von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
856-1017
2.27e-32
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: 124.82 E-value: 2.27e-32
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
386-549
5.75e-32
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: 123.67 E-value: 5.75e-32
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
40-192
1.48e-25
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: 105.18 E-value: 1.48e-25
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
1056-1128
5.64e-25
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: 100.11 E-value: 5.64e-25
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
588-660
1.88e-16
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: 75.84 E-value: 1.88e-16
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: 74.28 E-value: 3.77e-16
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
2351-2434
2.91e-14
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.
:
Pssm-ID: 214482 Cd Length: 82 Bit Score: 70.12 E-value: 2.91e-14
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: 58.87 E-value: 1.02e-10
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1217-1583
5.12e-08
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
The actual alignment was detected with superfamily member pfam05109:
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 58.77 E-value: 5.12e-08
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: 49.24 E-value: 2.80e-07
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
245-297
4.35e-07
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: 49.30 E-value: 4.35e-07
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1554-1962
3.73e-06
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
The actual alignment was detected with superfamily member pfam05109:
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 52.61 E-value: 3.73e-06
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
856-1017
2.27e-32
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: 124.82 E-value: 2.27e-32
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
386-549
5.75e-32
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: 123.67 E-value: 5.75e-32
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
397-549
1.08e-31
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: 122.48 E-value: 1.08e-31
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
868-1017
6.56e-26
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: 105.92 E-value: 6.56e-26
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
40-192
1.48e-25
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: 105.18 E-value: 1.48e-25
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
1056-1128
5.64e-25
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: 100.11 E-value: 5.64e-25
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
45-193
5.96e-25
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: 103.22 E-value: 5.96e-25
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
1060-1127
3.61e-21
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: 88.98 E-value: 3.61e-21
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
588-660
1.88e-16
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: 75.84 E-value: 1.88e-16
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: 74.28 E-value: 3.77e-16
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
591-660
1.88e-15
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: 72.80 E-value: 1.88e-15
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
302-357
3.23e-15
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: 71.65 E-value: 3.23e-15
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
2351-2434
2.91e-14
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.
Pssm-ID: 214482 Cd Length: 82 Bit Score: 70.12 E-value: 2.91e-14
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: 58.87 E-value: 1.02e-10
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
764-827
3.49e-09
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: 54.70 E-value: 3.49e-09
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1217-1583
5.12e-08
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 58.77 E-value: 5.12e-08
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: 49.24 E-value: 2.80e-07
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
245-297
4.35e-07
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: 49.30 E-value: 4.35e-07
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1554-1962
3.73e-06
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 52.61 E-value: 3.73e-06
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
664-721
2.85e-05
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: 43.53 E-value: 2.85e-05
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
856-1017
2.27e-32
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: 124.82 E-value: 2.27e-32
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
386-549
5.75e-32
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: 123.67 E-value: 5.75e-32
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
397-549
1.08e-31
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: 122.48 E-value: 1.08e-31
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
868-1017
6.56e-26
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: 105.92 E-value: 6.56e-26
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
40-192
1.48e-25
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: 105.18 E-value: 1.48e-25
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
1056-1128
5.64e-25
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: 100.11 E-value: 5.64e-25
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
45-193
5.96e-25
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: 103.22 E-value: 5.96e-25
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
1060-1127
3.61e-21
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: 88.98 E-value: 3.61e-21
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
588-660
1.88e-16
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: 75.84 E-value: 1.88e-16
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: 74.28 E-value: 3.77e-16
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
591-660
1.88e-15
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: 72.80 E-value: 1.88e-15
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
302-357
3.23e-15
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: 71.65 E-value: 3.23e-15
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
2351-2434
2.91e-14
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.
Pssm-ID: 214482 Cd Length: 82 Bit Score: 70.12 E-value: 2.91e-14
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: 58.87 E-value: 1.02e-10
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
764-827
3.49e-09
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: 54.70 E-value: 3.49e-09
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1217-1583
5.12e-08
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 58.77 E-value: 5.12e-08
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: 49.24 E-value: 2.80e-07
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
245-297
4.35e-07
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: 49.30 E-value: 4.35e-07
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1554-1962
3.73e-06
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 52.61 E-value: 3.73e-06
Domain of unknown function (DUF6721); This presumed domain is functionally uncharacterized. ...
1886-1963
2.50e-05
Domain of unknown function (DUF6721); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically a 100 amino acids in length.
Pssm-ID: 466630 [Multi-domain] Cd Length: 96 Bit Score: 45.07 E-value: 2.50e-05
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
664-721
2.85e-05
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: 43.53 E-value: 2.85e-05
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1339-1728
1.79e-04
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 47.07 E-value: 1.79e-04
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1269-1739
3.16e-04
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.06 E-value: 3.16e-04
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1722-2038
3.83e-03
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 42.83 E-value: 3.83e-03
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1890-2010
4.03e-03
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 42.45 E-value: 4.03e-03
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,
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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.
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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
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Domains are color coded according to superfamilies
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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
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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)
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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
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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
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