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 ...
85-1236
2.03e-142
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: 463.61 E-value: 2.03e-142
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ...
85-1236
2.03e-142
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: 463.61 E-value: 2.03e-142
Niemann-Pick C1 N terminus; This is the N-terminal domain of Niemann-Pick C1 family proteins. ...
29-241
9.85e-40
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: 147.75 E-value: 9.85e-40
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ...
85-1236
2.03e-142
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: 463.61 E-value: 2.03e-142
Niemann-Pick C1 N terminus; This is the N-terminal domain of Niemann-Pick C1 family proteins. ...
29-241
9.85e-40
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: 147.75 E-value: 9.85e-40
Patched family; The transmembrane protein Patched is a receptor for the morphogene Sonic ...
494-1235
9.05e-28
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: 121.31 E-value: 9.05e-28
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ...
619-785
1.83e-19
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: 86.48 E-value: 1.83e-19
MMPL family; Members of this family are putative integral membrane proteins from bacteria. ...
1107-1236
8.30e-05
MMPL family; Members of this family are putative integral membrane proteins from bacteria. Several of the members are mycobacterial proteins. Many of the proteins contain two copies of this aligned region. The function of these proteins is not known, although it has been suggested that they may be involved in lipid transport.
Pssm-ID: 308676 [Multi-domain] Cd Length: 332 Bit Score: 46.13 E-value: 8.30e-05
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
1096-1233
7.83e-03
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins appear to be related to the RND family of export proteins, particularly the hydrophobe/amphiphile efflux-3 (HAE3) family represented by TIGR00921.
Pssm-ID: 274598 [Multi-domain] Cd Length: 862 Bit Score: 40.75 E-value: 7.83e-03
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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