NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|20988826|gb|AAH30218|]
View 

Endoplasmic reticulum protein 27 [Homo sapiens]

Protein Classification

thioredoxin domain-containing protein 16; thioredoxin family protein( domain architecture ID 12155891)

thioredoxin domain-containing protein 16 (TXNDC16), or ERP90, is a protein disulfide isomerase (PDI) family protein that interacts with ERFAD, a flavoprotein involved in ER-associated degradation (ERAD); thioredoxin family protein with similarity to thiol:disulfide interchange protein DsbD that facilitates the formation of correct disulfide bonds in some periplasmic proteins and is required for the assembly of the periplasmic c-type cytochromes

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
64-250 1.08e-50

Thioredoxin-like domain;


:

Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 164.46  E-value: 1.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826    64 FQDLEIPAVPILHSMVQKFPG-VSFGISTDSEVLTHYNITGNTICLFRLVDNEQLNLEdedIESIDATKLSRFIEINSLH 142
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGdVRFGITFSKEVADKYNIKEPAILLFRKFDEETVHYP---GDSINFEDLKKFIQKNCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826   143 MVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEYEENMHRYQKAAKLFQGKILFILVDsgMKENGKVISFFKLKESQLPAL 222
Cdd:pfam13848  78 LVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVD--AKSFGRPLEYFGLSESDLPVI 155

                         170       180
                  ....*....|....*....|....*...
gi 20988826   223 AIYQTLDDEWDTLPTAEVSVEHVQNFCD 250
Cdd:pfam13848 156 VIVDSFSHMYKYFPSDEFSPESLKEFIN 183
 
Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
64-250 1.08e-50

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 164.46  E-value: 1.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826    64 FQDLEIPAVPILHSMVQKFPG-VSFGISTDSEVLTHYNITGNTICLFRLVDNEQLNLEdedIESIDATKLSRFIEINSLH 142
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGdVRFGITFSKEVADKYNIKEPAILLFRKFDEETVHYP---GDSINFEDLKKFIQKNCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826   143 MVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEYEENMHRYQKAAKLFQGKILFILVDsgMKENGKVISFFKLKESQLPAL 222
Cdd:pfam13848  78 LVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVD--AKSFGRPLEYFGLSESDLPVI 155

                         170       180
                  ....*....|....*....|....*...
gi 20988826   223 AIYQTLDDEWDTLPTAEVSVEHVQNFCD 250
Cdd:pfam13848 156 VIVDSFSHMYKYFPSDEFSPESLKEFIN 183
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 20-257 1.92e-25

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: 104.37  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826    20 AAEVAAEVEKSSdGPGAAQeptwLTDVPAAMEFIAATEVAVIGFFQDLEIPAVPILHSMVQKFPGVSFGISTDS--EVLT 97
Cdd:TIGR01130  98 ADGIVKYMKKQS-GPAVKE----IETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRDVYFFFAHSSdvAAFA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826    98 HYNITGNTICLFR--LVDNEQLNLEDEDIESIDAtkLSRFIEINSLHMVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEY 175
Cdd:TIGR01130 173 KLGAFPDSVVLFKpkDEDEKFSKVDGEMDTDVSD--LEKFIRAESLPLVGEFTQETAAKYFESGPLVVLYYNVDESLDPF 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826   176 EENMHRYQKAAKLFQGKilFILVDSGMKE-NGKVISFFKLKESQLPALAIYQTLDDEWDTLPTAEVSVEHVQNFCDGFLS 254
Cdd:TIGR01130 251 EELRNRFLEAAKKFRGK--FVNFAVADEEdFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLD 328


                  ...
gi 20988826   255 GKL 257
Cdd:TIGR01130 329 GKL 331
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 151-253 8.80e-20

Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity.


Pssm-ID: 239280 [Multi-domain]  Cd Length: 103  Bit Score: 81.93  E-value: 8.80e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826 151 TVIGLFNSVIQ--IHLLLIMNKASPEYEENMHRYQKAAKLFQGKILFILVDSgmKENGKVISFFKLKESQLPALAIYQTL 228
Cdd:cd02982   1 NAETFFNYEESgkPLLVLFYNKDDSESEELRERFKEVAKKFKGKLLFVVVDA--DDFGRHLEYFGLKEEDLPVIAIINLS 78

                        90       100
                ....*....|....*....|....*
gi 20988826 229 DDEWDTLPTAEVSVEHVQNFCDGFL 253
Cdd:cd02982  79 DGKKYLMPEEELTAESLEEFVEDFL 103
 
Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
64-250 1.08e-50

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 164.46  E-value: 1.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826    64 FQDLEIPAVPILHSMVQKFPG-VSFGISTDSEVLTHYNITGNTICLFRLVDNEQLNLEdedIESIDATKLSRFIEINSLH 142
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGdVRFGITFSKEVADKYNIKEPAILLFRKFDEETVHYP---GDSINFEDLKKFIQKNCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826   143 MVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEYEENMHRYQKAAKLFQGKILFILVDsgMKENGKVISFFKLKESQLPAL 222
Cdd:pfam13848  78 LVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVD--AKSFGRPLEYFGLSESDLPVI 155

                         170       180
                  ....*....|....*....|....*...
gi 20988826   223 AIYQTLDDEWDTLPTAEVSVEHVQNFCD 250
Cdd:pfam13848 156 VIVDSFSHMYKYFPSDEFSPESLKEFIN 183
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 20-257 1.92e-25

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: 104.37  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826    20 AAEVAAEVEKSSdGPGAAQeptwLTDVPAAMEFIAATEVAVIGFFQDLEIPAVPILHSMVQKFPGVSFGISTDS--EVLT 97
Cdd:TIGR01130  98 ADGIVKYMKKQS-GPAVKE----IETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRDVYFFFAHSSdvAAFA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826    98 HYNITGNTICLFR--LVDNEQLNLEDEDIESIDAtkLSRFIEINSLHMVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEY 175
Cdd:TIGR01130 173 KLGAFPDSVVLFKpkDEDEKFSKVDGEMDTDVSD--LEKFIRAESLPLVGEFTQETAAKYFESGPLVVLYYNVDESLDPF 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826   176 EENMHRYQKAAKLFQGKilFILVDSGMKE-NGKVISFFKLKESQLPALAIYQTLDDEWDTLPTAEVSVEHVQNFCDGFLS 254
Cdd:TIGR01130 251 EELRNRFLEAAKKFRGK--FVNFAVADEEdFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLD 328


                  ...
gi 20988826   255 GKL 257
Cdd:TIGR01130 329 GKL 331
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 151-253 8.80e-20

Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity.


Pssm-ID: 239280 [Multi-domain]  Cd Length: 103  Bit Score: 81.93  E-value: 8.80e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826 151 TVIGLFNSVIQ--IHLLLIMNKASPEYEENMHRYQKAAKLFQGKILFILVDSgmKENGKVISFFKLKESQLPALAIYQTL 228
Cdd:cd02982   1 NAETFFNYEESgkPLLVLFYNKDDSESEELRERFKEVAKKFKGKLLFVVVDA--DDFGRHLEYFGLKEEDLPVIAIINLS 78

                        90       100
                ....*....|....*....|....*
gi 20988826 229 DDEWDTLPTAEVSVEHVQNFCDGFL 253
Cdd:cd02982  79 DGKKYLMPEEELTAESLEEFVEDFL 103
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 43-139 1.80e-11

Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition.


Pssm-ID: 239279  Cd Length: 97  Bit Score: 59.27  E-value: 1.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20988826  43 LTDVPAAMEFIAATEVAVIGFFQDLEIPAVPILHSMVQKFPG-VSFGISTDSEVLTHYNITGNTICLFRLVDNEQLNLED 121
Cdd:cd02981   4 LTSKEELEKFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRDdYGFGHTSDKEVAKKLKVKPGSVVLFKPFEEEPVEYDG 83

                        90
                ....*....|....*...
gi 20988826 122 EDiesiDATKLSRFIEIN 139
Cdd:cd02981  84 EF----TEESLVEFIKDN 97
 
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