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Conserved domains on  [gi|1720380728|ref|XP_030103875|]
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thioredoxin domain-containing protein 16 isoform X5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 395-493 2.09e-21

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: 89.59  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTS-DSIVLFYATWHAVSMAFLQSYIDVAIKLKGRSTILLTRINCADWSDICTKQNVTAFPVVKLYKE 473
Cdd:cd02961     1 VELTDDNFDELVKDSkDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                          90       100
                  ....*....|....*....|.
gi 1720380728 474 GES-PVSYAGMLATKDLLKFI 493
Cdd:cd02961    81 GSKePVKYEGPRTLESLVEFI 101
Thioredoxin_6 super family cl37871
Thioredoxin-like domain;
534-615 6.99e-11

Thioredoxin-like domain;


The actual alignment was detected with superfamily member pfam13848:

Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 61.99  E-value: 6.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 534 FSPAMASAKELFREAGKQLRGSVITGIYSEDDVWIlsnKYATTLPALLLARPKEGRIESVPLDTTLVQDMAQILANALLE 613
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFSKEVAD---KYNIKEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLP 77


                  ..
gi 1720380728 614 AF 615
Cdd:pfam13848  78 LV 79
ER_PDI_fam super family cl36828
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 65-493 1.18e-04

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: 45.05  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728  65 ELKEAVKPLQDYG--ISVAKVTCVEEEAsrYCGEEEglmkaylfrgnilLREFPTdILFDVNAI--------------IA 128
Cdd:TIGR01130  39 EYEKAADELKKKGppIKLAKVDATEEKD--LAQKYG-------------VSGYPT-LKIFRNGEdsvsdyngprdadgIV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 129 HVLFALLFNEVKYITTLEDLhsiENSLKGKSNMIFSYVEAIGTPEHRAVMEAA------FVYGTSyqfalTTEIALLENI 202
Cdd:TIGR01130 103 KYMKKQSGPAVKEIETVADL---EAFLADDDVVVIGFFKDLDSELNDTFLSVAeklrdvYFFFAH-----SSDVAAFAKL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 203 GSESIEHAHLYFFHcklvldltEHCRRTLMEQPLTTLN--IHVFVKTMNAPLLMEVAEDPQQvstvHLQLGLPLVFIISQ 280
Cdd:TIGR01130 175 GAFPDSVVLFKPKD--------EDEKFSKVDGEMDTDVsdLEKFIRAESLPLVGEFTQETAA----KYFESGPLVVLYYN 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 281 raTQEADRRTAEWvawhllgKAGVLLLLRDSMDVNIpqhaNVAFRRAEKDVPV-EFLVLNDVE----LIISHVKNNMHIE 355
Cdd:TIGR01130 243 --VDESLDPFEEL-------RNRFLEAAKKFRGKFV----NFAVADEEDFGRElEYFGLKAEKfpavAIQDLEGNKKYPM 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 356 EIQEDEGEDMEgpdlAVEDDEVAGTVYRDRK-KPLPLELS---VELTEETFNTTVM--TSDSIVLFYATW--HAVSMAfl 427
Cdd:TIGR01130 310 DQEEFSSENLE----AFVKDFLDGKLKPYLKsEPIPEDDEgpvKVLVGKNFDEIVLdeTKDVLVEFYAPWcgHCKNLA-- 383

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720380728 428 QSYIDVAIKLKGR-STILLTRINcADWSDIcTKQNVTAFPVVKLYKEGE--SPVSYAGMLATKDLLKFI 493
Cdd:TIGR01130 384 PIYEELAEKYKDAeSDVVIAKMD-ATANDV-PPFEVEGFPTIKFVPAGKksEPVPYDGDRTLEDFSKFI 450
 
Name Accession Description Interval E-value
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 395-493 2.09e-21

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: 89.59  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTS-DSIVLFYATWHAVSMAFLQSYIDVAIKLKGRSTILLTRINCADWSDICTKQNVTAFPVVKLYKE 473
Cdd:cd02961     1 VELTDDNFDELVKDSkDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                          90       100
                  ....*....|....*....|.
gi 1720380728 474 GES-PVSYAGMLATKDLLKFI 493
Cdd:cd02961    81 GSKePVKYEGPRTLESLVEFI 101
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
534-615 6.99e-11

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 61.99  E-value: 6.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 534 FSPAMASAKELFREAGKQLRGSVITGIYSEDDVWIlsnKYATTLPALLLARPKEGRIESVPLDTTLVQDMAQILANALLE 613
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFSKEVAD---KYNIKEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLP 77


                  ..
gi 1720380728 614 AF 615
Cdd:pfam13848  78 LV 79
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 395-606 1.38e-10

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: 64.31  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTSDSI-VLFYATW--HAVSMAflQSYIDVAIKLKGRST-ILLTRINCADWSDICTKQNVTAFPVVKL 470
Cdd:TIGR01130   4 LVLTKDNFDDFIKSHEFVlVEFYAPWcgHCKSLA--PEYEKAADELKKKGPpIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 471 YKEGESPVS-YAGMLATKDLLKFiqLNKISCP--VNIASIQEAEKYLrgelykdlpSSASVSVLGLFSPAMASAKELFRE 547
Cdd:TIGR01130  82 FRNGEDSVSdYNGPRDADGIVKY--MKKQSGPavKEIETVADLEAFL---------ADDDVVVIGFFKDLDSELNDTFLS 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720380728 548 AGKQLRgSVITGIYSEDDVWILSNKYATTLPALLLARPKEGRiESVPLDTTLVQDMAQI 606
Cdd:TIGR01130 151 VAEKLR-DVYFFFAHSSDVAAFAKLGAFPDSVVLFKPKDEDE-KFSKVDGEMDTDVSDL 207
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 395-493 5.25e-09

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: 54.16  E-value: 5.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTSDSIVL--FYATW--HAVSMAFLqsYIDVAIKLKGRSTILltRINCADWSDICTKQNVTAFPVVKL 470
Cdd:pfam00085   3 VVLTDANFDEVVQKSSKPVLvdFYAPWcgPCKMLAPE--YEELAQEYKGNVVFA--KVDVDENPDLASKYGVRGYPTLIF 78

                          90       100
                  ....*....|....*....|...
gi 1720380728 471 YKEGESPVSYAGMLATKDLLKFI 493
Cdd:pfam00085  79 FKNGQPVDDYVGARPKDALAAFL 101
PTZ00051 PTZ00051
thioredoxin; Provisional
 398-493 1.96e-05

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 43.71  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 398 TEETFNTTVmTSDSIVL--FYATWHAVSMAFLQSYIDVAiklKGRSTILLTRINCADWSDICTKQNVTAFPVVKLYKEGE 475
Cdd:PTZ00051    7 SQAEFESTL-SQNELVIvdFYAEWCGPCKRIAPFYEECS---KEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGS 82

                          90
                  ....*....|....*...
gi 1720380728 476 SPVSYAGmlATKDLLKFI 493
Cdd:PTZ00051   83 VVDTLLG--ANDEALKQL 98
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 65-493 1.18e-04

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 45.05  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728  65 ELKEAVKPLQDYG--ISVAKVTCVEEEAsrYCGEEEglmkaylfrgnilLREFPTdILFDVNAI--------------IA 128
Cdd:TIGR01130  39 EYEKAADELKKKGppIKLAKVDATEEKD--LAQKYG-------------VSGYPT-LKIFRNGEdsvsdyngprdadgIV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 129 HVLFALLFNEVKYITTLEDLhsiENSLKGKSNMIFSYVEAIGTPEHRAVMEAA------FVYGTSyqfalTTEIALLENI 202
Cdd:TIGR01130 103 KYMKKQSGPAVKEIETVADL---EAFLADDDVVVIGFFKDLDSELNDTFLSVAeklrdvYFFFAH-----SSDVAAFAKL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 203 GSESIEHAHLYFFHcklvldltEHCRRTLMEQPLTTLN--IHVFVKTMNAPLLMEVAEDPQQvstvHLQLGLPLVFIISQ 280
Cdd:TIGR01130 175 GAFPDSVVLFKPKD--------EDEKFSKVDGEMDTDVsdLEKFIRAESLPLVGEFTQETAA----KYFESGPLVVLYYN 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 281 raTQEADRRTAEWvawhllgKAGVLLLLRDSMDVNIpqhaNVAFRRAEKDVPV-EFLVLNDVE----LIISHVKNNMHIE 355
Cdd:TIGR01130 243 --VDESLDPFEEL-------RNRFLEAAKKFRGKFV----NFAVADEEDFGRElEYFGLKAEKfpavAIQDLEGNKKYPM 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 356 EIQEDEGEDMEgpdlAVEDDEVAGTVYRDRK-KPLPLELS---VELTEETFNTTVM--TSDSIVLFYATW--HAVSMAfl 427
Cdd:TIGR01130 310 DQEEFSSENLE----AFVKDFLDGKLKPYLKsEPIPEDDEgpvKVLVGKNFDEIVLdeTKDVLVEFYAPWcgHCKNLA-- 383

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720380728 428 QSYIDVAIKLKGR-STILLTRINcADWSDIcTKQNVTAFPVVKLYKEGE--SPVSYAGMLATKDLLKFI 493
Cdd:TIGR01130 384 PIYEELAEKYKDAeSDVVIAKMD-ATANDV-PPFEVEGFPTIKFVPAGKksEPVPYDGDRTLEDFSKFI 450
 
Name Accession Description Interval E-value
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 395-493 2.09e-21

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: 89.59  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTS-DSIVLFYATWHAVSMAFLQSYIDVAIKLKGRSTILLTRINCADWSDICTKQNVTAFPVVKLYKE 473
Cdd:cd02961     1 VELTDDNFDELVKDSkDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                          90       100
                  ....*....|....*....|.
gi 1720380728 474 GES-PVSYAGMLATKDLLKFI 493
Cdd:cd02961    81 GSKePVKYEGPRTLESLVEFI 101
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 395-493 3.55e-12

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


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 63.42  E-value: 3.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTS--DSIVLFYATW--HAVSMAflQSYIDVAIKLKGRSTILLTRINC-ADWSDICTKQNVTAFPVVK 469
Cdd:cd02998     3 VELTDSNFDKVVGDDkkDVLVEFYAPWcgHCKNLA--PEYEKLAAVFANEDDVVIAKVDAdEANKDLAKKYGVSGFPTLK 80

                          90       100
                  ....*....|....*....|....*
gi 1720380728 470 LYKEGES-PVSYAGMLATKDLLKFI 493
Cdd:cd02998    81 FFPKGSTePVKYEGGRDLEDLVKFV 105
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
534-615 6.99e-11

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 61.99  E-value: 6.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 534 FSPAMASAKELFREAGKQLRGSVITGIYSEDDVWIlsnKYATTLPALLLARPKEGRIESVPLDTTLVQDMAQILANALLE 613
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFSKEVAD---KYNIKEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLP 77


                  ..
gi 1720380728 614 AF 615
Cdd:pfam13848  78 LV 79
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 395-606 1.38e-10

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: 64.31  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTSDSI-VLFYATW--HAVSMAflQSYIDVAIKLKGRST-ILLTRINCADWSDICTKQNVTAFPVVKL 470
Cdd:TIGR01130   4 LVLTKDNFDDFIKSHEFVlVEFYAPWcgHCKSLA--PEYEKAADELKKKGPpIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 471 YKEGESPVS-YAGMLATKDLLKFiqLNKISCP--VNIASIQEAEKYLrgelykdlpSSASVSVLGLFSPAMASAKELFRE 547
Cdd:TIGR01130  82 FRNGEDSVSdYNGPRDADGIVKY--MKKQSGPavKEIETVADLEAFL---------ADDDVVVIGFFKDLDSELNDTFLS 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720380728 548 AGKQLRgSVITGIYSEDDVWILSNKYATTLPALLLARPKEGRiESVPLDTTLVQDMAQI 606
Cdd:TIGR01130 151 VAEKLR-DVYFFFAHSSDVAAFAKLGAFPDSVVLFKPKDEDE-KFSKVDGEMDTDVSDL 207
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 394-493 1.38e-10

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: 58.84  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 394 SVELTEETFNTTVMTSDS--IVLFYATWHAVSMAFLQSYIDVAIKLKGrsTILLTRINCADWSDICTKQNVTAFPVVKLY 471
Cdd:cd03004     3 VITLTPEDFPELVLNRKEpwLVDFYAPWCGPCQALLPELRKAARALKG--KVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                          90       100
                  ....*....|....*....|....
gi 1720380728 472 KEGESPV-SYAG-MLATKDLLKFI 493
Cdd:cd03004    81 PGNASKYhSYNGwHRDADSILEFI 104
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 394-489 1.42e-09

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


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 55.75  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 394 SVELTEETFNTTVMTSDSIVLFYATW--HAVSMAflQSYIDVAIKL-KGRSTILLTRINCADWSDICTKQNVTAFPVVKL 470
Cdd:cd03005     2 VLELTEDNFDHHIAEGNHFVKFFAPWcgHCKRLA--PTWEQLAKKFnNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLL 79

                          90
                  ....*....|....*....
gi 1720380728 471 YKEGESPVSYAGmlaTKDL 489
Cdd:cd03005    80 FKDGEKVDKYKG---TRDL 95
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 395-493 4.53e-09

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: 54.48  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTS--DSIVLFYATW--HAVSMAFLqsYIDVAIKLKGRSTILLTRINcADWSDICTKQNVTAFPVVKL 470
Cdd:cd02995     3 KVVVGKNFDEVVLDSdkDVLVEFYAPWcgHCKALAPI--YEELAEKLKGDDNVVIAKMD-ATANDVPSEFVVDGFPTILF 79

                          90       100
                  ....*....|....*....|....*
gi 1720380728 471 YKEG--ESPVSYAGMLATKDLLKFI 493
Cdd:cd02995    80 FPAGdkSNPIKYEGDRTLEDLIKFI 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 395-493 5.25e-09

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: 54.16  E-value: 5.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTSDSIVL--FYATW--HAVSMAFLqsYIDVAIKLKGRSTILltRINCADWSDICTKQNVTAFPVVKL 470
Cdd:pfam00085   3 VVLTDANFDEVVQKSSKPVLvdFYAPWcgPCKMLAPE--YEELAQEYKGNVVFA--KVDVDENPDLASKYGVRGYPTLIF 78

                          90       100
                  ....*....|....*....|...
gi 1720380728 471 YKEGESPVSYAGMLATKDLLKFI 493
Cdd:pfam00085  79 FKNGQPVDDYVGARPKDALAAFL 101
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 395-492 2.68e-07

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: 49.21  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTSDS--IVLFYATWHAVSMAFLQSYIDVAIKLKGrsTILLTRINCADWSDICTKQNVTAFPVVKLYK 472
Cdd:cd03001     3 VELTDSNFDKKVLNSDDvwLVEFYAPWCGHCKNLAPEWKKAAKALKG--IVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                          90       100
                  ....*....|....*....|.
gi 1720380728 473 EG-ESPVSYAGMLATKDLLKF 492
Cdd:cd03001    81 AGkNSPQDYQGGRTAKAIVSA 101
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 411-493 2.11e-06

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: 47.08  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 411 SIVLFYATWHAVSMAFLQSYIDVAIKLKgrSTILLTRINCADWSDICTKQ-NVTAFPVVKLYKEGESPVSYAGMLATKDL 489
Cdd:cd03006    32 SLVMYYAPWDAQSQAARQEFEQVAQKLS--DQVLFVAINCWWPQGKCRKQkHFFYFPVIHLYYRSRGPIEYKGPMRAPYM 109


                  ....
gi 1720380728 490 LKFI 493
Cdd:cd03006   110 EKFV 113
PTZ00051 PTZ00051
thioredoxin; Provisional
 398-493 1.96e-05

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 43.71  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 398 TEETFNTTVmTSDSIVL--FYATWHAVSMAFLQSYIDVAiklKGRSTILLTRINCADWSDICTKQNVTAFPVVKLYKEGE 475
Cdd:PTZ00051    7 SQAEFESTL-SQNELVIvdFYAEWCGPCKRIAPFYEECS---KEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGS 82

                          90
                  ....*....|....*...
gi 1720380728 476 SPVSYAGmlATKDLLKFI 493
Cdd:PTZ00051   83 VVDTLLG--ANDEALKQL 98
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 388-529 2.22e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 47.44  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 388 PLPLELSVELTEETFNTTVMTSDS-IVLFYATW--HAVSMAflQSYIDVAIKLKGR-STILLTRINCADWSDICTKQNVT 463
Cdd:PTZ00102   28 HFISEHVTVLTDSTFDKFITENEIvLVKFYAPWcgHCKRLA--PEYKKAAKMLKEKkSEIVLASVDATEEMELAQEFGVR 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720380728 464 AFPVVKLYKEGEsPVSYAGMLATKDLLKFIQlnKISCPVniasIQEAEKYLRGELYKDLPSSASVS 529
Cdd:PTZ00102  106 GYPTIKFFNKGN-PVNYSGGRTADGIVSWIK--KLTGPA----VTEVESASEIKLIAKKIFVAFYG 164
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 65-493 1.18e-04

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 45.05  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728  65 ELKEAVKPLQDYG--ISVAKVTCVEEEAsrYCGEEEglmkaylfrgnilLREFPTdILFDVNAI--------------IA 128
Cdd:TIGR01130  39 EYEKAADELKKKGppIKLAKVDATEEKD--LAQKYG-------------VSGYPT-LKIFRNGEdsvsdyngprdadgIV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 129 HVLFALLFNEVKYITTLEDLhsiENSLKGKSNMIFSYVEAIGTPEHRAVMEAA------FVYGTSyqfalTTEIALLENI 202
Cdd:TIGR01130 103 KYMKKQSGPAVKEIETVADL---EAFLADDDVVVIGFFKDLDSELNDTFLSVAeklrdvYFFFAH-----SSDVAAFAKL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 203 GSESIEHAHLYFFHcklvldltEHCRRTLMEQPLTTLN--IHVFVKTMNAPLLMEVAEDPQQvstvHLQLGLPLVFIISQ 280
Cdd:TIGR01130 175 GAFPDSVVLFKPKD--------EDEKFSKVDGEMDTDVsdLEKFIRAESLPLVGEFTQETAA----KYFESGPLVVLYYN 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 281 raTQEADRRTAEWvawhllgKAGVLLLLRDSMDVNIpqhaNVAFRRAEKDVPV-EFLVLNDVE----LIISHVKNNMHIE 355
Cdd:TIGR01130 243 --VDESLDPFEEL-------RNRFLEAAKKFRGKFV----NFAVADEEDFGRElEYFGLKAEKfpavAIQDLEGNKKYPM 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 356 EIQEDEGEDMEgpdlAVEDDEVAGTVYRDRK-KPLPLELS---VELTEETFNTTVM--TSDSIVLFYATW--HAVSMAfl 427
Cdd:TIGR01130 310 DQEEFSSENLE----AFVKDFLDGKLKPYLKsEPIPEDDEgpvKVLVGKNFDEIVLdeTKDVLVEFYAPWcgHCKNLA-- 383

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720380728 428 QSYIDVAIKLKGR-STILLTRINcADWSDIcTKQNVTAFPVVKLYKEGE--SPVSYAGMLATKDLLKFI 493
Cdd:TIGR01130 384 PIYEELAEKYKDAeSDVVIAKMD-ATANDV-PPFEVEGFPTIKFVPAGKksEPVPYDGDRTLEDFSKFI 450
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 395-492 2.22e-04

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: 40.97  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 395 VELTEETFNTTVMTSDS-IVLFYATW--HAVSMAflQSYIDVAIKLKGrsTILLTRINCADWSDICTKQNVTAFPVVKLY 471
Cdd:cd03003     4 VTLDRGDFDAAVNSGEIwFVNFYSPRcsHCHDLA--PTWREFAKEMDG--VIRIGAVNCGDDRMLCRSQGVNSYPSLYVF 79

                          90       100
                  ....*....|....*....|.
gi 1720380728 472 KEGESPVSYAGMLATKDLLKF 492
Cdd:cd03003    80 PSGMNPEKYYGDRSKESLVKF 100
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 394-493 4.15e-04

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: 40.45  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720380728 394 SVELTEETFNTTVMTSD-SIVLFYATWHAVSMAFLQSYIDVAIKLK----GRSTILLTRINCADWSDICTKQNVTAFPVV 468
Cdd:cd02996     3 IVSLTSGNIDDILQSAElVLVNFYADWCRFSQMLHPIFEEAAAKIKeefpDAGKVVWGKVDCDKESDIADRYRINKYPTL 82

                          90       100
                  ....*....|....*....|....*.
gi 1720380728 469 KLYKEGESP-VSYAGMLATKDLLKFI 493
Cdd:cd02996    83 KLFRNGMMMkREYRGQRSVEALAEFV 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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