prosaposin isoform A preproprotein [Rattus norvegicus]
Protein Classification
saposin domain-containing protein( domain architecture ID 12191173)
saposin domain-containing protein such as saposins, which are accessory proteins that aid in the degradation of sphingolipids by hydrolytic enzymes
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
438-512 | 1.76e-18 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. : Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 79.84 E-value: 1.76e-18
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
61-138 | 2.47e-17 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. : Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 76.76 E-value: 2.47e-17
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| SapA | pfam02199 | Saposin A-type domain; |
522-554 | 1.04e-16 | ||
Saposin A-type domain; : Pssm-ID: 460487 Cd Length: 33 Bit Score: 73.39 E-value: 1.04e-16
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
312-387 | 6.92e-15 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. : Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 69.83 E-value: 6.92e-15
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| SAPA | smart00162 | Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, ... |
21-54 | 5.07e-14 | ||
Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, respectively, in prosaposin and surfactant protein B. Single copies in acid sphingomyelinase, NK-lysin amoebapores and granulysin. Putative phospholipid membrane binding domains. : Pssm-ID: 128465 Cd Length: 34 Bit Score: 66.00 E-value: 5.07e-14
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
195-270 | 4.41e-13 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. : Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 64.44 E-value: 4.41e-13
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| Name | Accession | Description | Interval | E-value | ||
| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
438-512 | 1.76e-18 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 79.84 E-value: 1.76e-18
|
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
61-138 | 2.47e-17 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 76.76 E-value: 2.47e-17
|
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| SapA | pfam02199 | Saposin A-type domain; |
522-554 | 1.04e-16 | ||
Saposin A-type domain; Pssm-ID: 460487 Cd Length: 33 Bit Score: 73.39 E-value: 1.04e-16
|
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| SAPA | smart00162 | Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, ... |
521-554 | 3.27e-16 | ||
Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, respectively, in prosaposin and surfactant protein B. Single copies in acid sphingomyelinase, NK-lysin amoebapores and granulysin. Putative phospholipid membrane binding domains. Pssm-ID: 128465 Cd Length: 34 Bit Score: 72.16 E-value: 3.27e-16
|
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
312-387 | 6.92e-15 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 69.83 E-value: 6.92e-15
|
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| SAPA | smart00162 | Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, ... |
21-54 | 5.07e-14 | ||
Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, respectively, in prosaposin and surfactant protein B. Single copies in acid sphingomyelinase, NK-lysin amoebapores and granulysin. Putative phospholipid membrane binding domains. Pssm-ID: 128465 Cd Length: 34 Bit Score: 66.00 E-value: 5.07e-14
|
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
195-270 | 4.41e-13 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 64.44 E-value: 4.41e-13
|
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| SapA | pfam02199 | Saposin A-type domain; |
22-54 | 1.16e-10 | ||
Saposin A-type domain; Pssm-ID: 460487 Cd Length: 33 Bit Score: 56.44 E-value: 1.16e-10
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| SapB_1 | pfam05184 | Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for ... |
61-97 | 1.73e-08 | ||
Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease, and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 461575 Cd Length: 38 Bit Score: 50.29 E-value: 1.73e-08
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| SapB_1 | pfam05184 | Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for ... |
438-474 | 1.92e-08 | ||
Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease, and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 461575 Cd Length: 38 Bit Score: 50.29 E-value: 1.92e-08
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| SapB_1 | pfam05184 | Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for ... |
312-349 | 1.04e-05 | ||
Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease, and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 461575 Cd Length: 38 Bit Score: 42.59 E-value: 1.04e-05
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| SapB_2 | pfam03489 | Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ... |
238-270 | 1.32e-05 | ||
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 460945 Cd Length: 34 Bit Score: 42.18 E-value: 1.32e-05
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| Name | Accession | Description | Interval | E-value | ||
| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
438-512 | 1.76e-18 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 79.84 E-value: 1.76e-18
|
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
61-138 | 2.47e-17 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 76.76 E-value: 2.47e-17
|
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| SapA | pfam02199 | Saposin A-type domain; |
522-554 | 1.04e-16 | ||
Saposin A-type domain; Pssm-ID: 460487 Cd Length: 33 Bit Score: 73.39 E-value: 1.04e-16
|
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| SAPA | smart00162 | Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, ... |
521-554 | 3.27e-16 | ||
Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, respectively, in prosaposin and surfactant protein B. Single copies in acid sphingomyelinase, NK-lysin amoebapores and granulysin. Putative phospholipid membrane binding domains. Pssm-ID: 128465 Cd Length: 34 Bit Score: 72.16 E-value: 3.27e-16
|
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
312-387 | 6.92e-15 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 69.83 E-value: 6.92e-15
|
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| SAPA | smart00162 | Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, ... |
21-54 | 5.07e-14 | ||
Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, respectively, in prosaposin and surfactant protein B. Single copies in acid sphingomyelinase, NK-lysin amoebapores and granulysin. Putative phospholipid membrane binding domains. Pssm-ID: 128465 Cd Length: 34 Bit Score: 66.00 E-value: 5.07e-14
|
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| SapB | smart00741 | Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ... |
195-270 | 4.41e-13 | ||
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present. Pssm-ID: 214797 [Multi-domain] Cd Length: 76 Bit Score: 64.44 E-value: 4.41e-13
|
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| SapA | pfam02199 | Saposin A-type domain; |
22-54 | 1.16e-10 | ||
Saposin A-type domain; Pssm-ID: 460487 Cd Length: 33 Bit Score: 56.44 E-value: 1.16e-10
|
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| SapB_1 | pfam05184 | Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for ... |
61-97 | 1.73e-08 | ||
Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease, and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 461575 Cd Length: 38 Bit Score: 50.29 E-value: 1.73e-08
|
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| SapB_1 | pfam05184 | Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for ... |
438-474 | 1.92e-08 | ||
Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease, and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 461575 Cd Length: 38 Bit Score: 50.29 E-value: 1.92e-08
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| SapB_2 | pfam03489 | Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ... |
479-512 | 1.43e-06 | ||
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 460945 Cd Length: 34 Bit Score: 44.87 E-value: 1.43e-06
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| SapB_2 | pfam03489 | Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ... |
106-138 | 9.99e-06 | ||
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 460945 Cd Length: 34 Bit Score: 42.56 E-value: 9.99e-06
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| SapB_1 | pfam05184 | Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for ... |
312-349 | 1.04e-05 | ||
Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease, and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 461575 Cd Length: 38 Bit Score: 42.59 E-value: 1.04e-05
|
||||||
| SapB_2 | pfam03489 | Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ... |
238-270 | 1.32e-05 | ||
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes. Pssm-ID: 460945 Cd Length: 34 Bit Score: 42.18 E-value: 1.32e-05
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| Blast search parameters | ||||
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