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Conserved domains on  [gi|663854316|ref|NP_001287713|]
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endoplasmic reticulum resident protein 27 isoform 2 [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

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
11-149 1.03e-33

Thioredoxin-like domain;


:

Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 117.46  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663854316   11 VDNEQLNLEdedIESIDATKLSRFIEINSLHMVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEYEENMHRYQKAAKLFQG 90
Cdd:pfam13848  50 FDEETVHYP---GDSINFEDLKKFIQKNCLPLVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRG 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 663854316   91 KILFILVDsgMKENGKVISFFKLKESQLPALAIYQTLDDEWDTLPTAEVSVEHVQNFCD 149
Cdd:pfam13848 127 KINFALVD--AKSFGRPLEYFGLSESDLPVIVIVDSFSHMYKYFPSDEFSPESLKEFIN 183
 
Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
11-149 1.03e-33

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 117.46  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663854316   11 VDNEQLNLEdedIESIDATKLSRFIEINSLHMVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEYEENMHRYQKAAKLFQG 90
Cdd:pfam13848  50 FDEETVHYP---GDSINFEDLKKFIQKNCLPLVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRG 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 663854316   91 KILFILVDsgMKENGKVISFFKLKESQLPALAIYQTLDDEWDTLPTAEVSVEHVQNFCD 149
Cdd:pfam13848 127 KINFALVD--AKSFGRPLEYFGLSESDLPVIVIVDSFSHMYKYFPSDEFSPESLKEFIN 183
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 50-152 3.43e-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: 80.39  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663854316  50 TVIGLFNSVIQ--IHLLLIMNKASPEYEENMHRYQKAAKLFQGKILFILVDSgmKENGKVISFFKLKESQLPALAIYQTL 127
Cdd:cd02982    1 NAETFFNYEESgkPLLVLFYNKDDSESEELRERFKEVAKKFKGKLLFVVVDA--DDFGRHLEYFGLKEEDLPVIAIINLS 78

                         90       100
                 ....*....|....*....|....*
gi 663854316 128 DDEWDTLPTAEVSVEHVQNFCDGFL 152
Cdd:cd02982   79 DGKKYLMPEEELTAESLEEFVEDFL 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 27-156 1.50e-17

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: 78.95  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663854316   27 DATKLSRFIEINSLHMVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEYEENMHRYQKAAKLFQGKilFILVDSGMKE-NG 105
Cdd:TIGR01130 203 DVSDLEKFIRAESLPLVGEFTQETAAKYFESGPLVVLYYNVDESLDPFEELRNRFLEAAKKFRGK--FVNFAVADEEdFG 280

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 663854316  106 KVISFFKLKESQLPALAIYQTLDDEWDTLPTAEVSVEHVQNFCDGFLSGKL 156
Cdd:TIGR01130 281 RELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLDGKL 331
 
Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
11-149 1.03e-33

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 117.46  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663854316   11 VDNEQLNLEdedIESIDATKLSRFIEINSLHMVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEYEENMHRYQKAAKLFQG 90
Cdd:pfam13848  50 FDEETVHYP---GDSINFEDLKKFIQKNCLPLVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRG 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 663854316   91 KILFILVDsgMKENGKVISFFKLKESQLPALAIYQTLDDEWDTLPTAEVSVEHVQNFCD 149
Cdd:pfam13848 127 KINFALVD--AKSFGRPLEYFGLSESDLPVIVIVDSFSHMYKYFPSDEFSPESLKEFIN 183
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 50-152 3.43e-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: 80.39  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663854316  50 TVIGLFNSVIQ--IHLLLIMNKASPEYEENMHRYQKAAKLFQGKILFILVDSgmKENGKVISFFKLKESQLPALAIYQTL 127
Cdd:cd02982    1 NAETFFNYEESgkPLLVLFYNKDDSESEELRERFKEVAKKFKGKLLFVVVDA--DDFGRHLEYFGLKEEDLPVIAIINLS 78

                         90       100
                 ....*....|....*....|....*
gi 663854316 128 DDEWDTLPTAEVSVEHVQNFCDGFL 152
Cdd:cd02982   79 DGKKYLMPEEELTAESLEEFVEDFL 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 27-156 1.50e-17

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: 78.95  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663854316   27 DATKLSRFIEINSLHMVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEYEENMHRYQKAAKLFQGKilFILVDSGMKE-NG 105
Cdd:TIGR01130 203 DVSDLEKFIRAESLPLVGEFTQETAAKYFESGPLVVLYYNVDESLDPFEELRNRFLEAAKKFRGK--FVNFAVADEEdFG 280

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 663854316  106 KVISFFKLKESQLPALAIYQTLDDEWDTLPTAEVSVEHVQNFCDGFLSGKL 156
Cdd:TIGR01130 281 RELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLDGKL 331
 
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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