agrin [Notechis scutatus]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Laminin_G_1 | pfam00054 | Laminin G domain; |
987-1118 | 4.73e-47 | |||
Laminin G domain; : Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 164.80 E-value: 4.73e-47
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Laminin_G_1 | pfam00054 | Laminin G domain; |
1502-1633 | 4.98e-42 | |||
Laminin G domain; : Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 150.55 E-value: 4.98e-42
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Laminin_G_1 | pfam00054 | Laminin G domain; |
1255-1386 | 7.73e-39 | |||
Laminin G domain; : Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 141.30 E-value: 7.73e-39
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SEA | smart00200 | Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ... |
719-844 | 4.56e-24 | |||
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains. : Pssm-ID: 214554 Cd Length: 121 Bit Score: 98.64 E-value: 4.56e-24
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
330-375 | 1.21e-13 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. : Pssm-ID: 197624 Cd Length: 46 Bit Score: 66.55 E-value: 1.21e-13
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
36-82 | 3.80e-12 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. : Pssm-ID: 197624 Cd Length: 46 Bit Score: 62.31 E-value: 3.80e-12
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
501-548 | 1.46e-10 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. : Pssm-ID: 197624 Cd Length: 46 Bit Score: 57.69 E-value: 1.46e-10
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
124-157 | 1.47e-10 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. : Pssm-ID: 197624 Cd Length: 46 Bit Score: 57.69 E-value: 1.47e-10
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Laminin_EGF | pfam00053 | Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-462 | 9.84e-10 | |||
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. : Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.44 E-value: 9.84e-10
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
186-229 | 7.97e-09 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. : Pssm-ID: 197624 Cd Length: 46 Bit Score: 52.68 E-value: 7.97e-09
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
260-301 | 1.74e-08 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. : Pssm-ID: 197624 Cd Length: 46 Bit Score: 51.91 E-value: 1.74e-08
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EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
1409-1439 | 1.36e-06 | |||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. : Pssm-ID: 238011 Cd Length: 38 Bit Score: 46.48 E-value: 1.36e-06
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EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
922-950 | 3.55e-05 | |||
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: 41.98 E-value: 3.55e-05
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EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
1140-1171 | 6.91e-05 | |||
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: 41.21 E-value: 6.91e-05
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Name | Accession | Description | Interval | E-value | |||
Laminin_G_1 | pfam00054 | Laminin G domain; |
987-1118 | 4.73e-47 | |||
Laminin G domain; Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 164.80 E-value: 4.73e-47
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LamG | cd00110 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
963-1113 | 6.16e-47 | |||
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules. Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 165.28 E-value: 6.16e-47
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LamG | smart00282 | Laminin G domain; |
982-1115 | 1.63e-42 | |||
Laminin G domain; Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 152.11 E-value: 1.63e-42
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Laminin_G_1 | pfam00054 | Laminin G domain; |
1502-1633 | 4.98e-42 | |||
Laminin G domain; Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 150.55 E-value: 4.98e-42
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Laminin_G_1 | pfam00054 | Laminin G domain; |
1255-1386 | 7.73e-39 | |||
Laminin G domain; Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 141.30 E-value: 7.73e-39
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LamG | smart00282 | Laminin G domain; |
1497-1630 | 3.93e-34 | |||
Laminin G domain; Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 127.84 E-value: 3.93e-34
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LamG | cd00110 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1484-1628 | 4.07e-34 | |||
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules. Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 128.69 E-value: 4.07e-34
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LamG | cd00110 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1227-1380 | 2.76e-31 | |||
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules. Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 120.60 E-value: 2.76e-31
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LamG | smart00282 | Laminin G domain; |
1250-1382 | 1.07e-30 | |||
Laminin G domain; Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 118.21 E-value: 1.07e-30
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SEA | smart00200 | Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ... |
719-844 | 4.56e-24 | |||
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains. Pssm-ID: 214554 Cd Length: 121 Bit Score: 98.64 E-value: 4.56e-24
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
330-375 | 1.21e-13 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 66.55 E-value: 1.21e-13
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SEA | pfam01390 | SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ... |
737-821 | 1.93e-13 | |||
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain. Pssm-ID: 460188 Cd Length: 100 Bit Score: 67.65 E-value: 1.93e-13
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
36-82 | 3.80e-12 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 62.31 E-value: 3.80e-12
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
335-375 | 4.27e-12 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 61.90 E-value: 4.27e-12
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
42-82 | 3.53e-11 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 59.21 E-value: 3.53e-11
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
501-548 | 1.46e-10 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 57.69 E-value: 1.46e-10
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
124-157 | 1.47e-10 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 57.69 E-value: 1.47e-10
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Laminin_EGF | pfam00053 | Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-462 | 9.84e-10 | |||
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.44 E-value: 9.84e-10
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
124-157 | 4.92e-09 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 53.43 E-value: 4.92e-09
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
186-229 | 7.97e-09 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 52.68 E-value: 7.97e-09
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
260-301 | 1.74e-08 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 51.91 E-value: 1.74e-08
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
507-548 | 4.73e-08 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 50.35 E-value: 4.73e-08
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
261-301 | 5.37e-08 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 50.35 E-value: 5.37e-08
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EGF_Lam | cd00055 | Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-462 | 6.86e-08 | |||
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.43 E-value: 6.86e-08
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
189-229 | 9.02e-08 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 49.58 E-value: 9.02e-08
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EGF_Lam | smart00180 | Laminin-type epidermal growth factor-like domai; |
426-462 | 1.14e-07 | |||
Laminin-type epidermal growth factor-like domai; Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 1.14e-07
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Kazal_1 | pfam00050 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
189-229 | 2.88e-07 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family. Pssm-ID: 395004 Cd Length: 49 Bit Score: 48.44 E-value: 2.88e-07
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
330-375 | 4.93e-07 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 47.87 E-value: 4.93e-07
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EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
1409-1439 | 1.36e-06 | |||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 46.48 E-value: 1.36e-06
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
41-82 | 2.63e-05 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 42.87 E-value: 2.63e-05
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EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
922-950 | 3.55e-05 | |||
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: 41.98 E-value: 3.55e-05
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EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
1409-1439 | 4.32e-05 | |||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 42.23 E-value: 4.32e-05
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
499-548 | 5.88e-05 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 42.09 E-value: 5.88e-05
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EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
1140-1171 | 6.91e-05 | |||
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: 41.21 E-value: 6.91e-05
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
112-157 | 1.72e-04 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 40.94 E-value: 1.72e-04
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EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
922-954 | 6.79e-04 | |||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 38.77 E-value: 6.79e-04
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EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
1138-1172 | 2.28e-03 | |||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 37.23 E-value: 2.28e-03
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
258-301 | 5.66e-03 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 36.32 E-value: 5.66e-03
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EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
1408-1435 | 6.29e-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: 35.82 E-value: 6.29e-03
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EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
922-954 | 7.78e-03 | |||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 35.69 E-value: 7.78e-03
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Name | Accession | Description | Interval | E-value | |||
Laminin_G_1 | pfam00054 | Laminin G domain; |
987-1118 | 4.73e-47 | |||
Laminin G domain; Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 164.80 E-value: 4.73e-47
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LamG | cd00110 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
963-1113 | 6.16e-47 | |||
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules. Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 165.28 E-value: 6.16e-47
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LamG | smart00282 | Laminin G domain; |
982-1115 | 1.63e-42 | |||
Laminin G domain; Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 152.11 E-value: 1.63e-42
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Laminin_G_1 | pfam00054 | Laminin G domain; |
1502-1633 | 4.98e-42 | |||
Laminin G domain; Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 150.55 E-value: 4.98e-42
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Laminin_G_1 | pfam00054 | Laminin G domain; |
1255-1386 | 7.73e-39 | |||
Laminin G domain; Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 141.30 E-value: 7.73e-39
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LamG | smart00282 | Laminin G domain; |
1497-1630 | 3.93e-34 | |||
Laminin G domain; Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 127.84 E-value: 3.93e-34
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LamG | cd00110 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1484-1628 | 4.07e-34 | |||
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules. Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 128.69 E-value: 4.07e-34
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LamG | cd00110 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1227-1380 | 2.76e-31 | |||
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules. Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 120.60 E-value: 2.76e-31
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LamG | smart00282 | Laminin G domain; |
1250-1382 | 1.07e-30 | |||
Laminin G domain; Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 118.21 E-value: 1.07e-30
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Laminin_G_2 | pfam02210 | Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
987-1115 | 2.38e-30 | |||
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily. Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 117.14 E-value: 2.38e-30
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Laminin_G_2 | pfam02210 | Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1502-1630 | 5.35e-26 | |||
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily. Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 104.42 E-value: 5.35e-26
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SEA | smart00200 | Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ... |
719-844 | 4.56e-24 | |||
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains. Pssm-ID: 214554 Cd Length: 121 Bit Score: 98.64 E-value: 4.56e-24
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Laminin_G_2 | pfam02210 | Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1255-1383 | 1.46e-20 | |||
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily. Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 89.02 E-value: 1.46e-20
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
330-375 | 1.21e-13 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 66.55 E-value: 1.21e-13
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SEA | pfam01390 | SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ... |
737-821 | 1.93e-13 | |||
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain. Pssm-ID: 460188 Cd Length: 100 Bit Score: 67.65 E-value: 1.93e-13
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
36-82 | 3.80e-12 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 62.31 E-value: 3.80e-12
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
335-375 | 4.27e-12 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 61.90 E-value: 4.27e-12
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
42-82 | 3.53e-11 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 59.21 E-value: 3.53e-11
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
501-548 | 1.46e-10 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 57.69 E-value: 1.46e-10
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
124-157 | 1.47e-10 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 57.69 E-value: 1.47e-10
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Laminin_EGF | pfam00053 | Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
426-462 | 9.84e-10 | |||
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.44 E-value: 9.84e-10
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
124-157 | 4.92e-09 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 53.43 E-value: 4.92e-09
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
186-229 | 7.97e-09 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 52.68 E-value: 7.97e-09
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
260-301 | 1.74e-08 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 51.91 E-value: 1.74e-08
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
507-548 | 4.73e-08 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 50.35 E-value: 4.73e-08
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
261-301 | 5.37e-08 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 50.35 E-value: 5.37e-08
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EGF_Lam | cd00055 | Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
425-462 | 6.86e-08 | |||
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.43 E-value: 6.86e-08
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
189-229 | 9.02e-08 | |||
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 49.58 E-value: 9.02e-08
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EGF_Lam | smart00180 | Laminin-type epidermal growth factor-like domai; |
426-462 | 1.14e-07 | |||
Laminin-type epidermal growth factor-like domai; Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 1.14e-07
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KAZAL_PSTI | cd01327 | Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ... |
189-229 | 1.82e-07 | |||
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins. Pssm-ID: 238648 Cd Length: 45 Bit Score: 48.82 E-value: 1.82e-07
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Kazal_1 | pfam00050 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
189-229 | 2.88e-07 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family. Pssm-ID: 395004 Cd Length: 49 Bit Score: 48.44 E-value: 2.88e-07
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KAZAL_PSTI | cd01327 | Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ... |
332-375 | 3.51e-07 | |||
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins. Pssm-ID: 238648 Cd Length: 45 Bit Score: 48.05 E-value: 3.51e-07
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
330-375 | 4.93e-07 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 47.87 E-value: 4.93e-07
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EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
1409-1439 | 1.36e-06 | |||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 46.48 E-value: 1.36e-06
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KAZAL_PSTI | cd01327 | Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ... |
42-82 | 1.00e-05 | |||
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins. Pssm-ID: 238648 Cd Length: 45 Bit Score: 44.20 E-value: 1.00e-05
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FSL_SPARC | cd01328 | Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ... |
308-363 | 1.57e-05 | |||
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins. Pssm-ID: 238649 [Multi-domain] Cd Length: 86 Bit Score: 44.78 E-value: 1.57e-05
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
41-82 | 2.63e-05 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 42.87 E-value: 2.63e-05
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Kazal_1 | pfam00050 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
334-375 | 3.26e-05 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family. Pssm-ID: 395004 Cd Length: 49 Bit Score: 42.66 E-value: 3.26e-05
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EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
922-950 | 3.55e-05 | |||
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: 41.98 E-value: 3.55e-05
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EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
1409-1439 | 4.32e-05 | |||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 42.23 E-value: 4.32e-05
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
499-548 | 5.88e-05 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 42.09 E-value: 5.88e-05
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EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
1140-1171 | 6.91e-05 | |||
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: 41.21 E-value: 6.91e-05
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
112-157 | 1.72e-04 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 40.94 E-value: 1.72e-04
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EGF | cd00053 | Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
1407-1439 | 1.83e-04 | |||
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium. Pssm-ID: 238010 Cd Length: 36 Bit Score: 40.15 E-value: 1.83e-04
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
186-225 | 5.32e-04 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 39.40 E-value: 5.32e-04
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KAZAL_PSTI | cd01327 | Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ... |
124-157 | 5.49e-04 | |||
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins. Pssm-ID: 238648 Cd Length: 45 Bit Score: 39.19 E-value: 5.49e-04
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Kazal_1 | pfam00050 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
38-82 | 6.05e-04 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family. Pssm-ID: 395004 Cd Length: 49 Bit Score: 39.19 E-value: 6.05e-04
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EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
922-954 | 6.79e-04 | |||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 38.77 E-value: 6.79e-04
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Kazal_1 | pfam00050 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
122-157 | 1.29e-03 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family. Pssm-ID: 395004 Cd Length: 49 Bit Score: 38.03 E-value: 1.29e-03
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EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
1138-1172 | 2.28e-03 | |||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 37.23 E-value: 2.28e-03
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MFS_SLCO_OATP | cd17336 | Solute carrier organic anion transporters of the Major Facilitator Superfamily of transporters; ... |
329-354 | 3.18e-03 | |||
Solute carrier organic anion transporters of the Major Facilitator Superfamily of transporters; Solute carrier organic anion transporters (SLCOs) are also called organic anion transporting polypeptides (OATPs) or SLC21 (Solute carrier family 21) proteins. They are sodium-independent transporters that mediate the transport of a broad range of endo- as well as xenobiotics. Their substrates are mainly amphipathic organic anions with a molecular weight of more than 300Da, although there are a few known neutral or positively charged substrates. These include drugs including statins, angiotensin-converting enzyme inhibitors, angiotensin receptor blockers, antibiotics, antihistaminics, antihypertensives, and anticancer drugs. SLCOs/OATPs can be classified into 6 families (SLCO1-6 or OATP1-6) and each family may have subfamilies (e.g. OATP1A, OATP1B, OATP1C). Within the subfamilies, individual members are numbered according to the chronology of their identification and if there is already an ortholog known, they are given the same number. For example, the first SLCO identified, is rat OATP1A1 (encoded by the Slco1a1 gene). The second SLCO identified is the first human SLCO from the same subfamily and is called OATP1A2 (encoded by the SLCO1A2 gene). There are 11 human SLCOs/OATPs. SLCOs belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Pssm-ID: 340894 [Multi-domain] Cd Length: 411 Bit Score: 41.84 E-value: 3.18e-03
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FSL_SPARC | cd01328 | Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ... |
87-143 | 3.86e-03 | |||
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins. Pssm-ID: 238649 [Multi-domain] Cd Length: 86 Bit Score: 38.23 E-value: 3.86e-03
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FSL_SPARC | cd01328 | Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ... |
12-68 | 4.34e-03 | |||
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins. Pssm-ID: 238649 [Multi-domain] Cd Length: 86 Bit Score: 37.84 E-value: 4.34e-03
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EGF | cd00053 | Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
923-954 | 5.30e-03 | |||
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium. Pssm-ID: 238010 Cd Length: 36 Bit Score: 36.30 E-value: 5.30e-03
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
258-301 | 5.66e-03 | |||
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Pssm-ID: 400135 Cd Length: 50 Bit Score: 36.32 E-value: 5.66e-03
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EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
1408-1435 | 6.29e-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: 35.82 E-value: 6.29e-03
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Laminin_G_3 | pfam13385 | Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
1019-1086 | 6.52e-03 | |||
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily. Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 38.90 E-value: 6.52e-03
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EGF_CA | smart00179 | Calcium-binding EGF-like domain; |
922-954 | 7.78e-03 | |||
Calcium-binding EGF-like domain; Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 35.69 E-value: 7.78e-03
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Blast search parameters | ||||
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