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Conserved domains on  [gi|195584814|ref|XP_002082199|]
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protein windbeutel [Drosophila simulans]

Protein Classification

endoplasmic reticulum resident protein 29; protein disulfide isomerase family protein( domain architecture ID 11171922)

endoplasmic reticulum resident protein 29 plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER; protein disulfide isomerase family protein similar to Saccharomyces cerevisiae protein disulfide-isomerase MPD1 that participates in the folding of proteins containing disulfide bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ERp29_N pfam07912
ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and ...
 22-147 1.24e-76

ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organized into a thioredoxin-like fold that resembles the a domain of human protein disulphide isomerase (PDI). However, this domain lacks the C-X-X-C motif required for the redox function of PDI; it is therefore thought that ERp29's function is similar to the chaperone function of PDI. The N-terminal domain is exclusively responsible for the homodimerization of the protein, without covalent linkages or additional contacts with other domains.


:

Pssm-ID: 400320  Cd Length: 126  Bit Score: 227.81  E-value: 1.24e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814   22 VTCTGCVDLDELSFQKTVERFPYSIVKFDIAYPYGEKHEAFTAFSKSAHKATKDLLIATVGVKDYGELENKALGDRYKVD 101
Cdd:pfam07912   1 LTTKGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAKENSASTEELLVAEVGIKDYGEKLNMELGERYKLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 195584814  102 DKNFPSIFLFKGNADEYVQLPSHVDVTLDNLKAFVSANTPLYIGRD 147
Cdd:pfam07912  81 KESYPVIYLFRGDLENPVLYPSNGAVTVDALQRFLKGQTGLYIGMP 126
ERp29 pfam07749
Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed ...
 148-242 2.48e-27

Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein found in mammals. ERp29 is comprised of two domains. This domain, the C-terminal domain, has an all helical fold. ERp29 is thought to form part of the thyroglobulin folding complex.


:

Pssm-ID: 462253  Cd Length: 95  Bit Score: 101.11  E-value: 2.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814  148 GCIKEFNEVLKNYANIPDAEQLKLIEELQAKQEQLTDPEQQqNARAYLIYMRKIHEVGYDFLEEETKRLLR-LKAGKVTE 226
Cdd:pfam07749   1 GRIEELDALAAEFVAAAKDERKELLEEAKKAAEKLKEAEKK-YAKYYVKVMEKILEKGEEYVEKELARLEKlLAKGKLSP 79

                          90
                  ....*....|....*.
gi 195584814  227 AKKEELLRKLNILEVF 242
Cdd:pfam07749  80 EKKDELQIRLNILRSF 95
 
Name Accession Description Interval E-value
ERp29_N pfam07912
ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and ...
 22-147 1.24e-76

ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organized into a thioredoxin-like fold that resembles the a domain of human protein disulphide isomerase (PDI). However, this domain lacks the C-X-X-C motif required for the redox function of PDI; it is therefore thought that ERp29's function is similar to the chaperone function of PDI. The N-terminal domain is exclusively responsible for the homodimerization of the protein, without covalent linkages or additional contacts with other domains.


Pssm-ID: 400320  Cd Length: 126  Bit Score: 227.81  E-value: 1.24e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814   22 VTCTGCVDLDELSFQKTVERFPYSIVKFDIAYPYGEKHEAFTAFSKSAHKATKDLLIATVGVKDYGELENKALGDRYKVD 101
Cdd:pfam07912   1 LTTKGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAKENSASTEELLVAEVGIKDYGEKLNMELGERYKLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 195584814  102 DKNFPSIFLFKGNADEYVQLPSHVDVTLDNLKAFVSANTPLYIGRD 147
Cdd:pfam07912  81 KESYPVIYLFRGDLENPVLYPSNGAVTVDALQRFLKGQTGLYIGMP 126
PDI_a_ERp29_N cd03007
PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ...
 25-140 3.63e-66

PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ER-resident protein expressed in high levels in secretory cells. It forms homodimers and higher oligomers in vitro and in vivo. It contains a redox inactive TRX-like domain at the N-terminus, which is homologous to the redox active TRX (a) domains of PDI, and a C-terminal helical domain similar to the C-terminal domain of P5. The expression profile of ERp29 suggests a role in secretory protein production distinct from that of PDI. It has also been identified as a member of the thyroglobulin folding complex. The Drosophila homolog, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase.


Pssm-ID: 239305  Cd Length: 116  Bit Score: 201.23  E-value: 3.63e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814  25 TGCVDLDELSFQKTVERFPYSIVKFDIAYPYGEKHEAFTAFSKSAHKATKDLLIATVGVKDYGELENKALGDRYKVDDKN 104
Cdd:cd03007    1 KGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAESSASATDDLLVAEVGIKDYGEKLNMELGERYKLDKES 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 195584814 105 FPSIFLFKGNADEYVQLPSHVDVTLDNLKAFVSANT 140
Cdd:cd03007   81 YPVIYLFHGGDFENPVPYSGADVTVDALQRFLKGNT 116
ERp29 pfam07749
Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed ...
 148-242 2.48e-27

Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein found in mammals. ERp29 is comprised of two domains. This domain, the C-terminal domain, has an all helical fold. ERp29 is thought to form part of the thyroglobulin folding complex.


Pssm-ID: 462253  Cd Length: 95  Bit Score: 101.11  E-value: 2.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814  148 GCIKEFNEVLKNYANIPDAEQLKLIEELQAKQEQLTDPEQQqNARAYLIYMRKIHEVGYDFLEEETKRLLR-LKAGKVTE 226
Cdd:pfam07749   1 GRIEELDALAAEFVAAAKDERKELLEEAKKAAEKLKEAEKK-YAKYYVKVMEKILEKGEEYVEKELARLEKlLAKGKLSP 79

                          90
                  ....*....|....*.
gi 195584814  227 AKKEELLRKLNILEVF 242
Cdd:pfam07749  80 EKKDELQIRLNILRSF 95
ERp29c cd00238
ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like ...
 150-242 2.41e-23

ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like proteins ERp29 and ERp38. ERp29 (also called ERp28) is a ubiquitous endoplasmic reticulum (ER)-resident protein expressed in high levels in secretory cells. It contains a redox inactive TRX-like domain at the N-terminus. The expression profile of ERp29 suggests a role in secretory protein production, distinct from that of PDI. It has also been identified as a member of the thyroglobulin folding complex and is essential in regulating the secretion of thyroglobulin. The Drosophila homolog, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase. ERp38 is a P5-like protein, first isolated from alfalfa (the cDNA clone was named G1), which contains two redox active TRX domains at the N-terminus, like human P5. However, unlike human P5, ERp38 also contains a C-terminal domain with homology to the C-terminal domain of ERp29. It may be a glucose-regulated protein. The function of the all-helical C-terminal domain of ERp29 and ERp38 remains unclear. The C-terminal domain of Wind is thought to provide a distinct site required for interaction with its substrate, Pipe.


Pssm-ID: 238146  Cd Length: 93  Bit Score: 90.44  E-value: 2.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814 150 IKEFNEVLKNYANIPDAEQLKLIEELQAKQEQLTdPEQQQNARAYLIYMRKIHEVGYDFLEEETKRLLRLKAGKV-TEAK 228
Cdd:cd00238    1 IEELDELAKEFVDASDEERKELLEKVKEAVEKLK-EAEAKYAKYYVKVMEKILEKGEDYVEKELARLERLLEKKGlAPEK 79

                         90
                 ....*....|....
gi 195584814 229 KEELLRKLNILEVF 242
Cdd:cd00238   80 ADELTRRLNILRSF 93
 
Name Accession Description Interval E-value
ERp29_N pfam07912
ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and ...
 22-147 1.24e-76

ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organized into a thioredoxin-like fold that resembles the a domain of human protein disulphide isomerase (PDI). However, this domain lacks the C-X-X-C motif required for the redox function of PDI; it is therefore thought that ERp29's function is similar to the chaperone function of PDI. The N-terminal domain is exclusively responsible for the homodimerization of the protein, without covalent linkages or additional contacts with other domains.


Pssm-ID: 400320  Cd Length: 126  Bit Score: 227.81  E-value: 1.24e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814   22 VTCTGCVDLDELSFQKTVERFPYSIVKFDIAYPYGEKHEAFTAFSKSAHKATKDLLIATVGVKDYGELENKALGDRYKVD 101
Cdd:pfam07912   1 LTTKGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAKENSASTEELLVAEVGIKDYGEKLNMELGERYKLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 195584814  102 DKNFPSIFLFKGNADEYVQLPSHVDVTLDNLKAFVSANTPLYIGRD 147
Cdd:pfam07912  81 KESYPVIYLFRGDLENPVLYPSNGAVTVDALQRFLKGQTGLYIGMP 126
PDI_a_ERp29_N cd03007
PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ...
 25-140 3.63e-66

PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ER-resident protein expressed in high levels in secretory cells. It forms homodimers and higher oligomers in vitro and in vivo. It contains a redox inactive TRX-like domain at the N-terminus, which is homologous to the redox active TRX (a) domains of PDI, and a C-terminal helical domain similar to the C-terminal domain of P5. The expression profile of ERp29 suggests a role in secretory protein production distinct from that of PDI. It has also been identified as a member of the thyroglobulin folding complex. The Drosophila homolog, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase.


Pssm-ID: 239305  Cd Length: 116  Bit Score: 201.23  E-value: 3.63e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814  25 TGCVDLDELSFQKTVERFPYSIVKFDIAYPYGEKHEAFTAFSKSAHKATKDLLIATVGVKDYGELENKALGDRYKVDDKN 104
Cdd:cd03007    1 KGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAESSASATDDLLVAEVGIKDYGEKLNMELGERYKLDKES 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 195584814 105 FPSIFLFKGNADEYVQLPSHVDVTLDNLKAFVSANT 140
Cdd:cd03007   81 YPVIYLFHGGDFENPVPYSGADVTVDALQRFLKGNT 116
ERp29 pfam07749
Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed ...
 148-242 2.48e-27

Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein found in mammals. ERp29 is comprised of two domains. This domain, the C-terminal domain, has an all helical fold. ERp29 is thought to form part of the thyroglobulin folding complex.


Pssm-ID: 462253  Cd Length: 95  Bit Score: 101.11  E-value: 2.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814  148 GCIKEFNEVLKNYANIPDAEQLKLIEELQAKQEQLTDPEQQqNARAYLIYMRKIHEVGYDFLEEETKRLLR-LKAGKVTE 226
Cdd:pfam07749   1 GRIEELDALAAEFVAAAKDERKELLEEAKKAAEKLKEAEKK-YAKYYVKVMEKILEKGEEYVEKELARLEKlLAKGKLSP 79

                          90
                  ....*....|....*.
gi 195584814  227 AKKEELLRKLNILEVF 242
Cdd:pfam07749  80 EKKDELQIRLNILRSF 95
ERp29c cd00238
ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like ...
 150-242 2.41e-23

ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like proteins ERp29 and ERp38. ERp29 (also called ERp28) is a ubiquitous endoplasmic reticulum (ER)-resident protein expressed in high levels in secretory cells. It contains a redox inactive TRX-like domain at the N-terminus. The expression profile of ERp29 suggests a role in secretory protein production, distinct from that of PDI. It has also been identified as a member of the thyroglobulin folding complex and is essential in regulating the secretion of thyroglobulin. The Drosophila homolog, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase. ERp38 is a P5-like protein, first isolated from alfalfa (the cDNA clone was named G1), which contains two redox active TRX domains at the N-terminus, like human P5. However, unlike human P5, ERp38 also contains a C-terminal domain with homology to the C-terminal domain of ERp29. It may be a glucose-regulated protein. The function of the all-helical C-terminal domain of ERp29 and ERp38 remains unclear. The C-terminal domain of Wind is thought to provide a distinct site required for interaction with its substrate, Pipe.


Pssm-ID: 238146  Cd Length: 93  Bit Score: 90.44  E-value: 2.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814 150 IKEFNEVLKNYANIPDAEQLKLIEELQAKQEQLTdPEQQQNARAYLIYMRKIHEVGYDFLEEETKRLLRLKAGKV-TEAK 228
Cdd:cd00238    1 IEELDELAKEFVDASDEERKELLEKVKEAVEKLK-EAEAKYAKYYVKVMEKILEKGEDYVEKELARLERLLEKKGlAPEK 79

                         90
                 ....*....|....
gi 195584814 229 KEELLRKLNILEVF 242
Cdd:cd00238   80 ADELTRRLNILRSF 93
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 28-136 3.23e-04

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 39.13  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195584814  28 VDLDELSFQKTVERFPYSIVKFDIAY--PYGEKHEAFTAFSKSAhKATKDLLIATVGVKdygelENKALGDRYKVddKNF 105
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWcgHCKALAPEYEKLAKEL-KGDGKVVVAKVDCT-----ANNDLCSEYGV--RGY 72

                         90       100       110
                 ....*....|....*....|....*....|.
gi 195584814 106 PSIFLFKGNADEYVQLPShvDVTLDNLKAFV 136
Cdd:cd02961   73 PTIKLFPNGSKEPVKYEG--PRTLESLVEFI 101
 
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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