Niemann-Pick C (NPC) type protein family is essential for sterol homeostasis that drive sterol integration into the lysosomal membrane before redistribution to other cellular membranes
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ...
22-1284
1.63e-166
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in eukaryotes. The defective protein has been associated with Niemann-Pick disease which is described in humans as autosomal recessive lipidosis. It is characterized by the lysosomal accumulation of unestrified cholesterol. It is an integral membrane protein, which indicates that this protein is most likely involved in cholesterol transport or acts as some component of cholesterol homeostasis. [Transport and binding proteins, Other]
The actual alignment was detected with superfamily member TIGR00917:
Pssm-ID: 273337 [Multi-domain] Cd Length: 1205 Bit Score: 531.41 E-value: 1.63e-166
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ...
22-1284
1.63e-166
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in eukaryotes. The defective protein has been associated with Niemann-Pick disease which is described in humans as autosomal recessive lipidosis. It is characterized by the lysosomal accumulation of unestrified cholesterol. It is an integral membrane protein, which indicates that this protein is most likely involved in cholesterol transport or acts as some component of cholesterol homeostasis. [Transport and binding proteins, Other]
Pssm-ID: 273337 [Multi-domain] Cd Length: 1205 Bit Score: 531.41 E-value: 1.63e-166
Niemann-Pick C1 N terminus; This is the N-terminal domain of Niemann-Pick C1 family proteins. ...
21-251
8.53e-48
Niemann-Pick C1 N terminus; This is the N-terminal domain of Niemann-Pick C1 family proteins. This family of proteins mediates transport of cholesterol from the intestinal lumen to enterocytes. This domain contains a cholesterol-binding pocket.
Pssm-ID: 465110 Cd Length: 239 Bit Score: 170.86 E-value: 8.53e-48
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ...
22-1284
1.63e-166
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in eukaryotes. The defective protein has been associated with Niemann-Pick disease which is described in humans as autosomal recessive lipidosis. It is characterized by the lysosomal accumulation of unestrified cholesterol. It is an integral membrane protein, which indicates that this protein is most likely involved in cholesterol transport or acts as some component of cholesterol homeostasis. [Transport and binding proteins, Other]
Pssm-ID: 273337 [Multi-domain] Cd Length: 1205 Bit Score: 531.41 E-value: 1.63e-166
Niemann-Pick C1 N terminus; This is the N-terminal domain of Niemann-Pick C1 family proteins. ...
21-251
8.53e-48
Niemann-Pick C1 N terminus; This is the N-terminal domain of Niemann-Pick C1 family proteins. This family of proteins mediates transport of cholesterol from the intestinal lumen to enterocytes. This domain contains a cholesterol-binding pocket.
Pssm-ID: 465110 Cd Length: 239 Bit Score: 170.86 E-value: 8.53e-48
Patched family; The transmembrane protein Patched is a receptor for the morphogene Sonic ...
545-1281
1.08e-34
Patched family; The transmembrane protein Patched is a receptor for the morphogene Sonic Hedgehog. This protein associates with the smoothened protein to transduce hedgehog signals.
Pssm-ID: 308203 [Multi-domain] Cd Length: 793 Bit Score: 143.65 E-value: 1.08e-34
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ...
660-814
7.86e-25
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins (SREBPs) are membrane-bound transcription factors that promote lipid synthesis in animal cells. They are embedded in the membranes of the endoplasmic reticulum (ER) in a helical hairpin orientation and are released from the ER by a two-step proteolytic process. Proteolysis begins when the SREBPs are cleaved at Site-1, which is located at a leucine residue in the middle of the hydrophobic loop in the lumen of the ER. Upon proteolytic processing SREBP can activate the expression of genes involved in cholesterol biosynthesis and uptake. SCAP stimulates cleavage of SREBPs via fusion of the their two C-termini. This domain is the transmembrane region that traverses the membrane eight times and is the sterol-sensing domain of the cleavage protein. WD40 domains are found towards the C-terminus.
Pssm-ID: 463544 [Multi-domain] Cd Length: 153 Bit Score: 101.89 E-value: 7.86e-25
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized ...
1097-1351
7.01e-06
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. They fall into seven phylogenetic families, this family (2.A.6.7) consists of uncharacterised putative transporters, largely in the Archaea. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273340 [Multi-domain] Cd Length: 719 Bit Score: 50.61 E-value: 7.01e-06
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized ...
1136-1280
4.41e-04
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. They fall into seven phylogenetic families, this family (2.A.6.7) consists of uncharacterised putative transporters, largely in the Archaea. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273340 [Multi-domain] Cd Length: 719 Bit Score: 44.83 E-value: 4.41e-04
AcrB/AcrD/AcrF family; Members of this family are integral membrane proteins. Some are ...
1089-1289
8.36e-04
AcrB/AcrD/AcrF family; Members of this family are integral membrane proteins. Some are involved in drug resistance. AcrB cooperates with a membrane fusion protein, AcrA, and an outer membrane channel TolC. The structure shows the AcrB forms a homotrimer.
Pssm-ID: 395701 [Multi-domain] Cd Length: 1021 Bit Score: 43.82 E-value: 8.36e-04
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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