PREDICTED: zonadhesin [Ceratotherium simum simum]
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 ... |
797-949 | 3.76e-50 | ||||
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: 175.25 E-value: 3.76e-50
|
||||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1182-1335 | 8.60e-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: 171.40 E-value: 8.60e-49
|
||||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1570-1723 | 8.98e-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: 154.07 E-value: 8.98e-43
|
||||||||
MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
384-546 | 6.47e-42 | ||||
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: 151.75 E-value: 6.47e-42
|
||||||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
49-213 | 4.43e-40 | ||||
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: 146.37 E-value: 4.43e-40
|
||||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1967-2121 | 1.51e-38 | ||||
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods. : Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 142.12 E-value: 1.51e-38
|
||||||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
222-376 | 2.69e-27 | ||||
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: 109.77 E-value: 2.69e-27
|
||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
990-1063 | 1.43e-20 | ||||
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: 87.78 E-value: 1.43e-20
|
||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1378-1449 | 3.72e-20 | ||||
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: 86.63 E-value: 3.72e-20
|
||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
2175-2250 | 4.55e-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: 83.54 E-value: 4.55e-19
|
||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1906-1960 | 5.50e-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: 71.18 E-value: 5.50e-15
|
||||||||
Herpes_BLLF1 super family | cl37540 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
486-690 | 1.06e-14 | ||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. The actual alignment was detected with superfamily member pfam05109: Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 80.35 E-value: 1.06e-14
|
||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1066-1119 | 4.78e-14 | ||||
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation. : Pssm-ID: 410995 Cd Length: 55 Bit Score: 68.50 E-value: 4.78e-14
|
||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1509-1563 | 8.61e-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: 67.71 E-value: 8.61e-14
|
||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2253-2306 | 1.13e-12 | ||||
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: 64.72 E-value: 1.13e-12
|
||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
737-790 | 2.50e-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: 63.48 E-value: 2.50e-12
|
||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1452-1507 | 4.27e-12 | ||||
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: 62.79 E-value: 4.27e-12
|
||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
686-735 | 4.33e-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: 60.09 E-value: 4.33e-11
|
||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1121-1175 | 7.50e-11 | ||||
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: 7.50e-11
|
||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1848-1904 | 6.37e-10 | ||||
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9. : Pssm-ID: 460351 Cd Length: 55 Bit Score: 56.63 E-value: 6.37e-10
|
||||||||
C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1777-1844 | 1.55e-09 | ||||
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: 56.23 E-value: 1.55e-09
|
||||||||
VWC super family | cl17735 | von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
2308-2361 | 4.39e-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: 54.23 E-value: 4.39e-09
|
||||||||
EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
2366-2395 | 3.35e-03 | ||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. : Pssm-ID: 394967 Cd Length: 31 Bit Score: 36.98 E-value: 3.35e-03
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
797-949 | 3.76e-50 | ||||
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: 175.25 E-value: 3.76e-50
|
||||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1182-1335 | 8.60e-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: 171.40 E-value: 8.60e-49
|
||||||||
VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
1174-1335 | 9.80e-45 | ||||
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: 159.87 E-value: 9.80e-45
|
||||||||
VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
789-948 | 7.72e-43 | ||||
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: 154.48 E-value: 7.72e-43
|
||||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1570-1723 | 8.98e-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: 154.07 E-value: 8.98e-43
|
||||||||
MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
384-546 | 6.47e-42 | ||||
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: 151.75 E-value: 6.47e-42
|
||||||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
49-213 | 4.43e-40 | ||||
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: 146.37 E-value: 4.43e-40
|
||||||||
MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
380-545 | 5.72e-40 | ||||
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: 146.33 E-value: 5.72e-40
|
||||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1967-2121 | 1.51e-38 | ||||
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods. Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 142.12 E-value: 1.51e-38
|
||||||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
384-545 | 1.50e-37 | ||||
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: 139.44 E-value: 1.50e-37
|
||||||||
VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
1570-1723 | 4.22e-36 | ||||
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: 135.22 E-value: 4.22e-36
|
||||||||
VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
1967-2120 | 2.66e-33 | ||||
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: 127.13 E-value: 2.66e-33
|
||||||||
MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
49-214 | 7.51e-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: 122.86 E-value: 7.51e-32
|
||||||||
MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
48-213 | 1.82e-28 | ||||
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: 113.21 E-value: 1.82e-28
|
||||||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
222-376 | 2.69e-27 | ||||
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: 109.77 E-value: 2.69e-27
|
||||||||
MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
222-378 | 1.29e-24 | ||||
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: 102.44 E-value: 1.29e-24
|
||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
990-1063 | 1.43e-20 | ||||
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: 87.78 E-value: 1.43e-20
|
||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1378-1449 | 3.72e-20 | ||||
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: 86.63 E-value: 3.72e-20
|
||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
2175-2250 | 4.55e-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: 83.54 E-value: 4.55e-19
|
||||||||
C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1382-1448 | 1.44e-15 | ||||
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826. Pssm-ID: 462584 Cd Length: 68 Bit Score: 73.18 E-value: 1.44e-15
|
||||||||
C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
994-1062 | 2.04e-15 | ||||
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826. Pssm-ID: 462584 Cd Length: 68 Bit Score: 72.80 E-value: 2.04e-15
|
||||||||
C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
2179-2249 | 2.34e-15 | ||||
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826. Pssm-ID: 462584 Cd Length: 68 Bit Score: 72.41 E-value: 2.34e-15
|
||||||||
MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
222-377 | 3.48e-15 | ||||
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: 75.46 E-value: 3.48e-15
|
||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1906-1960 | 5.50e-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: 71.18 E-value: 5.50e-15
|
||||||||
Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
486-690 | 1.06e-14 | ||||
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: 80.35 E-value: 1.06e-14
|
||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1066-1119 | 4.78e-14 | ||||
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation. Pssm-ID: 410995 Cd Length: 55 Bit Score: 68.50 E-value: 4.78e-14
|
||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1509-1563 | 8.61e-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: 67.71 E-value: 8.61e-14
|
||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1066-1119 | 3.83e-13 | ||||
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: 65.87 E-value: 3.83e-13
|
||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2253-2306 | 1.13e-12 | ||||
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: 64.72 E-value: 1.13e-12
|
||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
737-790 | 2.50e-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: 63.48 E-value: 2.50e-12
|
||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1452-1507 | 4.27e-12 | ||||
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: 62.79 E-value: 4.27e-12
|
||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1452-1507 | 6.38e-12 | ||||
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: 62.33 E-value: 6.38e-12
|
||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
686-735 | 4.33e-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: 60.09 E-value: 4.33e-11
|
||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1121-1175 | 7.50e-11 | ||||
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: 7.50e-11
|
||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
686-735 | 1.07e-10 | ||||
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation. Pssm-ID: 410995 Cd Length: 55 Bit Score: 58.87 E-value: 1.07e-10
|
||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2253-2296 | 1.09e-10 | ||||
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation. Pssm-ID: 410995 Cd Length: 55 Bit Score: 58.87 E-value: 1.09e-10
|
||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
548-694 | 5.09e-10 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 65.73 E-value: 5.09e-10
|
||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1848-1904 | 6.37e-10 | ||||
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9. Pssm-ID: 460351 Cd Length: 55 Bit Score: 56.63 E-value: 6.37e-10
|
||||||||
C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1777-1844 | 1.55e-09 | ||||
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: 56.23 E-value: 1.55e-09
|
||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1848-1904 | 2.23e-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: 2.23e-09
|
||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2308-2361 | 4.39e-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: 54.23 E-value: 4.39e-09
|
||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1788-1845 | 2.08e-08 | ||||
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. Pssm-ID: 214843 Cd Length: 76 Bit Score: 53.11 E-value: 2.08e-08
|
||||||||
PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
534-715 | 1.58e-07 | ||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 56.70 E-value: 1.58e-07
|
||||||||
PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
547-706 | 8.30e-07 | ||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 54.39 E-value: 8.30e-07
|
||||||||
VWC_out | smart00215 | von Willebrand factor (vWF) type C domain; |
2308-2371 | 1.57e-06 | ||||
von Willebrand factor (vWF) type C domain; Pssm-ID: 214565 Cd Length: 67 Bit Score: 47.56 E-value: 1.57e-06
|
||||||||
2A1904 | TIGR00927 | K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
572-694 | 4.67e-05 | ||||
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 48.84 E-value: 4.67e-05
|
||||||||
EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
2366-2395 | 3.35e-03 | ||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. Pssm-ID: 394967 Cd Length: 31 Bit Score: 36.98 E-value: 3.35e-03
|
||||||||
Name | Accession | Description | Interval | E-value | |||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
797-949 | 3.76e-50 | |||||
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: 175.25 E-value: 3.76e-50
|
|||||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1182-1335 | 8.60e-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: 171.40 E-value: 8.60e-49
|
|||||||||
VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
1174-1335 | 9.80e-45 | |||||
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: 159.87 E-value: 9.80e-45
|
|||||||||
VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
789-948 | 7.72e-43 | |||||
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: 154.48 E-value: 7.72e-43
|
|||||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1570-1723 | 8.98e-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: 154.07 E-value: 8.98e-43
|
|||||||||
MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
384-546 | 6.47e-42 | |||||
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: 151.75 E-value: 6.47e-42
|
|||||||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
49-213 | 4.43e-40 | |||||
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: 146.37 E-value: 4.43e-40
|
|||||||||
MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
380-545 | 5.72e-40 | |||||
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: 146.33 E-value: 5.72e-40
|
|||||||||
VWD | pfam00094 | von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
1967-2121 | 1.51e-38 | |||||
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods. Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 142.12 E-value: 1.51e-38
|
|||||||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
384-545 | 1.50e-37 | |||||
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: 139.44 E-value: 1.50e-37
|
|||||||||
VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
1570-1723 | 4.22e-36 | |||||
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: 135.22 E-value: 4.22e-36
|
|||||||||
VWD | smart00216 | von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
1967-2120 | 2.66e-33 | |||||
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: 127.13 E-value: 2.66e-33
|
|||||||||
MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
49-214 | 7.51e-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: 122.86 E-value: 7.51e-32
|
|||||||||
MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
48-213 | 1.82e-28 | |||||
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: 113.21 E-value: 1.82e-28
|
|||||||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
222-376 | 2.69e-27 | |||||
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: 109.77 E-value: 2.69e-27
|
|||||||||
MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
222-378 | 1.29e-24 | |||||
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: 102.44 E-value: 1.29e-24
|
|||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
990-1063 | 1.43e-20 | |||||
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: 87.78 E-value: 1.43e-20
|
|||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1378-1449 | 3.72e-20 | |||||
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: 86.63 E-value: 3.72e-20
|
|||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
2175-2250 | 4.55e-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: 83.54 E-value: 4.55e-19
|
|||||||||
C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1382-1448 | 1.44e-15 | |||||
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826. Pssm-ID: 462584 Cd Length: 68 Bit Score: 73.18 E-value: 1.44e-15
|
|||||||||
C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
994-1062 | 2.04e-15 | |||||
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826. Pssm-ID: 462584 Cd Length: 68 Bit Score: 72.80 E-value: 2.04e-15
|
|||||||||
C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
2179-2249 | 2.34e-15 | |||||
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826. Pssm-ID: 462584 Cd Length: 68 Bit Score: 72.41 E-value: 2.34e-15
|
|||||||||
MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
222-377 | 3.48e-15 | |||||
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: 75.46 E-value: 3.48e-15
|
|||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1906-1960 | 5.50e-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: 71.18 E-value: 5.50e-15
|
|||||||||
Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
486-690 | 1.06e-14 | |||||
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: 80.35 E-value: 1.06e-14
|
|||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1066-1119 | 4.78e-14 | |||||
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation. Pssm-ID: 410995 Cd Length: 55 Bit Score: 68.50 E-value: 4.78e-14
|
|||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1509-1563 | 8.61e-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: 67.71 E-value: 8.61e-14
|
|||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1066-1119 | 3.83e-13 | |||||
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: 65.87 E-value: 3.83e-13
|
|||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
2253-2306 | 1.13e-12 | |||||
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: 64.72 E-value: 1.13e-12
|
|||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
737-790 | 2.50e-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: 63.48 E-value: 2.50e-12
|
|||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1452-1507 | 4.27e-12 | |||||
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: 62.79 E-value: 4.27e-12
|
|||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1452-1507 | 6.38e-12 | |||||
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: 62.33 E-value: 6.38e-12
|
|||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
686-735 | 4.33e-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: 60.09 E-value: 4.33e-11
|
|||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
1121-1175 | 7.50e-11 | |||||
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: 7.50e-11
|
|||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
686-735 | 1.07e-10 | |||||
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation. Pssm-ID: 410995 Cd Length: 55 Bit Score: 58.87 E-value: 1.07e-10
|
|||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
2253-2296 | 1.09e-10 | |||||
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation. Pssm-ID: 410995 Cd Length: 55 Bit Score: 58.87 E-value: 1.09e-10
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
548-694 | 5.09e-10 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 65.73 E-value: 5.09e-10
|
|||||||||
TIL | pfam01826 | Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
1848-1904 | 6.37e-10 | |||||
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9. Pssm-ID: 460351 Cd Length: 55 Bit Score: 56.63 E-value: 6.37e-10
|
|||||||||
DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
479-694 | 9.50e-10 | |||||
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: 63.83 E-value: 9.50e-10
|
|||||||||
DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
482-714 | 1.04e-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: 63.44 E-value: 1.04e-09
|
|||||||||
C8 | pfam08742 | C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1777-1844 | 1.55e-09 | |||||
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: 56.23 E-value: 1.55e-09
|
|||||||||
TIL | cd19941 | trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1848-1904 | 2.23e-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: 2.23e-09
|
|||||||||
Metaviral_G | pfam09595 | Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ... |
588-707 | 2.97e-09 | |||||
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated. Pssm-ID: 462833 [Multi-domain] Cd Length: 183 Bit Score: 58.81 E-value: 2.97e-09
|
|||||||||
TILa | pfam12714 | TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ... |
2308-2361 | 4.39e-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: 54.23 E-value: 4.39e-09
|
|||||||||
C8 | smart00832 | This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1788-1845 | 2.08e-08 | |||||
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. Pssm-ID: 214843 Cd Length: 76 Bit Score: 53.11 E-value: 2.08e-08
|
|||||||||
Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
502-706 | 2.61e-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: 59.54 E-value: 2.61e-08
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
548-714 | 7.01e-08 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.41 E-value: 7.01e-08
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
546-688 | 7.44e-08 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.41 E-value: 7.44e-08
|
|||||||||
PHA03378 | PHA03378 | EBNA-3B; Provisional |
541-690 | 8.38e-08 | |||||
EBNA-3B; Provisional Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 58.15 E-value: 8.38e-08
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
548-707 | 1.57e-07 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.26 E-value: 1.57e-07
|
|||||||||
PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
534-715 | 1.58e-07 | |||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 56.70 E-value: 1.58e-07
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
546-707 | 1.90e-07 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.26 E-value: 1.90e-07
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
548-706 | 5.71e-07 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 5.71e-07
|
|||||||||
PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
547-706 | 8.30e-07 | |||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 54.39 E-value: 8.30e-07
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
548-714 | 9.53e-07 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.94 E-value: 9.53e-07
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
548-706 | 1.18e-06 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.56 E-value: 1.18e-06
|
|||||||||
VWC_out | smart00215 | von Willebrand factor (vWF) type C domain; |
2308-2371 | 1.57e-06 | |||||
von Willebrand factor (vWF) type C domain; Pssm-ID: 214565 Cd Length: 67 Bit Score: 47.56 E-value: 1.57e-06
|
|||||||||
PLN03209 | PLN03209 | translocon at the inner envelope of chloroplast subunit 62; Provisional |
554-707 | 2.58e-06 | |||||
translocon at the inner envelope of chloroplast subunit 62; Provisional Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 52.62 E-value: 2.58e-06
|
|||||||||
PLN03209 | PLN03209 | translocon at the inner envelope of chloroplast subunit 62; Provisional |
543-707 | 8.31e-06 | |||||
translocon at the inner envelope of chloroplast subunit 62; Provisional Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 51.08 E-value: 8.31e-06
|
|||||||||
TALPID3 | pfam15324 | Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ... |
547-717 | 1.39e-05 | |||||
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for Hedgehog signalling. Mutations in this gene noticed first in chickens lead to multiple abnormalities of development. Pssm-ID: 434634 [Multi-domain] Cd Length: 1288 Bit Score: 50.66 E-value: 1.39e-05
|
|||||||||
DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
549-688 | 1.58e-05 | |||||
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: 49.96 E-value: 1.58e-05
|
|||||||||
PHA02682 | PHA02682 | ORF080 virion core protein; Provisional |
565-706 | 2.90e-05 | |||||
ORF080 virion core protein; Provisional Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 48.32 E-value: 2.90e-05
|
|||||||||
PHA02682 | PHA02682 | ORF080 virion core protein; Provisional |
564-679 | 4.42e-05 | |||||
ORF080 virion core protein; Provisional Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 47.93 E-value: 4.42e-05
|
|||||||||
2A1904 | TIGR00927 | K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
572-694 | 4.67e-05 | |||||
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 48.84 E-value: 4.67e-05
|
|||||||||
PRK14950 | PRK14950 | DNA polymerase III subunits gamma and tau; Provisional |
575-691 | 5.77e-05 | |||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 48.27 E-value: 5.77e-05
|
|||||||||
PRK10905 | PRK10905 | cell division protein DamX; Validated |
582-685 | 6.63e-05 | |||||
cell division protein DamX; Validated Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 47.63 E-value: 6.63e-05
|
|||||||||
Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
544-715 | 7.11e-05 | |||||
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: 48.37 E-value: 7.11e-05
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
548-707 | 8.56e-05 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.40 E-value: 8.56e-05
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
546-685 | 1.11e-04 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.01 E-value: 1.11e-04
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
539-734 | 1.26e-04 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 1.26e-04
|
|||||||||
PRK14950 | PRK14950 | DNA polymerase III subunits gamma and tau; Provisional |
574-663 | 1.75e-04 | |||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 46.73 E-value: 1.75e-04
|
|||||||||
PHA03378 | PHA03378 | EBNA-3B; Provisional |
548-705 | 1.78e-04 | |||||
EBNA-3B; Provisional Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 46.98 E-value: 1.78e-04
|
|||||||||
PRK07003 | PRK07003 | DNA polymerase III subunit gamma/tau; |
547-706 | 3.04e-04 | |||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.38 E-value: 3.04e-04
|
|||||||||
SAP130_C | pfam16014 | Histone deacetylase complex subunit SAP130 C-terminus; |
575-698 | 3.18e-04 | |||||
Histone deacetylase complex subunit SAP130 C-terminus; Pssm-ID: 464973 [Multi-domain] Cd Length: 371 Bit Score: 45.69 E-value: 3.18e-04
|
|||||||||
PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
546-706 | 3.52e-04 | |||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.32 E-value: 3.52e-04
|
|||||||||
Cu_amine_oxidN1 | pfam07833 | Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ... |
853-915 | 3.77e-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: 41.43 E-value: 3.77e-04
|
|||||||||
PRK11901 | PRK11901 | hypothetical protein; Reviewed |
616-692 | 3.89e-04 | |||||
hypothetical protein; Reviewed Pssm-ID: 237015 [Multi-domain] Cd Length: 327 Bit Score: 45.06 E-value: 3.89e-04
|
|||||||||
PHA03269 | PHA03269 | envelope glycoprotein C; Provisional |
589-707 | 4.08e-04 | |||||
envelope glycoprotein C; Provisional Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 45.49 E-value: 4.08e-04
|
|||||||||
PRK14951 | PRK14951 | DNA polymerase III subunits gamma and tau; Provisional |
614-707 | 4.40e-04 | |||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 45.48 E-value: 4.40e-04
|
|||||||||
rne | PRK10811 | ribonuclease E; Reviewed |
554-711 | 4.72e-04 | |||||
ribonuclease E; Reviewed Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 45.80 E-value: 4.72e-04
|
|||||||||
PRK11633 | PRK11633 | cell division protein DedD; Provisional |
581-690 | 5.97e-04 | |||||
cell division protein DedD; Provisional Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 43.84 E-value: 5.97e-04
|
|||||||||
PRK11901 | PRK11901 | hypothetical protein; Reviewed |
582-682 | 6.02e-04 | |||||
hypothetical protein; Reviewed Pssm-ID: 237015 [Multi-domain] Cd Length: 327 Bit Score: 44.67 E-value: 6.02e-04
|
|||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
549-705 | 6.91e-04 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 6.91e-04
|
|||||||||
SOBP | pfam15279 | Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ... |
543-700 | 7.16e-04 | |||||
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein. Pssm-ID: 464609 [Multi-domain] Cd Length: 325 Bit Score: 44.42 E-value: 7.16e-04
|
|||||||||
PRK14951 | PRK14951 | DNA polymerase III subunits gamma and tau; Provisional |
547-688 | 1.26e-03 | |||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.93 E-value: 1.26e-03
|
|||||||||
VWC | smart00214 | von Willebrand factor (vWF) type C domain; |
2308-2354 | 1.62e-03 | |||||
von Willebrand factor (vWF) type C domain; Pssm-ID: 214564 Cd Length: 59 Bit Score: 38.65 E-value: 1.62e-03
|
|||||||||
2A1904 | TIGR00927 | K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
562-664 | 1.75e-03 | |||||
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.83 E-value: 1.75e-03
|
|||||||||
PRK14950 | PRK14950 | DNA polymerase III subunits gamma and tau; Provisional |
626-706 | 2.28e-03 | |||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 43.26 E-value: 2.28e-03
|
|||||||||
EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
2366-2395 | 3.35e-03 | |||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. Pssm-ID: 394967 Cd Length: 31 Bit Score: 36.98 E-value: 3.35e-03
|
|||||||||
Blast search parameters | ||||
|