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Conserved domains on  [gi|1952691707|ref|XP_038308829|]
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pulmonary surfactant-associated protein B isoform X1 [Canis lupus familiaris]

Protein Classification

SapA and SapB domain-containing protein( domain architecture ID 11636085)

SapA and SapB domain-containing protein

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 ...
 66-142 7.70e-16

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: 71.75  E-value: 7.70e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952691707   66 DLCQECQDIVRILTKMTKEAIFQDMVRKFLEHECDVLPlKLLTPQCHHMLGTYFPVVVDYFQSQINPKIICKHLGLC 142
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapA super family cl02494
Saposin A-type domain;
29-60 1.31e-12

Saposin A-type domain;


The actual alignment was detected with superfamily member smart00162:

Pssm-ID: 470592  Cd Length: 34  Bit Score: 61.38  E-value: 1.31e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1952691707   29 LACARGPAFWCQSLEQALQCRALGHCLQEVWG 60
Cdd:smart00162   3 KRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 287-354 2.04e-09

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: 53.65  E-value: 2.04e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952691707  287 CQLCMFVTTQAG-----NHSEQATPQAIRQACLSSWL-DRQKCEQFVEQHMPQLQTLASGGRDAHTTCQALGAC 354
Cdd:smart00741   3 CELCEFVVKQLEnllkdNKTEEEIKKALEKVCKKLPKsLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 192-263 2.60e-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: 50.57  E-value: 2.60e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952691707  192 PYCWLCRTLIKRIQAMIPKGV----LAVTVGQVCHVVPLVVGGICQCLAERYTVLLLDALLGRMLPQLVCGLVLRC 263
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 ...
 66-142 7.70e-16

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: 71.75  E-value: 7.70e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952691707   66 DLCQECQDIVRILTKMTKEAIFQDMVRKFLEHECDVLPlKLLTPQCHHMLGTYFPVVVDYFQSQINPKIICKHLGLC 142
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SAPA smart00162
Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, ...
 29-60 1.31e-12

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: 61.38  E-value: 1.31e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1952691707   29 LACARGPAFWCQSLEQALQCRALGHCLQEVWG 60
Cdd:smart00162   3 KRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
SapA pfam02199
Saposin A-type domain;
31-59 2.88e-10

Saposin A-type domain;


Pssm-ID: 460487  Cd Length: 33  Bit Score: 54.90  E-value: 2.88e-10
                          10        20
                  ....*....|....*....|....*....
gi 1952691707  31 CARGPAFWCQSLEQALQCRALGHCLQEVW 59
Cdd:pfam02199   4 CTWGPSYWCQDLETAKECGAVEHCQQHVW 32
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 287-354 2.04e-09

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: 53.65  E-value: 2.04e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952691707  287 CQLCMFVTTQAG-----NHSEQATPQAIRQACLSSWL-DRQKCEQFVEQHMPQLQTLASGGRDAHTTCQALGAC 354
Cdd:smart00741   3 CELCEFVVKQLEnllkdNKTEEEIKKALEKVCKKLPKsLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 192-263 2.60e-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: 50.57  E-value: 2.60e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952691707  192 PYCWLCRTLIKRIQAMIPKGV----LAVTVGQVCHVVPLVVGGICQCLAERYTVLLLDALLGRMLPQLVCGLVLRC 263
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKteeeIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 110-142 3.75e-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: 42.95  E-value: 3.75e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1952691707 110 QCHHMLGTYFPVVVDYFQSQINPKIICKHLGLC 142
Cdd:pfam03489   2 ECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 321-354 1.83e-03

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: 35.63  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1952691707 321 QKCEQFVEQHMPQLQTLASGGRDAHTTCQALGAC 354
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 ...
 66-142 7.70e-16

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: 71.75  E-value: 7.70e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952691707   66 DLCQECQDIVRILTKMTKEAIFQDMVRKFLEHECDVLPlKLLTPQCHHMLGTYFPVVVDYFQSQINPKIICKHLGLC 142
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKTEEEIKKALEKVCKKLP-KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SAPA smart00162
Saposin/surfactant protein-B A-type DOMAIN; Present as four and three degenerate copies, ...
 29-60 1.31e-12

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: 61.38  E-value: 1.31e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1952691707   29 LACARGPAFWCQSLEQALQCRALGHCLQEVWG 60
Cdd:smart00162   3 KRCTWGPSVWCQNLETASQCNAVKHCLQRVWS 34
SapA pfam02199
Saposin A-type domain;
31-59 2.88e-10

Saposin A-type domain;


Pssm-ID: 460487  Cd Length: 33  Bit Score: 54.90  E-value: 2.88e-10
                          10        20
                  ....*....|....*....|....*....
gi 1952691707  31 CARGPAFWCQSLEQALQCRALGHCLQEVW 59
Cdd:pfam02199   4 CTWGPSYWCQDLETAKECGAVEHCQQHVW 32
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 287-354 2.04e-09

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: 53.65  E-value: 2.04e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952691707  287 CQLCMFVTTQAG-----NHSEQATPQAIRQACLSSWL-DRQKCEQFVEQHMPQLQTLASGGRDAHTTCQALGAC 354
Cdd:smart00741   3 CELCEFVVKQLEnllkdNKTEEEIKKALEKVCKKLPKsLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 192-263 2.60e-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: 50.57  E-value: 2.60e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952691707  192 PYCWLCRTLIKRIQAMIPKGV----LAVTVGQVCHVVPLVVGGICQCLAERYTVLLLDALLGRMLPQLVCGLVLRC 263
Cdd:smart00741   1 LLCELCEFVVKQLENLLKDNKteeeIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 110-142 3.75e-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: 42.95  E-value: 3.75e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1952691707 110 QCHHMLGTYFPVVVDYFQSQINPKIICKHLGLC 142
Cdd:pfam03489   2 ECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
SapB_1 pfam05184
Saposin-like type B, region 1; Saposin B is a small non-enzymatic glycoprotein required for ...
 66-103 1.26e-04

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: 38.74  E-value: 1.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1952691707  66 DLCQECQDIVRILTKMTKEAIFQDMVRKFLEHECDVLP 103
Cdd:pfam05184   1 PLCDLCEFVVKELEKLLKDNKTEEEIIKALEKVCSKLP 38
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 321-354 1.83e-03

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: 35.63  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1952691707 321 QKCEQFVEQHMPQLQTLASGGRDAHTTCQALGAC 354
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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