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Conserved domains on  [gi|74354413|gb|AAI04407|]
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Endoplasmic reticulum protein 27 [Mus musculus]

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

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
64-250 2.49e-51

Thioredoxin-like domain;


:

Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 166.00  E-value: 2.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413    64 FQDLEIPIVSVFRSMARQFQ-DVSFGISNHSEVLTHYNVTSSSICLFRLVDDQQLHLNAEDIenlDAAKLSRFIHMNNLH 142
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKgDVRFGITFSKEVADKYNIKEPAILLFRKFDEETVHYPGDSI---NFEDLKKFIQKNCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413   143 WVTEYSPMIAAGLFNTMVQTHLLLMMKKTSPEYEESMRRYREAAKLFQGQILFVLVDSGKreNGKVMSYFKLKESQLPAL 222
Cdd:pfam13848  78 LVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAKS--FGRPLEYFGLSESDLPVI 155

                         170       180
                  ....*....|....*....|....*...
gi 74354413   223 AIYESVDDKWDTLPIAEVTVEKVRGFCE 250
Cdd:pfam13848 156 VIVDSFSHMYKYFPSDEFSPESLKEFIN 183
 
Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
64-250 2.49e-51

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 166.00  E-value: 2.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413    64 FQDLEIPIVSVFRSMARQFQ-DVSFGISNHSEVLTHYNVTSSSICLFRLVDDQQLHLNAEDIenlDAAKLSRFIHMNNLH 142
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKgDVRFGITFSKEVADKYNIKEPAILLFRKFDEETVHYPGDSI---NFEDLKKFIQKNCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413   143 WVTEYSPMIAAGLFNTMVQTHLLLMMKKTSPEYEESMRRYREAAKLFQGQILFVLVDSGKreNGKVMSYFKLKESQLPAL 222
Cdd:pfam13848  78 LVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAKS--FGRPLEYFGLSESDLPVI 155

                         170       180
                  ....*....|....*....|....*...
gi 74354413   223 AIYESVDDKWDTLPIAEVTVEKVRGFCE 250
Cdd:pfam13848 156 VIVDSFSHMYKYFPSDEFSPESLKEFIN 183
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 43-264 1.43e-27

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: 110.15  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413    43 LTDVPATVELIAAAEVAVIGFFQDLEIPIVSVFRSMARQFQDVSFGI--SNHSEVLTHYNVTSSSICLFRLVDDQQLHLN 120
Cdd:TIGR01130 116 IETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRDVYFFFahSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSK 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413   121 AEDIENLDAAKLSRFIHMNNLHWVTEYSPMIAAGLFNTMVQTHLLLMMKKTSPEYEESMRRYREAAKLFQGQilFVLVDS 200
Cdd:TIGR01130 196 VDGEMDTDVSDLEKFIRAESLPLVGEFTQETAAKYFESGPLVVLYYNVDESLDPFEELRNRFLEAAKKFRGK--FVNFAV 273

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74354413   201 G-KRENGKVMSYFKLKESQLPALAIYESVDDKWDTLPIAEVTVEKVRGFCEGFLKGLLQRDLEAE 264
Cdd:TIGR01130 274 AdEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLDGKLKPYLKSE 338
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 152-253 5.23e-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: 82.32  E-value: 5.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413 152 AAGLFNTMVQ--THLLLMMKKTSPEYEESMRRYREAAKLFQGQILFVLVDSgkRENGKVMSYFKLKESQLPALAIYESVD 229
Cdd:cd02982   2 AETFFNYEESgkPLLVLFYNKDDSESEELRERFKEVAKKFKGKLLFVVVDA--DDFGRHLEYFGLKEEDLPVIAIINLSD 79

                        90       100
                ....*....|....*....|....
gi 74354413 230 DKWDTLPIAEVTVEKVRGFCEGFL 253
Cdd:cd02982  80 GKKYLMPEEELTAESLEEFVEDFL 103
 
Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
64-250 2.49e-51

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 166.00  E-value: 2.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413    64 FQDLEIPIVSVFRSMARQFQ-DVSFGISNHSEVLTHYNVTSSSICLFRLVDDQQLHLNAEDIenlDAAKLSRFIHMNNLH 142
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKgDVRFGITFSKEVADKYNIKEPAILLFRKFDEETVHYPGDSI---NFEDLKKFIQKNCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413   143 WVTEYSPMIAAGLFNTMVQTHLLLMMKKTSPEYEESMRRYREAAKLFQGQILFVLVDSGKreNGKVMSYFKLKESQLPAL 222
Cdd:pfam13848  78 LVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAKS--FGRPLEYFGLSESDLPVI 155

                         170       180
                  ....*....|....*....|....*...
gi 74354413   223 AIYESVDDKWDTLPIAEVTVEKVRGFCE 250
Cdd:pfam13848 156 VIVDSFSHMYKYFPSDEFSPESLKEFIN 183
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 43-264 1.43e-27

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: 110.15  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413    43 LTDVPATVELIAAAEVAVIGFFQDLEIPIVSVFRSMARQFQDVSFGI--SNHSEVLTHYNVTSSSICLFRLVDDQQLHLN 120
Cdd:TIGR01130 116 IETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRDVYFFFahSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSK 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413   121 AEDIENLDAAKLSRFIHMNNLHWVTEYSPMIAAGLFNTMVQTHLLLMMKKTSPEYEESMRRYREAAKLFQGQilFVLVDS 200
Cdd:TIGR01130 196 VDGEMDTDVSDLEKFIRAESLPLVGEFTQETAAKYFESGPLVVLYYNVDESLDPFEELRNRFLEAAKKFRGK--FVNFAV 273

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74354413   201 G-KRENGKVMSYFKLKESQLPALAIYESVDDKWDTLPIAEVTVEKVRGFCEGFLKGLLQRDLEAE 264
Cdd:TIGR01130 274 AdEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLDGKLKPYLKSE 338
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 152-253 5.23e-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: 82.32  E-value: 5.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413 152 AAGLFNTMVQ--THLLLMMKKTSPEYEESMRRYREAAKLFQGQILFVLVDSgkRENGKVMSYFKLKESQLPALAIYESVD 229
Cdd:cd02982   2 AETFFNYEESgkPLLVLFYNKDDSESEELRERFKEVAKKFKGKLLFVVVDA--DDFGRHLEYFGLKEEDLPVIAIINLSD 79

                        90       100
                ....*....|....*....|....
gi 74354413 230 DKWDTLPIAEVTVEKVRGFCEGFL 253
Cdd:cd02982  80 GKKYLMPEEELTAESLEEFVEDFL 103
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 43-139 5.80e-10

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: 55.04  E-value: 5.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413  43 LTDVPATVELIAAAEVAVIGFFQDLEIPIVSVFRSMARQFQ-DVSFGISNHSEVLTHYNVTSSSICLFRLVDDQQLHLNA 121
Cdd:cd02981   4 LTSKEELEKFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRdDYGFGHTSDKEVAKKLKVKPGSVVLFKPFEEEPVEYDG 83

                        90
                ....*....|....*...
gi 74354413 122 EdienLDAAKLSRFIHMN 139
Cdd:cd02981  84 E----FTEESLVEFIKDN 97
PDI_b_ERp57 cd03069
PDIb family, ERp57 subfamily, first redox inactive TRX-like domain b; ERp57 (or ERp60) ...
 53-139 2.92e-03

PDIb family, ERp57 subfamily, first redox inactive TRX-like domain b; ERp57 (or ERp60) exhibits both disulfide oxidase and reductase functions like PDI, by catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER and acting as isomerases to correct any non-native disulfide bonds. It also displays chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. ERp57 contains two redox-active TRX (a) domains and two redox inactive TRX-like (b) domains. It shares the same domain arrangement of abb'a' as PDI, but lacks the C-terminal acid-rich region (c domain) that is present in PDI. ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins. Similar to PDI, the b domain of ERp57 is likely involved in binding to substrates.


Pssm-ID: 239367  Cd Length: 104  Bit Score: 36.54  E-value: 2.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74354413  53 IAAAEVAVIGFFQDLEIPIVSVFRSMARQFQD-VSFGISNHSEVLTHYNVTsSSICLFRlvdDQQLHLNAED-----IEN 126
Cdd:cd03069  15 LSDDDASVVGFFEDEDSKLLSEFLKAADTLREsFRFAHTSDKQLLEKYGYG-EGVVLFR---PPRLSNKFEDssvkfDGD 90

                        90
                ....*....|...
gi 74354413 127 LDAAKLSRFIHMN 139
Cdd:cd03069  91 LDSSKIKKFIREN 103
 
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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