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Conserved domains on  [gi|1734330106|ref|NP_001360604|]
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Thioredoxin domain-containing protein [Caenorhabditis elegans]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 21-126 1.63e-43

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd02996:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 108  Bit Score: 147.54  E-value: 1.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  21 CNLESITSTNHDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYPDR-KTVWGNVDCMAEDYLMNKYSITKFP 99
Cdd:cd02996     1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAgKVVWGKVDCDKESDIADRYRINKYP 80

                          90       100
                  ....*....|....*....|....*...
gi 1734330106 100 TMKVFFYGYMMT-EYRGSRQVKGLIEYI 126
Cdd:cd02996    81 TLKLFRNGMMMKrEYRGQRSVEALAEFV 108
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 235-345 1.96e-22

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03072:

Pssm-ID: 469754  Cd Length: 111  Bit Score: 91.30  E-value: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 235 VRELTFENMEEMVEDGKPLLILLRKKDDIETEKQFVTTIRREL-DQDTLLKlaPVMADGKVLTAVLRHFNKGLDDLPFLL 313
Cdd:cd03072     1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLiSEKGAIN--FLTADGDKFRHPLLHLGKTPADLPVIA 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1734330106 314 IDQFTHSFPSPwKGNEIFAEGNIKQFVADLFN 345
Cdd:cd03072    79 IDSFRHMYLFP-DFEDVYVPGKLKQFVLDLHS 109
 
Name Accession Description Interval E-value
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 21-126 1.63e-43

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 147.54  E-value: 1.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  21 CNLESITSTNHDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYPDR-KTVWGNVDCMAEDYLMNKYSITKFP 99
Cdd:cd02996     1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAgKVVWGKVDCDKESDIADRYRINKYP 80

                          90       100
                  ....*....|....*....|....*...
gi 1734330106 100 TMKVFFYGYMMT-EYRGSRQVKGLIEYI 126
Cdd:cd02996    81 TLKLFRNGMMMKrEYRGQRSVEALAEFV 108
PDI_b'_ERp44 cd03072
PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an ...
 235-345 1.96e-22

PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an endoplasmic reticulum (ER)-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. Through the formation of reversible mixed disulfides, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. ERp44 also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol. Similar to PDI, the b' domain of ERp44 is likely involved in substrate recognition and may be the primary binding site.


Pssm-ID: 239370  Cd Length: 111  Bit Score: 91.30  E-value: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 235 VRELTFENMEEMVEDGKPLLILLRKKDDIETEKQFVTTIRREL-DQDTLLKlaPVMADGKVLTAVLRHFNKGLDDLPFLL 313
Cdd:cd03072     1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLiSEKGAIN--FLTADGDKFRHPLLHLGKTPADLPVIA 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1734330106 314 IDQFTHSFPSPwKGNEIFAEGNIKQFVADLFN 345
Cdd:cd03072    79 IDSFRHMYLFP-DFEDVYVPGKLKQFVLDLHS 109
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
166-342 1.31e-21

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 91.27  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 166 SPPFELILKAIALIHSQLVVVVPISENLLKH----EDHQLWFSLDGEHVERFEGSVSNFKEIVEWIKKKSAGMVRELTFE 241
Cdd:pfam13848   6 SPLYEIFRKAAKELKGDVRFGITFSKEVADKynikEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLPLVREFTPE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 242 NMEEMVEDGKP-LLILLRKKDDIETE--KQFVTTIRRELdqdtLLKLAPVMADGKVLTAVLRHFNKGLDDLPFL-LIDQF 317
Cdd:pfam13848  86 NAEELFEEGIPpLLLLFLKKDDESTEefKKALEKVAKKF----RGKINFALVDAKSFGRPLEYFGLSESDLPVIvIVDSF 161

                         170       180
                  ....*....|....*....|....*
gi 1734330106 318 THSFPSPWKGneIFAEGNIKQFVAD 342
Cdd:pfam13848 162 SHMYKYFPSD--EFSPESLKEFIND 184
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 25-348 1.47e-12

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: 68.93  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  25 SITSTNHDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYPDRKTvwGNVDCMAEDYLMNKYSITKFPTMKVF 104
Cdd:TIGR01130   5 VLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKL--AKVDATEEKDLAQKYGVSGYPTLKIF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 105 FYG-YMMTEYRGSRQVKGLIEYIEKMENTSSlvnlNEAESLTQWQNYVIPQKGTLILWFPRGSPPF-------------- 169
Cdd:TIGR01130  83 RNGeDSVSDYNGPRDADGIVKYMKKQSGPAV----KEIETVADLEAFLADDDVVVIGFFKDLDSELndtflsvaeklrdv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 170 ---------ELILKAIALIHSQLVVVVPisenllKHEDHQLwFSLDGEhverfegSVSNFKEIVEWIKKKSAGMVRELTF 240
Cdd:TIGR01130 159 yfffahssdVAAFAKLGAFPDSVVLFKP------KDEDEKF-SKVDGE-------MDTDVSDLEKFIRAESLPLVGEFTQ 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 241 ENMEEMVEdGKPLLILLRKkddIETEKQFVTTIRreldqDTLLKLAPVMADGKVLTAV---------LRHFNKGLDDLPF 311
Cdd:TIGR01130 225 ETAAKYFE-SGPLVVLYYN---VDESLDPFEELR-----NRFLEAAKKFRGKFVNFAVadeedfgreLEYFGLKAEKFPA 295

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1734330106 312 LLIDQFTHSFPSPWKGNEIFAEgNIKQFVADLFNDNH 348
Cdd:TIGR01130 296 VAIQDLEGNKKYPMDQEEFSSE-NLEAFVKDFLDGKL 331
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 25-129 3.26e-12

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 67.85  E-value: 3.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  25 SITSTNHDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYPDrkTVWGNVDCMAEDYLMNKYSITKFPTMKvF 104
Cdd:PTZ00102   36 VLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSE--IVLASVDATEEMELAQEFGVRGYPTIK-F 112

                          90       100
                  ....*....|....*....|....*
gi 1734330106 105 FYGYMMTEYRGSRQVKGLIEYIEKM 129
Cdd:PTZ00102  113 FNKGNPVNYSGGRTADGIVSWIKKL 137
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 24-128 1.96e-08

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 51.85  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  24 ESITSTNHDEIIQN-SRLTFVAFTASWCPfSRKLMSSFSQAAADyqaKYPDRKTVwGNVDCMAEDYLMNKYSITKFPTMK 102
Cdd:pfam00085   3 VVLTDANFDEVVQKsSKPVLVDFYAPWCG-PCKMLAPEYEELAQ---EYKGNVVF-AKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|....*.
gi 1734330106 103 VFFYGYMMTEYRGSRQVKGLIEYIEK 128
Cdd:pfam00085  78 FFKNGQPVDDYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 22-128 3.00e-08

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 51.36  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  22 NLESITSTNHDE-IIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYpdrktVWGNVDCMAEDYLMNKYSITKFPT 100
Cdd:COG3118     1 AVVELTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKV-----KFVKVDVDENPELAAQFGVRSIPT 75

                          90       100
                  ....*....|....*....|....*...
gi 1734330106 101 MKVFFYGYMMTEYRGSRQVKGLIEYIEK 128
Cdd:COG3118    76 LLLFKDGQPVDRFVGALPKEQLREFLDK 103
 
Name Accession Description Interval E-value
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 21-126 1.63e-43

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 147.54  E-value: 1.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  21 CNLESITSTNHDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYPDR-KTVWGNVDCMAEDYLMNKYSITKFP 99
Cdd:cd02996     1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAgKVVWGKVDCDKESDIADRYRINKYP 80

                          90       100
                  ....*....|....*....|....*...
gi 1734330106 100 TMKVFFYGYMMT-EYRGSRQVKGLIEYI 126
Cdd:cd02996    81 TLKLFRNGMMMKrEYRGQRSVEALAEFV 108
PDI_b'_ERp44 cd03072
PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an ...
 235-345 1.96e-22

PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an endoplasmic reticulum (ER)-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. Through the formation of reversible mixed disulfides, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. ERp44 also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol. Similar to PDI, the b' domain of ERp44 is likely involved in substrate recognition and may be the primary binding site.


Pssm-ID: 239370  Cd Length: 111  Bit Score: 91.30  E-value: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 235 VRELTFENMEEMVEDGKPLLILLRKKDDIETEKQFVTTIRREL-DQDTLLKlaPVMADGKVLTAVLRHFNKGLDDLPFLL 313
Cdd:cd03072     1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLiSEKGAIN--FLTADGDKFRHPLLHLGKTPADLPVIA 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1734330106 314 IDQFTHSFPSPwKGNEIFAEGNIKQFVADLFN 345
Cdd:cd03072    79 IDSFRHMYLFP-DFEDVYVPGKLKQFVLDLHS 109
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
166-342 1.31e-21

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 91.27  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 166 SPPFELILKAIALIHSQLVVVVPISENLLKH----EDHQLWFSLDGEHVERFEGSVSNFKEIVEWIKKKSAGMVRELTFE 241
Cdd:pfam13848   6 SPLYEIFRKAAKELKGDVRFGITFSKEVADKynikEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLPLVREFTPE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 242 NMEEMVEDGKP-LLILLRKKDDIETE--KQFVTTIRRELdqdtLLKLAPVMADGKVLTAVLRHFNKGLDDLPFL-LIDQF 317
Cdd:pfam13848  86 NAEELFEEGIPpLLLLFLKKDDESTEefKKALEKVAKKF----RGKINFALVDAKSFGRPLEYFGLSESDLPVIvIVDSF 161

                         170       180
                  ....*....|....*....|....*
gi 1734330106 318 THSFPSPWKGneIFAEGNIKQFVAD 342
Cdd:pfam13848 162 SHMYKYFPSD--EFSPESLKEFIND 184
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 24-126 1.14e-20

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: 86.13  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  24 ESITSTNHDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQakyPDRKTVWGNVDCMAEDYLMNKYSITKFPTMKV 103
Cdd:cd02961     1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELK---GDGKVVVAKVDCTANNDLCSEYGVRGYPTIKL 77

                          90       100
                  ....*....|....*....|....
gi 1734330106 104 FFYGY-MMTEYRGSRQVKGLIEYI 126
Cdd:cd02961    78 FPNGSkEPVKYEGPRTLESLVEFI 101
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 26-126 7.50e-13

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 64.26  E-value: 7.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  26 ITSTNHDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAkypDRKTVWGNVDC--MAEDYLMNKYSITKFPTMKV 103
Cdd:cd02997     5 LTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKE---DGKGVLAAVDCtkPEHDALKEEYNVKGFPTFKY 81

                          90       100
                  ....*....|....*....|...
gi 1734330106 104 FFYGYMMTEYRGSRQVKGLIEYI 126
Cdd:cd02997    82 FENGKFVEKYEGERTAEDIIEFM 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 25-348 1.47e-12

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: 68.93  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  25 SITSTNHDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYPDRKTvwGNVDCMAEDYLMNKYSITKFPTMKVF 104
Cdd:TIGR01130   5 VLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKL--AKVDATEEKDLAQKYGVSGYPTLKIF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 105 FYG-YMMTEYRGSRQVKGLIEYIEKMENTSSlvnlNEAESLTQWQNYVIPQKGTLILWFPRGSPPF-------------- 169
Cdd:TIGR01130  83 RNGeDSVSDYNGPRDADGIVKYMKKQSGPAV----KEIETVADLEAFLADDDVVVIGFFKDLDSELndtflsvaeklrdv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 170 ---------ELILKAIALIHSQLVVVVPisenllKHEDHQLwFSLDGEhverfegSVSNFKEIVEWIKKKSAGMVRELTF 240
Cdd:TIGR01130 159 yfffahssdVAAFAKLGAFPDSVVLFKP------KDEDEKF-SKVDGE-------MDTDVSDLEKFIRAESLPLVGEFTQ 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 241 ENMEEMVEdGKPLLILLRKkddIETEKQFVTTIRreldqDTLLKLAPVMADGKVLTAV---------LRHFNKGLDDLPF 311
Cdd:TIGR01130 225 ETAAKYFE-SGPLVVLYYN---VDESLDPFEELR-----NRFLEAAKKFRGKFVNFAVadeedfgreLEYFGLKAEKFPA 295

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1734330106 312 LLIDQFTHSFPSPWKGNEIFAEgNIKQFVADLFNDNH 348
Cdd:TIGR01130 296 VAIQDLEGNKKYPMDQEEFSSE-NLEAFVKDFLDGKL 331
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 22-126 3.13e-12

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 62.65  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  22 NLESITSTNHDEIIQNSRL-TFVAFTASWCPFSRKLMSSFSQAAADYQAkypDRKTVWGNVDCMAEDY-LMNKYSITKFP 99
Cdd:cd02998     1 NVVELTDSNFDKVVGDDKKdVLVEFYAPWCGHCKNLAPEYEKLAAVFAN---EDDVVIAKVDADEANKdLAKKYGVSGFP 77

                          90       100
                  ....*....|....*....|....*...
gi 1734330106 100 TMKVFFYGYMMTE-YRGSRQVKGLIEYI 126
Cdd:cd02998    78 TLKFFPKGSTEPVkYEGGRDLEDLVKFV 105
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 25-129 3.26e-12

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 67.85  E-value: 3.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  25 SITSTNHDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYPDrkTVWGNVDCMAEDYLMNKYSITKFPTMKvF 104
Cdd:PTZ00102   36 VLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSE--IVLASVDATEEMELAQEFGVRGYPTIK-F 112

                          90       100
                  ....*....|....*....|....*
gi 1734330106 105 FYGYMMTEYRGSRQVKGLIEYIEKM 129
Cdd:PTZ00102  113 FNKGNPVNYSGGRTADGIVSWIKKL 137
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 27-126 2.76e-09

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 54.29  E-value: 2.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  27 TSTNHDEIIQNSR-LTFVAFTASWCPFSRKLMSSFSQAAADYqakypDRKTVWGNVDCmaeDYLMNK-----YSITKFPT 100
Cdd:cd03002     6 TPKNFDKVVHNTNyTTLVEFYAPWCGHCKNLKPEYAKAAKEL-----DGLVQVAAVDC---DEDKNKplcgkYGVQGFPT 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1734330106 101 MKVF-----FYGYMMTEYRGSRQVKGLIEYI 126
Cdd:cd03002    78 LKVFrppkkASKHAVEDYNGERSAKAIVDFV 108
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 25-126 4.17e-09

PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 53.44  E-value: 4.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  25 SITSTNHDEIIQNSrLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYPDRKTVwgNVDCMAEDYLMNKYSITKFPTMKVF 104
Cdd:cd03005     4 ELTEDNFDHHIAEG-NHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIA--KVDCTQHRELCSEFQVRGYPTLLLF 80

                          90       100
                  ....*....|....*....|..
gi 1734330106 105 FYGYMMTEYRGSRQVKGLIEYI 126
Cdd:cd03005    81 KDGEKVDKYKGTRDLDSLKEFV 102
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 24-128 1.96e-08

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 51.85  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  24 ESITSTNHDEIIQN-SRLTFVAFTASWCPfSRKLMSSFSQAAADyqaKYPDRKTVwGNVDCMAEDYLMNKYSITKFPTMK 102
Cdd:pfam00085   3 VVLTDANFDEVVQKsSKPVLVDFYAPWCG-PCKMLAPEYEELAQ---EYKGNVVF-AKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|....*.
gi 1734330106 103 VFFYGYMMTEYRGSRQVKGLIEYIEK 128
Cdd:pfam00085  78 FFKNGQPVDDYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 22-128 3.00e-08

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 51.36  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  22 NLESITSTNHDE-IIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYpdrktVWGNVDCMAEDYLMNKYSITKFPT 100
Cdd:COG3118     1 AVVELTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKV-----KFVKVDVDENPELAAQFGVRSIPT 75

                          90       100
                  ....*....|....*....|....*...
gi 1734330106 101 MKVFFYGYMMTEYRGSRQVKGLIEYIEK 128
Cdd:COG3118    76 LLLFKDGQPVDRFVGALPKEQLREFLDK 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 26-124 5.26e-08

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 50.36  E-value: 5.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  26 ITSTN-HDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYPdrktvWGNVDCMAEDYLMNKYSITKFPTMKVF 104
Cdd:cd03001     5 LTDSNfDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVK-----VGAVDADVHQSLAQQYGVRGFPTIKVF 79

                          90       100
                  ....*....|....*....|.
gi 1734330106 105 FYG-YMMTEYRGSRQVKGLIE 124
Cdd:cd03001    80 GAGkNSPQDYQGGRTAKAIVS 100
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 42-129 1.23e-06

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 46.68  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  42 FVAFTASWCPFSRKLMSSFSQAAADYQAKYPDRKTvwGNVDCMAEDYLMNKYSITKFPTMKvFFYGYMMTEYRGSRQVKG 121
Cdd:cd03000    19 LVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRV--GKLDATAYSSIASEFGVRGYPTIK-LLKGDLAYNYRGPRTKDD 95


                  ....*...
gi 1734330106 122 LIEYIEKM 129
Cdd:cd03000    96 IVEFANRV 103
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 32-127 1.69e-06

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 46.01  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  32 DEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQakypdrKTVWGNVDCMAEDYLMNKYSITKFPTMKVFFYGYMMT 111
Cdd:cd02947     4 EELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYP------KVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVD 77

                          90
                  ....*....|....*.
gi 1734330106 112 EYRGSRQVKGLIEYIE 127
Cdd:cd02947    78 RVVGADPKEELEEFLE 93
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 22-119 4.20e-06

PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -> dithiol of the QSOX TRX domain -> dithiols of the QSOX ERV1p domain -> FAD -> oxygen.


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 45.34  E-value: 4.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  22 NLESITSTNHDEIIQNSRLTFVA-FTASWCPFSRKLMSSFSQAAADYQAKYPDRKTvwGNVDCMAE--DYLMNKYSITKF 98
Cdd:cd02992     2 PVIVLDAASFNSALLGSPSAWLVeFYASWCGHCRAFAPTWKKLARDLRKWRPVVRV--AAVDCADEenVALCRDFGVTGY 79

                          90       100
                  ....*....|....*....|.
gi 1734330106  99 PTMKvFFYGYMMTEYRGSRQV 119
Cdd:cd02992    80 PTLR-YFPPFSKEATDGLKQE 99
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 23-126 1.05e-05

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 43.82  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  23 LESITSTN-HDEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAaadyqAKYPDRKTVWGNVDCMAEDYLMNKYSITKFPTM 101
Cdd:cd03004     3 VITLTPEDfPELVLNRKEPWLVDFYAPWCGPCQALLPELRKA-----ARALKGKVKVGSVDCQKYESLCQQANIRAYPTI 77

                          90       100
                  ....*....|....*....|....*..
gi 1734330106 102 KVFFYGYMMT-EYRG-SRQVKGLIEYI 126
Cdd:cd03004    78 RLYPGNASKYhSYNGwHRDADSILEFI 104
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 22-128 2.59e-05

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 42.75  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  22 NLESITSTNHDEIIQNSRLtfVAFTASWCPFSRKLMS---SFSQAAADYQAKYpdrktvwGNVDCMAEDYLMNKYSITKF 98
Cdd:cd02994     2 NVVELTDSNWTLVLEGEWM--IEFYAPWCPACQQLQPeweEFADWSDDLGINV-------AKVDVTQEPGLSGRFFVTAL 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1734330106  99 PTM-----KVFfygymmTEYRGSRQVKGLIEYIEK 128
Cdd:cd02994    73 PTIyhakdGVF------RRYQGPRDKEDLISFIEE 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 30-128 6.72e-05

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: 45.05  E-value: 6.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  30 NHDEII-QNSRLTFVAFTASWCPFSRKLMSSFSQAAADYQAKYPDrkTVWGNVDCMAEDylMNKYSITKFPTMKVFFYG- 107
Cdd:TIGR01130 355 NFDEIVlDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESD--VVIAKMDATAND--VPPFEVEGFPTIKFVPAGk 430

                          90       100
                  ....*....|....*....|..
gi 1734330106 108 -YMMTEYRGSRQVKGLIEYIEK 128
Cdd:TIGR01130 431 kSEPVPYDGDRTLEDFSKFIAK 452
PTZ00051 PTZ00051
thioredoxin; Provisional
 32-116 1.58e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 40.63  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  32 DEIIQNSRLTFVAFTASWCPFSRKLMSSFSQAAAdyqaKYPDRKTVWGNVDCMAEdyLMNKYSITKFPTMKVFFYGYMMT 111
Cdd:PTZ00051   12 ESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSK----EYTKMVFVKVDVDELSE--VAEKENITSMPTFKVFKNGSVVD 85


                  ....*
gi 1734330106 112 EYRGS 116
Cdd:PTZ00051   86 TLLGA 90
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
36-105 6.32e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 38.94  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106  36 QNSRLTFVAFTASWCPFSRKLMSSFSQaAADYQAKY-PDRKTVWGNVDCMAEDY-----------LMNKYSITKFPTMkV 103
Cdd:pfam13098   2 GNGKPVLVVFTDPDCPYCKKLKKELLE-DPDVTVYLgPNFVFIAVNIWCAKEVAkaftdilenkeLGRKYGVRGTPTI-V 79


                  ..
gi 1734330106 104 FF 105
Cdd:pfam13098  80 FF 81
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 239-344 1.27e-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: 38.02  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734330106 239 TFENMEEMVEDGKPLLILLRKKDDIETE--KQFVTTIRRELDQdtllKLAPVMADGKVLTAVLRHFNKGLDDLPFLLIDQ 316
Cdd:cd02982     1 NAETFFNYEESGKPLLVLFYNKDDSESEelRERFKEVAKKFKG----KLLFVVVDADDFGRHLEYFGLKEEDLPVIAIIN 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1734330106 317 FT--HSFpspWKGNEIFAEGNIKQFVADLF 344
Cdd:cd02982    77 LSdgKKY---LMPEEELTAESLEEFVEDFL 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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