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Conserved domains on  [gi|5803013|ref|NP_006808|]
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endoplasmic reticulum resident protein 29 isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_ERp29_N cd03007
PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ...
 36-149 3.61e-65

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: 198.53  E-value: 3.61e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013   36 KGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSAS-SDDLLVAEVGISDYGDKLNMELSEKYKLDKES 114
Cdd:cd03007   1 KGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAESSASaTDDLLVAEVGIKDYGEKLNMELGERYKLDKES 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 5803013  115 YPVFYLFRDGDFENPVPYTGA-VKVGAIQRWLKGQG 149
Cdd:cd03007  81 YPVIYLFHGGDFENPVPYSGAdVTVDALQRFLKGNT 116
ERp29 pfam07749
Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed ...
 156-251 1.12e-31

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: 112.28  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013    156 GCLPVYDALAGEFIrASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSD 235
Cdd:pfam07749   1 GRIEELDALAAEFV-AAAKDERKELLEEAKKAAEKLKEAEKKYAKYYVKVMEKILEKGEEYVEKELARLEKLLAKGKLSP 79

                          90
                  ....*....|....*.
gi 5803013    236 GKKEELQKSLNILTAF 251
Cdd:pfam07749  80 EKKDELQIRLNILRSF 95
 
Name Accession Description Interval E-value
PDI_a_ERp29_N cd03007
PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ...
 36-149 3.61e-65

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: 198.53  E-value: 3.61e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013   36 KGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSAS-SDDLLVAEVGISDYGDKLNMELSEKYKLDKES 114
Cdd:cd03007   1 KGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAESSASaTDDLLVAEVGIKDYGEKLNMELGERYKLDKES 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 5803013  115 YPVFYLFRDGDFENPVPYTGA-VKVGAIQRWLKGQG 149
Cdd:cd03007  81 YPVIYLFHGGDFENPVPYSGAdVTVDALQRFLKGNT 116
ERp29_N pfam07912
ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and ...
 33-155 1.70e-64

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: 197.38  E-value: 1.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013     33 LHTKGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLA-ENSASSDDLLVAEVGISDYGDKLNMELSEKYKLD 111
Cdd:pfam07912   1 LTTKGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAkENSASTEELLVAEVGIKDYGEKLNMELGERYKLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 5803013    112 KESYPVFYLFRdGDFENPV--PYTGAVKVGAIQRWLKGQ-GVYLGMP 155
Cdd:pfam07912  81 KESYPVIYLFR-GDLENPVlyPSNGAVTVDALQRFLKGQtGLYIGMP 126
ERp29 pfam07749
Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed ...
 156-251 1.12e-31

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: 112.28  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013    156 GCLPVYDALAGEFIrASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSD 235
Cdd:pfam07749   1 GRIEELDALAAEFV-AAAKDERKELLEEAKKAAEKLKEAEKKYAKYYVKVMEKILEKGEEYVEKELARLEKLLAKGKLSP 79

                          90
                  ....*....|....*.
gi 5803013    236 GKKEELQKSLNILTAF 251
Cdd:pfam07749  80 EKKDELQIRLNILRSF 95
ERp29c cd00238
ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like ...
 158-251 4.36e-29

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: 105.46  E-value: 4.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013  158 LPVYDALAGEFIRASgVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSDGK 237
Cdd:cd00238   1 IEELDELAKEFVDAS-DEERKELLEKVKEAVEKLKEAEAKYAKYYVKVMEKILEKGEDYVEKELARLERLLEKKGLAPEK 79

                        90
                ....*....|....
gi 5803013  238 KEELQKSLNILTAF 251
Cdd:cd00238  80 ADELTRRLNILRSF 93
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 45-146 4.43e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 41.27  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013    45 TFYKVIPKSKFVLVKFdtqypYGEKQDEFKRLA-ENSASSDDL--LVAEVGISDYGDKLNMELSEKYKLdkESYPVFYLF 121
Cdd:PTZ00102  41 TFDKFITENEIVLVKF-----YAPWCGHCKRLApEYKKAAKMLkeKKSEIVLASVDATEEMELAQEFGV--RGYPTIKFF 113

                         90       100
                 ....*....|....*....|....*
gi 5803013   122 RDGdfeNPVPYTGAVKVGAIQRWLK 146
Cdd:PTZ00102 114 NKG---NPVNYSGGRTADGIVSWIK 135
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 39-148 8.78e-03

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 36.96  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013     39 LPLDTVTFYKVIPKSKFVLVKFdtqY-PY-GEKQD---EFKRLAEN-SASSDDLLVAEVGISDygdklNMELSEKYKLdk 112
Cdd:TIGR01130   4 LVLTKDNFDDFIKSHEFVLVEF---YaPWcGHCKSlapEYEKAADElKKKGPPIKLAKVDATE-----EKDLAQKYGV-- 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 5803013    113 ESYPVFYLFRDGDFeNPVPYTGAVKVGAIQRWLKGQ 148
Cdd:TIGR01130  74 SGYPTLKIFRNGED-SVSDYNGPRDADGIVKYMKKQ 108
 
Name Accession Description Interval E-value
PDI_a_ERp29_N cd03007
PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ...
 36-149 3.61e-65

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: 198.53  E-value: 3.61e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013   36 KGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSAS-SDDLLVAEVGISDYGDKLNMELSEKYKLDKES 114
Cdd:cd03007   1 KGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAESSASaTDDLLVAEVGIKDYGEKLNMELGERYKLDKES 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 5803013  115 YPVFYLFRDGDFENPVPYTGA-VKVGAIQRWLKGQG 149
Cdd:cd03007  81 YPVIYLFHGGDFENPVPYSGAdVTVDALQRFLKGNT 116
ERp29_N pfam07912
ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and ...
 33-155 1.70e-64

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: 197.38  E-value: 1.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013     33 LHTKGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLA-ENSASSDDLLVAEVGISDYGDKLNMELSEKYKLD 111
Cdd:pfam07912   1 LTTKGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAkENSASTEELLVAEVGIKDYGEKLNMELGERYKLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 5803013    112 KESYPVFYLFRdGDFENPV--PYTGAVKVGAIQRWLKGQ-GVYLGMP 155
Cdd:pfam07912  81 KESYPVIYLFR-GDLENPVlyPSNGAVTVDALQRFLKGQtGLYIGMP 126
ERp29 pfam07749
Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed ...
 156-251 1.12e-31

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: 112.28  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013    156 GCLPVYDALAGEFIrASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSD 235
Cdd:pfam07749   1 GRIEELDALAAEFV-AAAKDERKELLEEAKKAAEKLKEAEKKYAKYYVKVMEKILEKGEEYVEKELARLEKLLAKGKLSP 79

                          90
                  ....*....|....*.
gi 5803013    236 GKKEELQKSLNILTAF 251
Cdd:pfam07749  80 EKKDELQIRLNILRSF 95
ERp29c cd00238
ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like ...
 158-251 4.36e-29

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: 105.46  E-value: 4.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013  158 LPVYDALAGEFIRASgVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSDGK 237
Cdd:cd00238   1 IEELDELAKEFVDAS-DEERKELLEKVKEAVEKLKEAEAKYAKYYVKVMEKILEKGEDYVEKELARLERLLEKKGLAPEK 79

                        90
                ....*....|....
gi 5803013  238 KEELQKSLNILTAF 251
Cdd:cd00238  80 ADELTRRLNILRSF 93
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 39-145 1.83e-12

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: 61.86  E-value: 1.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013   39 LPLDTVTFYKVIPKSKFVLVKFDTQY--PYGEKQDEFKRLAENSASSDDLLVAEVGISDygdklNMELSEKYKLdkESYP 116
Cdd:cd02961   1 VELTDDNFDELVKDSKDVLVEFYAPWcgHCKALAPEYEKLAKELKGDGKVVVAKVDCTA-----NNDLCSEYGV--RGYP 73

                        90       100
                ....*....|....*....|....*....
gi 5803013  117 VFYLFRDGDfENPVPYTGAVKVGAIQRWL 145
Cdd:cd02961  74 TIKLFPNGS-KEPVKYEGPRTLESLVEFI 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 45-146 4.43e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 41.27  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013    45 TFYKVIPKSKFVLVKFdtqypYGEKQDEFKRLA-ENSASSDDL--LVAEVGISDYGDKLNMELSEKYKLdkESYPVFYLF 121
Cdd:PTZ00102  41 TFDKFITENEIVLVKF-----YAPWCGHCKRLApEYKKAAKMLkeKKSEIVLASVDATEEMELAQEFGV--RGYPTIKFF 113

                         90       100
                 ....*....|....*....|....*
gi 5803013   122 RDGdfeNPVPYTGAVKVGAIQRWLK 146
Cdd:PTZ00102 114 NKG---NPVNYSGGRTADGIVSWIK 135
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 49-145 4.52e-03

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are 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. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 36.00  E-value: 4.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013   49 VIPKSKFVLVKFDTQY--------PYgekqdeFKRLAENSASSDDLLVAEVGISdygdkLNMELSEKYKldkESYPVFYL 120
Cdd:cd02995  14 VLDSDKDVLVEFYAPWcghckalaPI------YEELAEKLKGDDNVVIAKMDAT-----ANDVPSEFVV---DGFPTILF 79

                        90       100
                ....*....|....*....|....*
gi 5803013  121 FRDGDFENPVPYTGAVKVGAIQRWL 145
Cdd:cd02995  80 FPAGDKSNPIKYEGDRTLEDLIKFI 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 39-148 8.78e-03

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 36.96  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803013     39 LPLDTVTFYKVIPKSKFVLVKFdtqY-PY-GEKQD---EFKRLAEN-SASSDDLLVAEVGISDygdklNMELSEKYKLdk 112
Cdd:TIGR01130   4 LVLTKDNFDDFIKSHEFVLVEF---YaPWcGHCKSlapEYEKAADElKKKGPPIKLAKVDATE-----EKDLAQKYGV-- 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 5803013    113 ESYPVFYLFRDGDFeNPVPYTGAVKVGAIQRWLKGQ 148
Cdd:TIGR01130  74 SGYPTLKIFRNGED-SVSDYNGPRDADGIVKYMKKQ 108
 
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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