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Conserved domains on  [gi|2072556034|pdb|7JR1|J]
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Chain J, Kunitz-type inihibitor

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
beta-trefoil_STI_BbKI-like cd23364
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides ...
3-164 1.23e-123

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides Kunitz-type serine protease inhibitor BbKI and similar proteins; This subfamily includes Bauhinia bauhinioides BbKI, BbCI, Bauhinia rufa BrTI, and similar proteins. BbKI inhibits bovine trypsin, human plasma kallikrein and plasmin, and weakly inhibits bovine chymotrypsin. BbCI inhibits cruzipain, a cysteine proteinase from Trypanosoma cruzi. It also inhibits cathepsin L, a cysteine proteinase with high homology to cruzipain, but not cathepsin B, papain, bromelain, or ficin. BrTI acts as an inhibitor of trypsin and human plasma kallikrein. It does not inhibit chymotrypsin, porcine pancreatic elastase, human neutrophil elastase, coagulation factor Xa, human thrombin, porcine pancreatic kallikrein or plasmin. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


:

Pssm-ID: 467389  Cd Length: 162  Bit Score: 344.31  E-value: 1.23e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        3 SVVVDTNGQPVSNGADAYYLVPVSHGHAGLALAKIGNEAEPRAVVLDPHHRPGLPVRFESPLFINIIKESYFLNIKFGPS 82
Cdd:cd23364   1 SVVVDTNGQPVSNGADAYYLVPVSHGHAGLALAKIGNEAEPRAVVLDPHHRPGLPVRFESPLRINIIKESYFLNIKFGPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       83 SSDSGVWDVIQQDPIGLAVKVTDTKSLLGPFKVEKEGEGYKIVYYPERGQTGLDIGLVHRNDKYYLAVKDGEPCVFKIRK 162
Cdd:cd23364  81 SSDSGVWDVIQQDPIGLAVKVTDTKSLLGPFKVEKEGEGYKIVYYPERGQTGLDIGLVHRNDKYYLAVKDGEPCVFKIRK 160

                ..
7JR1_J      163 AT 164
Cdd:cd23364 161 AT 162
 
Name Accession Description Interval E-value
beta-trefoil_STI_BbKI-like cd23364
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides ...
3-164 1.23e-123

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides Kunitz-type serine protease inhibitor BbKI and similar proteins; This subfamily includes Bauhinia bauhinioides BbKI, BbCI, Bauhinia rufa BrTI, and similar proteins. BbKI inhibits bovine trypsin, human plasma kallikrein and plasmin, and weakly inhibits bovine chymotrypsin. BbCI inhibits cruzipain, a cysteine proteinase from Trypanosoma cruzi. It also inhibits cathepsin L, a cysteine proteinase with high homology to cruzipain, but not cathepsin B, papain, bromelain, or ficin. BrTI acts as an inhibitor of trypsin and human plasma kallikrein. It does not inhibit chymotrypsin, porcine pancreatic elastase, human neutrophil elastase, coagulation factor Xa, human thrombin, porcine pancreatic kallikrein or plasmin. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467389  Cd Length: 162  Bit Score: 344.31  E-value: 1.23e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        3 SVVVDTNGQPVSNGADAYYLVPVSHGHAGLALAKIGNEAEPRAVVLDPHHRPGLPVRFESPLFINIIKESYFLNIKFGPS 82
Cdd:cd23364   1 SVVVDTNGQPVSNGADAYYLVPVSHGHAGLALAKIGNEAEPRAVVLDPHHRPGLPVRFESPLRINIIKESYFLNIKFGPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       83 SSDSGVWDVIQQDPIGLAVKVTDTKSLLGPFKVEKEGEGYKIVYYPERGQTGLDIGLVHRNDKYYLAVKDGEPCVFKIRK 162
Cdd:cd23364  81 SSDSGVWDVIQQDPIGLAVKVTDTKSLLGPFKVEKEGEGYKIVYYPERGQTGLDIGLVHRNDKYYLAVKDGEPCVFKIRK 160

                ..
7JR1_J      163 AT 164
Cdd:cd23364 161 AT 162
STI smart00452
Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;
5-164 1.68e-25

Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;


Pssm-ID: 214670  Cd Length: 172  Bit Score: 95.86  E-value: 1.68e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J           5 VVDTNGQPVSNGADaYYLVPVSHGH-AGLALAKIGNEAEPRAVVLDP-HHRPGLPVRFESPLFI-NIIKESYFLNIKFG- 80
Cdd:smart00452   1 VLDTDGNPLRNGGT-YYILPAIRGHgGGLTLAATGNEICPLTVVQSPnEVDNGLPVKFSPPNPSdFIIRESTDLNIEFDa 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J          81 -PSSSDSGVWDVIQQD-PIGLAVKVTDTKSLL-GPFKVEKEGE---GYKIVYYP--ERGQTGLDIGLVH-RNDKYYLAVK 151
Cdd:smart00452  80 pPLCAQSTVWTVDEDStPGGLAVKTGGYPGVNdSWFKIEKYSGesnGYKLVYCPngSDDDKCGDVGIFIdPNGGRRLVLS 159
                          170
                   ....*....|...
7JR1_J         152 DGEPCVFKIRKAT 164
Cdd:smart00452 160 NENPLVVVFKKAD 172
Kunitz_legume pfam00197
Trypsin and protease inhibitor;
5-162 8.53e-25

Trypsin and protease inhibitor;


Pssm-ID: 395144  Cd Length: 174  Bit Score: 93.91  E-value: 8.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J          5 VVDTNGQPVSNGADaYYLVPV-SHGHAG-LALAKIGNEAEPRAVVLDPHHR-PGLPVRFESP-LFINIIKESYFLNIKFG 80
Cdd:pfam00197   1 VLDTDGNPLRAGVE-YYILPAiGGGSGGgLTLASRGNGTCPLDVVQEPSEVsKGLPVKFSPSnSKKGVIRESTDLNIEFF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J         81 PSSS---DSGVWDVIQQDPIGLAVKVTDTKSLLGP--------FKVEKEGEGYKIVYYPERGQTGL--DIGLVHRNDKYY 147
Cdd:pfam00197  80 SAPTicvQSTVWKVGDGDPETGRRFVVTGGVVGNPgpdtvsnwFKIEKTGGGYKLVFCPSVCCKVKcgDVGIFVDDNGNR 159
                         170
                  ....*....|....*
7JR1_J        148 LAVKDGEPCVFKIRK 162
Cdd:pfam00197 160 RLALSDEPFPVVFKK 174
 
Name Accession Description Interval E-value
beta-trefoil_STI_BbKI-like cd23364
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides ...
3-164 1.23e-123

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Bauhinia bauhinioides Kunitz-type serine protease inhibitor BbKI and similar proteins; This subfamily includes Bauhinia bauhinioides BbKI, BbCI, Bauhinia rufa BrTI, and similar proteins. BbKI inhibits bovine trypsin, human plasma kallikrein and plasmin, and weakly inhibits bovine chymotrypsin. BbCI inhibits cruzipain, a cysteine proteinase from Trypanosoma cruzi. It also inhibits cathepsin L, a cysteine proteinase with high homology to cruzipain, but not cathepsin B, papain, bromelain, or ficin. BrTI acts as an inhibitor of trypsin and human plasma kallikrein. It does not inhibit chymotrypsin, porcine pancreatic elastase, human neutrophil elastase, coagulation factor Xa, human thrombin, porcine pancreatic kallikrein or plasmin. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467389  Cd Length: 162  Bit Score: 344.31  E-value: 1.23e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        3 SVVVDTNGQPVSNGADAYYLVPVSHGHAGLALAKIGNEAEPRAVVLDPHHRPGLPVRFESPLFINIIKESYFLNIKFGPS 82
Cdd:cd23364   1 SVVVDTNGQPVSNGADAYYLVPVSHGHAGLALAKIGNEAEPRAVVLDPHHRPGLPVRFESPLRINIIKESYFLNIKFGPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       83 SSDSGVWDVIQQDPIGLAVKVTDTKSLLGPFKVEKEGEGYKIVYYPERGQTGLDIGLVHRNDKYYLAVKDGEPCVFKIRK 162
Cdd:cd23364  81 SSDSGVWDVIQQDPIGLAVKVTDTKSLLGPFKVEKEGEGYKIVYYPERGQTGLDIGLVHRNDKYYLAVKDGEPCVFKIRK 160

                ..
7JR1_J      163 AT 164
Cdd:cd23364 161 AT 162
beta-trefoil_STI cd00178
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold; The STI-like domain is found ...
20-162 1.37e-29

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold; The STI-like domain is found in the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. They inhibit proteases by binding with high affinity to their active sites. Plant Kunitz-type inhibitors are thought to be important in defense, especially against insect pests. The STI-like domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467384  Cd Length: 161  Bit Score: 105.90  E-value: 1.37e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       20 YYLVPVSHGH-AGLALAKIGNEAEPRAVVLDPHH-RPGLPVRFESPLF-INIIKESYFLNIKF---GPSSSDSGVWDVIQ 93
Cdd:cd00178   4 YYILPAIWGGgGGLTLAKTGNETCPLDVVQSPSDtDNGLPVTFSPANPkDGVIRESTDLNIKFsadTTCCAESTVWKVVG 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7JR1_J       94 QDPIG-LAVKVTDTKS---LLGPFKVEKEG--EGYKIVYYPERGQTGL---DIGLVHRNDKYYLAVKDGEPCVFKIRK 162
Cdd:cd00178  84 DDSTGgRFVTTGGVKGnetLNSWFKIEKAGngNGYKLVFCPSVCGCKVvcgDVGIVVDNGNRRLALTEGEPLEVVFKK 161
beta-trefoil_STI_WCI3-like cd23362
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus ...
5-164 2.38e-29

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus tetragonolobus chymotrypsin inhibitor 3 (WCI-3) and similar proteins; This subfamily includes Psophocarpus tetragonolobus WCI-3, trypsin inhibitor 1 (WTI-1), and trypsin inhibitor DE-3 from Erythrina caffra (ETI). WTI-1 is a Kunitz type protease inhibitor that inhibits bovine trypsin stoichiometrically, but not bovine alpha-chymotrypsin. WCI-3 is a Kunitz-type winged bean chymotrypsin inhibitor (WbCI) that inhibits alpha-chymotrypsin at the molar ratio of 1:2 instead of 1:1, the usual ratio of 1:1 common to other members of the family. ETI is a trypsin inhibitor that shows high homology to other Kunitz trypsin protease inhibitors, but has the unique ability to bind and inhibit tissue plasminogen activator. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467387  Cd Length: 170  Bit Score: 105.39  E-value: 2.38e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGAdAYYLVPVSHGH-AGLALAKIGNEAEPRAVV--LDPHHRpGLPVRFESPLFINIIKESYFLNIKFG- 80
Cdd:cd23362   2 VVDTDGNPVENGG-TYYILPVIWGKgGGIELAATGNETCPLTVVqsPNEVSK-GLPIRISSPLRIAFIPEGLLLRIGFTa 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       81 --PSSSDSGVWDVIQQDPIGLAVKVTDTKSLL-GPFKVEK---EGEGYKIVYYPERGQTGLDIGlVHRNDKYY--LAVKD 152
Cdd:cd23362  80 vpPCAPTPSWWTVVKGLPEGPAVKLTGYKNTVdGWFKIEKvssDLNSYKLLFCPEDDDSCGDIG-IHRDDKGNrrLVVTE 158
                       170
                ....*....|..
7JR1_J      153 GEPCVFKIRKAT 164
Cdd:cd23362 159 ENPLVVVFQKAE 170
beta-trefoil_STI_LlTI-like cd23365
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Leucaena leucocephala ...
4-163 5.61e-26

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Leucaena leucocephala trypsin inhibitor (LlTI) and similar proteins; LlTI is a Kunitz-type trypsin inhibitor that inhibits trypsin, plasmin, human plasma kallikrein, chymotrypsin, and factor XIIa activity. This subfamily also includes tamarind Kunitz inhibitor (TKI), Enterolobium contortisiliquum trypsin inhibitor (EcTI), Acacia confusa trypsin inhibitor (AcTI), Bauhinia ungulata factor Xa inhibitor BuXI, and Phanera variegata trypsin inhibitor BvTI. TKI is a Kunitz-type dual inhibitor (TKI) of factor Xa (FXa) and trypsin. It shows prolongation of blood coagulation time. EcTI also belongs to the Kunitz family of plant inhibitors, common in plant seeds. It inhibits trypsin, chymotrypsin, plasma kallikrein, plasmin, human neutrophil elastase, and Factor XIIa in the stoichiometric ratio 1:1, but not thrombin, bovine pancreatic elastase, or Factor Xa. It is involved in the inhibition of the invasion of gastric cancer cells through alterations in integrin-dependent cell signaling pathway. AcTI inhibits trypsin and alpha-chymotrypsin stoichiometrically at the molar ratio of 1:1 and 2:1 respectively. BuXI inhibits bovine trypsin and chymotrypsin, and human plasmin, plasma kallikrein, factor XIIa, and factor Xa. BvTI inhibits bovine trypsin and chymotrypsin, and human plasmin, plasma kallikrein and factor XIIa. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467390  Cd Length: 170  Bit Score: 96.80  E-value: 5.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        4 VVVDTNGQPVSNGAdAYYLVPVSHGHAG-LALAKIGNEAEPRAVVLDP-HHRPGLPVRFESPLFINIIKESYFLNIKFGP 81
Cdd:cd23365   1 TLLDTDGDPLNNGG-QYYILPALRGKGGgLELARTGDETCPLTVVQARsETSRGLPVRISSPPRIAIITTAFYLNIEFQP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       82 SSS---DSGVWDVIQQDPIGLAVKVT-DTKSLLGPFKVEKEGEGYKIVYYP--ERGQTGLDIGL-VHRNDKYYLAVKDGE 154
Cdd:cd23365  80 APAclpKPLRWRIEQESSSEGEVKIApDEERLFGPFQIKPYREDYKLVYCEssSDDDSCRDLGIsIDDENNRRLVVKDGD 159

                ....*....
7JR1_J      155 PCVFKIRKA 163
Cdd:cd23365 160 PLAVRFKKA 168
STI smart00452
Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;
5-164 1.68e-25

Soybean trypsin inhibitor (Kunitz) family of protease inhibitors;


Pssm-ID: 214670  Cd Length: 172  Bit Score: 95.86  E-value: 1.68e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J           5 VVDTNGQPVSNGADaYYLVPVSHGH-AGLALAKIGNEAEPRAVVLDP-HHRPGLPVRFESPLFI-NIIKESYFLNIKFG- 80
Cdd:smart00452   1 VLDTDGNPLRNGGT-YYILPAIRGHgGGLTLAATGNEICPLTVVQSPnEVDNGLPVKFSPPNPSdFIIRESTDLNIEFDa 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J          81 -PSSSDSGVWDVIQQD-PIGLAVKVTDTKSLL-GPFKVEKEGE---GYKIVYYP--ERGQTGLDIGLVH-RNDKYYLAVK 151
Cdd:smart00452  80 pPLCAQSTVWTVDEDStPGGLAVKTGGYPGVNdSWFKIEKYSGesnGYKLVYCPngSDDDKCGDVGIFIdPNGGRRLVLS 159
                          170
                   ....*....|...
7JR1_J         152 DGEPCVFKIRKAT 164
Cdd:smart00452 160 NENPLVVVFKKAD 172
Kunitz_legume pfam00197
Trypsin and protease inhibitor;
5-162 8.53e-25

Trypsin and protease inhibitor;


Pssm-ID: 395144  Cd Length: 174  Bit Score: 93.91  E-value: 8.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J          5 VVDTNGQPVSNGADaYYLVPV-SHGHAG-LALAKIGNEAEPRAVVLDPHHR-PGLPVRFESP-LFINIIKESYFLNIKFG 80
Cdd:pfam00197   1 VLDTDGNPLRAGVE-YYILPAiGGGSGGgLTLASRGNGTCPLDVVQEPSEVsKGLPVKFSPSnSKKGVIRESTDLNIEFF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J         81 PSSS---DSGVWDVIQQDPIGLAVKVTDTKSLLGP--------FKVEKEGEGYKIVYYPERGQTGL--DIGLVHRNDKYY 147
Cdd:pfam00197  80 SAPTicvQSTVWKVGDGDPETGRRFVVTGGVVGNPgpdtvsnwFKIEKTGGGYKLVFCPSVCCKVKcgDVGIFVDDNGNR 159
                         170
                  ....*....|....*
7JR1_J        148 LAVKDGEPCVFKIRK 162
Cdd:pfam00197 160 RLALSDEPFPVVFKK 174
beta-trefoil_STI_SKTI cd23363
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in the soybean Kunitz ...
4-162 1.70e-20

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in the soybean Kunitz trypsin inhibitor (SKTI) subfamily; SKTI is extracted from soybean (Glycine max L.) seeds. It shows inhibition of trypsin and possesses insect resistance and anti-tumor properties. This subfamily includes KTI1-3. KTI1 and KTI2 probably do not possess trypsin inhibitor activity. KTI3, also called trypsin inhibitor A, is responsible for most of the Kunitz trypsin inhibitor activity and protein found in soybean seeds. Members of this subfamily contain a soybean trypsin inhibitor (STI)-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467388  Cd Length: 175  Bit Score: 82.90  E-value: 1.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        4 VVVDTNGQPVSNGADaYYLVPVSHGH-AGLALAKIGNEAEPRAVVLDPH-HRPGLPVRFESPLFINIIKESYFLNIKFG- 80
Cdd:cd23363   2 FVLDTDGNPLQNGGT-YYVLPVIRGAgGGIRVAPTGNERCPLTVVQSRNeLDKGIGTIISSPYRIRFIAEGHPLSIKFDs 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       81 -----PSSSDSGVWDVIQQDPIGLAVKVTDTKSLL-GPFKVEK----EGEGYKIVY--YPERGQTGLDIGlVHRNDKYY- 147
Cdd:cd23363  81 favipLCVPIPTEWSVVEDLPEGPAVKIGENKNAVdGWFRIERvsddEFNGYKLVFcpQQAEDDKCGDIG-ISIDDDGIr 159
                       170
                ....*....|....*.
7JR1_J      148 -LAVKDGEPCVFKIRK 162
Cdd:cd23363 160 rLVVSKNKPLVVQFQK 175
beta-trefoil_STI_VvMLP-like cd23375
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Vitis vinifera ...
5-162 4.16e-16

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Vitis vinifera miraculin-like protein (VvMLP) and similar proteins; This subfamily includes VvMLP, Synsepalum dulcificum miraculin (SdMIR), and Arabidopsis thaliana Kunitz trypsin inhibitor 5 (AtKTI5, also known as AtKTI2). VvMLP exhibits significant homology to miraculin. However, it exists as a monomer in solution with no detectable taste-modifying activity. It can act as a moderate trypsin inhibitor. SdMIR has the property of modifying a sour taste into a sweet taste. This alteration of taste perception persists for many minutes. AtKTI5 can inhibit both serine proteases and cysteine proteases. It may be involved in the modulation of the proteases that participate in the hydrolysis of dietary proteins in the gut of spider mites. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467400  Cd Length: 177  Bit Score: 71.48  E-value: 4.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGADaYYLVPVSHGHA-GLALAKIGNEAEPRAVVLDPH-HRPGLPVRFeSPlfIN----IIKESYFLNIK 78
Cdd:cd23375   5 VLDTAGKILRTGVN-YYILPVNRGRGgGLTLASTGNETCPLDVVQEQNeVNNGLPLTF-SP--VNpkkgVIRVSTDLNIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       79 FGPSSS--DSGVWDVIQQDPI--GLAVKVTDTKSLLGP------FKVEKEGEGYKIVYYPE-----RGQTGlDIGLVHRN 143
Cdd:cd23375  81 FSASTScpESTVWKLDDYDEStgQYFVTTGGVEGNPGRetirnwFKIEKYEDGYKLVYCPSvcnycKVICK-DVGIYIDN 159
                       170
                ....*....|....*....
7JR1_J      144 DKYYLAVKDgEPCVFKIRK 162
Cdd:cd23375 160 GVRRLALSD-KPLKVKFKK 177
beta-trefoil_STI_MkMLP-like cd23370
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Murraya koenigii ...
5-162 9.94e-13

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Murraya koenigii miraculin-like protein (MkMLP) and similar proteins; This subfamily includes Theobroma cacao 21 kDa seed protein (TcASP) and Murraya koenigii miraculin-like protein (MkMLP). TcASP shows homology to the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. MkMLP is closer to miraculin, a taste modifying protein, rather than classical Kunitz family members like soybean Kunitz-type trypsin inhibitor (STI). MkMLP is functionally unstable at higher temperatures. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467395  Cd Length: 179  Bit Score: 62.72  E-value: 9.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGADaYYLVPV--SHGHAGLALAKIGNEAEPRAVVLDPHH-RPGLPVRFeSPLFIN--IIKESYFLNIKF 79
Cdd:cd23370   2 VLDINGNKVRTGTE-YYIVSAiwGAGGGGLSLFRGRNGTCPLDVIQLRSDlDRGLPLTF-SPADYNdgVVYESTDLNIKF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       80 GP---SSSDSGVWDVIQQDPIGLAVKVTD--------TKSLLGPFKVEKEGEG--YKIVYYPERGQTGL----DIGLVHR 142
Cdd:cd23370  80 SAadaLCNESTVWKVDNYDESTGKWFITTggvegnpgAQTLLNWFKIEKVGTGntYKIVHCPSVCDSCVtlcnDVGRSSD 159
                       170       180
                ....*....|....*....|
7JR1_J      143 NDKYYLAVKDGEPCVFKIRK 162
Cdd:cd23370 160 DGVRRLALSDDPPFPVVFIK 179
beta-trefoil_STI_DrTI cd23376
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Delonix regia ...
5-138 2.73e-12

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Delonix regia Kunitz-type serine protease inhibitor DrTI and similar proteins; DrTI is a Kunitz-type trypsin inhibitor that inhibits bovine trypsin and human plasma kallikrein, but not chymotrypsin and tissue kallikrein. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467401  Cd Length: 174  Bit Score: 61.19  E-value: 2.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGAdAYYLVPVSHGHAG--LALAKIGNEAEPRAVVLDPHH-RPGLPVRFeSPLFIN--IIKESYFLNIKF 79
Cdd:cd23376   3 VKDTNGNPLSPGA-EYYILPANSGPGGggLRLGKTGNSTCPLTVLQEYSElFLGLPVKF-NVQGSSdgIILTGTPLDIEF 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
7JR1_J       80 --GPSSSDSGVWDVIQQD-------PIGLAVKVTDTKSLLGPFKVEKEGEGYKIVYYP-ERGQTGLDIG 138
Cdd:cd23376  81 veKPDCAESSKWVVVKDDfyptkwvGIGGGEDHPGKEIVDGVFKIEKYGEGYKLVFCPkGSSGTCFDIG 149
beta-trefoil_STI_AtKTI6-like cd23369
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana ...
4-151 2.75e-11

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana Kunitz trypsin inhibitor 6 (AtKTI6) and similar proteins; This subfamily includes AtKTI6 and AtKTI7, which exhibit Kunitz trypsin protease inhibitor activity. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467394  Cd Length: 170  Bit Score: 58.55  E-value: 2.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        4 VVVDTNGQPVSNGADAYYLVPVSHGHaGLALAKIGNEAE---PRAVVL--DPHHRPGLPVRF-ESPLFINIIKESYFLNI 77
Cdd:cd23369   5 VVLDTNGNPVKPGAPYYILDATNYGR-GISRSQVGPDDPnpcPQTVVLgsDPLISAPPPVAFvLESSSDDVVRVSTELSI 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7JR1_J       78 KF-GPS-SSDSGVWDVIQQDPIGLAVKVTDTKSLL-GPFKVEKEGEG-YKIVYYPERGQTglDIGLVHRNDKYYLAVK 151
Cdd:cd23369  84 RFaEPShCAESGYWRVANSSSPKKEVVLTGSKSSNdSTFTIKKSDDGyYKFAFGSADKPT--PLGLENYDDIYRLVLS 159
beta-trefoil_STI_COTI cd23379
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Senna obtusifolia ...
4-162 2.04e-10

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Senna obtusifolia trypsin inhibitor 1 (COTI) and similar proteins; COTI is a specific inhibitor of bovine trypsin. It also exhibits strong inhibitory effect on midgut trypsin from Pieris rapae, Helicoverpa armigera, Spodoptera exigua, and Spodoptera litura. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467404  Cd Length: 172  Bit Score: 56.33  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        4 VVVDTNGQPVSNGAdAYYLVPVSHGHAGLALA-KIGNEAEPRAVVLDPHHRPGLPVRFESPLFINIIKESYFLNIKFG-- 80
Cdd:cd23379   1 LVYDSDGDILRNGG-KYFISPPNGGGAILAAAiSHGSDRSCSLAVIQALSYIGWPVTISTPFPPTFITTSFPLNISFAyl 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       81 --PSSSDSGVWDVIQQDPIGLAVKVTDTKSLLGP----FKVEKEGEG---YKIVY-YPERGQTGlDIGL-VHRNDKYYLA 149
Cdd:cd23379  80 ppNVCTKSPDWVVVKSNPLGEPVMVGDFEEFDNPvsgyFYIKSYDSSkgyYKLVFcYGGDDSCG-NIGVdKDSNGFRRLV 158
                       170
                ....*....|....
7JR1_J      150 VKDG-EPCVFKIRK 162
Cdd:cd23379 159 VTDDrEPLVFKFDK 172
beta-trefoil_STI_KPI104-like cd23367
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Medicago truncatula ...
5-159 6.86e-10

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Medicago truncatula Kunitz type trypsin inhibitor 104 (KPI104) and similar proteins; This subfamily includes Medicago truncatula KPI104, KPI106, and KPI111. They are protease inhibitors involved in the control of mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis). KPI104 interacts with cysteine protease (CP). It shows a stronger affinity for serine carboxypeptidase (SCP1) than for CP. KPI111 only interacts with SCP1. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467392  Cd Length: 170  Bit Score: 54.66  E-value: 6.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGADaYYLVPVSHGHAGlALAKI-GNEAEPRAVVLDP-HHRPGLPVRFeSPLF--INIIKESYFLNIKFG 80
Cdd:cd23367   3 VLDTNGKPLESGVE-YYIKPAITDVGG-ALTLVnRNNSCPLYVGQENvTPSSGLPVKF-TPFVdgETVVREGRDFTITFQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       81 PSSS--DSGVWDVIQQDPI-GLAVKVTDTKSLLGP-FKVEKEGEG-YKIVYYPE------RGQTGlDIGLVHRNDKYYLA 149
Cdd:cd23367  80 ASTTcgQSTEWRVGERDPVsGRRLITTGGENGYGNyFRIVRSNRGgYNLRWCPTevcpncRFRCG-TVGILTENGKRLLA 158
                       170
                ....*....|.
7JR1_J      150 VKDGE-PCVFK 159
Cdd:cd23367 159 LDGPAlPVVFE 169
beta-trefoil_STI_WSCP_II cd23360
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in class II ...
4-127 2.48e-08

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in class II water-soluble chlorophyll proteins (WSCPs) and similar proteins; There are two kinds of water-soluble chlorophyll (Chl) proteins (WSCPs): Chenopodium-type (Class I, a WSCP from Chenopodium, Atriplex, Polygonum, and Amaranthus species) and Brassica-type (Class II, a WSCP from Brassica, Raphanus, and Lepidium species). Classes I and II WSCPs differ mainly in their photoconvertiblity. Class I WSCPs show a light-induced absorption change, whereas Class II WSCPs do not. This family includes Class II WSCPs. They possess the complete motif of the Kunitz-type proteinase inhibitor but may not inhibit trypsin, whose activity is inhibited strongly by one Kunitz-proteinase inhibitor, the soybean trypsin inhibitor (STI). Members of this subfamily contain a STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467385  Cd Length: 176  Bit Score: 50.53  E-value: 2.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        4 VVVDTNGQPVSNGADaYYLVPVSHGHAGlALAkigneaePRAVVLDP-----------HHRPGLPVRFESPLFI--NIIK 70
Cdd:cd23360   2 PVKDTAGNPLKTGAQ-YFIQPVKTNNGG-GLV-------PAAIDLLPlcplgitqtllPYQPGLPVSFSLPLSSvgNTVR 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7JR1_J       71 ESYFLNIKFGPS-----SSDSGVWDV------IQQDPIGLAVKVTDTKSLlgpFKVEKEGEG---YKIVYY 127
Cdd:cd23360  73 TSTDVNIEFKSPiwpvcKEFSKLWAVdssssaPKEPAIIIGGKPGSRNSL---FKIEKAGGGantYKLTTL 140
beta-trefoil_STI_WBA1 cd23361
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus ...
5-132 1.12e-07

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Psophocarpus tetragonolobus albumin-1 and similar proteins; Albumin-1, also called WBA-1, or winged bean albumin 1, acts as a 2S seed storage protein that is homologous with Kunitz-type seed trypsin inhibitors. It contains a soybean trypsin inhibitor (STI)-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467386  Cd Length: 174  Bit Score: 49.02  E-value: 1.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGADaYYLVPVSHGhAGLALAKIGNEAE--PRAVVLDPHHRPGLPVrFES----PLFINIIKESYFLNIK 78
Cdd:cd23361   5 VYDAEGNKLVNRGK-YTIVSFSDG-AGIDVVATGNENPedPLSIVKSTRNIMYATS-ISSedktPPQPRNILENMRLKIN 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
7JR1_J       79 FGPSSSDSGVWDVIQQDPIGLAVKV-----TDTKSLLGPFKVEKEGEGYKIVYYPERGQ 132
Cdd:cd23361  82 FATDPHKGDVWSVVDFQPDGQQLKLagrypNQVKGAFTIQKGSNTPRTYKLLFCPVGSP 140
beta-trefoil_STI_AtTPI-like cd23366
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana ...
5-163 1.18e-07

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Arabidopsis thaliana trypsin protease inhibitor (AtTPI) and similar proteins; AtTPI, also called kunitz trypsin inhibitor 4 (AtKTI4), or Kunitz trypsin inhibitor 1 (AtKTI1), exhibits Kunitz trypsin protease inhibitor activity. It is involved in modulating programmed cell death (PCD) in plant-pathogen interactions. It can also inhibit both serine proteases and cysteine proteases. It may be involved in the modulation of proteases that participate in the hydrolysis of dietary proteins in the gut of spider mites. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467391  Cd Length: 195  Bit Score: 48.97  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGAdaYYLVPVSHGHA--GLALAKIGNEAEPRAVVLDPHHRP-GLPVRFES-PLFINIIKESYFLNIKFG 80
Cdd:cd23366  23 VLDSDGDIIFNGS--YYVLPVIRGTGggGLTLSGLGSEPCPLYVGQESSEVNeGIPVKFSNwKSKVGFVPESENLNIEMD 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       81 PSSS---DSGVWDVIQQDPIGLAVKVT-------DTKSLLGPFKVEKEGE---GYKIVYYPeRGQTGLDIGL-VHRNDKY 146
Cdd:cd23366 101 VGATiciQSTYWWLGEFDKERKALFVAagpkpegFKDSLKSFFQIKKSEDllgGYKIVFCP-SDPSCTDVGIfVDENGVR 179
                       170
                ....*....|....*..
7JR1_J      147 YLAVKDgEPCVFKIRKA 163
Cdd:cd23366 180 RLALSD-KPFEVVFVKA 195
beta-trefoil_STI_CrataBL-like cd23374
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Crateva tapia bark ...
12-139 1.28e-07

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Crateva tapia bark lectin (CrataBL) and similar proteins; CrataBL is both a Kunitz-type plant protease inhibitor and a glucose- and N-acetylglucosamine-binding lectin. It has hemagglutinating activity against human and rabbit erythrocytes which does not require divalent cations. It inhibits factor Xa and, to a lesser extent, trypsin. It does not inhibit neutrophil elastase, human plasma kallikrein, papain, human plasmin, porcine pancreatic kallikrein and bovine chymotrypsin. CrataBL has insecticidal activity against the termite species Nasutitermes corniger. It induces apoptosis in prostate cancer cell lines DU145 and PC3. The family includes CrataBL-form I and CrataBL-form II. This subfamily also includes Arabidopsis thaliana Kunitz trypsin inhibitor 3 (AtKTI3) that exhibits Kunitz trypsin protease inhibitor activity. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467399  Cd Length: 160  Bit Score: 48.63  E-value: 1.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       12 PVSNGAdAYYLVPVSHGH-AGL---ALAKIGNEAEPRAVVLDPH-HRPGLPVRFeSPLF--INIIKESYFLNIKFGPSSS 84
Cdd:cd23374   1 PVLAGV-PYYILPAKIGTgGGLipsNRRKNTQQLCPLDIVQSQFpFVLGVPVTF-TPLNskLKVVPLSTNLNIEFDSDVW 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
7JR1_J       85 ---DSGVW--DVIQQDPiGLAVKVTDTKSLLGP-FKVEKEGEGYKIVYYPeRGQTGLDIGL 139
Cdd:cd23374  79 lcpESKVWtvDSSQWLR-GSYVSTGGEKGSGGSwFRIERDGDSYKLVHCP-RGTSCRDVGI 137
beta-trefoil_STI_MP4-like cd23377
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Mucuna pruriens MP-4 ...
5-138 4.74e-07

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Mucuna pruriens MP-4 and similar proteins; This subfamily includes Mucuna pruriens MP-4, Canavalia lineata subtilisin inhibitor CLSI-II, Cicer arietinum trypsin protein inhibitor 2 (CaTI2), Pisum sativum Kunitz-type trypsin inhibitor-like 1 protein (PIP20-1) and Kunitz-type trypsin inhibitor-like 2 protein (PIP20-2). MP-4 contributes significantly to the snake venom neutralization activity of Mucuna pruriens seeds through an indirect antibody-mediated mechanism and not through direct inhibition of venom proteases. CLSI-II inhibits subtilisin-type microbial serine proteases including proteinase K, subtilisin BPN', subtilisin Carlsberg and subtilisin E in a non-stoichiometric manner. It weakly inhibits Aspergillus oryzae protease and some metalloproteases including pronase E. It does not inhibit trypsin, chymotrypsin, Streptomyces griseus alkaline protease or Achromobacter lyticus lysyl endopeptidase. CLSI-II has a wider inhibitory specificity than CLSI-III. CaTI2 is a Kunitz trypsin inhibitor (KTI) with antifungal effect on Fusarium oxysporum f. sp. ciceris, a fungal pathogen known to cause severe damage to chickpea crop. It may be binding to the trypsin active pocket in a non-substrate like manner. PIP20-1 (also called protease inhibitor from pea 1 or FUC1) and PIP20-2 (also called protease inhibitor from pea 2 or FUC2) may act as protease inhibitors involved in plant defense responses. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467402  Cd Length: 179  Bit Score: 47.27  E-value: 4.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGAdAYYLVPVSHGHA--GLALAKIGNEAEPRAVVLD-PHHRPGLPVRFESP-LFINIIKESYFLNIKFG 80
Cdd:cd23377   4 VRDTNGNPIFPGG-RYYIMPAIFGPAggGVKLGKTGNSTCPVTVLQDySEVVNGLPVKFTIPgISPGIIFTGTPLDIEFT 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7JR1_J       81 --PSSSDSGVWDVIQQDP-------IGLAVKVTDTKSLLGPFKVEKEG--EGYKIVYYPERGQTG--LDIG 138
Cdd:cd23377  83 kkPNCAESSKWLVFVDDFipkacvgIGGPEDHPGKQILSGKFNIQKYGsgNGYKLVFCPDGSAPGncSDIG 153
beta-trefoil_STI_GWIN3 cd23380
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Populus sp. ...
5-161 4.05e-06

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Populus sp. wound-responsive protein GWIN3 and similar proteins; GWIN3 may play a role in wound response. It shows high sequence similarity with sweet potato sporamins and legume Kunitz trypsin inhibitors. It remains unclear if GWIN3 is a trypsin inhibitor, but proteinase inhibitor function would be consistent with its wound-regulated behavior. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467405  Cd Length: 168  Bit Score: 44.43  E-value: 4.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGADAYYLVPVSHGHAGLALAKIGneAEPRAVVLDPHHrPGLPVRFeSPLFI---NIIKESYFLNIKFG- 80
Cdd:cd23380   4 VLDFNGNEVLAGAYYYIAPEDSLPFLVVAAIRPG--TCWSDVILERFL-DGLPIKF-SPVAPsndSVIRESTYLNIEFNa 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       81 ---PSSSDSGVWDVIQQDPIGLAVKVTDTKSLLGPFKVEKEGEG---YKIVYYPERGQT--GLDIGLVHRNDKYYLAVKD 152
Cdd:cd23380  80 elcKVCGVTTMWKVEFNATMQQPFVTTGGVDRLNWFKITKAEEDnrfYQLSYCPVSGIQcpCVTVGISNRNGTERLALND 159

                ....*....
7JR1_J      153 gEPCVFKIR 161
Cdd:cd23380 160 -EPLPFVFR 167
beta-trefoil_STI_LSPI cd23371
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Carica papaya latex ...
5-119 1.34e-05

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Carica papaya latex serine proteinase inhibitor (LSPI) and similar proteins; LSPI, also called papaya protease inhibitor (PPI), is a double-headed Kunitz-type serine protease inhibitor. A single LSPI molecule can bind two trypsin units at the same time. LSPI may serve as a defense protein as it is induced by wounding and is inactive against endogenous proteases from C. papaya. LSPI belongs to the miraculin family of taste-modifying proteins, which are active against serine proteases. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467396  Cd Length: 183  Bit Score: 43.38  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGADaYYLVPV--SHGHAGLALAKIGNEAE-PRAVVLDPHHRP-GLPVRFESPLFI--NIIKESYFLNIK 78
Cdd:cd23371   3 IVDIDGKPLRYGVD-YFVVSAiwGAGGGGLSLYGPGNKKKcPLSVVQDPFDSDnGIPVKFSAVKNVkdNIVRESTDLNVK 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
7JR1_J       79 FGP--SSSDSGVWDViQQDP--IGLAVKVTDTKSLLGP------FKVEKEG 119
Cdd:cd23371  82 FNItiNCNETTVWKV-DRFPgvIGWTVTLGGVKGYHGFesthsmFKIKRAG 131
beta-trefoil_STI_SPOR cd23368
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Ipomoea batatas ...
5-128 1.63e-05

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Ipomoea batatas sporamin and similar proteins; This subfamily includes Ipomoea batatas sporamin A and sporamin B. They are major tuberous root proteins that belong to the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. They exhibit antitumor activity in a number of types of tumor cells. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467393  Cd Length: 174  Bit Score: 42.73  E-value: 1.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGaDAYYLVPV--SHGHAGLALAKIGNEAE-PRAVVLDPHHRPGLPVRFeSPLFINI--IKESYFLNIKF 79
Cdd:cd23368   3 VLDTDGDELRAG-GTYYITSAtwGAGGGGVRLVRLDSTTKcPSDVIISRSLDDGDPITI-TPADPNAtvVLPSTFQSFKF 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
7JR1_J       80 GPSSS----DSGVWDVIQQDPIGLA-VKVTDTKSLL-GPFKVEKEGEG---YKIVYYP 128
Cdd:cd23368  81 NIPTNplcvNNVYWGIQYDPESGQYfVKAGEFVSNNsNQFKIEVVPDNlnaYKITYCP 138
beta-trefoil_STI_ASI cd23373
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in alpha-amylase ...
5-162 1.98e-04

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in alpha-amylase/subtilisin inhibitor (ASI) and similar proteins; This subfamily includes rice ASI (RASI) and barley ASI (BASI). RASI can inhibit alpha-amylase from larvae of the red flour beetle (Tribolium castaneum) and subtilisin from Bacillus subtilis. BASI is a bifunctional protein that can simultaneously inhibit alpha-amylase isozyme (AMY2) and serine proteases of the subtilisin family. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467398  Cd Length: 176  Bit Score: 39.66  E-value: 1.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J        5 VVDTNGQPVSNGADaYYLVPVSHGHAG-LALAKIGNEAEPRAVVLDPHHR-PGLPVRFeSPLFIN-----IIKESYFLNI 77
Cdd:cd23373   5 VYDTDGHELSSDAS-YYVLPANRGHGGgLTMAPGWLRRCPLFVSQEPDEAlVGFPVRF-TPLGNSsssdaAIRLSTDVRI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       78 KFGPSSS--DSGVWDVIQQDPIGL---AVKVTDTKSLLGP---FKVEKEG---EGYKIVYYPERGQTGlDIGLVHRNDKY 146
Cdd:cd23373  83 EFRAITTcvQSLEWHVSSEPSTGRrhvAAGPVEGPSPPGRefvFRVERYSgaeKGYKLVSCGDKDPCR-DLGLYRDKKKW 161
                       170
                ....*....|....*.
7JR1_J      147 YLAVKDgEPCVFKIRK 162
Cdd:cd23373 162 WLTVSD-PPHVVVFKK 176
beta-trefoil_STI_CPI-like cd23372
soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Solanum tuberosum ...
34-163 1.64e-03

soybean trypsin inhibitor (STI)-like domain, beta-trefoil fold, found in Solanum tuberosum cysteine protease inhibitor (CPI), serine protease inhibitor (SPI), aspartic protease inhibitor (API) and similar proteins; This subfamily includes Solanum tuberosum CPI, SPI, API, and similar proteins. CPI is a Kunitz-type potato cathepsin D inhibitor. It acts as a potent inhibitor of cathepsin l (cysteine protease) but does not inhibit trypsin or chymotrypsin (serine proteases). SPI is a potent inhibitor of serine proteases (chymotrypsin and trypsin). It inhibits tightly human leukocyte elastase (HLE). It does not inhibit papain, pepsin nor cathepsin D (cysteine and aspartic proteases). API functions as the inhibitor of cathepsin D (aspartic protease). It may also inhibit trypsin and chymotrypsin (serine proteases). CPI, SPI, and API protect plants by inhibiting proteases of invading organisms. Members of this subfamily contain an STI-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467397  Cd Length: 171  Bit Score: 37.01  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7JR1_J       34 LAKIGNEAE--PRAVVLdphHRP-----GLPVRF-ESPLFINIIKESYFLNIKFGPSSS----DSGVWDVIQQDpIGLAV 101
Cdd:cd23372  20 LGKIPNSDApcPNGVFQ---YNSdvgpsGTPVRFiPLSEYSGVIFENQDLNIQFSIPTSklcvNYTVWKVGDEN-ASLGT 95
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7JR1_J      102 KVTDTKSLLGP-----FKVEK---EGEGYKIVYYPER------GQTGLDIGLVHRNDKYYLAVKDGEPCVFKIRKA 163
Cdd:cd23372  96 MLLETGGTIGQadsswFKIVKsslMKFGYKLLYCPSTsicprdDLFCADVGVVFQNGYRRLALVNDNPLDVVFQKV 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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