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Conserved domains on  [gi|21619229|gb|AAH32785|]
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Surfactant protein B [Homo sapiens]

Protein Classification

saposin domain-containing protein( domain architecture ID 11636085)

saposin domain-containing protein such as saposins, which are accessory proteins that aid in the degradation of sphingolipids by hydrolytic enzymes

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 ...
 67-143 2.50e-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: 75.99  E-value: 2.50e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21619229     67 DLCQECEDIVHILNKMAKEAIFQDTMRKFLEQECNVLPlKLLMPQCNQVLDDYFPLVIDYFQNQTDSNGICMHLGLC 143
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapA super family cl02494
Saposin A-type domain;
28-61 7.73e-13

Saposin A-type domain;


The actual alignment was detected with superfamily member smart00162:

Pssm-ID: 470592  Cd Length: 34  Bit Score: 62.15  E-value: 7.73e-13
                           10        20        30
                   ....*....|....*....|....*....|....
gi 21619229     28 SSLACAQGPEFWCQSLEQALQCRALGHCLQEVWG 61
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 297-366 8.84e-12

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: 60.20  E-value: 8.84e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21619229    297 SECHLCMSVTTQAG-----NSSEQAIPQAMLQACVGSWL-DREKCKQFVEQHTPQLLTLVPRGWDAHTTCQALGVC 366
Cdd:smart00741   1 LLCELCEFVVKQLEnllkdNKTEEEIKKALEKVCKKLPKsLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 206-277 3.72e-08

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: 50.18  E-value: 3.72e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21619229    206 PYCWLCRALIKRIQAMIPKGA----LAVAVAQVCRVVPLVAGGICQCLAERYSVILLDTLLGRMLPQLVCRLVLRC 277
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKteeeIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
 
Name Accession Description Interval E-value
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 67-143 2.50e-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: 75.99  E-value: 2.50e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21619229     67 DLCQECEDIVHILNKMAKEAIFQDTMRKFLEQECNVLPlKLLMPQCNQVLDDYFPLVIDYFQNQTDSNGICMHLGLC 143
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SAPA smart00162
Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, ...
 28-61 7.73e-13

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: 62.15  E-value: 7.73e-13
                           10        20        30
                   ....*....|....*....|....*....|....
gi 21619229     28 SSLACAQGPEFWCQSLEQALQCRALGHCLQEVWG 61
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 297-366 8.84e-12

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: 60.20  E-value: 8.84e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21619229    297 SECHLCMSVTTQAG-----NSSEQAIPQAMLQACVGSWL-DREKCKQFVEQHTPQLLTLVPRGWDAHTTCQALGVC 366
Cdd:smart00741   1 LLCELCEFVVKQLEnllkdNKTEEEIKKALEKVCKKLPKsLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapA pfam02199
Saposin A-type domain;
32-60 4.96e-10

Saposin A-type domain;


Pssm-ID: 460487  Cd Length: 33  Bit Score: 54.13  E-value: 4.96e-10
                          10        20
                  ....*....|....*....|....*....
gi 21619229    32 CAQGPEFWCQSLEQALQCRALGHCLQEVW 60
Cdd:pfam02199   4 CTWGPSYWCQDLETAKECGAVEHCQQHVW 32
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 206-277 3.72e-08

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: 50.18  E-value: 3.72e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21619229    206 PYCWLCRALIKRIQAMIPKGA----LAVAVAQVCRVVPLVAGGICQCLAERYSVILLDTLLGRMLPQLVCRLVLRC 277
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKteeeIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB_1 pfam05184
Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for ...
 67-104 2.35e-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: 41.05  E-value: 2.35e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 21619229    67 DLCQECEDIVHILNKMAKEAIFQDTMRKFLEQECNVLP 104
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 333-366 1.10e-04

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: 39.10  E-value: 1.10e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 21619229   333 EKCKQFVEQHTPQLLTLVPRGWDAHTTCQALGVC 366
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 ...
 67-143 2.50e-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: 75.99  E-value: 2.50e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21619229     67 DLCQECEDIVHILNKMAKEAIFQDTMRKFLEQECNVLPlKLLMPQCNQVLDDYFPLVIDYFQNQTDSNGICMHLGLC 143
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SAPA smart00162
Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, ...
 28-61 7.73e-13

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: 62.15  E-value: 7.73e-13
                           10        20        30
                   ....*....|....*....|....*....|....
gi 21619229     28 SSLACAQGPEFWCQSLEQALQCRALGHCLQEVWG 61
Cdd:smart00162   1 GPKRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 297-366 8.84e-12

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: 60.20  E-value: 8.84e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21619229    297 SECHLCMSVTTQAG-----NSSEQAIPQAMLQACVGSWL-DREKCKQFVEQHTPQLLTLVPRGWDAHTTCQALGVC 366
Cdd:smart00741   1 LLCELCEFVVKQLEnllkdNKTEEEIKKALEKVCKKLPKsLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapA pfam02199
Saposin A-type domain;
32-60 4.96e-10

Saposin A-type domain;


Pssm-ID: 460487  Cd Length: 33  Bit Score: 54.13  E-value: 4.96e-10
                          10        20
                  ....*....|....*....|....*....
gi 21619229    32 CAQGPEFWCQSLEQALQCRALGHCLQEVW 60
Cdd:pfam02199   4 CTWGPSYWCQDLETAKECGAVEHCQQHVW 32
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 206-277 3.72e-08

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: 50.18  E-value: 3.72e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21619229    206 PYCWLCRALIKRIQAMIPKGA----LAVAVAQVCRVVPLVAGGICQCLAERYSVILLDTLLGRMLPQLVCRLVLRC 277
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKteeeIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB_1 pfam05184
Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for ...
 67-104 2.35e-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: 41.05  E-value: 2.35e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 21619229    67 DLCQECEDIVHILNKMAKEAIFQDTMRKFLEQECNVLP 104
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 111-143 2.52e-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: 40.64  E-value: 2.52e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 21619229   111 QCNQVLDDYFPLVIDYFQNQTDSNGICMHLGLC 143
Cdd:pfam03489   2 ECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 333-366 1.10e-04

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: 39.10  E-value: 1.10e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 21619229   333 EKCKQFVEQHTPQLLTLVPRGWDAHTTCQALGVC 366
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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