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 795519772   419 FCEVCKKLVGYLDRNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIGAC 493
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 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 795519772    61 LPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPnMSASCKEIVDSYLPVILDIIKGEMDfqqdifpchqsrPG 140
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKS-LSDQCKEFVDQYGPEIIDLLEQGLD------------PK 67

                   ....*....
gi 795519772   141 EVCSALNLC 149
Cdd:smart00741  68 DVCQKLGLC 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 795519772   207 DVCQDCIQMVTDIQTAVRTNSTfVQALVEHVKEECDRLGPGMADMCKNYISQYSEIAIQMMM-HMQPKEICALVGFC 282
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKT-EEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEqGLDPKDVCQKLGLC 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 795519772   419 FCEVCKKLVGYLDRNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIGAC 493
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 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 795519772    61 LPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPnMSASCKEIVDSYLPVILDIIKGEMDfqqdifpchqsrPG 140
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKS-LSDQCKEFVDQYGPEIIDLLEQGLD------------PK 67

                   ....*....
gi 795519772   141 EVCSALNLC 149
Cdd:smart00741  68 DVCQKLGLC 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 795519772    21 GMKECTRGSAVWCQNVKTASDCGAVKHCLQTVWN 54
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 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 795519772   207 DVCQDCIQMVTDIQTAVRTNSTfVQALVEHVKEECDRLGPGMADMCKNYISQYSEIAIQMMM-HMQPKEICALVGFC 282
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKT-EEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEqGLDPKDVCQKLGLC 76

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 795519772  326 CEVCEFLVKEVTKLIDNNKTEKEILDTFDKMCSKLP 361
Cdd:pfam05184   3 CDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 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 795519772  250 DMCKNYISQYSEIAIQMMM-HMQPKEICALVGFC 282
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 795519772   419 FCEVCKKLVGYLDRNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIGAC 493
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 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 795519772    61 LPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPnMSASCKEIVDSYLPVILDIIKGEMDfqqdifpchqsrPG 140
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKS-LSDQCKEFVDQYGPEIIDLLEQGLD------------PK 67

                   ....*....
gi 795519772   141 EVCSALNLC 149
Cdd:smart00741  68 DVCQKLGLC 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 795519772    21 GMKECTRGSAVWCQNVKTASDCGAVKHCLQTVWN 54
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 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 795519772   207 DVCQDCIQMVTDIQTAVRTNSTfVQALVEHVKEECDRLGPGMADMCKNYISQYSEIAIQMMM-HMQPKEICALVGFC 282
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKT-EEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEqGLDPKDVCQKLGLC 76

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 795519772  326 CEVCEFLVKEVTKLIDNNKTEKEILDTFDKMCSKLP 361
Cdd:pfam05184   3 CDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 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 795519772  366 EECQEVVDTYGSSILSILLQEVSPELVCSMLRLC 399
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 795519772  250 DMCKNYISQYSEIAIQMMM-HMQPKEICALVGFC 282
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLEsELDPKDVCTALGLC 34