zonadhesin isoform X1 [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | |||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1710-1860 | 3.20e-49 | |||||||
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: 173.71 E-value: 3.20e-49
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VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1326-1478 | 6.66e-43 | |||||||
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: 155.61 E-value: 6.66e-43
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VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
4904-5057 | 3.19e-39 | |||||||
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: 144.82 E-value: 3.19e-39
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
375-540 | 1.87e-37 | |||||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. : Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 140.17 E-value: 1.87e-37
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VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
2097-2255 | 2.62e-36 | |||||||
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: 136.73 E-value: 2.62e-36
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
217-373 | 5.59e-32 | |||||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. : Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 124.40 E-value: 5.59e-32
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
47-208 | 2.52e-31 | |||||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. : Pssm-ID: 99706 Cd Length: 157 Bit Score: 122.49 E-value: 2.52e-31
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1906-1977 | 1.14e-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: 91.63 E-value: 1.14e-21
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1516-1591 | 4.21e-19 | |||||||
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: 84.31 E-value: 4.21e-19
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3516-3570 | 1.71e-18 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 81.97 E-value: 1.71e-18
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3756-3810 | 3.34e-18 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 81.20 E-value: 3.34e-18
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3159-3213 | 1.68e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 79.27 E-value: 1.68e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3039-3093 | 1.80e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 79.27 E-value: 1.80e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2799-2853 | 2.05e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 78.88 E-value: 2.05e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2439-2493 | 2.24e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 78.88 E-value: 2.24e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3992-4046 | 3.43e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 78.11 E-value: 3.43e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4128-4179 | 7.56e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 77.34 E-value: 7.56e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3396-3450 | 1.06e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 76.96 E-value: 1.06e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2559-2613 | 2.58e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 75.80 E-value: 2.58e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3636-3690 | 3.46e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 75.42 E-value: 3.46e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4483-4537 | 3.63e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 75.42 E-value: 3.63e-16
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
5110-5186 | 7.63e-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: 75.07 E-value: 7.63e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3279-3333 | 1.25e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 73.88 E-value: 1.25e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4363-4417 | 1.96e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 73.49 E-value: 1.96e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2919-2973 | 2.08e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 73.11 E-value: 2.08e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4843-4897 | 3.17e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 72.72 E-value: 3.17e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2679-2733 | 5.01e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 72.34 E-value: 5.01e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4248-4295 | 5.69e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 71.95 E-value: 5.69e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3876-3926 | 8.16e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 71.57 E-value: 8.16e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4723-4777 | 1.15e-14 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 71.18 E-value: 1.15e-14
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4603-4657 | 2.74e-14 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 70.03 E-value: 2.74e-14
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DUF5585 super family | cl39316 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
486-913 | 1.02e-13 | |||||||
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. The actual alignment was detected with superfamily member pfam17823: Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 77.69 E-value: 1.02e-13
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1649-1703 | 8.04e-12 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 63.09 E-value: 8.04e-12
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1594-1647 | 2.19e-11 | |||||||
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: 61.95 E-value: 2.19e-11
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1266-1319 | 1.62e-10 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. : Pssm-ID: 432736 Cd Length: 54 Bit Score: 59.24 E-value: 1.62e-10
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1980-2034 | 1.43e-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: 56.63 E-value: 1.43e-09
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
5189-5242 | 1.50e-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: 56.63 E-value: 1.50e-09
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4543-4601 | 3.21e-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: 55.86 E-value: 3.21e-09
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VWC super family | cl17735 | von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
5244-5297 | 6.71e-09 | |||||||
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094. The actual alignment was detected with superfamily member pfam12714: Pssm-ID: 450195 Cd Length: 54 Bit Score: 54.62 E-value: 6.71e-09
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3932-3990 | 2.44e-08 | |||||||
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: 53.16 E-value: 2.44e-08
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4068-4126 | 1.45e-07 | |||||||
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: 50.85 E-value: 1.45e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3099-3157 | 2.19e-07 | |||||||
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: 50.46 E-value: 2.19e-07
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C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
2309-2375 | 2.30e-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: 50.84 E-value: 2.30e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2379-2437 | 3.98e-07 | |||||||
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: 49.62 E-value: 3.98e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3456-3514 | 5.88e-07 | |||||||
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: 49.31 E-value: 5.88e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2859-2917 | 6.12e-07 | |||||||
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: 6.12e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4783-4841 | 8.05e-07 | |||||||
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: 48.85 E-value: 8.05e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4303-4361 | 8.05e-07 | |||||||
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: 48.85 E-value: 8.05e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2499-2557 | 9.42e-07 | |||||||
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: 48.92 E-value: 9.42e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3219-3277 | 1.12e-06 | |||||||
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: 48.54 E-value: 1.12e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1215-1264 | 1.18e-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: 48.47 E-value: 1.18e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2619-2677 | 1.25e-06 | |||||||
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: 48.54 E-value: 1.25e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3339-3394 | 1.54e-06 | |||||||
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: 48.15 E-value: 1.54e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2739-2797 | 2.66e-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: 47.31 E-value: 2.66e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4188-4246 | 3.40e-06 | |||||||
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: 47.00 E-value: 3.40e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2979-3037 | 8.15e-06 | |||||||
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: 46.23 E-value: 8.15e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4663-4721 | 9.92e-06 | |||||||
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: 45.84 E-value: 9.92e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4423-4481 | 4.20e-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: 43.92 E-value: 4.20e-05
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3816-3874 | 4.82e-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: 43.92 E-value: 4.82e-05
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VWC super family | cl17735 | von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
2036-2091 | 6.06e-05 | |||||||
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094. The actual alignment was detected with superfamily member pfam12714: Pssm-ID: 450195 Cd Length: 54 Bit Score: 43.45 E-value: 6.06e-05
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3576-3634 | 1.80e-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: 42.37 E-value: 1.80e-04
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Name | Accession | Description | Interval | E-value | |||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1710-1860 | 3.20e-49 | |||||||
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: 173.71 E-value: 3.20e-49
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VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1326-1478 | 6.66e-43 | |||||||
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: 155.61 E-value: 6.66e-43
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VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
1702-1858 | 1.13e-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: 146.39 E-value: 1.13e-39
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VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
4904-5057 | 3.19e-39 | |||||||
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: 144.82 E-value: 3.19e-39
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
375-540 | 1.87e-37 | |||||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 140.17 E-value: 1.87e-37
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
379-541 | 2.77e-37 | |||||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 139.42 E-value: 2.77e-37
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VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
2097-2255 | 2.62e-36 | |||||||
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: 136.73 E-value: 2.62e-36
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
379-540 | 1.81e-33 | |||||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 128.65 E-value: 1.81e-33
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
217-373 | 5.59e-32 | |||||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 124.40 E-value: 5.59e-32
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
47-208 | 2.52e-31 | |||||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 122.49 E-value: 2.52e-31
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
217-371 | 6.57e-30 | |||||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 118.25 E-value: 6.57e-30
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VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
1324-1477 | 5.57e-29 | |||||||
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: 115.96 E-value: 5.57e-29
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VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
4903-5056 | 2.51e-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: 105.56 E-value: 2.51e-25
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
47-209 | 8.80e-25 | |||||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 103.60 E-value: 8.80e-25
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VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
2095-2255 | 1.11e-21 | |||||||
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: 95.16 E-value: 1.11e-21
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1906-1977 | 1.14e-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: 91.63 E-value: 1.14e-21
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
47-208 | 6.65e-20 | |||||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 89.71 E-value: 6.65e-20
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1516-1591 | 4.21e-19 | |||||||
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: 84.31 E-value: 4.21e-19
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3516-3570 | 1.71e-18 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 81.97 E-value: 1.71e-18
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3756-3810 | 3.34e-18 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 81.20 E-value: 3.34e-18
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3159-3213 | 1.68e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 79.27 E-value: 1.68e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3039-3093 | 1.80e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 79.27 E-value: 1.80e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2799-2853 | 2.05e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 78.88 E-value: 2.05e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2439-2493 | 2.24e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 78.88 E-value: 2.24e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3992-4046 | 3.43e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 78.11 E-value: 3.43e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4128-4179 | 7.56e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 77.34 E-value: 7.56e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3396-3450 | 1.06e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 76.96 E-value: 1.06e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2559-2613 | 2.58e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 75.80 E-value: 2.58e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3636-3690 | 3.46e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 75.42 E-value: 3.46e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4483-4537 | 3.63e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 75.42 E-value: 3.63e-16
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
5110-5186 | 7.63e-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: 75.07 E-value: 7.63e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3279-3333 | 1.25e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 73.88 E-value: 1.25e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4363-4417 | 1.96e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 73.49 E-value: 1.96e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2919-2973 | 2.08e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 73.11 E-value: 2.08e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4843-4897 | 3.17e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 72.72 E-value: 3.17e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2679-2733 | 5.01e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 72.34 E-value: 5.01e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4248-4295 | 5.69e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 71.95 E-value: 5.69e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3876-3926 | 8.16e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 71.57 E-value: 8.16e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4723-4777 | 1.15e-14 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 71.18 E-value: 1.15e-14
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
217-372 | 1.17e-14 | |||||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 74.69 E-value: 1.17e-14
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C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1909-1976 | 1.26e-14 | |||||||
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: 71.64 E-value: 1.26e-14
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4603-4657 | 2.74e-14 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 70.03 E-value: 2.74e-14
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DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
486-913 | 1.02e-13 | |||||||
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 77.69 E-value: 1.02e-13
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C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1522-1590 | 7.53e-13 | |||||||
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: 66.63 E-value: 7.53e-13
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C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
5115-5185 | 5.41e-12 | |||||||
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: 63.94 E-value: 5.41e-12
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1649-1703 | 8.04e-12 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 63.09 E-value: 8.04e-12
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1594-1647 | 2.19e-11 | |||||||
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: 61.95 E-value: 2.19e-11
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1594-1647 | 6.18e-11 | |||||||
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: 60.48 E-value: 6.18e-11
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1266-1319 | 1.62e-10 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 59.24 E-value: 1.62e-10
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PHA03255 | PHA03255 | BDLF3; Provisional |
702-857 | 1.69e-10 | |||||||
BDLF3; Provisional Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 64.54 E-value: 1.69e-10
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1980-2034 | 1.43e-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: 56.63 E-value: 1.43e-09
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
5189-5242 | 1.50e-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: 56.63 E-value: 1.50e-09
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4543-4601 | 3.21e-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: 55.86 E-value: 3.21e-09
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1980-2034 | 5.09e-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: 55.02 E-value: 5.09e-09
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
5244-5297 | 6.71e-09 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 54.62 E-value: 6.71e-09
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4543-4601 | 1.14e-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: 54.25 E-value: 1.14e-08
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3932-3990 | 2.44e-08 | |||||||
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: 53.16 E-value: 2.44e-08
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3932-3990 | 8.71e-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: 51.55 E-value: 8.71e-08
|
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4068-4126 | 1.45e-07 | |||||||
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: 50.85 E-value: 1.45e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3099-3157 | 2.19e-07 | |||||||
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: 50.46 E-value: 2.19e-07
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C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
2309-2375 | 2.30e-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: 50.84 E-value: 2.30e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4068-4126 | 2.34e-07 | |||||||
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: 50.39 E-value: 2.34e-07
|
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3099-3157 | 3.33e-07 | |||||||
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: 50.01 E-value: 3.33e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2379-2437 | 3.98e-07 | |||||||
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: 49.62 E-value: 3.98e-07
|
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3456-3514 | 5.88e-07 | |||||||
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: 49.31 E-value: 5.88e-07
|
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2859-2917 | 6.12e-07 | |||||||
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: 6.12e-07
|
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2379-2437 | 7.09e-07 | |||||||
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: 48.92 E-value: 7.09e-07
|
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4783-4841 | 8.05e-07 | |||||||
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: 48.85 E-value: 8.05e-07
|
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4303-4361 | 8.05e-07 | |||||||
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: 48.85 E-value: 8.05e-07
|
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2859-2917 | 8.21e-07 | |||||||
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: 48.92 E-value: 8.21e-07
|
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4783-4841 | 8.29e-07 | |||||||
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: 48.92 E-value: 8.29e-07
|
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2499-2557 | 9.42e-07 | |||||||
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: 48.92 E-value: 9.42e-07
|
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3219-3277 | 1.12e-06 | |||||||
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: 48.54 E-value: 1.12e-06
|
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1215-1264 | 1.18e-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: 48.47 E-value: 1.18e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2619-2677 | 1.25e-06 | |||||||
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: 48.54 E-value: 1.25e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3219-3277 | 1.31e-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: 48.47 E-value: 1.31e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4303-4361 | 1.31e-06 | |||||||
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: 48.15 E-value: 1.31e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3339-3394 | 1.54e-06 | |||||||
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: 48.15 E-value: 1.54e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
5189-5233 | 1.85e-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: 48.08 E-value: 1.85e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3339-3394 | 1.95e-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: 47.70 E-value: 1.95e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3456-3514 | 2.21e-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: 47.70 E-value: 2.21e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2499-2557 | 2.56e-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: 47.31 E-value: 2.56e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2739-2797 | 2.66e-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: 47.31 E-value: 2.66e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4188-4246 | 3.40e-06 | |||||||
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: 47.00 E-value: 3.40e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1215-1264 | 5.67e-06 | |||||||
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: 46.61 E-value: 5.67e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2739-2797 | 6.13e-06 | |||||||
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: 46.61 E-value: 6.13e-06
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COG3291 | COG3291 | Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
636-928 | 6.83e-06 | |||||||
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 51.98 E-value: 6.83e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2979-3037 | 8.15e-06 | |||||||
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: 46.23 E-value: 8.15e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4663-4721 | 9.92e-06 | |||||||
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: 45.84 E-value: 9.92e-06
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
2319-2376 | 1.39e-05 | |||||||
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: 46.18 E-value: 1.39e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2619-2677 | 1.56e-05 | |||||||
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: 45.39 E-value: 1.56e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4188-4246 | 1.97e-05 | |||||||
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: 45.00 E-value: 1.97e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4663-4721 | 2.22e-05 | |||||||
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: 45.00 E-value: 2.22e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2979-3037 | 2.73e-05 | |||||||
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: 44.62 E-value: 2.73e-05
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4423-4481 | 4.20e-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: 43.92 E-value: 4.20e-05
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3816-3874 | 4.82e-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: 43.92 E-value: 4.82e-05
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2036-2091 | 6.06e-05 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 43.45 E-value: 6.06e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4423-4481 | 9.21e-05 | |||||||
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: 43.07 E-value: 9.21e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3816-3874 | 1.42e-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: 42.69 E-value: 1.42e-04
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3576-3634 | 1.80e-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: 42.37 E-value: 1.80e-04
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3576-3634 | 2.17e-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: 41.92 E-value: 2.17e-04
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Name | Accession | Description | Interval | E-value | |||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1710-1860 | 3.20e-49 | |||||||
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: 173.71 E-value: 3.20e-49
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VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1326-1478 | 6.66e-43 | |||||||
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: 155.61 E-value: 6.66e-43
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VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
1702-1858 | 1.13e-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: 146.39 E-value: 1.13e-39
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VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
4904-5057 | 3.19e-39 | |||||||
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: 144.82 E-value: 3.19e-39
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
375-540 | 1.87e-37 | |||||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 140.17 E-value: 1.87e-37
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
379-541 | 2.77e-37 | |||||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 139.42 E-value: 2.77e-37
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VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
2097-2255 | 2.62e-36 | |||||||
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: 136.73 E-value: 2.62e-36
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
379-540 | 1.81e-33 | |||||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 128.65 E-value: 1.81e-33
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
217-373 | 5.59e-32 | |||||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 124.40 E-value: 5.59e-32
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
47-208 | 2.52e-31 | |||||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 122.49 E-value: 2.52e-31
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
217-371 | 6.57e-30 | |||||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 118.25 E-value: 6.57e-30
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VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
1324-1477 | 5.57e-29 | |||||||
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: 115.96 E-value: 5.57e-29
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VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
4903-5056 | 2.51e-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: 105.56 E-value: 2.51e-25
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
47-209 | 8.80e-25 | |||||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 103.60 E-value: 8.80e-25
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VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
2095-2255 | 1.11e-21 | |||||||
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: 95.16 E-value: 1.11e-21
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1906-1977 | 1.14e-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: 91.63 E-value: 1.14e-21
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
47-208 | 6.65e-20 | |||||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 89.71 E-value: 6.65e-20
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1516-1591 | 4.21e-19 | |||||||
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: 84.31 E-value: 4.21e-19
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3516-3570 | 1.71e-18 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 81.97 E-value: 1.71e-18
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3756-3810 | 3.34e-18 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 81.20 E-value: 3.34e-18
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3159-3213 | 1.68e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 79.27 E-value: 1.68e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3039-3093 | 1.80e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 79.27 E-value: 1.80e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2799-2853 | 2.05e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 78.88 E-value: 2.05e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2439-2493 | 2.24e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 78.88 E-value: 2.24e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3992-4046 | 3.43e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 78.11 E-value: 3.43e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4128-4179 | 7.56e-17 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 77.34 E-value: 7.56e-17
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3396-3450 | 1.06e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 76.96 E-value: 1.06e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2559-2613 | 2.58e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 75.80 E-value: 2.58e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3636-3690 | 3.46e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 75.42 E-value: 3.46e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4483-4537 | 3.63e-16 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 75.42 E-value: 3.63e-16
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
5110-5186 | 7.63e-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: 75.07 E-value: 7.63e-16
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3279-3333 | 1.25e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 73.88 E-value: 1.25e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4363-4417 | 1.96e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 73.49 E-value: 1.96e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2919-2973 | 2.08e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 73.11 E-value: 2.08e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4843-4897 | 3.17e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 72.72 E-value: 3.17e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2679-2733 | 5.01e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 72.34 E-value: 5.01e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4248-4295 | 5.69e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 71.95 E-value: 5.69e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
3876-3926 | 8.16e-15 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 71.57 E-value: 8.16e-15
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4723-4777 | 1.15e-14 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 71.18 E-value: 1.15e-14
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
217-372 | 1.17e-14 | |||||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 74.69 E-value: 1.17e-14
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C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1909-1976 | 1.26e-14 | |||||||
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: 71.64 E-value: 1.26e-14
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
4603-4657 | 2.74e-14 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 70.03 E-value: 2.74e-14
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DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
486-913 | 1.02e-13 | |||||||
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 77.69 E-value: 1.02e-13
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C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1522-1590 | 7.53e-13 | |||||||
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: 66.63 E-value: 7.53e-13
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Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
546-940 | 3.18e-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: 73.80 E-value: 3.18e-12
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C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
5115-5185 | 5.41e-12 | |||||||
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: 63.94 E-value: 5.41e-12
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1649-1703 | 8.04e-12 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 63.09 E-value: 8.04e-12
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DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
621-938 | 8.36e-12 | |||||||
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 71.53 E-value: 8.36e-12
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1594-1647 | 2.19e-11 | |||||||
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: 61.95 E-value: 2.19e-11
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1594-1647 | 6.18e-11 | |||||||
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: 60.48 E-value: 6.18e-11
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1266-1319 | 1.62e-10 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 59.24 E-value: 1.62e-10
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PHA03255 | PHA03255 | BDLF3; Provisional |
702-857 | 1.69e-10 | |||||||
BDLF3; Provisional Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 64.54 E-value: 1.69e-10
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1980-2034 | 1.43e-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: 56.63 E-value: 1.43e-09
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
5189-5242 | 1.50e-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: 56.63 E-value: 1.50e-09
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4543-4601 | 3.21e-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: 55.86 E-value: 3.21e-09
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1980-2034 | 5.09e-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: 55.02 E-value: 5.09e-09
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DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
725-1062 | 6.25e-09 | |||||||
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 62.28 E-value: 6.25e-09
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
5244-5297 | 6.71e-09 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 54.62 E-value: 6.71e-09
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4543-4601 | 1.14e-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: 54.25 E-value: 1.14e-08
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rne | PRK10811 | ribonuclease E; Reviewed |
652-832 | 1.31e-08 | |||||||
ribonuclease E; Reviewed Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 61.98 E-value: 1.31e-08
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3932-3990 | 2.44e-08 | |||||||
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: 53.16 E-value: 2.44e-08
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Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
560-921 | 3.72e-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: 60.32 E-value: 3.72e-08
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PHA03255 | PHA03255 | BDLF3; Provisional |
638-794 | 5.63e-08 | |||||||
BDLF3; Provisional Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 57.22 E-value: 5.63e-08
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3932-3990 | 8.71e-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: 51.55 E-value: 8.71e-08
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4068-4126 | 1.45e-07 | |||||||
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: 50.85 E-value: 1.45e-07
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Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
629-910 | 2.01e-07 | |||||||
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: 58.00 E-value: 2.01e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3099-3157 | 2.19e-07 | |||||||
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: 50.46 E-value: 2.19e-07
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C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
2309-2375 | 2.30e-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: 50.84 E-value: 2.30e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4068-4126 | 2.34e-07 | |||||||
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: 50.39 E-value: 2.34e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3099-3157 | 3.33e-07 | |||||||
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: 50.01 E-value: 3.33e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2379-2437 | 3.98e-07 | |||||||
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: 49.62 E-value: 3.98e-07
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rne | PRK10811 | ribonuclease E; Reviewed |
559-792 | 5.42e-07 | |||||||
ribonuclease E; Reviewed Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 56.59 E-value: 5.42e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3456-3514 | 5.88e-07 | |||||||
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: 49.31 E-value: 5.88e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2859-2917 | 6.12e-07 | |||||||
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: 6.12e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2379-2437 | 7.09e-07 | |||||||
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: 48.92 E-value: 7.09e-07
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rne | PRK10811 | ribonuclease E; Reviewed |
624-878 | 7.27e-07 | |||||||
ribonuclease E; Reviewed Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 56.20 E-value: 7.27e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4783-4841 | 8.05e-07 | |||||||
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: 48.85 E-value: 8.05e-07
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4303-4361 | 8.05e-07 | |||||||
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: 48.85 E-value: 8.05e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2859-2917 | 8.21e-07 | |||||||
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: 48.92 E-value: 8.21e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4783-4841 | 8.29e-07 | |||||||
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: 48.92 E-value: 8.29e-07
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2499-2557 | 9.42e-07 | |||||||
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: 48.92 E-value: 9.42e-07
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rne | PRK10811 | ribonuclease E; Reviewed |
668-939 | 1.08e-06 | |||||||
ribonuclease E; Reviewed Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 55.43 E-value: 1.08e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3219-3277 | 1.12e-06 | |||||||
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: 48.54 E-value: 1.12e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1215-1264 | 1.18e-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: 48.47 E-value: 1.18e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2619-2677 | 1.25e-06 | |||||||
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: 48.54 E-value: 1.25e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3219-3277 | 1.31e-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: 48.47 E-value: 1.31e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4303-4361 | 1.31e-06 | |||||||
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: 48.15 E-value: 1.31e-06
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rne | PRK10811 | ribonuclease E; Reviewed |
620-794 | 1.38e-06 | |||||||
ribonuclease E; Reviewed Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 55.05 E-value: 1.38e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3339-3394 | 1.54e-06 | |||||||
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: 48.15 E-value: 1.54e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
5189-5233 | 1.85e-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: 48.08 E-value: 1.85e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3339-3394 | 1.95e-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: 47.70 E-value: 1.95e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3456-3514 | 2.21e-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: 47.70 E-value: 2.21e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2499-2557 | 2.56e-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: 47.31 E-value: 2.56e-06
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2739-2797 | 2.66e-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: 47.31 E-value: 2.66e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4188-4246 | 3.40e-06 | |||||||
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: 47.00 E-value: 3.40e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1215-1264 | 5.67e-06 | |||||||
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: 46.61 E-value: 5.67e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2739-2797 | 6.13e-06 | |||||||
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: 46.61 E-value: 6.13e-06
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
552-906 | 6.18e-06 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 6.18e-06
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COG3291 | COG3291 | Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
636-928 | 6.83e-06 | |||||||
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 51.98 E-value: 6.83e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2979-3037 | 8.15e-06 | |||||||
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: 46.23 E-value: 8.15e-06
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4663-4721 | 9.92e-06 | |||||||
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: 45.84 E-value: 9.92e-06
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C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
2319-2376 | 1.39e-05 | |||||||
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: 46.18 E-value: 1.39e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2619-2677 | 1.56e-05 | |||||||
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: 45.39 E-value: 1.56e-05
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YjdB | COG5492 | Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ... |
573-910 | 1.76e-05 | |||||||
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only]; Pssm-ID: 444243 [Multi-domain] Cd Length: 613 Bit Score: 51.23 E-value: 1.76e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4188-4246 | 1.97e-05 | |||||||
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: 45.00 E-value: 1.97e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4663-4721 | 2.22e-05 | |||||||
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: 45.00 E-value: 2.22e-05
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PHA03255 | PHA03255 | BDLF3; Provisional |
777-932 | 2.65e-05 | |||||||
BDLF3; Provisional Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 49.13 E-value: 2.65e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2979-3037 | 2.73e-05 | |||||||
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: 44.62 E-value: 2.73e-05
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YbbR | COG4856 | Cyclic di-AMP synthase regulator CdaR, YbbR domain [Signal transduction mechanisms]; |
636-905 | 3.73e-05 | |||||||
Cyclic di-AMP synthase regulator CdaR, YbbR domain [Signal transduction mechanisms]; Pssm-ID: 443884 [Multi-domain] Cd Length: 392 Bit Score: 49.67 E-value: 3.73e-05
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
4423-4481 | 4.20e-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: 43.92 E-value: 4.20e-05
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3816-3874 | 4.82e-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: 43.92 E-value: 4.82e-05
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
534-871 | 5.78e-05 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 5.78e-05
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TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2036-2091 | 6.06e-05 | |||||||
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative. Pssm-ID: 432736 Cd Length: 54 Bit Score: 43.45 E-value: 6.06e-05
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DUF3246 | pfam11596 | Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ... |
545-750 | 6.38e-05 | |||||||
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose members, Swiss:A3LUS4 from Pichia stipitis is described as being an extremely serine rich protein-mucin-like protein. Pssm-ID: 371619 [Multi-domain] Cd Length: 241 Bit Score: 48.15 E-value: 6.38e-05
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YjdB | COG5492 | Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ... |
614-941 | 7.29e-05 | |||||||
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only]; Pssm-ID: 444243 [Multi-domain] Cd Length: 613 Bit Score: 49.30 E-value: 7.29e-05
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
4423-4481 | 9.21e-05 | |||||||
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: 43.07 E-value: 9.21e-05
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Cu_amine_oxidN1 | pfam07833 | Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ... |
1383-1444 | 1.25e-04 | |||||||
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other. Pssm-ID: 400265 [Multi-domain] Cd Length: 93 Bit Score: 43.75 E-value: 1.25e-04
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3816-3874 | 1.42e-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: 42.69 E-value: 1.42e-04
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DUF3246 | pfam11596 | Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ... |
613-829 | 1.64e-04 | |||||||
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose members, Swiss:A3LUS4 from Pichia stipitis is described as being an extremely serine rich protein-mucin-like protein. Pssm-ID: 371619 [Multi-domain] Cd Length: 241 Bit Score: 46.61 E-value: 1.64e-04
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TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
3576-3634 | 1.80e-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: 42.37 E-value: 1.80e-04
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Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
549-895 | 1.95e-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: 47.99 E-value: 1.95e-04
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PTZ00449 | PTZ00449 | 104 kDa microneme/rhoptry antigen; Provisional |
519-775 | 1.95e-04 | |||||||
104 kDa microneme/rhoptry antigen; Provisional Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 1.95e-04
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TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
3576-3634 | 2.17e-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: 41.92 E-value: 2.17e-04
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YjdB | COG5492 | Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ... |
576-936 | 3.04e-04 | |||||||
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only]; Pssm-ID: 444243 [Multi-domain] Cd Length: 613 Bit Score: 47.38 E-value: 3.04e-04
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DUF3246 | pfam11596 | Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ... |
707-926 | 5.01e-04 | |||||||
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose members, Swiss:A3LUS4 from Pichia stipitis is described as being an extremely serine rich protein-mucin-like protein. Pssm-ID: 371619 [Multi-domain] Cd Length: 241 Bit Score: 45.45 E-value: 5.01e-04
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rne | PRK10811 | ribonuclease E; Reviewed |
800-949 | 7.27e-04 | |||||||
ribonuclease E; Reviewed Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.19 E-value: 7.27e-04
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PRK11907 | PRK11907 | bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase; |
777-886 | 9.68e-04 | |||||||
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase; Pssm-ID: 237019 [Multi-domain] Cd Length: 814 Bit Score: 45.61 E-value: 9.68e-04
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DUF3246 | pfam11596 | Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ... |
755-936 | 1.13e-03 | |||||||
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose members, Swiss:A3LUS4 from Pichia stipitis is described as being an extremely serine rich protein-mucin-like protein. Pssm-ID: 371619 [Multi-domain] Cd Length: 241 Bit Score: 44.30 E-value: 1.13e-03
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ClfA | COG4932 | Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ... |
626-936 | 1.22e-03 | |||||||
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443959 [Multi-domain] Cd Length: 689 Bit Score: 45.35 E-value: 1.22e-03
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YjdB | COG5492 | Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ... |
575-936 | 1.38e-03 | |||||||
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only]; Pssm-ID: 444243 [Multi-domain] Cd Length: 613 Bit Score: 45.07 E-value: 1.38e-03
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PRK11907 | PRK11907 | bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase; |
691-804 | 2.05e-03 | |||||||
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase; Pssm-ID: 237019 [Multi-domain] Cd Length: 814 Bit Score: 44.84 E-value: 2.05e-03
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COG3291 | COG3291 | Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
580-848 | 2.14e-03 | |||||||
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 43.89 E-value: 2.14e-03
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PHA03255 | PHA03255 | BDLF3; Provisional |
519-715 | 4.14e-03 | |||||||
BDLF3; Provisional Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 42.58 E-value: 4.14e-03
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COG1470 | COG1470 | Uncharacterized membrane protein [Function unknown]; |
731-940 | 5.78e-03 | |||||||
Uncharacterized membrane protein [Function unknown]; Pssm-ID: 441079 [Multi-domain] Cd Length: 475 Bit Score: 42.92 E-value: 5.78e-03
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Blast search parameters | ||||
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