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Conserved domains on  [gi|1179910175|ref|NP_001337444|]
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protein disulfide-isomerase TMX3 isoform 5 [Homo sapiens]

Protein Classification

PDI_b'_family domain-containing protein( domain architecture ID 12155891)

PDI_b'_family domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
19-197 1.84e-23

Thioredoxin-like domain;


:

Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 94.74  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175  19 ESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLKEmPAVLVFKDET----YFVYDEYEDGDLSSWINRERFQNYLAMD 94
Cdd:pfam13848   5 DSPLYEIFRKAAKELKGDVRFGITFSKEVADKYNIKE-PAILLFRKFDeetvHYPGDSINFEDLKKFIQKNCLPLVREFT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175  95 GFLLYELGDTGKLVALAVIDEKNtSVEHTRLKSIIQEVARDYRDLFHrdFQFGHMDGND-YINTLLMDELTVPTVVVLNT 173
Cdd:pfam13848  84 PENAEELFEEGIPPLLLLFLKKD-DESTEEFKKALEKVAKKFRGKIN--FALVDAKSFGrPLEYFGLSESDLPVIVIVDS 160

                         170       180
                  ....*....|....*....|....
gi 1179910175 174 SNQQYFLLDRQIKNVEDMVQFINN 197
Cdd:pfam13848 161 FSHMYKYFPSDEFSPESLKEFIND 184
 
Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
19-197 1.84e-23

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 94.74  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175  19 ESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLKEmPAVLVFKDET----YFVYDEYEDGDLSSWINRERFQNYLAMD 94
Cdd:pfam13848   5 DSPLYEIFRKAAKELKGDVRFGITFSKEVADKYNIKE-PAILLFRKFDeetvHYPGDSINFEDLKKFIQKNCLPLVREFT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175  95 GFLLYELGDTGKLVALAVIDEKNtSVEHTRLKSIIQEVARDYRDLFHrdFQFGHMDGND-YINTLLMDELTVPTVVVLNT 173
Cdd:pfam13848  84 PENAEELFEEGIPPLLLLFLKKD-DESTEEFKKALEKVAKKFRGKIN--FALVDAKSFGrPLEYFGLSESDLPVIVIVDS 160

                         170       180
                  ....*....|....*....|....
gi 1179910175 174 SNQQYFLLDRQIKNVEDMVQFINN 197
Cdd:pfam13848 161 FSHMYKYFPSDEFSPESLKEFIND 184
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 11-205 3.72e-07

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: 51.21  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175  11 VFFVYVGGESPLKEKYIDAASELIVYTYFFSAS--EEVVPEYVTLKEMPAVLVFKDE--TYFVYD---EYEDGDLSSWIN 83
Cdd:TIGR01130 133 VIGFFKDLDSELNDTFLSVAEKLRDVYFFFAHSsdVAAFAKLGAFPDSVVLFKPKDEdeKFSKVDgemDTDVSDLEKFIR 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175  84 RE--RFQNYLAMDGFLLYELGDTGKLVALAVIDEKNTSVEhtrLKSIIQEVARDYRDLFHRdFQFGHMDGNDYI-NTLLM 160
Cdd:TIGR01130 213 AEslPLVGEFTQETAAKYFESGPLVVLYYNVDESLDPFEE---LRNRFLEAAKKFRGKFVN-FAVADEEDFGRElEYFGL 288

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1179910175 161 DELTVPTVVVLNTSNQQYFLLDRQIKNVEDMVQFINNILDGTVEA 205
Cdd:TIGR01130 289 KAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLDGKLKP 333
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 116-199 2.44e-03

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: 36.87  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175 116 KNTSVEHTRLKSIIQEVARDYRDLFHrdfqFGHMDGNDY---INTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMV 192
Cdd:cd02982    21 NKDDSESEELRERFKEVAKKFKGKLL----FVVVDADDFgrhLEYFGLKEEDLPVIAIINLSDGKKYLMPEEELTAESLE 96


                  ....*..
gi 1179910175 193 QFINNIL 199
Cdd:cd02982    97 EFVEDFL 103
 
Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
19-197 1.84e-23

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 94.74  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175  19 ESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLKEmPAVLVFKDET----YFVYDEYEDGDLSSWINRERFQNYLAMD 94
Cdd:pfam13848   5 DSPLYEIFRKAAKELKGDVRFGITFSKEVADKYNIKE-PAILLFRKFDeetvHYPGDSINFEDLKKFIQKNCLPLVREFT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175  95 GFLLYELGDTGKLVALAVIDEKNtSVEHTRLKSIIQEVARDYRDLFHrdFQFGHMDGND-YINTLLMDELTVPTVVVLNT 173
Cdd:pfam13848  84 PENAEELFEEGIPPLLLLFLKKD-DESTEEFKKALEKVAKKFRGKIN--FALVDAKSFGrPLEYFGLSESDLPVIVIVDS 160

                         170       180
                  ....*....|....*....|....
gi 1179910175 174 SNQQYFLLDRQIKNVEDMVQFINN 197
Cdd:pfam13848 161 FSHMYKYFPSDEFSPESLKEFIND 184
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 11-205 3.72e-07

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: 51.21  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175  11 VFFVYVGGESPLKEKYIDAASELIVYTYFFSAS--EEVVPEYVTLKEMPAVLVFKDE--TYFVYD---EYEDGDLSSWIN 83
Cdd:TIGR01130 133 VIGFFKDLDSELNDTFLSVAEKLRDVYFFFAHSsdVAAFAKLGAFPDSVVLFKPKDEdeKFSKVDgemDTDVSDLEKFIR 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175  84 RE--RFQNYLAMDGFLLYELGDTGKLVALAVIDEKNTSVEhtrLKSIIQEVARDYRDLFHRdFQFGHMDGNDYI-NTLLM 160
Cdd:TIGR01130 213 AEslPLVGEFTQETAAKYFESGPLVVLYYNVDESLDPFEE---LRNRFLEAAKKFRGKFVN-FAVADEEDFGRElEYFGL 288

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1179910175 161 DELTVPTVVVLNTSNQQYFLLDRQIKNVEDMVQFINNILDGTVEA 205
Cdd:TIGR01130 289 KAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEAFVKDFLDGKLKP 333
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 116-199 2.44e-03

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: 36.87  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179910175 116 KNTSVEHTRLKSIIQEVARDYRDLFHrdfqFGHMDGNDY---INTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMV 192
Cdd:cd02982    21 NKDDSESEELRERFKEVAKKFKGKLL----FVVVDADDFgrhLEYFGLKEEDLPVIAIINLSDGKKYLMPEEELTAESLE 96


                  ....*..
gi 1179910175 193 QFINNIL 199
Cdd:cd02982    97 EFVEDFL 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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