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Conserved domains on  [gi|7108344|ref|NP_006424|]
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granulysin isoform 2 precursor [Homo sapiens]

Protein Classification

saposin domain-containing protein( domain architecture ID 12219188)

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 ...
68-138 4.04e-10

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: 52.88  E-value: 4.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7108344      68 TCLTIVQKLKKMVDKP-TQRSVSNAATRVCRTGRSRWRDVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLC 138
Cdd:smart00741   5 LCEFVVKQLENLLKDNkTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
 
Name Accession Description Interval E-value
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
68-138 4.04e-10

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: 52.88  E-value: 4.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7108344      68 TCLTIVQKLKKMVDKP-TQRSVSNAATRVCRTGRSRWRDVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLC 138
Cdd:smart00741   5 LCEFVVKQLENLLKDNkTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
105-138 3.63e-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: 33.32  E-value: 3.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 7108344    105 DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLC 138
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 ...
68-138 4.04e-10

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: 52.88  E-value: 4.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7108344      68 TCLTIVQKLKKMVDKP-TQRSVSNAATRVCRTGRSRWRDVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLC 138
Cdd:smart00741   5 LCEFVVKQLENLLKDNkTEEEIKKALEKVCKKLPKSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
105-138 3.63e-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: 33.32  E-value: 3.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 7108344    105 DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLC 138
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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