IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
1994-2288
8.06e-67
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
:
Pssm-ID: 465430 Cd Length: 292 Bit Score: 229.16 E-value: 8.06e-67
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
1094-1388
5.38e-66
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
:
Pssm-ID: 465430 Cd Length: 292 Bit Score: 226.85 E-value: 5.38e-66
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
1544-1838
1.06e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
:
Pssm-ID: 465430 Cd Length: 292 Bit Score: 226.08 E-value: 1.06e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
2444-2738
3.26e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
:
Pssm-ID: 465430 Cd Length: 292 Bit Score: 224.54 E-value: 3.26e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
194-488
7.11e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
:
Pssm-ID: 465430 Cd Length: 292 Bit Score: 223.38 E-value: 7.11e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
644-938
7.11e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
:
Pssm-ID: 465430 Cd Length: 292 Bit Score: 223.38 E-value: 7.11e-65
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
2779-2948
3.25e-41
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
:
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 150.63 E-value: 3.25e-41
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
3183-3341
2.45e-34
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
:
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 130.98 E-value: 2.45e-34
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
3380-3455
9.11e-33
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
:
Pssm-ID: 214843 Cd Length: 76 Bit Score: 122.83 E-value: 9.11e-33
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
2996-3065
4.44e-23
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
:
Pssm-ID: 462584 Cd Length: 68 Bit Score: 95.14 E-value: 4.44e-23
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
:
Pssm-ID: 410995 Cd Length: 55 Bit Score: 85.45 E-value: 6.71e-20
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
:
Pssm-ID: 410995 Cd Length: 55 Bit Score: 81.59 E-value: 1.65e-18
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
3565-3723
8.68e-16
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
The actual alignment was detected with superfamily member smart00216:
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 77.44 E-value: 8.68e-16
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
1994-2288
8.06e-67
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 229.16 E-value: 8.06e-67
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
1094-1388
5.38e-66
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 226.85 E-value: 5.38e-66
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
1544-1838
1.06e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 226.08 E-value: 1.06e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
2444-2738
3.26e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 224.54 E-value: 3.26e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
194-488
7.11e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 223.38 E-value: 7.11e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
644-938
7.11e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 223.38 E-value: 7.11e-65
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
2779-2948
3.25e-41
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 150.63 E-value: 3.25e-41
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2793-2949
1.53e-40
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 148.29 E-value: 1.53e-40
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
3183-3341
2.45e-34
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 130.98 E-value: 2.45e-34
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
3186-3341
8.92e-34
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 129.03 E-value: 8.92e-34
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
3380-3455
9.11e-33
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 122.83 E-value: 9.11e-33
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
3386-3454
3.21e-28
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 109.78 E-value: 3.21e-28
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
2996-3065
4.44e-23
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 95.14 E-value: 4.44e-23
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2992-3066
1.07e-21
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 91.25 E-value: 1.07e-21
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 85.45 E-value: 6.71e-20
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
3069-3122
1.52e-19
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 84.75 E-value: 1.52e-19
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 81.59 E-value: 1.65e-18
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
3458-3511
4.60e-18
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 80.51 E-value: 4.60e-18
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
3565-3723
8.68e-16
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 77.44 E-value: 8.68e-16
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
3581-3724
3.93e-14
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 72.40 E-value: 3.93e-14
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
1994-2288
8.06e-67
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 229.16 E-value: 8.06e-67
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
1094-1388
5.38e-66
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 226.85 E-value: 5.38e-66
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
1544-1838
1.06e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 226.08 E-value: 1.06e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
2444-2738
3.26e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 224.54 E-value: 3.26e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
194-488
7.11e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 223.38 E-value: 7.11e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
644-938
7.11e-65
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.
Pssm-ID: 465430 Cd Length: 292 Bit Score: 223.38 E-value: 7.11e-65
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
2779-2948
3.25e-41
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 150.63 E-value: 3.25e-41
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2793-2949
1.53e-40
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 148.29 E-value: 1.53e-40
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
3183-3341
2.45e-34
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 130.98 E-value: 2.45e-34
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
3186-3341
8.92e-34
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 129.03 E-value: 8.92e-34
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
3380-3455
9.11e-33
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 122.83 E-value: 9.11e-33
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
3386-3454
3.21e-28
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 109.78 E-value: 3.21e-28
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
2996-3065
4.44e-23
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 95.14 E-value: 4.44e-23
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2992-3066
1.07e-21
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 91.25 E-value: 1.07e-21
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 85.45 E-value: 6.71e-20
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
3069-3122
1.52e-19
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 84.75 E-value: 1.52e-19
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 81.59 E-value: 1.65e-18
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
3458-3511
4.60e-18
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 80.51 E-value: 4.60e-18
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
3565-3723
8.68e-16
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 77.44 E-value: 8.68e-16
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
3581-3724
3.93e-14
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 72.40 E-value: 3.93e-14
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
mapped to the query sequence.
Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
(CDART).
Modify your query to search against a different database and/or use advanced search options
