NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|112293264|ref|NP_031978|]
View 

protein disulfide-isomerase A3 precursor [Mus musculus]

Protein Classification

protein disulfide isomerase family protein( domain architecture ID 1001536)

protein disulfide isomerase family protein may act as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ER_PDI_fam super family cl36828
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 26-487 7.56e-180

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).


The actual alignment was detected with superfamily member TIGR01130:

Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 512.68  E-value: 7.56e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264   26 DVLELTDENFESRVSdtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLK---GIVPLAKVDCTANTNTCNKYGVSGYPT 102
Cdd:TIGR01130   2 DVLVLTKDNFDDFIK---SHEFVLVEFYAPWCGHCKSLAPEYEKAADELKkkgPPIKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  103 LKIFRDGEEAGA-YDGPRTADGIVSHLKKQAGPASVPLRTEEEFKKFISDKDASVVGFFRDLFSDGHSEFLKAASNLRDN 181
Cdd:TIGR01130  79 LKIFRNGEDSVSdYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRDV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  182 YR-FAHTNIESLVKEYDDNGEGITIFRPLHLANKFEdktVAYTEKKMTSGKIKKFIQDSIFGLCPHMTEDNKDLIQGKDL 260
Cdd:TIGR01130 159 YFfFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFS---KVDGEMDTDVSDLEKFIRAESLPLVGEFTQETAAKYFESGP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  261 L-TAYYDVDYEKNAkgSNYWRNRVMMVAKKFldAGHKLNFAVASRKTFSHELSDFGLEstTGEVPVVAIRT-AKGEKFVM 338
Cdd:TIGR01130 236 LvVLYYNVDESLDP--FEELRNRFLEAAKKF--RGKFVNFAVADEEDFGRELEYFGLK--AEKFPAVAIQDlEGNKKYPM 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  339 -QEEFSRDgkALEQFLQEYFDGNLKRYLKSEPIPESNEGPVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYK 417
Cdd:TIGR01130 310 dQEEFSSE--NLEAFVKDFLDGKLKPYLKSEPIPEDDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYE 387

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112293264  418 ELGEKLSK-DPNIVIAKMDATANDVPsPYEVKGFPTIYFSPANKKLTPKKYEGGRELNDFISYLQREATNP 487
Cdd:TIGR01130 388 ELAEKYKDaESDVVIAKMDATANDVP-PFEVEGFPTIKFVPAGKKSEPVPYDGDRTLEDFSKFIAKHATFP 457
 
Name Accession Description Interval E-value
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 26-487 7.56e-180

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: 512.68  E-value: 7.56e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264   26 DVLELTDENFESRVSdtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLK---GIVPLAKVDCTANTNTCNKYGVSGYPT 102
Cdd:TIGR01130   2 DVLVLTKDNFDDFIK---SHEFVLVEFYAPWCGHCKSLAPEYEKAADELKkkgPPIKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  103 LKIFRDGEEAGA-YDGPRTADGIVSHLKKQAGPASVPLRTEEEFKKFISDKDASVVGFFRDLFSDGHSEFLKAASNLRDN 181
Cdd:TIGR01130  79 LKIFRNGEDSVSdYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRDV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  182 YR-FAHTNIESLVKEYDDNGEGITIFRPLHLANKFEdktVAYTEKKMTSGKIKKFIQDSIFGLCPHMTEDNKDLIQGKDL 260
Cdd:TIGR01130 159 YFfFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFS---KVDGEMDTDVSDLEKFIRAESLPLVGEFTQETAAKYFESGP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  261 L-TAYYDVDYEKNAkgSNYWRNRVMMVAKKFldAGHKLNFAVASRKTFSHELSDFGLEstTGEVPVVAIRT-AKGEKFVM 338
Cdd:TIGR01130 236 LvVLYYNVDESLDP--FEELRNRFLEAAKKF--RGKFVNFAVADEEDFGRELEYFGLK--AEKFPAVAIQDlEGNKKYPM 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  339 -QEEFSRDgkALEQFLQEYFDGNLKRYLKSEPIPESNEGPVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYK 417
Cdd:TIGR01130 310 dQEEFSSE--NLEAFVKDFLDGKLKPYLKSEPIPEDDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYE 387

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112293264  418 ELGEKLSK-DPNIVIAKMDATANDVPsPYEVKGFPTIYFSPANKKLTPKKYEGGRELNDFISYLQREATNP 487
Cdd:TIGR01130 388 ELAEKYKDaESDVVIAKMDATANDVP-PFEVEGFPTIKFVPAGKKSEPVPYDGDRTLEDFSKFIAKHATFP 457
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 26-487 8.10e-91

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 285.49  E-value: 8.10e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  26 DVLELTDENFESRVSDTGsagLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVP---LAKVDCTANTNTCNKYGVSGYPT 102
Cdd:PTZ00102  33 HVTVLTDSTFDKFITENE---IVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSeivLASVDATEEMELAQEFGVRGYPT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 103 LKIFRDGEEAGaYDGPRTADGIVSHLKKQAGPASVPLRTEEEFKkfiSDKDASVVGFFRDLF---SDGHSEFLKAASNLR 179
Cdd:PTZ00102 110 IKFFNKGNPVN-YSGGRTADGIVSWIKKLTGPAVTEVESASEIK---LIAKKIFVAFYGEYTskdSELYKKFEEVADKHR 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 180 DNYRFahtniesLVKeYDDNGEGITIFRplhlanKFEDKTVAYTEKkmTSGKIKKFIQDSIFGLCPHMTEDNKDLIQGKD 259
Cdd:PTZ00102 186 EHAKF-------FVK-KHEGKNKIYVLH------KDEEGVELFMGK--TKEELEEFVSTESFPLFAEINAENYRRYISSG 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 260 LLTAYYDVDYEKNAKgsnyWRNRVMMVAKKFLdagHKLNFA-VASRKTFSHELSDFGLEsttgEVPVVAIRTAKGeKFVM 338
Cdd:PTZ00102 250 KDLVWFCGTTEDYDK----YKSVVRKVARKLR---EKYAFVwLDTEQFGSHAKEHLLIE----EFPGLAYQSPAG-RYLL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 339 QEEFSR--DGKALEQFLQEYFDGNLKRYLKSEPIPESNEGPVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKY 416
Cdd:PTZ00102 318 PPAKESfdSVEALIEFFKDVEAGKVEKSIKSEPIPEEQDGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVY 397

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112293264 417 KELGEKLSKDPNIVIAKMDATANDVP-SPYEVKGFPTIYFSPANKKlTPKKYEGGRELNDFISYLQREATNP 487
Cdd:PTZ00102 398 NELGEKYKDNDSIIVAKMNGTANETPlEEFSWSAFPTILFVKAGER-TPIPYEGERTVEGFKEFVNKHATNP 468
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 377-480 5.09e-59

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are 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. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 190.07  E-value: 5.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 377 PVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVKGFPTIYFS 456
Cdd:cd02995    1 PVKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSEFVVDGFPTILFF 80

                         90       100
                 ....*....|....*....|....
gi 112293264 457 PANKKLTPKKYEGGRELNDFISYL 480
Cdd:cd02995   81 PAGDKSNPIKYEGDRTLEDLIKFI 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 27-130 1.14e-40

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: 141.60  E-value: 1.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264   27 VLELTDENFESRVSDtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIF 106
Cdd:pfam00085   2 VVVLTDANFDEVVQK--SSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF 79

                          90       100
                  ....*....|....*....|....
gi 112293264  107 RDGEEAGAYDGPRTADGIVSHLKK 130
Cdd:pfam00085  80 KNGQPVDDYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 27-130 2.98e-28

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: 107.98  E-value: 2.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFESRVSDtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIF 106
Cdd:COG3118    2 VVELTDENFEEEVLE--SDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                         90       100
                 ....*....|....*....|....
gi 112293264 107 RDGEEAGAYDGPRTADGIVSHLKK 130
Cdd:COG3118   80 KDGQPVDRFVGALPKEQLREFLDK 103
 
Name Accession Description Interval E-value
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 26-487 7.56e-180

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: 512.68  E-value: 7.56e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264   26 DVLELTDENFESRVSdtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLK---GIVPLAKVDCTANTNTCNKYGVSGYPT 102
Cdd:TIGR01130   2 DVLVLTKDNFDDFIK---SHEFVLVEFYAPWCGHCKSLAPEYEKAADELKkkgPPIKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  103 LKIFRDGEEAGA-YDGPRTADGIVSHLKKQAGPASVPLRTEEEFKKFISDKDASVVGFFRDLFSDGHSEFLKAASNLRDN 181
Cdd:TIGR01130  79 LKIFRNGEDSVSdYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRDV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  182 YR-FAHTNIESLVKEYDDNGEGITIFRPLHLANKFEdktVAYTEKKMTSGKIKKFIQDSIFGLCPHMTEDNKDLIQGKDL 260
Cdd:TIGR01130 159 YFfFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFS---KVDGEMDTDVSDLEKFIRAESLPLVGEFTQETAAKYFESGP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  261 L-TAYYDVDYEKNAkgSNYWRNRVMMVAKKFldAGHKLNFAVASRKTFSHELSDFGLEstTGEVPVVAIRT-AKGEKFVM 338
Cdd:TIGR01130 236 LvVLYYNVDESLDP--FEELRNRFLEAAKKF--RGKFVNFAVADEEDFGRELEYFGLK--AEKFPAVAIQDlEGNKKYPM 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  339 -QEEFSRDgkALEQFLQEYFDGNLKRYLKSEPIPESNEGPVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYK 417
Cdd:TIGR01130 310 dQEEFSSE--NLEAFVKDFLDGKLKPYLKSEPIPEDDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYE 387

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112293264  418 ELGEKLSK-DPNIVIAKMDATANDVPsPYEVKGFPTIYFSPANKKLTPKKYEGGRELNDFISYLQREATNP 487
Cdd:TIGR01130 388 ELAEKYKDaESDVVIAKMDATANDVP-PFEVEGFPTIKFVPAGKKSEPVPYDGDRTLEDFSKFIAKHATFP 457
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 26-487 8.10e-91

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 285.49  E-value: 8.10e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  26 DVLELTDENFESRVSDTGsagLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVP---LAKVDCTANTNTCNKYGVSGYPT 102
Cdd:PTZ00102  33 HVTVLTDSTFDKFITENE---IVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSeivLASVDATEEMELAQEFGVRGYPT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 103 LKIFRDGEEAGaYDGPRTADGIVSHLKKQAGPASVPLRTEEEFKkfiSDKDASVVGFFRDLF---SDGHSEFLKAASNLR 179
Cdd:PTZ00102 110 IKFFNKGNPVN-YSGGRTADGIVSWIKKLTGPAVTEVESASEIK---LIAKKIFVAFYGEYTskdSELYKKFEEVADKHR 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 180 DNYRFahtniesLVKeYDDNGEGITIFRplhlanKFEDKTVAYTEKkmTSGKIKKFIQDSIFGLCPHMTEDNKDLIQGKD 259
Cdd:PTZ00102 186 EHAKF-------FVK-KHEGKNKIYVLH------KDEEGVELFMGK--TKEELEEFVSTESFPLFAEINAENYRRYISSG 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 260 LLTAYYDVDYEKNAKgsnyWRNRVMMVAKKFLdagHKLNFA-VASRKTFSHELSDFGLEsttgEVPVVAIRTAKGeKFVM 338
Cdd:PTZ00102 250 KDLVWFCGTTEDYDK----YKSVVRKVARKLR---EKYAFVwLDTEQFGSHAKEHLLIE----EFPGLAYQSPAG-RYLL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 339 QEEFSR--DGKALEQFLQEYFDGNLKRYLKSEPIPESNEGPVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKY 416
Cdd:PTZ00102 318 PPAKESfdSVEALIEFFKDVEAGKVEKSIKSEPIPEEQDGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVY 397

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112293264 417 KELGEKLSKDPNIVIAKMDATANDVP-SPYEVKGFPTIYFSPANKKlTPKKYEGGRELNDFISYLQREATNP 487
Cdd:PTZ00102 398 NELGEKYKDNDSIIVAKMNGTANETPlEEFSWSAFPTILFVKAGER-TPIPYEGERTVEGFKEFVNKHATNP 468
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 377-480 5.09e-59

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are 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. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 190.07  E-value: 5.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 377 PVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVKGFPTIYFS 456
Cdd:cd02995    1 PVKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSEFVVDGFPTILFF 80

                         90       100
                 ....*....|....*....|....
gi 112293264 457 PANKKLTPKKYEGGRELNDFISYL 480
Cdd:cd02995   81 PAGDKSNPIKYEGDRTLEDLIKFI 104
PDI_b'_ERp72_ERp57 cd03073
PDIb' family, ERp72 and ERp57 subfamily, second redox inactive TRX-like domain b'; ERp72 and ...
 244-357 1.00e-54

PDIb' family, ERp72 and ERp57 subfamily, second redox inactive TRX-like domain b'; ERp72 and ER57 are involved in oxidative protein folding in the ER, like PDI. They exhibit both disulfide oxidase and reductase functions, by catalyzing the formation of disulfide bonds of newly synthesized polypeptides and acting as isomerases to correct any non-native disulfide bonds. They also display 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. ERp72 contains one additional redox-active TRX (a) domain at the N-terminus with a molecular structure of a"abb'a'. ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. The b' domain of ERp57 is the primary binding site and is adapted for ER lectin association. Similarly, the b' domain of ERp72 is likely involved in substrate recognition.


Pssm-ID: 239371  Cd Length: 111  Bit Score: 179.07  E-value: 1.00e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 244 CPHMTEDNKDLIQGKDLLTAYYDVDYEKNAKGSNYWRNRVMMVAKKFLDagHKLNFAVASRKTFSHELSDFGLESTTGEV 323
Cdd:cd03073    1 VGHRTKDNRAQFTKKPLVVAYYNVDYSKNPKGTNYWRNRVLKVAKDFPD--RKLNFAVADKEDFSHELEEFGLDFSGGEK 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 112293264 324 PVVAIRTAKGEKFVMQEEFSrDGKALEQFLQEYF 357
Cdd:cd03073   79 PVVAIRTAKGKKYVMEEEFS-DVDALEEFLEDFF 111
PDI_b_ERp57 cd03069
PDIb family, ERp57 subfamily, first redox inactive TRX-like domain b; ERp57 (or ERp60) ...
 135-240 7.53e-44

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: 150.17  E-value: 7.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 135 ASVPLRTEEEFKKFISDKDASVVGFFRDLFSDGHSEFLKAASNLRDNYRFAHTNIESLVKEYDDnGEGITIFRPLHLANK 214
Cdd:cd03069    1 ASVELRTEAEFEKFLSDDDASVVGFFEDEDSKLLSEFLKAADTLRESFRFAHTSDKQLLEKYGY-GEGVVLFRPPRLSNK 79

                         90       100
                 ....*....|....*....|....*.
gi 112293264 215 FEDKTVAYTEKKMtSGKIKKFIQDSI 240
Cdd:cd03069   80 FEDSSVKFDGDLD-SSKIKKFIRENI 104
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 381-484 1.31e-42

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 146.66  E-value: 1.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  381 VVAENFDDIVNEeDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVP-SPYEVKGFPTIYFSPAN 459
Cdd:TIGR01126   1 LTASNFDEIVLS-NKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDPKIVLAKVDATAEKDLaSRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|....*
gi 112293264  460 KKltPKKYEGGRELNDFISYLQREA 484
Cdd:TIGR01126  80 SK--PVDYEGGRDLEAIVEFVNEKS 102
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 26-126 1.21e-41

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: 144.35  E-value: 1.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  26 DVLELTDENFESRVSDtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKI 105
Cdd:cd03001    1 DVVELTDSNFDKKVLN--SDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKV 78

                         90       100
                 ....*....|....*....|..
gi 112293264 106 FRDG-EEAGAYDGPRTADGIVS 126
Cdd:cd03001   79 FGAGkNSPQDYQGGRTAKAIVS 100
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 27-130 1.14e-40

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: 141.60  E-value: 1.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264   27 VLELTDENFESRVSDtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIF 106
Cdd:pfam00085   2 VVVLTDANFDEVVQK--SSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF 79

                          90       100
                  ....*....|....*....|....
gi 112293264  107 RDGEEAGAYDGPRTADGIVSHLKK 130
Cdd:pfam00085  80 KNGQPVDDYVGARPKDALAAFLKA 103
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 30-132 2.57e-40

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 140.89  E-value: 2.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264   30 LTDENFESRVsdtGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGI--VPLAKVDCTANTNTCNKYGVSGYPTLKIFR 107
Cdd:TIGR01126   1 LTASNFDEIV---LSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDpkIVLAKVDATAEKDLASRFGVSGFPTIKFFP 77

                          90       100
                  ....*....|....*....|....*
gi 112293264  108 DGEEAGAYDGPRTADGIVSHLKKQA 132
Cdd:TIGR01126  78 KGSKPVDYEGGRDLEAIVEFVNEKS 102
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 379-480 1.16e-38

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: 136.20  E-value: 1.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 379 KVVVAENFDDIVNEEdKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATAN-DVPSPYEVKGFPTIYFSP 457
Cdd:cd02961    1 VELTDDNFDELVKDS-KDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANnDLCSEYGVRGYPTIKLFP 79

                         90       100
                 ....*....|....*....|...
gi 112293264 458 ANKKlTPKKYEGGRELNDFISYL 480
Cdd:cd02961   80 NGSK-EPVKYEGPRTLESLVEFI 101
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 378-480 2.37e-38

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: 135.46  E-value: 2.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 378 VKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATAN--DVPSPYEVKGFPTIYF 455
Cdd:cd02998    2 VVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEAnkDLAKKYGVSGFPTLKF 81

                         90       100
                 ....*....|....*....|....*
gi 112293264 456 SPANKKlTPKKYEGGRELNDFISYL 480
Cdd:cd02998   82 FPKGST-EPVKYEGGRDLEDLVKFV 105
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 28-128 1.79e-37

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: 133.12  E-value: 1.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  28 LELTDENFESRVSDTGsagLMLVEFFAPWCGHCKRLAPEYEAAATRLK--GIVPLAKVDCTANTNTCNKYGVSGYPTLKI 105
Cdd:cd02961    1 VELTDDNFDELVKDSK---DVLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKL 77

                         90       100
                 ....*....|....*....|....
gi 112293264 106 FRDGEEAGA-YDGPRTADGIVSHL 128
Cdd:cd02961   78 FPNGSKEPVkYEGPRTLESLVEFI 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 377-482 1.56e-34

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: 125.04  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  377 PVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKdpNIVIAKMDATAN-DVPSPYEVKGFPTIYF 455
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKG--NVVFAKVDVDENpDLASKYGVRGYPTLIF 78

                          90       100
                  ....*....|....*....|....*..
gi 112293264  456 SPANKKltPKKYEGGRELNDFISYLQR 482
Cdd:pfam00085  79 FKNGQP--VDDYVGARPKDALAAFLKA 103
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 27-126 2.10e-34

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: 125.17  E-value: 2.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFESRVSDTGSAglMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTN--TCNKYGVSGYPTLK 104
Cdd:cd03002    2 VYELTPKNFDKVVHNTNYT--TLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKNkpLCGKYGVQGFPTLK 79

                         90       100
                 ....*....|....*....|....*..
gi 112293264 105 IFRDGEEAGA-----YDGPRTADGIVS 126
Cdd:cd03002   80 VFRPPKKASKhavedYNGERSAKAIVD 106
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 27-122 6.58e-32

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: 118.16  E-value: 6.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFEsrvsDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGI---VPLAKVDCTANTNTCNKYGVSGYPTL 103
Cdd:cd03005    2 VLELTEDNFD----HHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNEnpsVKIAKVDCTQHRELCSEFQVRGYPTL 77

                         90
                 ....*....|....*....
gi 112293264 104 KIFRDGEEAGAYDGPRTAD 122
Cdd:cd03005   78 LLFKDGEKVDKYKGTRDLD 96
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 26-126 8.14e-31

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: 115.04  E-value: 8.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  26 DVLELTDENFESRVSDTGSAglMLVEFFAPWCGHCKRLAPEYEAAATRLKG--IVPLAKVDCT-ANTNTCNKYGVSGYPT 102
Cdd:cd02998    1 NVVELTDSNFDKVVGDDKKD--VLVEFYAPWCGHCKNLAPEYEKLAAVFANedDVVIAKVDADeANKDLAKKYGVSGFPT 78

                         90       100
                 ....*....|....*....|....*
gi 112293264 103 LKIFRDGEEAG-AYDGPRTADGIVS 126
Cdd:cd02998   79 LKFFPKGSTEPvKYEGGRDLEDLVK 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 27-130 2.98e-28

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: 107.98  E-value: 2.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFESRVSDtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIF 106
Cdd:COG3118    2 VVELTDENFEEEVLE--SDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                         90       100
                 ....*....|....*....|....
gi 112293264 107 RDGEEAGAYDGPRTADGIVSHLKK 130
Cdd:COG3118   80 KDGQPVDRFVGALPKEQLREFLDK 103
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 26-128 9.93e-28

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: 106.63  E-value: 9.93e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  26 DVLELTDENFESRVSDTGSaglMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVP--LAKVDCT--ANTNTCNKYGVSGYP 101
Cdd:cd02997    1 DVVHLTDEDFRKFLKKEKH---VLVMFYAPWCGHCKKMKPEFTKAATELKEDGKgvLAAVDCTkpEHDALKEEYNVKGFP 77

                         90       100
                 ....*....|....*....|....*..
gi 112293264 102 TLKIFRDGEEAGAYDGPRTADGIVSHL 128
Cdd:cd02997   78 TFKYFENGKFVEKYEGERTAEDIIEFM 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 27-106 6.50e-25

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: 98.90  E-value: 6.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFESRVSDtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIF 106
Cdd:cd03004    3 VITLTPEDFPELVLN--RKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 377-478 1.32e-24

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: 97.74  E-value: 1.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 377 PVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSkdpNIV-IAKMDATAND-VPSPYEVKGFPTIY 454
Cdd:cd03001    1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALK---GIVkVGAVDADVHQsLAQQYGVRGFPTIK 77

                         90       100
                 ....*....|....*....|....
gi 112293264 455 FSPANKKlTPKKYEGGRELNDFIS 478
Cdd:cd03001   78 VFGAGKN-SPQDYQGGRTAKAIVS 100
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 378-480 1.47e-23

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: 95.04  E-value: 1.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 378 VKVVVAENFDDIVNEedKDVLIEFYAPWCGHCKNLEPKYKELGEKL-SKDPNIVIAKMDATA-NDVPSPYEVKGFPTIYF 455
Cdd:cd03005    2 VLELTEDNFDHHIAE--GNHFVKFFAPWCGHCKRLAPTWEQLAKKFnNENPSVKIAKVDCTQhRELCSEFQVRGYPTLLL 79

                         90       100
                 ....*....|....*....|....*
gi 112293264 456 SPANKKltPKKYEGGRELNDFISYL 480
Cdd:cd03005   80 FKDGEK--VDKYKGTRDLDSLKEFV 102
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
164-355 1.09e-22

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 95.12  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  164 FSDGHSE----FLKAASNLRDNYRFAHTNIESLVKEYDDNGEGITIFRplhlanKFEDKTVAYTEKKMTSGKIKKFIQDS 239
Cdd:pfam13848   1 FEDKDSPlyeiFRKAAKELKGDVRFGITFSKEVADKYNIKEPAILLFR------KFDEETVHYPGDSINFEDLKKFIQKN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  240 IFGLCPHMTEDNKDLIQGKDLLTAYYdVDYEKNAKGSNYWRNRVMMVAKKFLDaghKLNFAVASRKTFSHELSDFGLesT 319
Cdd:pfam13848  75 CLPLVREFTPENAEELFEEGIPPLLL-LFLKKDDESTEEFKKALEKVAKKFRG---KINFALVDAKSFGRPLEYFGL--S 148

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 112293264  320 TGEVPVVAIR-TAKGEKFVMQEEFSRDGKaLEQFLQE 355
Cdd:pfam13848 149 ESDLPVIVIVdSFSHMYKYFPSDEFSPES-LKEFIND 184
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 27-132 4.52e-22

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: 90.98  E-value: 4.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFESRVSDtgsagLMLVEFFAPWCGHCKRLAPEYEAAATRLKGI---VPLAKVDCTANTNTCNKYGVSGYPTL 103
Cdd:cd03000    2 VLDLDDSFKDVRKED-----IWLVDFYAPWCGHCKKLEPVWNEVGAELKSSgspVRVGKLDATAYSSIASEFGVRGYPTI 76

                         90       100
                 ....*....|....*....|....*....
gi 112293264 104 KIFRdGEEAGAYDGPRTADGIVSHLKKQA 132
Cdd:cd03000   77 KLLK-GDLAYNYRGPRTKDDIVEFANRVA 104
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 27-125 3.46e-21

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are 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. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 88.38  E-value: 3.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFESRVSDTGSAglMLVEFFAPWCGHCKRLAPEYEAAATRLKGI--VPLAKVDCTANtNTCNKYGVSGYPTLK 104
Cdd:cd02995    2 VKVVVGKNFDEVVLDSDKD--VLVEFYAPWCGHCKALAPIYEELAEKLKGDdnVVIAKMDATAN-DVPSEFVVDGFPTIL 78

                         90       100
                 ....*....|....*....|...
gi 112293264 105 IF--RDGEEAGAYDGPRTADGIV 125
Cdd:cd02995   79 FFpaGDKSNPIKYEGDRTLEDLI 101
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 381-480 1.32e-20

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: 86.60  E-value: 1.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 381 VVAENFDDIVNEEdKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATAND---VPSPYEVKGFPTI-YFS 456
Cdd:cd02997    5 LTDEDFRKFLKKE-KHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAAVDCTKPEhdaLKEEYNVKGFPTFkYFE 83

                         90       100
                 ....*....|....*....|....
gi 112293264 457 panKKLTPKKYEGGRELNDFISYL 480
Cdd:cd02997   84 ---NGKFVEKYEGERTAEDIIEFM 104
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 27-173 1.63e-20

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 90.07  E-value: 1.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFE--SRVSDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLK 104
Cdd:PTZ00443  32 LVLLNDKNFEklTQASTGATTGPWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLL 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112293264 105 IFRDGEEAGAYDGPRTADGI----VSHLKKQAG-PASVPLrteeefkkfisdkdaSVVGFFRDLFSDGHSEFLK 173
Cdd:PTZ00443 112 LFDKGKMYQYEGGDRSTEKLaafaLGDFKKALGaPVPAPL---------------SFFALTIDFFVSGTNEALR 170
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 33-129 1.69e-20

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: 86.07  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  33 ENFESRVSdtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRlKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEA 112
Cdd:cd02947    1 EEFEELIK---SAKPVVVDFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEV 76

                         90
                 ....*....|....*..
gi 112293264 113 GAYDGPRTADGIVSHLK 129
Cdd:cd02947   77 DRVVGADPKEELEEFLE 93
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 27-107 2.26e-20

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: 86.17  E-value: 2.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFESRVSDTGSAglMLVEFFAPWCGHCKRLAPEYEAAATRLK---GIVPLAKVDCTANTN--TCNKYGVSGYP 101
Cdd:cd02992    3 VIVLDAASFNSALLGSPSA--WLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDCADEENvaLCRDFGVTGYP 80


                 ....*.
gi 112293264 102 TLKIFR 107
Cdd:cd02992   81 TLRYFP 86
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 136-238 2.33e-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, 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: 85.85  E-value: 2.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 136 SVPLRTEEEFKKFISDKDASVVGFFRDLFSDGHSEFLKAASNLRDNYRFAHTNIESLVKEYDDNGEGITIFRPlhlankF 215
Cdd:cd02981    1 VKELTSKEELEKFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRDDYGFGHTSDKEVAKKLKVKPGSVVLFKP------F 74

                         90       100
                 ....*....|....*....|...
gi 112293264 216 EDKTVAYTEkKMTSGKIKKFIQD 238
Cdd:cd02981   75 EEEPVEYDG-EFTEESLVEFIKD 96
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 377-479 1.42e-19

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: 83.95  E-value: 1.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 377 PVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATAN-DVPSPYEVKGFPTI-Y 454
Cdd:cd03002    1 PVYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKNkPLCGKYGVQGFPTLkV 80

                         90       100
                 ....*....|....*....|....*..
gi 112293264 455 FSPANK--KLTPKKYEGGRELNDFISY 479
Cdd:cd03002   81 FRPPKKasKHAVEDYNGERSAKAIVDF 107
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 30-111 1.47e-19

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 83.49  E-value: 1.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264   30 LTDENFESRVSDtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDG 109
Cdd:TIGR01068   1 LTDANFDETIAS--SDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNG 78


                  ..
gi 112293264  110 EE 111
Cdd:TIGR01068  79 KE 80
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 246-357 1.58e-18

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: 80.78  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 246 HMTEDNKDlIQGKDLLTAYYDVDYEknakGSNYWRNRVMMVAKKFLDaghKLNFAVASRKTFSHELSDFGLESTtgEVPV 325
Cdd:cd02982    2 AETFFNYE-ESGKPLLVLFYNKDDS----ESEELRERFKEVAKKFKG---KLLFVVVDADDFGRHLEYFGLKEE--DLPV 71

                         90       100       110
                 ....*....|....*....|....*....|...
gi 112293264 326 VAI-RTAKGEKFVMQEEFsRDGKALEQFLQEYF 357
Cdd:cd02982   72 IAIiNLSDGKKYLMPEEE-LTAESLEEFVEDFL 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 378-484 3.91e-18

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: 79.86  E-value: 3.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 378 VKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLskDPNIVIAKMDATAN-DVPSPYEVKGFPTIYFs 456
Cdd:COG3118    2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY--GGKVKFVKVDVDENpELAAQFGVRSIPTLLL- 78

                         90       100
                 ....*....|....*....|....*...
gi 112293264 457 pankkltpkkYEGGRELNDFISYLQREA 484
Cdd:COG3118   79 ----------FKDGQPVDRFVGALPKEQ 96
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 384-484 3.69e-17

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: 77.11  E-value: 3.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 384 ENFDD--IVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSK-DPNIVIAKMDATA-NDVPSPYEVKGFPTIYFSPAN 459
Cdd:cd03000    3 LDLDDsfKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSsGSPVRVGKLDATAySSIASEFGVRGYPTIKLLKGD 82

                         90       100
                 ....*....|....*....|....*
gi 112293264 460 KKLTpkkYEGGRELNDFISYLQREA 484
Cdd:cd03000   83 LAYN---YRGPRTKDDIVEFANRVA 104
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 26-124 4.54e-16

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: 73.96  E-value: 4.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  26 DVLELTDENFESRVsdtGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLK------GIVPLAKVDCTANTNTCNKYGVSG 99
Cdd:cd02996    2 EIVSLTSGNIDDIL---QSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKeefpdaGKVVWGKVDCDKESDIADRYRINK 78

                         90       100
                 ....*....|....*....|....*.
gi 112293264 100 YPTLKIFRDGEEAGA-YDGPRTADGI 124
Cdd:cd02996   79 YPTLKLFRNGMMMKReYRGQRSVEAL 104
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 376-480 1.34e-15

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: 72.41  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 376 GPVKVVVAENFDDIVNEEdkdVLIEFYAPWCGHCKNLEPKYKELGEKlSKDPNIVIAKMDATANDVPS-PYEVKGFPTIY 454
Cdd:cd02994    1 SNVVELTDSNWTLVLEGE---WMIEFYAPWCPACQQLQPEWEEFADW-SDDLGINVAKVDVTQEPGLSgRFFVTALPTIY 76

                         90       100
                 ....*....|....*....|....*.
gi 112293264 455 FSpanKKLTPKKYEGGRELNDFISYL 480
Cdd:cd02994   77 HA---KDGVFRRYQGPRDKEDLISFI 99
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 377-482 2.05e-15

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: 72.30  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 377 PVKVVVAENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIV-IAKMDATA---NDVPSPYEVKGFPT 452
Cdd:cd02992    2 PVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVrVAAVDCADeenVALCRDFGVTGYPT 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 112293264 453 IYFSPANKKLTP--KKYEG-GRELNDFISYLQR 482
Cdd:cd02992   82 LRYFPPFSKEATdgLKQEGpERDVNELREALIL 114
trxA PRK09381
thioredoxin TrxA;
27-117 2.96e-15

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 71.63  E-value: 2.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFESRVsdTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIF 106
Cdd:PRK09381   5 IIHLTDDSFDTDV--LKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF 82

                         90
                 ....*....|.
gi 112293264 107 RDGEEAGAYDG 117
Cdd:PRK09381  83 KNGEVAATKVG 93
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 383-455 1.02e-14

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 70.01  E-value: 1.02e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112293264  383 AENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDpnIVIAKMDATAN-DVPSPYEVKGFPTIYF 455
Cdd:TIGR01068   3 DANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGK--VKFVKLNVDENpDIAAKYGIRSIPTLLL 74
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 384-484 1.82e-14

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: 68.74  E-value: 1.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 384 ENFDDIVnEEDKDVLIEFYAPWCGHCKNLEPKYKELGEklsKDPNIVIAKMDATAN-DVPSPYEVKGFPTIYFspankkl 462
Cdd:cd02947    1 EEFEELI-KSAKPVVVDFWAPWCGPCKAIAPVLEELAE---EYPKVKFVKVDVDENpELAEEYGVRSIPTFLF------- 69

                         90       100
                 ....*....|....*....|..
gi 112293264 463 tpkkYEGGRELNDFISYLQREA 484
Cdd:cd02947   70 ----FKNGKEVDRVVGADPKEE 87
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 34-143 1.07e-12

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 70.16  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  34 NFESRVSDTGSAglMLVEFFAPWCGHCKRLAPEYEAAATRLK--GIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEE 111
Cdd:PTZ00102 366 TFEEIVFKSDKD--VLLEIYAPWCGHCKNLEPVYNELGEKYKdnDSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGER 443

                         90       100       110
                 ....*....|....*....|....*....|...
gi 112293264 112 -AGAYDGPRTADGIVSHLKKQAGPASVPLRTEE 143
Cdd:PTZ00102 444 tPIPYEGERTVEGFKEFVNKHATNPFEDDTHEE 476
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 26-126 1.56e-12

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 63.70  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  26 DVLELTDENFESRVSdtgSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKI 105
Cdd:cd03003    2 EIVTLDRGDFDAAVN---SGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYV 78

                         90       100
                 ....*....|....*....|.
gi 112293264 106 FRDGEEAGAYDGPRTADGIVS 126
Cdd:cd03003   79 FPSGMNPEKYYGDRSKESLVK 99
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 394-471 2.83e-12

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 63.24  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 394 DKDVLIEFYAPWCGHCKNLEPKYKELGEKLSkDPNIVIAKMDATANDVPSPYE---VKGFPTIYFSPANKKlTPKKYEGG 470
Cdd:cd02993   21 NQSTLVVLYAPWCPFCQAMEASYEELAEKLA-GSNVKVAKFNADGEQREFAKEelqLKSFPTILFFPKNSR-QPIKYPSE 98


                 .
gi 112293264 471 R 471
Cdd:cd02993   99 Q 99
PTZ00051 PTZ00051
thioredoxin; Provisional
 31-117 6.39e-12

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 61.82  E-value: 6.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  31 TDENFESRVSDTGsagLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVpLAKVDCTANTNTCNKYGVSGYPTLKIFRDGE 110
Cdd:PTZ00051   7 SQAEFESTLSQNE---LVIVDFYAEWCGPCKRIAPFYEECSKEYTKMV-FVKVDVDELSEVAEKENITSMPTFKVFKNGS 82


                 ....*..
gi 112293264 111 EAGAYDG 117
Cdd:PTZ00051  83 VVDTLLG 89
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 26-130 9.11e-12

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: 61.63  E-value: 9.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  26 DVLELTDENFeSRVSDtgsaGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGI-VPLAKVDCTANTNTCNKYGVSGYPTLK 104
Cdd:cd02994    2 NVVELTDSNW-TLVLE----GEWMIEFYAPWCPACQQLQPEWEEFADWSDDLgINVAKVDVTQEPGLSGRFFVTALPTIY 76

                         90       100
                 ....*....|....*....|....*.
gi 112293264 105 IFRDGeEAGAYDGPRTADGIVSHLKK 130
Cdd:cd02994   77 HAKDG-VFRRYQGPRDKEDLISFIEE 101
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 384-469 1.62e-11

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: 60.77  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 384 ENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLskDPNIVIAKMDATA-NDVPSPYEVKGFPTIYFSPANKKl 462
Cdd:cd03004    9 EDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARAL--KGKVKVGSVDCQKyESLCQQANIRAYPTIRLYPGNAS- 85


                 ....*..
gi 112293264 463 TPKKYEG 469
Cdd:cd03004   86 KYHSYNG 92
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 49-110 4.21e-10

Thioredoxin (TRX) superfamily; 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 TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 55.78  E-value: 4.21e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112293264  49 LVEFFAPWCGHCKRLAPEYEAAATRLKGiVPLAKVDCTANTNTCN---KYGVSGYPTLKIFRDGE 110
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKG-VKFEAVDVDEDPALEKelkRYGVGGVPTLVVFGPGI 64
PRK10996 PRK10996
thioredoxin 2; Provisional
 26-110 4.35e-10

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 57.77  E-value: 4.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  26 DVLELTDENFESRVSDTGSaglMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKI 105
Cdd:PRK10996  36 EVINATGETLDKLLQDDLP---VVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMI 112


                 ....*
gi 112293264 106 FRDGE 110
Cdd:PRK10996 113 FKNGQ 117
PDI_b_ERp72 cd03068
PDIb family, ERp72 subfamily, first redox inactive TRX-like domain b; ERp72 exhibits both ...
 135-236 9.63e-10

PDIb family, ERp72 subfamily, first redox inactive TRX-like domain b; ERp72 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. ERp72 contains three redox-active TRX (a) domains and two redox inactive TRX-like (b) domains. Its molecular structure is a"abb'a', compared to the abb'a' structure of PDI. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. Similar to PDI, the b domain of ERp72 is likely involved in binding to substrates.


Pssm-ID: 239366  Cd Length: 107  Bit Score: 55.95  E-value: 9.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 135 ASVPLRTEEEFKKFISD-KDASVVGFFRDLFSDGHSEFLKAASNLRDNYRFAHTNIESLVKEYDDNGEGITIFRPLHLAN 213
Cdd:cd03068    1 PSKQLQTLKQVQEFLRDgDDVIIIGVFSGEEDPAYQLYQDAANSLREDYKFHHTFDSEIFKSLKVSPGQLVVFQPEKFQS 80

                         90       100
                 ....*....|....*....|....
gi 112293264 214 KFEDKTVAYTEKKMTS-GKIKKFI 236
Cdd:cd03068   81 KYEPKSHVLNKKDSTSeDELKDFF 104
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 28-130 2.93e-09

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 55.47  E-value: 2.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  28 LELTDENFESRVSDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIV---------------PLAKVDCT------ 86
Cdd:COG0526   11 FTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVfvgvdvdenpeavkaFLKELGLPypvlld 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 112293264  87 ANTNTCNKYGVSGYPTLKIF-RDGEEAGAYDGPRTADGIVSHLKK 130
Cdd:COG0526   91 PDGELAKAYGVRGIPTTVLIdKDGKIVARHVGPLSPEELEEALEK 135
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 398-491 1.79e-08

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 55.02  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 398 LIEFYAPWCGHCKNLEPKYKELGEKLSKDPNivIAKMDATAN-DVPSPYEVKGFPTIYFSPANKKLtpkKYEGG----RE 472
Cdd:PTZ00443  56 FVKFYAPWCSHCRKMAPAWERLAKALKGQVN--VADLDATRAlNLAKRFAIKGYPTLLLFDKGKMY---QYEGGdrstEK 130

                         90
                 ....*....|....*....
gi 112293264 473 LNDFISYLQREATNPPIIQ 491
Cdd:PTZ00443 131 LAAFALGDFKKALGAPVPA 149
PTZ00051 PTZ00051
thioredoxin; Provisional
 377-452 2.27e-08

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 51.80  E-value: 2.27e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112293264 377 PVKVVVA-ENFDDIVnEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLskdPNIVIAKMDA-TANDVPSPYEVKGFPT 452
Cdd:PTZ00051   1 MVHIVTSqAEFESTL-SQNELVIVDFYAEWCGPCKRIAPFYEECSKEY---TKMVFVKVDVdELSEVAEKENITSMPT 74
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 27-128 2.75e-08

PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase (ThOX), also called Duox. ThOX proteins are responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. EFP1 was isolated through a yeast two-hybrid method using the EF-hand fragment of dog Duox1 as a bait. It could be one of the partners in the assembly of a multiprotein complex constituting the thyroid hydrogen peroxide generating system. EFP1 contains two TRX domains related to the redox active TRX domains of protein disulfide isomerase (PDI). This subfamily is composed of the N-terminal TRX domain of EFP1, which contains a CXXS sequence in place of the typical CXXC motif, similar to ERp44. The CXXS motif allows the formation of stable mixed disulfides, crucial for the ER-retention function of ERp44.


Pssm-ID: 239304  Cd Length: 113  Bit Score: 52.09  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  27 VLELTDENFESRVSDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNK-YGVSGYPTLKI 105
Cdd:cd03006   11 VLDFYKGQLDYAEELRTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCWWPQGKCRKqKHFFYFPVIHL 90

                         90       100
                 ....*....|....*....|...
gi 112293264 106 FRDGEEAGAYDGPRTADGIVSHL 128
Cdd:cd03006   91 YYRSRGPIEYKGPMRAPYMEKFV 113
PLN02309 PLN02309
5'-adenylylsulfate reductase
 381-467 3.35e-07

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 52.48  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 381 VVAENFDDIVN-----EEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSkDPNIVIAKMDATANDVP---SPYEVKGFPT 452
Cdd:PLN02309 347 VVALSRAGIENllkleNRKEPWLVVLYAPWCPFCQAMEASYEELAEKLA-GSGVKVAKFRADGDQKEfakQELQLGSFPT 425

                         90
                 ....*....|....*
gi 112293264 453 IYFSPANKKlTPKKY 467
Cdd:PLN02309 426 ILLFPKNSS-RPIKY 439
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 49-124 3.79e-07

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 48.04  E-value: 3.79e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 112293264  49 LVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAGAYDGPRTADGI 124
Cdd:cd02956   16 VVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGAQPEEQL 91
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 48-125 1.05e-06

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 46.97  E-value: 1.05e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112293264  48 MLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAgAYDGPRTADGIV 125
Cdd:cd02999   21 TAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILLFNSTPRV-RYNGTRTLDSLA 97
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 345-480 2.87e-06

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 49.63  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  345 DGKALEQFLQEyfdGNLKRylksEPIPESNEGPVKVVVAENFDD----------IVN----EEDKDV-LIEFYAPWCGHC 409
Cdd:TIGR00424 314 DAKAKECGLHK---GNIKE----ETLDGAVNGNGSDAVADIFDSnnvvslsrpgIENllklEERKEAwLVVLYAPWCPFC 386

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112293264  410 KNLEPKYKELGEKLSKDpNIVIAKMDATAND---VPSPYEVKGFPTIYFSPANKKlTPKKYEG-GRELNDFISYL 480
Cdd:TIGR00424 387 QAMEASYLELAEKLAGS-GVKVAKFRADGDQkefAKQELQLGSFPTILFFPKHSS-RPIKYPSeKRDVDSLMSFV 459
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 384-480 3.27e-06

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: 45.84  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 384 ENFDDIVNEEDKdVLIEFYAPWCGHCKNLEPKYKELGEKL-SKDPN---IVIAKMDA-TANDVPSPYEVKGFPT--IYFs 456
Cdd:cd02996    9 GNIDDILQSAEL-VLVNFYADWCRFSQMLHPIFEEAAAKIkEEFPDagkVVWGKVDCdKESDIADRYRINKYPTlkLFR- 86

                         90       100
                 ....*....|....*....|....
gi 112293264 457 paNKKLTPKKYEGGRELNDFISYL 480
Cdd:cd02996   87 --NGMMMKREYRGQRSVEALAEFV 108
trxA PRK09381
thioredoxin TrxA;
384-453 4.30e-06

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 45.44  E-value: 4.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112293264 384 ENFDDIVNEEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKdpNIVIAKMDATANDVPSP-YEVKGFPTI 453
Cdd:PRK09381  11 DSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQG--KLTVAKLNIDQNPGTAPkYGIRGIPTL 79
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 385-479 6.86e-06

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 44.82  E-value: 6.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 385 NFDDIVNEEDKdVLIEFYAPWCGHCKNLEPKYKELGEKLskDPNIVIAKMDAtANDVP--SPYEVKGFPTIYFSPANkkL 462
Cdd:cd03003   10 DFDAAVNSGEI-WFVNFYSPRCSHCHDLAPTWREFAKEM--DGVIRIGAVNC-GDDRMlcRSQGVNSYPSLYVFPSG--M 83

                         90
                 ....*....|....*..
gi 112293264 463 TPKKYEGGRELNDFISY 479
Cdd:cd03003   84 NPEKYYGDRSKESLVKF 100
PRK10996 PRK10996
thioredoxin 2; Provisional
 383-453 2.54e-05

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 43.90  E-value: 2.54e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112293264 383 AENFDDIVNEeDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIViaKMDATAN-DVPSPYEVKGFPTI 453
Cdd:PRK10996  42 GETLDKLLQD-DLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFV--KVNTEAErELSARFRIRSIPTI 110
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 394-455 4.36e-05

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 43.48  E-value: 4.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 112293264 394 DKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDataNDVPSP----YEVKGFPTIYF 455
Cdd:cd02950   20 GKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVD---NPKWLPeidrYRVDGIPHFVF 82
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 394-455 9.05e-05

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 42.37  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 394 DKDVLIEFYAPWCGHCKNLEPKYKELGEK--------LSKDPNIVIAKMDATANDVPSP------------YEVKGFPTI 453
Cdd:COG0526   28 GKPVLVNFWATWCPPCRAEMPVLKELAEEyggvvfvgVDVDENPEAVKAFLKELGLPYPvlldpdgelakaYGVRGIPTT 107


                 ..
gi 112293264 454 YF 455
Cdd:COG0526  108 VL 109
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 398-455 9.86e-05

Thioredoxin (TRX) superfamily; 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 TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 40.76  E-value: 9.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112293264 398 LIEFYAPWCGHCKNLEPKYKELGEklsKDPNIVIAKMDATANDVPSP----YEVKGFPTIYF 455
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELAL---LNKGVKFEAVDVDEDPALEKelkrYGVGGVPTLVV 59
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 384-455 1.11e-04

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 41.10  E-value: 1.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112293264 384 ENFDDIVNEED-KDVLIEFYAPWCGHCKNLEPKYKELGEKLSKdpNIVIAKMDATAN-DVPSPYEVKGFPTIYF 455
Cdd:cd02956    1 QNFQQVLQESTqVPVVVDFWAPRSPPSKELLPLLERLAEEYQG--QFVLAKVNCDAQpQIAQQFGVQALPTVYL 72
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 391-481 3.06e-04

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 41.04  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 391 NEEDKDVLIEFYAPWCGHCKNLEPKY---KELGEKLSKdpNIVIAKMDA--------------TANDVPSPYEVKGFPTI 453
Cdd:COG2143   37 KAEGKPILLFFESDWCPYCKKLHKEVfsdPEVAAYLKE--NFVVVQLDAegdkevtdfdgetlTEKELARKYGVRGTPTL 114

                         90       100
                 ....*....|....*....|....*....
gi 112293264 454 -YFSPANKKLTPkkYEGGRELNDFISYLQ 481
Cdd:COG2143  115 vFFDAEGKEIAR--IPGYLKPETFLALLK 141
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 49-111 6.19e-04

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 39.12  E-value: 6.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112293264  49 LVEFFAPWCGHCKRL------APEYEAAATrlKGIVPLaKVDCTANTNT----CNKYGVSGYPTLKIFRDGEE 111
Cdd:cd02953   15 FVDFTADWCVTCKVNekvvfsDPEVQAALK--KDVVLL-RADWTKNDPEitalLKRFGVFGPPTYLFYGPGGE 84
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 394-454 7.96e-04

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 38.83  E-value: 7.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  394 DKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVI----------------AKMDATANDVP----------SPYEV 447
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNVEIvfvsldrdleefkdylKKMPKDWLSVPfdddernelkRKYGV 80


                  ....*..
gi 112293264  448 KGFPTIY 454
Cdd:pfam13905  81 NAIPTLV 87
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 44-110 9.28e-04

TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found only in oxygenic photosynthetic organisms containing both TRX and NTR domains. The TRX domain functions as a protein disulfide reductase via the reversible oxidation of an active center dithiol present in a CXXC motif, while the NTR domain functions as a reductant to oxidized TRX. The fusion protein is bifunctional, showing both TRX and NTR activities, but it is not an independent NTR/TRX system. In plants, the protein is found exclusively in shoots and mature leaves and is localized in the chloroplast. It is involved in plant protection against oxidative stress.


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 38.64  E-value: 9.28e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112293264  44 SAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGE 110
Cdd:cd02949   12 SDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKE 78
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 383-462 1.06e-03

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 38.41  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264 383 AENFDDIVNEEDKDVLI-EFYAPWCGHCKNLEPKYKELGEKlsKDPNIVIAKMDATAN-DVPSPYEVKGFPTIYFSPANK 460
Cdd:cd02984    2 EEEFEELLKSDASKLLVlHFWAPWAEPCKQMNQVFEELAKE--AFPSVLFLSIEAEELpEISEKFEITAVPTFVFFRNGT 79


                 ..
gi 112293264 461 KL 462
Cdd:cd02984   80 IV 81
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 48-113 2.60e-03

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 38.47  E-value: 2.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  48 MLVEFFAPWCGHCKRLAPEYEAAATRLKG---IVPLaKVDCTANTNTCNKYGVSGYPTLKIF-RDGEEAG 113
Cdd:cd02950   23 TLVEFYADWCTVCQEMAPDVAKLKQKYGDqvnFVML-NVDNPKWLPEIDRYRVDGIPHFVFLdREGNEEG 91
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
395-480 2.83e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.40  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293264  395 KDVLIEFYAPWCGHCKNLEP---KYKELGEKLSKDPNIVIAKMDATANDVPSP------------YEVKGFPTIYFSPAN 459
Cdd:pfam13098   5 KPVLVVFTDPDCPYCKKLKKellEDPDVTVYLGPNFVFIAVNIWCAKEVAKAFtdilenkelgrkYGVRGTPTIVFFDGK 84

                          90       100
                  ....*....|....*....|.
gi 112293264  460 KKLTpkKYEGGRELNDFISYL 480
Cdd:pfam13098  85 GELL--RLPGYVPAEEFLALL 103
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 392-426 8.14e-03

DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.


Pssm-ID: 239317 [Multi-domain]  Cd Length: 178  Bit Score: 37.27  E-value: 8.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 112293264 392 EEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKD 426
Cdd:cd03019   13 PSGKPEVIEFFSYGCPHCYNFEPILEAWVKKLPKD 47
 
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