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Conserved domains on  [gi|24418559|sp|Q9ERE7|]
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RecName: Full=LRP chaperone MESD; AltName: Full=LDLR chaperone MESD; AltName: Full=Mesoderm development candidate 2; AltName: Full=Mesoderm development protein; Flags: Precursor

Protein Classification

Mesd domain-containing protein( domain architecture ID 10562823)

Mesd domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mesd pfam10185
Chaperone for wingless signalling and trafficking of LDL receptor; Mesd is a family of highly ...
 43-192 8.94e-98

Chaperone for wingless signalling and trafficking of LDL receptor; Mesd is a family of highly conserved proteins found from nematodes to humans. The final C-terminal residues, KEDL, are the endoplasmic reticulum retention sequence as it is an ER protein specifically required for the intracellular trafficking of members of the low-density lipoprotein family of receptors (LDLRs). The N- and C-terminal sequences are predicted to adopt a random coil conformation, with the exception of an isolated predicted helix within the N-terminal region, The central folded domain flanked by natively unstructured regions is the necessary structure for facilitating maturation of LRP6 (Low-Density Lipoprotein Receptor-Related Protein 6 Maturation).


:

Pssm-ID: 462985  Cd Length: 155  Bit Score: 281.27  E-value: 8.94e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418559    43 KKDIRDYNDADMARLLEQWEKDDD-IEEGDLPEHKRPSAPIDFSKLDPGKPESILKMTKKGKTLMMFVTVSGNPTEKETE 121
Cdd:pfam10185   1 KKDIRDYNDADLERLLDQWEEDDEpLEPDELPEHLRPPPPIDFSKIDPSNPENLLKMSKKGKTLMMFVTVSGDPTEKETE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24418559   122 EITSLWQGSLFNANYDVQRFIVGSDRAIFMLRDGSYAWEIKDFLVSQDRCAEVTLEGQMYPGKGGGSKEKN 192
Cdd:pfam10185  81 EITKLWQTSLWNNHIQAERYIIDDNRAIFMFRDGSQAWEAKDFLVEQERCKEVTIEGQTYPGKGAKKDNKS 151
 
Name Accession Description Interval E-value
Mesd pfam10185
Chaperone for wingless signalling and trafficking of LDL receptor; Mesd is a family of highly ...
 43-192 8.94e-98

Chaperone for wingless signalling and trafficking of LDL receptor; Mesd is a family of highly conserved proteins found from nematodes to humans. The final C-terminal residues, KEDL, are the endoplasmic reticulum retention sequence as it is an ER protein specifically required for the intracellular trafficking of members of the low-density lipoprotein family of receptors (LDLRs). The N- and C-terminal sequences are predicted to adopt a random coil conformation, with the exception of an isolated predicted helix within the N-terminal region, The central folded domain flanked by natively unstructured regions is the necessary structure for facilitating maturation of LRP6 (Low-Density Lipoprotein Receptor-Related Protein 6 Maturation).


Pssm-ID: 462985  Cd Length: 155  Bit Score: 281.27  E-value: 8.94e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418559    43 KKDIRDYNDADMARLLEQWEKDDD-IEEGDLPEHKRPSAPIDFSKLDPGKPESILKMTKKGKTLMMFVTVSGNPTEKETE 121
Cdd:pfam10185   1 KKDIRDYNDADLERLLDQWEEDDEpLEPDELPEHLRPPPPIDFSKIDPSNPENLLKMSKKGKTLMMFVTVSGDPTEKETE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24418559   122 EITSLWQGSLFNANYDVQRFIVGSDRAIFMLRDGSYAWEIKDFLVSQDRCAEVTLEGQMYPGKGGGSKEKN 192
Cdd:pfam10185  81 EITKLWQTSLWNNHIQAERYIIDDNRAIFMFRDGSQAWEAKDFLVEQERCKEVTIEGQTYPGKGAKKDNKS 151
 
Name Accession Description Interval E-value
Mesd pfam10185
Chaperone for wingless signalling and trafficking of LDL receptor; Mesd is a family of highly ...
 43-192 8.94e-98

Chaperone for wingless signalling and trafficking of LDL receptor; Mesd is a family of highly conserved proteins found from nematodes to humans. The final C-terminal residues, KEDL, are the endoplasmic reticulum retention sequence as it is an ER protein specifically required for the intracellular trafficking of members of the low-density lipoprotein family of receptors (LDLRs). The N- and C-terminal sequences are predicted to adopt a random coil conformation, with the exception of an isolated predicted helix within the N-terminal region, The central folded domain flanked by natively unstructured regions is the necessary structure for facilitating maturation of LRP6 (Low-Density Lipoprotein Receptor-Related Protein 6 Maturation).


Pssm-ID: 462985  Cd Length: 155  Bit Score: 281.27  E-value: 8.94e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24418559    43 KKDIRDYNDADMARLLEQWEKDDD-IEEGDLPEHKRPSAPIDFSKLDPGKPESILKMTKKGKTLMMFVTVSGNPTEKETE 121
Cdd:pfam10185   1 KKDIRDYNDADLERLLDQWEEDDEpLEPDELPEHLRPPPPIDFSKIDPSNPENLLKMSKKGKTLMMFVTVSGDPTEKETE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24418559   122 EITSLWQGSLFNANYDVQRFIVGSDRAIFMLRDGSYAWEIKDFLVSQDRCAEVTLEGQMYPGKGGGSKEKN 192
Cdd:pfam10185  81 EITKLWQTSLWNNHIQAERYIIDDNRAIFMFRDGSQAWEAKDFLVEQERCKEVTIEGQTYPGKGAKKDNKS 151
 
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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