NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|25121980|ref|NP_277045|]
View 

protein dispatched homolog 2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Sterol-sensing super family cl48133
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ...
574-639 6.37e-04

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.


The actual alignment was detected with superfamily member pfam12349:

Pssm-ID: 463544 [Multi-domain]  Cd Length: 153  Bit Score: 41.80  E-value: 6.37e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25121980    574 PSGGLAQRVGRTMHHFGYLLLVSGLTTSAAFYASYLSRLPAVRCLALFMGTAVLVHLALTLVWLPA 639
Cdd:pfam12349   66 RSLDVSERIAEALGEVGPSITLTSLTEILAFLLGALTDMPAVQEFCLFAAVAVLFDFLLQMTFFVA 131
 
Name Accession Description Interval E-value
Sterol-sensing pfam12349
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ...
574-639 6.37e-04

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: 41.80  E-value: 6.37e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25121980    574 PSGGLAQRVGRTMHHFGYLLLVSGLTTSAAFYASYLSRLPAVRCLALFMGTAVLVHLALTLVWLPA 639
Cdd:pfam12349   66 RSLDVSERIAEALGEVGPSITLTSLTEILAFLLGALTDMPAVQEFCLFAAVAVLFDFLLQMTFFVA 131
MMPL COG1033
Predicted exporter protein, RND superfamily [General function prediction only];
593-643 9.92e-04

Predicted exporter protein, RND superfamily [General function prediction only];


Pssm-ID: 440656 [Multi-domain]  Cd Length: 767  Bit Score: 43.70  E-value: 9.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 25121980  593 LLVSGLTTSAAFYASYLSRLPAVRCLALFMGTAVLVHLALTLVWLPASAVL 643
Cdd:COG1033  321 VLLTSLTTAIGFLSLLFSDIPPIRDFGIVAAIGVLLAFLTSLTLLPALLSL 371
2A067 TIGR00921
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized ...
584-643 3.03e-03

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: 42.13  E-value: 3.03e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25121980    584 RTMHHFGYLLLVSGLTTSAAFYASYLSRLPAVRCLALFMGTAVLVHLALTLVWLPASAVL 643
Cdd:TIGR00921  660 HTMERTGPGILFSGLTTAGGFLSLLLSHFPIMRNFGLVQGIGVLSSLTAALVVFPALLVL 719
 
Name Accession Description Interval E-value
Sterol-sensing pfam12349
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ...
574-639 6.37e-04

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: 41.80  E-value: 6.37e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25121980    574 PSGGLAQRVGRTMHHFGYLLLVSGLTTSAAFYASYLSRLPAVRCLALFMGTAVLVHLALTLVWLPA 639
Cdd:pfam12349   66 RSLDVSERIAEALGEVGPSITLTSLTEILAFLLGALTDMPAVQEFCLFAAVAVLFDFLLQMTFFVA 131
MMPL COG1033
Predicted exporter protein, RND superfamily [General function prediction only];
593-643 9.92e-04

Predicted exporter protein, RND superfamily [General function prediction only];


Pssm-ID: 440656 [Multi-domain]  Cd Length: 767  Bit Score: 43.70  E-value: 9.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 25121980  593 LLVSGLTTSAAFYASYLSRLPAVRCLALFMGTAVLVHLALTLVWLPASAVL 643
Cdd:COG1033  321 VLLTSLTTAIGFLSLLFSDIPPIRDFGIVAAIGVLLAFLTSLTLLPALLSL 371
2A067 TIGR00921
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized ...
584-643 3.03e-03

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: 42.13  E-value: 3.03e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25121980    584 RTMHHFGYLLLVSGLTTSAAFYASYLSRLPAVRCLALFMGTAVLVHLALTLVWLPASAVL 643
Cdd:TIGR00921  660 HTMERTGPGILFSGLTTAGGFLSLLLSHFPIMRNFGLVQGIGVLSSLTAALVVFPALLVL 719
MMPL COG1033
Predicted exporter protein, RND superfamily [General function prediction only];
576-647 7.87e-03

Predicted exporter protein, RND superfamily [General function prediction only];


Pssm-ID: 440656 [Multi-domain]  Cd Length: 767  Bit Score: 40.61  E-value: 7.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25121980  576 GGLAQRVGRTMHHFGYLLLVSGLTTSAAFYASYLSRLPAVRCLALFMGTAVLVHLALTLVWLPASAVLHERY 647
Cdd:COG1033  691 GDLEEAIRRALRTTGKAILFTSLTLAAGFGVLLFSSFPPLADFGLLLALGLLVALLAALLLLPALLLLLDPR 762
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH