tissue-type plasminogen activator preproprotein [Mus musculus]
Protein Classification
calcium-binding EGF-like domain-containing protein; serine protease( domain architecture ID 12499197)
calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions| trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile; contains C-terminal DNA polymerase III subunits gamma and tau
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
311-556 | 1.59e-90 | |||||
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. : Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 278.01 E-value: 1.59e-90
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| KR | cd00108 | Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ... |
210-295 | 3.64e-26 | |||||
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides. : Pssm-ID: 238056 Cd Length: 83 Bit Score: 101.69 E-value: 3.64e-26
|
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| Kringle | pfam00051 | Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ... |
124-205 | 1.30e-25 | |||||
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. : Pssm-ID: 395005 Cd Length: 79 Bit Score: 100.07 E-value: 1.30e-25
|
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| FN1 | smart00058 | Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ... |
38-80 | 1.33e-08 | |||||
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, fibronectin. Found also in coagulation factor XII, HGF activator and tissue-type plasminogen activator. In t-PA and fibronectin, this domain type contributes to fibrin-binding. : Pssm-ID: 214494 Cd Length: 45 Bit Score: 50.81 E-value: 1.33e-08
|
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| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
83-115 | 9.97e-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: 33.90 E-value: 9.97e-03
|
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| Name | Accession | Description | Interval | E-value | |||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
311-556 | 1.59e-90 | |||||
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 278.01 E-value: 1.59e-90
|
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| Tryp_SPc | smart00020 | Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
308-553 | 2.01e-88 | |||||
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues. Pssm-ID: 214473 Cd Length: 229 Bit Score: 272.24 E-value: 2.01e-88
|
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| Trypsin | pfam00089 | Trypsin; |
309-553 | 8.71e-70 | |||||
Trypsin; Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 223.86 E-value: 8.71e-70
|
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| COG5640 | COG5640 | Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
305-557 | 2.56e-58 | |||||
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 195.25 E-value: 2.56e-58
|
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| KR | cd00108 | Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ... |
210-295 | 3.64e-26 | |||||
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides. Pssm-ID: 238056 Cd Length: 83 Bit Score: 101.69 E-value: 3.64e-26
|
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| Kringle | pfam00051 | Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ... |
124-205 | 1.30e-25 | |||||
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. Pssm-ID: 395005 Cd Length: 79 Bit Score: 100.07 E-value: 1.30e-25
|
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| KR | smart00130 | Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ... |
211-295 | 3.24e-24 | |||||
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides. Pssm-ID: 214527 Cd Length: 83 Bit Score: 96.31 E-value: 3.24e-24
|
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| Kringle | pfam00051 | Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ... |
213-294 | 1.44e-23 | |||||
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. Pssm-ID: 395005 Cd Length: 79 Bit Score: 94.30 E-value: 1.44e-23
|
|||||||||
| KR | cd00108 | Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ... |
122-206 | 6.60e-22 | |||||
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides. Pssm-ID: 238056 Cd Length: 83 Bit Score: 89.74 E-value: 6.60e-22
|
|||||||||
| KR | smart00130 | Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ... |
123-206 | 4.44e-21 | |||||
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides. Pssm-ID: 214527 Cd Length: 83 Bit Score: 87.45 E-value: 4.44e-21
|
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| FN1 | smart00058 | Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ... |
38-80 | 1.33e-08 | |||||
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, fibronectin. Found also in coagulation factor XII, HGF activator and tissue-type plasminogen activator. In t-PA and fibronectin, this domain type contributes to fibrin-binding. Pssm-ID: 214494 Cd Length: 45 Bit Score: 50.81 E-value: 1.33e-08
|
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| fn1 | pfam00039 | Fibronectin type I domain; |
38-75 | 2.06e-05 | |||||
Fibronectin type I domain; Pssm-ID: 459644 Cd Length: 40 Bit Score: 41.53 E-value: 2.06e-05
|
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| FN1 | cd00061 | Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ... |
37-78 | 2.00e-04 | |||||
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. FN1 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. FN1 domains also found in coagulation factor XII, HGF activator, and tissue-type plasminogen activator. In tissue plasminogen activator, FN1 domains may form functional fibrin-binding units with EGF-like domains C-terminal to FN1. Pssm-ID: 238018 Cd Length: 43 Bit Score: 38.85 E-value: 2.00e-04
|
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| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
83-115 | 9.97e-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: 33.90 E-value: 9.97e-03
|
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| Name | Accession | Description | Interval | E-value | |||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
311-556 | 1.59e-90 | |||||
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 278.01 E-value: 1.59e-90
|
|||||||||
| Tryp_SPc | smart00020 | Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
308-553 | 2.01e-88 | |||||
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues. Pssm-ID: 214473 Cd Length: 229 Bit Score: 272.24 E-value: 2.01e-88
|
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| Trypsin | pfam00089 | Trypsin; |
309-553 | 8.71e-70 | |||||
Trypsin; Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 223.86 E-value: 8.71e-70
|
|||||||||
| COG5640 | COG5640 | Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
305-557 | 2.56e-58 | |||||
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 195.25 E-value: 2.56e-58
|
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| KR | cd00108 | Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ... |
210-295 | 3.64e-26 | |||||
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides. Pssm-ID: 238056 Cd Length: 83 Bit Score: 101.69 E-value: 3.64e-26
|
|||||||||
| Kringle | pfam00051 | Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ... |
124-205 | 1.30e-25 | |||||
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. Pssm-ID: 395005 Cd Length: 79 Bit Score: 100.07 E-value: 1.30e-25
|
|||||||||
| KR | smart00130 | Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ... |
211-295 | 3.24e-24 | |||||
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides. Pssm-ID: 214527 Cd Length: 83 Bit Score: 96.31 E-value: 3.24e-24
|
|||||||||
| Kringle | pfam00051 | Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ... |
213-294 | 1.44e-23 | |||||
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. Pssm-ID: 395005 Cd Length: 79 Bit Score: 94.30 E-value: 1.44e-23
|
|||||||||
| KR | cd00108 | Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ... |
122-206 | 6.60e-22 | |||||
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides. Pssm-ID: 238056 Cd Length: 83 Bit Score: 89.74 E-value: 6.60e-22
|
|||||||||
| KR | smart00130 | Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ... |
123-206 | 4.44e-21 | |||||
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides. Pssm-ID: 214527 Cd Length: 83 Bit Score: 87.45 E-value: 4.44e-21
|
|||||||||
| FN1 | smart00058 | Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ... |
38-80 | 1.33e-08 | |||||
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, fibronectin. Found also in coagulation factor XII, HGF activator and tissue-type plasminogen activator. In t-PA and fibronectin, this domain type contributes to fibrin-binding. Pssm-ID: 214494 Cd Length: 45 Bit Score: 50.81 E-value: 1.33e-08
|
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| fn1 | pfam00039 | Fibronectin type I domain; |
38-75 | 2.06e-05 | |||||
Fibronectin type I domain; Pssm-ID: 459644 Cd Length: 40 Bit Score: 41.53 E-value: 2.06e-05
|
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| FN1 | cd00061 | Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ... |
37-78 | 2.00e-04 | |||||
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. FN1 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. FN1 domains also found in coagulation factor XII, HGF activator, and tissue-type plasminogen activator. In tissue plasminogen activator, FN1 domains may form functional fibrin-binding units with EGF-like domains C-terminal to FN1. Pssm-ID: 238018 Cd Length: 43 Bit Score: 38.85 E-value: 2.00e-04
|
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| DUF1986 | pfam09342 | Domain of unknown function (DUF1986); This domain is found in serine proteases and is ... |
321-442 | 6.37e-03 | |||||
Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds. Pssm-ID: 286432 Cd Length: 116 Bit Score: 36.76 E-value: 6.37e-03
|
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| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
83-115 | 9.97e-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: 33.90 E-value: 9.97e-03
|
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| Blast search parameters | ||||
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