHCPRgtSCRDVGIETDGGGVRRLVLGDRPLAVKFQK 160
beta-trefoil_STI_SKTI cd23363
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in the soybean Kunitz ...
 5-171 8.22e-17

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: 73.66  E-value: 8.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     5 VYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFtpwggaASPRTLRVSTD---VRI 81
Cdd:cd23363   3 VLDTDGNPLQNGGTYYVLPVIRGAGGGIRVAPTGNERCPLTVVQSRNELDKGIGTII------SSPYRIRFIAEghpLSI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    82 RFN---AATLCVqstewhvgdePLTGARRVVTGPLIGPSP--SGRENA----FRVEK----YGGGYKLVSC-----RDSC 143
Cdd:cd23363  77 KFDsfaVIPLCV----------PIPTEWSVVEDLPEGPAVkiGENKNAvdgwFRIERvsddEFNGYKLVFCpqqaeDDKC 146

                       170       180
                ....*....|....*....|....*....
gi 254616   144 QDLGVSRDGAGAAWIGASQ-PPHVVVFKK 171
Cdd:cd23363 147 GDIGISIDDDGIRRLVVSKnKPLVVQFQK 175
beta-trefoil_STI_WSCP_II cd23360
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in class II ...
 4-138 3.99e-16

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: 71.71  E-value: 3.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     4 PVYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIP-CPLLVAQETDERRKGFPVRF-TPWGGAASprTLRVSTDVRI 81
Cdd:cd23360   2 PVKDTAGNPLKTGAQYFIQPVKTNNGGGLVPAAIDLLPlCPLGITQTLLPYQPGLPVSFsLPLSSVGN--TVRTSTDVNI 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254616    82 RFNAAT--LCVQSTE-WHV------GDEPLTgarrvvtgpLIGPSPSGRENAFRVEKYGGG---YKLVS 138
Cdd:cd23360  80 EFKSPIwpVCKEFSKlWAVdssssaPKEPAI---------IIGGKPGSRNSLFKIEKAGGGantYKLTT 139
beta-trefoil_STI_SPOR cd23368
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Ipomoea batatas ...
 3-171 7.53e-16

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: 71.24  E-value: 7.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     3 PPVYDTEGHELSADGSYYVLPASPGHG-GGLTMAPRRVIP-CP--LLVAQETDerrKGFPVRFTPWGGAASprTLRVSTD 78
Cdd:cd23368   1 TPVLDTDGDELRAGGTYYITSATWGAGgGGVRLVRLDSTTkCPsdVIISRSLD---DGDPITITPADPNAT--VVLPSTF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    79 VRIRFNAAT--LCVQSTEWHVGDEPLTGARRVVTGPLIGPSPsgreNAFRVEKYGGG---YKLVSC---RDSCQDLGVSR 150
Cdd:cd23368  76 QSFKFNIPTnpLCVNNVYWGIQYDPESGQYFVKAGEFVSNNS----NQFKIEVVPDNlnaYKITYCpfgSDKCYNVGTYY 151

                       170       180
                ....*....|....*....|....*..
gi 254616   151 DgagaAWIGAS------QPPHVVVFKK 171
Cdd:cd23368 152 D----PLLRATrlalsdDSPFVVVFKK 174
beta-trefoil_STI_MP4-like cd23377
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Mucuna pruriens MP-4 ...
 4-172 3.63e-15

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: 69.23  E-value: 3.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     4 PVYDTEGHELSADGSYYVLPASPG-HGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRFTpwGGAASPRTLRVSTDVRIR 82
Cdd:cd23377   3 QVRDTNGNPIFPGGRYYIMPAIFGpAGGGVKLGKTGNSTCPVTVLQDYSEVVNGLPVKFT--IPGISPGIIFTGTPLDIE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    83 FNAATLCVQSTEWHVGDEPLTGARRVVTGpliGPSP-------SGRenaFRVEKYG--GGYKLVSCRD-----SCQDLGV 148
Cdd:cd23377  81 FTKKPNCAESSKWLVFVDDFIPKACVGIG---GPEDhpgkqilSGK---FNIQKYGsgNGYKLVFCPDgsapgNCSDIGR 154

                       170       180
                ....*....|....*....|....*
gi 254616   149 SRDG-AGAAWIGASQPPHVVVFKKA 172
Cdd:cd23377 155 YDNEeGGRRLVLTEDEPFEVVFVDA 179
beta-trefoil_STI_LSPI cd23371
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Carica papaya latex ...
 4-172 5.29e-15

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: 69.19  E-value: 5.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     4 PVYDTEGHELSADGSYYVLPASPGHGGG-LTMAP-RRVIPCPLLVAQETDERRKGFPVRFTPWGGAASpRTLRVSTDVRI 81
Cdd:cd23371   2 PIVDIDGKPLRYGVDYFVVSAIWGAGGGgLSLYGpGNKKKCPLSVVQDPFDSDNGIPVKFSAVKNVKD-NIVRESTDLNV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    82 RFNAATLCVQSTEWHVGDEPLTGARRVVTGPLIGPSPSGRENA-FRVEKYGG---GYKLVSCRD-------SCQDLGVSR 150
Cdd:cd23371  81 KFNITINCNETTVWKVDRFPGVIGWTVTLGGVKGYHGFESTHSmFKIKRAGLvsfSYKFRFCPSyprtrliPCNNVGVFS 160

                       170       180
                ....*....|....*....|..
gi 254616   151 DGAGAAWIGASQPPHVVVFKKA 172
Cdd:cd23371 161 DKYRIRRLVLTDDAKEFVFVKA 182
beta-trefoil_STI_GWIN3 cd23380
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Populus sp. ...
 2-151 3.81e-13

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: 63.69  E-value: 3.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     2 PPPVYDTEGHELSADGSYYVLPASPGHGGGLTMAprRVIPCPLLVAQETDErrKGFPVRFTPwggaASPRT---LRVSTD 78
Cdd:cd23380   1 PPAVLDFNGNEVLAGAYYYIAPEDSLPFLVVAAI--RPGTCWSDVILERFL--DGLPIKFSP----VAPSNdsvIRESTY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    79 VRIRFNAAT--LCVQSTEWHVGDEPLTGARRVVTGpligpsPSGRENAFRVEKYGGG---YKLVSC-----RDSCQDLGV 148
Cdd:cd23380  73 LNIEFNAELckVCGVTTMWKVEFNATMQQPFVTTG------GVDRLNWFKITKAEEDnrfYQLSYCpvsgiQCPCVTVGI 146


                ...
gi 254616   149 SRD 151
Cdd:cd23380 147 SNR 149
beta-trefoil_STI_CPI-like cd23372
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Solanum tuberosum ...
 16-172 8.72e-13

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: 62.82  E-value: 8.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    16 DGSYYVLPASPGHGGG---LTMAPRRVIPCPLLVAQE-TDERRKGFPVRFTPWGGAASPrtLRVSTDVRIRFNAAT--LC 89
Cdd:cd23372   1 GESYRIISILWGALGGdvyLGKIPNSDAPCPNGVFQYnSDVGPSGTPVRFIPLSEYSGV--IFENQDLNIQFSIPTskLC 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    90 VQSTEWHVGDEPLT-GARRVVTGPLIGpspsGRENAF----RVEKYGGGYKLVSCRDS---------CQDLGVSRDGAGA 155
Cdd:cd23372  79 VNYTVWKVGDENASlGTMLLETGGTIG----QADSSWfkivKSSLMKFGYKLLYCPSTsicprddlfCADVGVVFQNGYR 154

                       170
                ....*....|....*..
gi 254616   156 AWIGASQPPHVVVFKKA 172
Cdd:cd23372 155 RLALVNDNPLDVVFQKV 171
beta-trefoil_STI_AMTIN cd23378
Alocasia macrorrhizos trypsin/chymotrypsin inhibitor (AMTIN) and similar proteins; AMTIN, also ...
 4-173 1.80e-09

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: 54.18  E-value: 1.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     4 PVYDTEGHELSADGSYYVLpASPGHGGGLTMAPRRViPCPLLVAQETDERRKGFPVRFTPWGgaASPRTLRVSTDVRIRF 83
Cdd:cd23378   2 PVLDVDGNELQRGQLYYAT-SVMRPGSGLTLAAPSG-SCPLNVAQAPFNDYSGRPLAFFPEN--ADDDTVQEGSTLYIMF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    84 NAATLCVQSTEWHVGDEpltgARRVVTG----PLIGP-------------SPSGRENAFRVEKYGGGYKLVSCRDSCQ-D 145
Cdd:cd23378  78 PEPTECPQSTVWTLDRE----AGFVTTGgtssKAIGPhnsrfairragdaSSQPRDYQIEVCPCSTGVERPSCRMGCLgT 153

                       170       180
                ....*....|....*....|....*...
gi 254616   146 LGVSRDGAGAAWIGASQPPHVVVFKKAR 173
Cdd:cd23378 154 LGLAEGGKNVLLNINNESPHTIRFVKVK 181
beta-trefoil_STI_AtKTI6-like cd23369
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana ...
 5-134 1.12e-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: 1.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     5 VYDTEGHELSADGSYYVLPASPgHGGGLTMAPRR---VIPCP---LLVAQETDERRKgfPVRFTPwgGAASPRTLRVSTD 78
Cdd:cd23369   6 VLDTNGNPVKPGAPYYILDATN-YGRGISRSQVGpddPNPCPqtvVLGSDPLISAPP--PVAFVL--ESSSDDVVRVSTE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 254616    79 VRIRFNAATLCVQSTEWHVGDEPLTGARRVVTGpligpSPSGRENAFRVEKYGGGY 134
Cdd:cd23369  81 LSIRFAEPSHCAESGYWRVANSSSPKKEVVLTG-----SKSSNDSTFTIKKSDDGY 131
beta-trefoil_STI_BbKI-like cd23364
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides ...
 5-148 9.58e-08

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: 49.24  E-value: 9.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     5 VYDTEGHELS-ADGSYYVLPASPGHGG------GLTMAPRRVIPCPllvaqetdERRKGFPVRFTpwggaaSPRTLRVST 77
Cdd:cd23364   3 VVDTNGQPVSnGADAYYLVPVSHGHAGlalakiGNEAEPRAVVLDP--------HHRPGLPVRFE------SPLRINIIK 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254616    78 D---VRIRFNAATlcVQSTEWHVGDE-PLTGARRVV-TGPLIGPspsgrenaFRVEKYGGGYKLVSCRDSCQ---DLGV 148
Cdd:cd23364  69 EsyfLNIKFGPSS--SDSGVWDVIQQdPIGLAVKVTdTKSLLGP--------FKVEKEGEGYKIVYYPERGQtglDIGL 137
beta-trefoil_STI_WBA1 cd23361
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus ...
 1-144 4.97e-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: 47.48  E-value: 4.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     1 APPPVYDTEGHELSADGSYYVLPASPGHGGGLTMAPRRVIPCPLLVAQETDERRKGFPVRftpwGGAASPRTLRVSTDvR 80
Cdd:cd23361   1 ADDPVYDAEGNKLVNRGKYTIVSFSDGAGIDVVATGNENPEDPLSIVKSTRNIMYATSIS----SEDKTPPQPRNILE-N 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    81 IRFNAATLCVQSTewhvgDEPLTGARRVVTG---PLIGPSPSGRENAFRVEKYGGG---YKLVSCRDSCQ 144
Cdd:cd23361  76 MRLKINFATDPHK-----GDVWSVVDFQPDGqqlKLAGRYPNQVKGAFTIQKGSNTprtYKLLFCPVGSP 140
beta-trefoil_STI_COTI cd23379
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Senna obtusifolia ...
 5-151 2.15e-06

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: 45.55  E-value: 2.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616     5 VYDTEGHELSADGSYYVLPasPGHGGGLTMAPRR---VIPCPLLVAQEtdERRKGFPVRFTpwggaASPRTLRVSTD--V 79
Cdd:cd23379   2 VYDSDGDILRNGGKYFISP--PNGGGAILAAAIShgsDRSCSLAVIQA--LSYIGWPVTIS-----TPFPPTFITTSfpL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254616    80 RIRFN--AATLCVQSTEWHVGDEPltgarrvvtgPLIGPSPSGRE--------NAFRVEKYG---GGYKLVSC---RDSC 143
Cdd:cd23379  73 NISFAylPPNVCTKSPDWVVVKSN----------PLGEPVMVGDFeefdnpvsGYFYIKSYDsskGYYKLVFCyggDDSC 142


                ....*...
gi 254616   144 QDLGVSRD 151
Cdd:cd23379 143 GNIGVDKD 150
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH