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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17864128    535 PTCPLCLFAVEQAQMKIRDNKSKDNIKKVLNGLCSHLPNEIKEECVDFVNTYSNELIDMLITDFKPQEICVQLKLC 610
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864128     70 SICTICKDMVTQARDQLKSNQTEEELKEVFEGSCKLIPiKPIQKECIKVADDFLPELVEALASQMNPDQVCSVAGLC 146
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17864128    285 IPCELCEQLVKHLRDVLVANTTETEFKQVMEGFCKQ-SKGFKDECLSIVDQYYHVIYETLVSKLDANGACCMIGIC 359
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKlPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864128    859 LECGVCHGVTQALLPFLrekKDNVSEVTALQMTSVGCENLPAKYYKICSEMISIYGSSIKNLAKRpYIDQSHICAEIGKC 938
Cdd:smart00741   1 LLCELCEFVVKQLENLL---KDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQ-GLDPKDVCQKLGLC 76

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17864128    535 PTCPLCLFAVEQAQMKIRDNKSKDNIKKVLNGLCSHLPNEIKEECVDFVNTYSNELIDMLITDFKPQEICVQLKLC 610
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864128     70 SICTICKDMVTQARDQLKSNQTEEELKEVFEGSCKLIPiKPIQKECIKVADDFLPELVEALASQMNPDQVCSVAGLC 146
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17864128    285 IPCELCEQLVKHLRDVLVANTTETEFKQVMEGFCKQ-SKGFKDECLSIVDQYYHVIYETLVSKLDANGACCMIGIC 359
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKlPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76

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.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 17864128     27 GSSKCTWGPSYWCGNFSNSKECRATRHCIQTVW 59
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVW 33

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.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 17864128   577 EECVDFVNTYSNELIDMLITDFKPQEICVQLKLC 610
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34

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.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 17864128    72 CTICKDMVTQARDQLKSNQTEEELKEVFEGSCKLIP 107
Cdd:pfam05184   3 CDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38

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.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17864128   775 PTCVLCEFIMTKLDADLKNKTEQDDIKRAIEAVCNRLP 812
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38

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.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 17864128   326 DECLSIVDQYYHVIYETLVSKLDANGACCMIGIC 359
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17864128    535 PTCPLCLFAVEQAQMKIRDNKSKDNIKKVLNGLCSHLPNEIKEECVDFVNTYSNELIDMLITDFKPQEICVQLKLC 610
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864128     70 SICTICKDMVTQARDQLKSNQTEEELKEVFEGSCKLIPiKPIQKECIKVADDFLPELVEALASQMNPDQVCSVAGLC 146
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17864128    285 IPCELCEQLVKHLRDVLVANTTETEFKQVMEGFCKQ-SKGFKDECLSIVDQYYHVIYETLVSKLDANGACCMIGIC 359
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKlPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76

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.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 17864128     27 GSSKCTWGPSYWCGNFSNSKECRATRHCIQTVW 59
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVW 33

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.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 17864128   577 EECVDFVNTYSNELIDMLITDFKPQEICVQLKLC 610
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34

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.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17864128   535 PTCPLCLFAVEQAQMKIRDNKSKDNIKKVLNGLCSHLP 572
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38

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.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 17864128   436 LCTLCEYMLHFIQETLATPSTDDEIKHTVENICAKLP 472
Cdd:pfam05184   2 LCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38

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.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17864128   775 PTCVLCEFIMTKLDADLKNKTEQDDIKRAIEAVCNRLP 812
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38

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.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 17864128   113 KECIKVADDFLPELVEALASQMNPDQVCSVAGLC 146
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34

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.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 17864128   817 KQCDTFVDGYASAVLKLL-SDVPPKQVCQKLQLC 849
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLeSELDPKDVCTALGLC 34

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.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 17864128   285 IPCELCEQLVKHLRDVLVANTTETEFKQVMEGFCKQ 320
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSK 36