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Conserved domains on  [gi|21355437|ref|NP_650553|]
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Derlin-2 [Drosophila melanogaster]

Protein Classification

derlin( domain architecture ID 10517525)

derlin (or degradation in endoplasmic reticulum protein) may be a functional component of the endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not for misfolded non-glycoproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DER1 pfam04511
Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ...
 11-201 6.26e-92

Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae contains of proteolytic system able to selectively degrade misfolded lumenal secretory proteins. For examination of the components involved in this degradation process, mutants were isolated. They could be divided into four complementation groups. The mutations led to stabilization of two different substrates for this process. The mutant classes were called 'der' for 'degradation in the ER'. DER1 was cloned by complementation of the der1-2 mutation. The DER1 gene codes for a novel, hydrophobic protein, that is localized to the ER. Deletion of DER1 abolished degradation of the substrate proteins. The function of the Der1 protein seems to be specifically required for the degradation process associated with the ER. Interestingly this family seems distantly related to the Rhomboid family of membrane peptidases. Suggesting that this family may also mediate degradation of misfolded proteins (Bateman A pers. obs.).


:

Pssm-ID: 427988  Cd Length: 191  Bit Score: 269.22  E-value: 6.26e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355437    11 IPVVTRAYTTVCVLTTLAVHLDLVSPLQLYFNPTLIVRKFQIWRLATTFLYFGTIGISFFFNMVFTYRYCRMLEDGSFRG 90
Cdd:pfam04511   1 IPPVTRYWFTATVATTLLGRLGLISPFYLYLNWELVFRKFQIWRLITSFLYFGGTGFHFLMNLYFIYQYSTMLEEGSFRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355437    91 RSSDFVMMFIFGGVLMTFFGIFVNLLFLGQAFTLMLVYVWSRRNPLVPMNFFGVLNFQAPYLPWVLLCCSMILGNTVWVD 170
Cdd:pfam04511  81 RPADYLYMLLFGAVLITIFGLIVDIYFLGQALIAMIVYVWSQRNPDVIVSFWFGLRFQAKYLPWVLLGFSFILGGSVVVD 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 21355437   171 VIGMGVGHIYYVLEDVYPTLSNGYRLIKTPY 201
Cdd:pfam04511 161 LIGILVGHIYFFLEDVYPIDLGGKRLLSTPQ 191
 
Name Accession Description Interval E-value
DER1 pfam04511
Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ...
 11-201 6.26e-92

Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae contains of proteolytic system able to selectively degrade misfolded lumenal secretory proteins. For examination of the components involved in this degradation process, mutants were isolated. They could be divided into four complementation groups. The mutations led to stabilization of two different substrates for this process. The mutant classes were called 'der' for 'degradation in the ER'. DER1 was cloned by complementation of the der1-2 mutation. The DER1 gene codes for a novel, hydrophobic protein, that is localized to the ER. Deletion of DER1 abolished degradation of the substrate proteins. The function of the Der1 protein seems to be specifically required for the degradation process associated with the ER. Interestingly this family seems distantly related to the Rhomboid family of membrane peptidases. Suggesting that this family may also mediate degradation of misfolded proteins (Bateman A pers. obs.).


Pssm-ID: 427988  Cd Length: 191  Bit Score: 269.22  E-value: 6.26e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355437    11 IPVVTRAYTTVCVLTTLAVHLDLVSPLQLYFNPTLIVRKFQIWRLATTFLYFGTIGISFFFNMVFTYRYCRMLEDGSFRG 90
Cdd:pfam04511   1 IPPVTRYWFTATVATTLLGRLGLISPFYLYLNWELVFRKFQIWRLITSFLYFGGTGFHFLMNLYFIYQYSTMLEEGSFRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355437    91 RSSDFVMMFIFGGVLMTFFGIFVNLLFLGQAFTLMLVYVWSRRNPLVPMNFFGVLNFQAPYLPWVLLCCSMILGNTVWVD 170
Cdd:pfam04511  81 RPADYLYMLLFGAVLITIFGLIVDIYFLGQALIAMIVYVWSQRNPDVIVSFWFGLRFQAKYLPWVLLGFSFILGGSVVVD 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 21355437   171 VIGMGVGHIYYVLEDVYPTLSNGYRLIKTPY 201
Cdd:pfam04511 161 LIGILVGHIYFFLEDVYPIDLGGKRLLSTPQ 191
COG5291 COG5291
Predicted membrane protein [Function unknown];
9-210 8.37e-36

Predicted membrane protein [Function unknown];


Pssm-ID: 227611  Cd Length: 313  Bit Score: 129.72  E-value: 8.37e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355437   9 LEIPVVTRAYTTVCVLTTLAVHLDLVSPLQLYFNPTLIVRKFQIWRLATTFLYFGTIGISFFFNMVFTYRYCRMLEDGSF 88
Cdd:COG5291  17 LRIPPITRYMTLLISAVTILVYVDLVSPWYSLYYSPLFLKRLQIWRLFTSFLYFGKPTLDMFMHVYFLYRYSRMLEEGCF 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355437  89 RGRSSDFVMMFIF-GGVLMTFFGIFVNLLFLGQAFTLMLVYVWSRRNPLVPMNFFGVLNFQAPYLPWVLLCCSMILGNTV 167
Cdd:COG5291  97 NTSLVEYFWYLLViSLVIFAISNIYGGISALGTSFSATITYIWSKRNPRAIIQFFGFISVPGKYLPFILLGFSFLSRRGI 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21355437 168 WV-DVIGMGVGHIYYVLEDVYPTLsnGYRLIKTPYFLKRLFNEH 210
Cdd:COG5291 177 SIdDVLGFVVGHLFHYFGDIYPMI--GRDILSTPCWVKKLFNEH 218
 
Name Accession Description Interval E-value
DER1 pfam04511
Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae ...
 11-201 6.26e-92

Der1-like family; The endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae contains of proteolytic system able to selectively degrade misfolded lumenal secretory proteins. For examination of the components involved in this degradation process, mutants were isolated. They could be divided into four complementation groups. The mutations led to stabilization of two different substrates for this process. The mutant classes were called 'der' for 'degradation in the ER'. DER1 was cloned by complementation of the der1-2 mutation. The DER1 gene codes for a novel, hydrophobic protein, that is localized to the ER. Deletion of DER1 abolished degradation of the substrate proteins. The function of the Der1 protein seems to be specifically required for the degradation process associated with the ER. Interestingly this family seems distantly related to the Rhomboid family of membrane peptidases. Suggesting that this family may also mediate degradation of misfolded proteins (Bateman A pers. obs.).


Pssm-ID: 427988  Cd Length: 191  Bit Score: 269.22  E-value: 6.26e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355437    11 IPVVTRAYTTVCVLTTLAVHLDLVSPLQLYFNPTLIVRKFQIWRLATTFLYFGTIGISFFFNMVFTYRYCRMLEDGSFRG 90
Cdd:pfam04511   1 IPPVTRYWFTATVATTLLGRLGLISPFYLYLNWELVFRKFQIWRLITSFLYFGGTGFHFLMNLYFIYQYSTMLEEGSFRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355437    91 RSSDFVMMFIFGGVLMTFFGIFVNLLFLGQAFTLMLVYVWSRRNPLVPMNFFGVLNFQAPYLPWVLLCCSMILGNTVWVD 170
Cdd:pfam04511  81 RPADYLYMLLFGAVLITIFGLIVDIYFLGQALIAMIVYVWSQRNPDVIVSFWFGLRFQAKYLPWVLLGFSFILGGSVVVD 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 21355437   171 VIGMGVGHIYYVLEDVYPTLSNGYRLIKTPY 201
Cdd:pfam04511 161 LIGILVGHIYFFLEDVYPIDLGGKRLLSTPQ 191
COG5291 COG5291
Predicted membrane protein [Function unknown];
9-210 8.37e-36

Predicted membrane protein [Function unknown];


Pssm-ID: 227611  Cd Length: 313  Bit Score: 129.72  E-value: 8.37e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355437   9 LEIPVVTRAYTTVCVLTTLAVHLDLVSPLQLYFNPTLIVRKFQIWRLATTFLYFGTIGISFFFNMVFTYRYCRMLEDGSF 88
Cdd:COG5291  17 LRIPPITRYMTLLISAVTILVYVDLVSPWYSLYYSPLFLKRLQIWRLFTSFLYFGKPTLDMFMHVYFLYRYSRMLEEGCF 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355437  89 RGRSSDFVMMFIF-GGVLMTFFGIFVNLLFLGQAFTLMLVYVWSRRNPLVPMNFFGVLNFQAPYLPWVLLCCSMILGNTV 167
Cdd:COG5291  97 NTSLVEYFWYLLViSLVIFAISNIYGGISALGTSFSATITYIWSKRNPRAIIQFFGFISVPGKYLPFILLGFSFLSRRGI 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21355437 168 WV-DVIGMGVGHIYYVLEDVYPTLsnGYRLIKTPYFLKRLFNEH 210
Cdd:COG5291 177 SIdDVLGFVVGHLFHYFGDIYPMI--GRDILSTPCWVKKLFNEH 218
 
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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