Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family ...
1232-1383
4.33e-74
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family includes alpha-L-arabinofuranosidase B (ABF B)-like proteins and otogelin-like proteins. Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. Hungateiclostridium thermocellum anti-sigma-I factor RsgI5 shows high sequence similarity with ABF B. It negatively regulates SigI5 activity through direct interaction. The OTOG subfamily includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in OTOG or OTOGL genes may cause hearing loss. Members of the ABFB family contain an ABD 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. The ABD binds two arabinose molecules in the beta and gamma subdomains.
The actual alignment was detected with superfamily member cd23400:
Pssm-ID: 483964 Cd Length: 152 Bit Score: 243.91 E-value: 4.33e-74
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
501-656
6.40e-45
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: 160.61 E-value: 6.40e-45
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
964-1118
1.33e-39
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: 145.62 E-value: 1.33e-39
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
139-289
1.14e-38
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: 142.51 E-value: 1.14e-38
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2098-2252
5.92e-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: 120.55 E-value: 5.92e-31
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
1153-1227
1.01e-22
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: 93.94 E-value: 1.01e-22
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2288-2356
1.26e-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: 76.61 E-value: 1.26e-16
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
336-399
3.01e-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: 72.41 E-value: 3.01e-15
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
2828-2910
1.68e-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: 70.90 E-value: 1.68e-14
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
700-754
1.23e-10
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: 59.32 E-value: 1.23e-10
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
767-831
4.02e-10
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: 57.40 E-value: 4.02e-10
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: 42.69 E-value: 7.54e-05
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
2359-2420
3.36e-04
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: 40.83 E-value: 3.36e-04
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: 38.84 E-value: 1.66e-03
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin (OTOG) and similar ...
1232-1383
4.33e-74
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin (OTOG) and similar proteins; OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of the otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. Mutations in the OTOG gene may cause hearing loss. OTOG contains an ABD 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. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467810 Cd Length: 152 Bit Score: 243.91 E-value: 4.33e-74
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
501-656
6.40e-45
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: 160.61 E-value: 6.40e-45
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
490-655
1.04e-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: 151.79 E-value: 1.04e-41
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
964-1118
1.33e-39
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: 145.62 E-value: 1.33e-39
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
139-289
1.14e-38
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: 142.51 E-value: 1.14e-38
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
973-1119
1.96e-37
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: 139.04 E-value: 1.96e-37
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
134-288
1.11e-35
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: 134.45 E-value: 1.11e-35
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2098-2252
5.92e-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: 120.55 E-value: 5.92e-31
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
2087-2251
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 ...
1153-1227
1.01e-22
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: 93.94 E-value: 1.01e-22
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
1160-1226
1.50e-17
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: 78.96 E-value: 1.50e-17
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2288-2356
1.26e-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: 76.61 E-value: 1.26e-16
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
336-399
3.01e-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: 72.41 E-value: 3.01e-15
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
2828-2910
1.68e-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: 70.90 E-value: 1.68e-14
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
335-399
2.08e-13
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: 67.37 E-value: 2.08e-13
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
700-754
1.23e-10
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: 59.32 E-value: 1.23e-10
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
767-831
4.02e-10
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: 57.40 E-value: 4.02e-10
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: 54.63 E-value: 4.59e-09
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
695-754
2.18e-08
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: 53.11 E-value: 2.18e-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: 42.69 E-value: 7.54e-05
Alpha-L-arabinofuranosidase B (ABFB) domain; This family consists of several fungal ...
1249-1383
2.18e-04
Alpha-L-arabinofuranosidase B (ABFB) domain; This family consists of several fungal alpha-L-arabinofuranosidase B proteins. L-Arabinose is a constituent of plant-cell-wall poly-saccharides. It is found in a polymeric form in L-arabinan, in which the backbone is formed by 1,5-a- linked l-arabinose residues that can be branched via 1,2-a- and 1,3-a-linked l-arabinofuranose side chains. AbfB hydrolyses 1,5-a, 1,3-a and 1,2-a linkages in both oligosaccharides and polysaccharides, which contain terminal non-reducing l-arabinofuranoses in side chains.
Pssm-ID: 428401 Cd Length: 137 Bit Score: 43.69 E-value: 2.18e-04
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
2359-2420
3.36e-04
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: 40.83 E-value: 3.36e-04
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
414-461
3.82e-04
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: 40.45 E-value: 3.82e-04
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: 38.84 E-value: 1.66e-03
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin (OTOG) and similar ...
1232-1383
4.33e-74
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin (OTOG) and similar proteins; OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of the otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. Mutations in the OTOG gene may cause hearing loss. OTOG contains an ABD 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. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467810 Cd Length: 152 Bit Score: 243.91 E-value: 4.33e-74
Arabinose-binding domain (ABD), beta-trefoil fold, found in the otogelin (OTOG) family; The ...
1237-1383
8.28e-48
Arabinose-binding domain (ABD), beta-trefoil fold, found in the otogelin (OTOG) family; The OTOG family includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of the otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in the OTOG or OTOGL gene may cause hearing loss. Members of this family contain an ABD 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. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467808 Cd Length: 143 Bit Score: 168.27 E-value: 8.28e-48
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
501-656
6.40e-45
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: 160.61 E-value: 6.40e-45
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
490-655
1.04e-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: 151.79 E-value: 1.04e-41
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
964-1118
1.33e-39
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: 145.62 E-value: 1.33e-39
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
139-289
1.14e-38
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: 142.51 E-value: 1.14e-38
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
973-1119
1.96e-37
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: 139.04 E-value: 1.96e-37
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
134-288
1.11e-35
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: 134.45 E-value: 1.11e-35
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2098-2252
5.92e-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: 120.55 E-value: 5.92e-31
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin-like protein (OTOGL) and ...
1232-1381
5.89e-28
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin-like protein (OTOGL) and similar proteins; OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in the OTOGL gene may cause hearing loss. OTOGL contains an ABD 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. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467811 Cd Length: 154 Bit Score: 111.87 E-value: 5.89e-28
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
2087-2251
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 ...
1153-1227
1.01e-22
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: 93.94 E-value: 1.01e-22
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
1160-1226
1.50e-17
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: 78.96 E-value: 1.50e-17
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2288-2356
1.26e-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: 76.61 E-value: 1.26e-16
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family ...
1237-1381
2.10e-15
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family includes alpha-L-arabinofuranosidase B (ABF B)-like proteins and otogelin-like proteins. Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. Hungateiclostridium thermocellum anti-sigma-I factor RsgI5 shows high sequence similarity with ABF B. It negatively regulates SigI5 activity through direct interaction. The OTOG subfamily includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in OTOG or OTOGL genes may cause hearing loss. Members of the ABFB family contain an ABD 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. The ABD binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467807 Cd Length: 135 Bit Score: 75.39 E-value: 2.10e-15
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
336-399
3.01e-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: 72.41 E-value: 3.01e-15
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
2828-2910
1.68e-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: 70.90 E-value: 1.68e-14
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
335-399
2.08e-13
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: 67.37 E-value: 2.08e-13
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1454-1876
3.48e-12
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: 72.64 E-value: 3.48e-12
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
700-754
1.23e-10
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: 59.32 E-value: 1.23e-10
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1433-1827
2.11e-10
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: 66.86 E-value: 2.11e-10
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
767-831
4.02e-10
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: 57.40 E-value: 4.02e-10
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1516-1966
1.91e-09
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: 63.40 E-value: 1.91e-09
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: 54.63 E-value: 4.59e-09
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
695-754
2.18e-08
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: 53.11 E-value: 2.18e-08
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1477-1903
1.01e-07
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: 57.85 E-value: 1.01e-07
Arabinose-binding domain (ABD), beta-trefoil fold, found in alpha-L-arabinofuranosidase B (ABF ...
1292-1381
8.31e-07
Arabinose-binding domain (ABD), beta-trefoil fold, found in alpha-L-arabinofuranosidase B (ABF B) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. The family also includes Hungateiclostridium thermocellum anti-sigma-I factor RsgI5. It negatively regulates SigI5 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI5 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI5. Members of the ABFB family contain an ABD 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. The ABD binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467809 Cd Length: 138 Bit Score: 50.67 E-value: 8.31e-07
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family ...
1295-1382
3.75e-06
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family includes alpha-L-arabinofuranosidase B (ABF B)-like proteins and otogelin-like proteins. Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. Hungateiclostridium thermocellum anti-sigma-I factor RsgI5 shows high sequence similarity with ABF B. It negatively regulates SigI5 activity through direct interaction. The OTOG subfamily includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in OTOG or OTOGL genes may cause hearing loss. Members of the ABFB family contain an ABD 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. The ABD binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467807 Cd Length: 135 Bit Score: 48.81 E-value: 3.75e-06
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1453-1871
8.04e-06
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: 51.69 E-value: 8.04e-06
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: 42.69 E-value: 7.54e-05
Alpha-L-arabinofuranosidase B (ABFB) domain; This family consists of several fungal ...
1249-1383
2.18e-04
Alpha-L-arabinofuranosidase B (ABFB) domain; This family consists of several fungal alpha-L-arabinofuranosidase B proteins. L-Arabinose is a constituent of plant-cell-wall poly-saccharides. It is found in a polymeric form in L-arabinan, in which the backbone is formed by 1,5-a- linked l-arabinose residues that can be branched via 1,2-a- and 1,3-a-linked l-arabinofuranose side chains. AbfB hydrolyses 1,5-a, 1,3-a and 1,2-a linkages in both oligosaccharides and polysaccharides, which contain terminal non-reducing l-arabinofuranoses in side chains.
Pssm-ID: 428401 Cd Length: 137 Bit Score: 43.69 E-value: 2.18e-04
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
2359-2420
3.36e-04
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: 40.83 E-value: 3.36e-04
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
414-461
3.82e-04
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: 40.45 E-value: 3.82e-04
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: 38.84 E-value: 1.66e-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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