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Conserved domains on  [gi|298231223|ref|NP_037145|]
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prosaposin isoform A preproprotein [Rattus norvegicus]

Protein Classification

saposin domain-containing protein; MgtC/SapB family 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| uncharacterized MgtC/SapB family protein containing a DUF4010 domain; with similarity in its N-terminus to Brucella MgtC, a virulence factor required for growth in low Mg(2+) medium and for intramacrophage survival, and to Bacillus subtilis SapB

Graphical summary

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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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298231223   438 FCEVCKKLVIYLEHNLEKNSTKEEILAALEKGCSFLPDPYQKQCDEFVAEYEPLLLEILVEVMDPSFVCSKIGVC 512
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298231223    61 LPCDICKTVVTEAGNLLKDNATEEEILHYLEKTCAWIHdSSLSASCKEVVDSYLPVILDMIKGEMsNPGEVCSALNLC 138
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGL-DPKDVCQKLGLC 76
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
                          10        20        30
                  ....*....|....*....|....*....|...
gi 298231223  522 TEKCVWGPGYWCQNMETAARCNAVDHCKRHVWN 554
Cdd:pfam02199   1 PDECTWGPSYWCQDLETAKECGAVEHCQQHVWN 33
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298231223   312 IFCQVCQLVMRKLSELIINNATEELLIKGLSKACSLLPAPASTKCQEVLVTFGPSLLDVLMHEVNPNFLCGVISLC 387
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
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
                           10        20        30
                   ....*....|....*....|....*....|....
gi 298231223    21 DPKICSGGSAVVCRDVKTAVDCRAVKHCQQMVWS 54
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298231223   195 DVCQDCMKLVTDIQTAVRTNSSfVQGLVDHVKEDCDRLGPGVSDICKNYVDQYSEVAVQMMM-HMQPKEICVMVGFC 270
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKT-EEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEqGLDPKDVCQKLGLC 76
 
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298231223   438 FCEVCKKLVIYLEHNLEKNSTKEEILAALEKGCSFLPDPYQKQCDEFVAEYEPLLLEILVEVMDPSFVCSKIGVC 512
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298231223    61 LPCDICKTVVTEAGNLLKDNATEEEILHYLEKTCAWIHdSSLSASCKEVVDSYLPVILDMIKGEMsNPGEVCSALNLC 138
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGL-DPKDVCQKLGLC 76
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
                          10        20        30
                  ....*....|....*....|....*....|...
gi 298231223  522 TEKCVWGPGYWCQNMETAARCNAVDHCKRHVWN 554
Cdd:pfam02199   1 PDECTWGPSYWCQDLETAKECGAVEHCQQHVWN 33
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
                           10        20        30
                   ....*....|....*....|....*....|....
gi 298231223   521 GTEKCVWGPGYWCQNMETAARCNAVDHCKRHVWN 554
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298231223   312 IFCQVCQLVMRKLSELIINNATEELLIKGLSKACSLLPAPASTKCQEVLVTFGPSLLDVLMHEVNPNFLCGVISLC 387
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
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
                           10        20        30
                   ....*....|....*....|....*....|....
gi 298231223    21 DPKICSGGSAVVCRDVKTAVDCRAVKHCQQMVWS 54
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298231223   195 DVCQDCMKLVTDIQTAVRTNSSfVQGLVDHVKEDCDRLGPGVSDICKNYVDQYSEVAVQMMM-HMQPKEICVMVGFC 270
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKT-EEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEqGLDPKDVCQKLGLC 76
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
                          10        20        30
                  ....*....|....*....|....*....|...
gi 298231223   22 PKICSGGSAVVCRDVKTAVDCRAVKHCQQMVWS 54
Cdd:pfam02199   1 PDECTWGPSYWCQDLETAKECGAVEHCQQHVWN 33
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
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 298231223   61 LPCDICKTVVTEAGNLLKDNATEEEILHYLEKTCAWI 97
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKL 37
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
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 298231223  438 FCEVCKKLVIYLEHNLEKNSTKEEILAALEKGCSFLP 474
Cdd:pfam05184   2 LCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38
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
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 298231223  312 IFCQVCQLVMRKLSELIINNATEELLIKGLSKACSLLP 349
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38
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
                          10        20        30
                  ....*....|....*....|....*....|....
gi 298231223  238 DICKNYVDQYSEVAVQMMM-HMQPKEICVMVGFC 270
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLEsELDPKDVCTALGLC 34
 
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298231223   438 FCEVCKKLVIYLEHNLEKNSTKEEILAALEKGCSFLPDPYQKQCDEFVAEYEPLLLEILVEVMDPSFVCSKIGVC 512
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298231223    61 LPCDICKTVVTEAGNLLKDNATEEEILHYLEKTCAWIHdSSLSASCKEVVDSYLPVILDMIKGEMsNPGEVCSALNLC 138
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGL-DPKDVCQKLGLC 76
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
                          10        20        30
                  ....*....|....*....|....*....|...
gi 298231223  522 TEKCVWGPGYWCQNMETAARCNAVDHCKRHVWN 554
Cdd:pfam02199   1 PDECTWGPSYWCQDLETAKECGAVEHCQQHVWN 33
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
                           10        20        30
                   ....*....|....*....|....*....|....
gi 298231223   521 GTEKCVWGPGYWCQNMETAARCNAVDHCKRHVWN 554
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298231223   312 IFCQVCQLVMRKLSELIINNATEELLIKGLSKACSLLPAPASTKCQEVLVTFGPSLLDVLMHEVNPNFLCGVISLC 387
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
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
                           10        20        30
                   ....*....|....*....|....*....|....
gi 298231223    21 DPKICSGGSAVVCRDVKTAVDCRAVKHCQQMVWS 54
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
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
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298231223   195 DVCQDCMKLVTDIQTAVRTNSSfVQGLVDHVKEDCDRLGPGVSDICKNYVDQYSEVAVQMMM-HMQPKEICVMVGFC 270
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKT-EEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEqGLDPKDVCQKLGLC 76
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
                          10        20        30
                  ....*....|....*....|....*....|...
gi 298231223   22 PKICSGGSAVVCRDVKTAVDCRAVKHCQQMVWS 54
Cdd:pfam02199   1 PDECTWGPSYWCQDLETAKECGAVEHCQQHVWN 33
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
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 298231223   61 LPCDICKTVVTEAGNLLKDNATEEEILHYLEKTCAWI 97
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKL 37
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
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 298231223  438 FCEVCKKLVIYLEHNLEKNSTKEEILAALEKGCSFLP 474
Cdd:pfam05184   2 LCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38
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
                          10        20        30
                  ....*....|....*....|....*....|....
gi 298231223  479 KQCDEFVAEYEPLLLEILVEVMDPSFVCSKIGVC 512
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
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
                          10        20        30
                  ....*....|....*....|....*....|...
gi 298231223  106 CKEVVDSYLPVILDMIKGEMsNPGEVCSALNLC 138
Cdd:pfam03489   3 CKSLVDQYGPLIIDLLESEL-DPKDVCTALGLC 34
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
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 298231223  312 IFCQVCQLVMRKLSELIINNATEELLIKGLSKACSLLP 349
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38
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
                          10        20        30
                  ....*....|....*....|....*....|....
gi 298231223  238 DICKNYVDQYSEVAVQMMM-HMQPKEICVMVGFC 270
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLEsELDPKDVCTALGLC 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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