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Conserved domains on  [gi|568951425|ref|XP_006508277|]
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protein disulfide-isomerase-like protein of the testis isoform X1 [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

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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 ...
 44-498 1.25e-79

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: 258.45  E-value: 1.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425   44 VLTPAGLTQTLNETRFLMVIFHNPSLKQSRKLAKELGKAAEIFGKGKNGLGFGKVDITKETELQQEFDITHAPELKLFFE 123
Cdd:TIGR01130   5 VLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  124 GNRlKPISCKDVVESTALVVWLRRQISKKALLFNNSDEVADFVKSRPLVIVGFFQDLEEEVAELFY---DTIKDFPElTF 200
Cdd:TIGR01130  85 GED-SVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLsvaEKLRDVYF-FF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  201 GAIQIKNSFGRFHVILDSVLVFKKGKIVKRQELINDS--TNKDHLNQVIKQQLTGFVIELNPENKDLIYELNILNHMLLF 278
Cdd:TIGR01130 163 AHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEmdTDVSDLEKFIRAESLPLVGEFTQETAAKYFESGPLVVLYYN 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  279 ISKSSEPYSTISRHYRQIAKEFQNKILfVLVNADEPKNKRIFEYFQISRVNVPSVQILNLSSDGRYKMPTDDINFESLKK 358
Cdd:TIGR01130 243 VDESLDPFEELRNRFLEAAKKFRGKFV-NFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  359 FCNSFLSKTAKKHKASEEIPKYwDQGPVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNH-STV 437
Cdd:TIGR01130 322 FVKDFLDGKLKPYLKSEPIPED-DEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAeSDV 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568951425  438 IIAKIDITANDIQLANPEQYPFFRLFPTDSQ-EAVMYKGEHTMKGFCDFLESHVKVRIEEED 498
Cdd:TIGR01130 401 VIAKMDATANDVPPFEVEGFPTIKFVPAGKKsEPVPYDGDRTLEDFSKFIAKHATFPLEGKA 462
 
Name Accession Description Interval E-value
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 44-498 1.25e-79

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: 258.45  E-value: 1.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425   44 VLTPAGLTQTLNETRFLMVIFHNPSLKQSRKLAKELGKAAEIFGKGKNGLGFGKVDITKETELQQEFDITHAPELKLFFE 123
Cdd:TIGR01130   5 VLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  124 GNRlKPISCKDVVESTALVVWLRRQISKKALLFNNSDEVADFVKSRPLVIVGFFQDLEEEVAELFY---DTIKDFPElTF 200
Cdd:TIGR01130  85 GED-SVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLsvaEKLRDVYF-FF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  201 GAIQIKNSFGRFHVILDSVLVFKKGKIVKRQELINDS--TNKDHLNQVIKQQLTGFVIELNPENKDLIYELNILNHMLLF 278
Cdd:TIGR01130 163 AHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEmdTDVSDLEKFIRAESLPLVGEFTQETAAKYFESGPLVVLYYN 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  279 ISKSSEPYSTISRHYRQIAKEFQNKILfVLVNADEPKNKRIFEYFQISRVNVPSVQILNLSSDGRYKMPTDDINFESLKK 358
Cdd:TIGR01130 243 VDESLDPFEELRNRFLEAAKKFRGKFV-NFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  359 FCNSFLSKTAKKHKASEEIPKYwDQGPVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNH-STV 437
Cdd:TIGR01130 322 FVKDFLDGKLKPYLKSEPIPED-DEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAeSDV 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568951425  438 IIAKIDITANDIQLANPEQYPFFRLFPTDSQ-EAVMYKGEHTMKGFCDFLESHVKVRIEEED 498
Cdd:TIGR01130 401 VIAKMDATANDVPPFEVEGFPTIKFVPAGKKsEPVPYDGDRTLEDFSKFIAKHATFPLEGKA 462
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 35-500 5.26e-47

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 171.47  E-value: 5.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  35 HILEDHnLMVLTPAGLTQTLNETRFLMVIFHNPSLKQSRKLAKELGKAAEIFGKGKNGLGFGKVDITKETELQQEFDITH 114
Cdd:PTZ00102  28 HFISEH-VTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRG 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 115 APELKLFFEGNRLKPISCKDvveSTALVVWLRrQISKKALLF--NNSDEVADFVKsrplVIVGFFQDLEEEVAELFydti 192
Cdd:PTZ00102 107 YPTIKFFNKGNPVNYSGGRT---ADGIVSWIK-KLTGPAVTEveSASEIKLIAKK----IFVAFYGEYTSKDSELY---- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 193 KDFPELTFGAIQIKNSFGRFHVILDSVLVFKKGKivKRQELINDSTnKDHLNQVIKQQLTGFVIELNPENkdliYELNIL 272
Cdd:PTZ00102 175 KKFEEVADKHREHAKFFVKKHEGKNKIYVLHKDE--EGVELFMGKT-KEELEEFVSTESFPLFAEINAEN----YRRYIS 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 273 NHM-LLFISKSSEPYSTISRHYRQIAKEFQNKILFVLVNADEPKNkRIFEYFQISRVNVPSVQilnlSSDGRYKMPTDDI 351
Cdd:PTZ00102 248 SGKdLVWFCGTTEDYDKYKSVVRKVARKLREKYAFVWLDTEQFGS-HAKEHLLIEEFPGLAYQ----SPAGRYLLPPAKE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 352 NFESLKKFCNSFLSKTAKKHK---ASEEIPKYwDQGPVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELG 428
Cdd:PTZ00102 323 SFDSVEALIEFFKDVEAGKVEksiKSEPIPEE-QDGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELG 401

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568951425 429 IKYQNHSTVIIAKIDITANDIQLA--NPEQYPFFRLFPTDSQEAVMYKGEHTMKGFCDFLESHVKVRIEEE--DEL 500
Cdd:PTZ00102 402 EKYKDNDSIIVAKMNGTANETPLEefSWSAFPTILFVKAGERTPIPYEGERTVEGFKEFVNKHATNPFEDDthEEL 477
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
177-362 1.74e-38

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 139.80  E-value: 1.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  177 FQDLEEEVAELFYDTIKDFP-ELTFGAIQIKNSFGRFHVILDSVLVFKKGKiVKRQELINDSTNKDHLNQVIKQQLTGFV 255
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKgDVRFGITFSKEVADKYNIKEPAILLFRKFD-EETVHYPGDSINFEDLKKFIQKNCLPLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  256 IELNPENKDLIYELNILNHMLLFISKSSEPYSTISRHYRQIAKEFQNKILFVLVNADepKNKRIFEYFQISRVNVPSVQI 335
Cdd:pfam13848  80 REFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAK--SFGRPLEYFGLSESDLPVIVI 157

                         170       180
                  ....*....|....*....|....*..
gi 568951425  336 LNLSSDGRYKMPTDDINFESLKKFCNS 362
Cdd:pfam13848 158 VDSFSHMYKYFPSDEFSPESLKEFIND 184
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 385-486 9.50e-33

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: 121.12  E-value: 9.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 385 PVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHSTVIIAKIDITANDIQLA-NPEQYPFFRLF 463
Cdd:cd02995    1 PVKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSEfVVDGFPTILFF 80

                         90       100
                 ....*....|....*....|....
gi 568951425 464 PT-DSQEAVMYKGEHTMKGFCDFL 486
Cdd:cd02995   81 PAgDKSNPIKYEGDRTLEDLIKFI 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 386-490 4.63e-10

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: 56.75  E-value: 4.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 386 VKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHstVIIAKIDITANDiQLAnpEQY-----PFF 460
Cdd:COG3118    2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK--VKFVKVDVDENP-ELA--AQFgvrsiPTL 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 568951425 461 RLFpTDSQEAVMYKGEHTMKGFCDFLESHV 490
Cdd:COG3118   77 LLF-KDGQPVDRFVGALPKEQLREFLDKVL 105
 
Name Accession Description Interval E-value
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 44-498 1.25e-79

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: 258.45  E-value: 1.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425   44 VLTPAGLTQTLNETRFLMVIFHNPSLKQSRKLAKELGKAAEIFGKGKNGLGFGKVDITKETELQQEFDITHAPELKLFFE 123
Cdd:TIGR01130   5 VLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  124 GNRlKPISCKDVVESTALVVWLRRQISKKALLFNNSDEVADFVKSRPLVIVGFFQDLEEEVAELFY---DTIKDFPElTF 200
Cdd:TIGR01130  85 GED-SVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLsvaEKLRDVYF-FF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  201 GAIQIKNSFGRFHVILDSVLVFKKGKIVKRQELINDS--TNKDHLNQVIKQQLTGFVIELNPENKDLIYELNILNHMLLF 278
Cdd:TIGR01130 163 AHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEmdTDVSDLEKFIRAESLPLVGEFTQETAAKYFESGPLVVLYYN 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  279 ISKSSEPYSTISRHYRQIAKEFQNKILfVLVNADEPKNKRIFEYFQISRVNVPSVQILNLSSDGRYKMPTDDINFESLKK 358
Cdd:TIGR01130 243 VDESLDPFEELRNRFLEAAKKFRGKFV-NFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSENLEA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  359 FCNSFLSKTAKKHKASEEIPKYwDQGPVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNH-STV 437
Cdd:TIGR01130 322 FVKDFLDGKLKPYLKSEPIPED-DEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAeSDV 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568951425  438 IIAKIDITANDIQLANPEQYPFFRLFPTDSQ-EAVMYKGEHTMKGFCDFLESHVKVRIEEED 498
Cdd:TIGR01130 401 VIAKMDATANDVPPFEVEGFPTIKFVPAGKKsEPVPYDGDRTLEDFSKFIAKHATFPLEGKA 462
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 35-500 5.26e-47

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 171.47  E-value: 5.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  35 HILEDHnLMVLTPAGLTQTLNETRFLMVIFHNPSLKQSRKLAKELGKAAEIFGKGKNGLGFGKVDITKETELQQEFDITH 114
Cdd:PTZ00102  28 HFISEH-VTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRG 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 115 APELKLFFEGNRLKPISCKDvveSTALVVWLRrQISKKALLF--NNSDEVADFVKsrplVIVGFFQDLEEEVAELFydti 192
Cdd:PTZ00102 107 YPTIKFFNKGNPVNYSGGRT---ADGIVSWIK-KLTGPAVTEveSASEIKLIAKK----IFVAFYGEYTSKDSELY---- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 193 KDFPELTFGAIQIKNSFGRFHVILDSVLVFKKGKivKRQELINDSTnKDHLNQVIKQQLTGFVIELNPENkdliYELNIL 272
Cdd:PTZ00102 175 KKFEEVADKHREHAKFFVKKHEGKNKIYVLHKDE--EGVELFMGKT-KEELEEFVSTESFPLFAEINAEN----YRRYIS 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 273 NHM-LLFISKSSEPYSTISRHYRQIAKEFQNKILFVLVNADEPKNkRIFEYFQISRVNVPSVQilnlSSDGRYKMPTDDI 351
Cdd:PTZ00102 248 SGKdLVWFCGTTEDYDKYKSVVRKVARKLREKYAFVWLDTEQFGS-HAKEHLLIEEFPGLAYQ----SPAGRYLLPPAKE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 352 NFESLKKFCNSFLSKTAKKHK---ASEEIPKYwDQGPVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELG 428
Cdd:PTZ00102 323 SFDSVEALIEFFKDVEAGKVEksiKSEPIPEE-QDGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELG 401

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568951425 429 IKYQNHSTVIIAKIDITANDIQLA--NPEQYPFFRLFPTDSQEAVMYKGEHTMKGFCDFLESHVKVRIEEE--DEL 500
Cdd:PTZ00102 402 EKYKDNDSIIVAKMNGTANETPLEefSWSAFPTILFVKAGERTPIPYEGERTVEGFKEFVNKHATNPFEDDthEEL 477
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
177-362 1.74e-38

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 139.80  E-value: 1.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  177 FQDLEEEVAELFYDTIKDFP-ELTFGAIQIKNSFGRFHVILDSVLVFKKGKiVKRQELINDSTNKDHLNQVIKQQLTGFV 255
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKgDVRFGITFSKEVADKYNIKEPAILLFRKFD-EETVHYPGDSINFEDLKKFIQKNCLPLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  256 IELNPENKDLIYELNILNHMLLFISKSSEPYSTISRHYRQIAKEFQNKILFVLVNADepKNKRIFEYFQISRVNVPSVQI 335
Cdd:pfam13848  80 REFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAK--SFGRPLEYFGLSESDLPVIVI 157

                         170       180
                  ....*....|....*....|....*..
gi 568951425  336 LNLSSDGRYKMPTDDINFESLKKFCNS 362
Cdd:pfam13848 158 VDSFSHMYKYFPSDEFSPESLKEFIND 184
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 385-486 9.50e-33

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: 121.12  E-value: 9.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 385 PVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHSTVIIAKIDITANDIQLA-NPEQYPFFRLF 463
Cdd:cd02995    1 PVKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSEfVVDGFPTILFF 80

                         90       100
                 ....*....|....*....|....
gi 568951425 464 PT-DSQEAVMYKGEHTMKGFCDFL 486
Cdd:cd02995   81 PAgDKSNPIKYEGDRTLEDLIKFI 104
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 387-486 4.15e-20

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 85.35  E-value: 4.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 387 KKLVGKNFNVVVLDkEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHSTVIIAKIDITAN-DI-QLANPEQYPFFRLFP 464
Cdd:cd02961    1 VELTDDNFDELVKD-SKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANnDLcSEYGVRGYPTIKLFP 79

                         90       100
                 ....*....|....*....|..
gi 568951425 465 TDSQEAVMYKGEHTMKGFCDFL 486
Cdd:cd02961   80 NGSKEPVKYEGPRTLESLVEFI 101
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 267-364 1.40e-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: 81.16  E-value: 1.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 267 YELNILNHMLLFISKSSEPYSTISRHYRQIAKEFQNKILFVLVNADEpkNKRIFEYFQISRVNVPSVQILNLSSDGRYKM 346
Cdd:cd02982    8 YEESGKPLLVLFYNKDDSESEELRERFKEVAKKFKGKLLFVVVDADD--FGRHLEYFGLKEEDLPVIAIINLSDGKKYLM 85

                         90
                 ....*....|....*...
gi 568951425 347 PTDDINFESLKKFCNSFL 364
Cdd:cd02982   86 PEEELTAESLEEFVEDFL 103
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 386-486 9.15e-18

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: 78.83  E-value: 9.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 386 VKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHSTVIIAKIDITANDIQLANP---EQYPFFRL 462
Cdd:cd02998    2 VVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEANKDLAKKygvSGFPTLKF 81

                         90       100
                 ....*....|....*....|....
gi 568951425 463 FPTDSQEAVMYKGEHTMKGFCDFL 486
Cdd:cd02998   82 FPKGSTEPVKYEGGRDLEDLVKFV 105
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 386-475 5.81e-14

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: 68.08  E-value: 5.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 386 VKKLVGKNFNVVVldKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHST-VIIAKIDITAnDIQLANPEQ---YPFFR 461
Cdd:cd03005    2 VLELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPsVKIAKVDCTQ-HRELCSEFQvrgYPTLL 78

                         90
                 ....*....|....
gi 568951425 462 LFpTDSQEAVMYKG 475
Cdd:cd03005   79 LF-KDGEKVDKYKG 91
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 385-488 1.38e-12

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: 64.18  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  385 PVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNhsTVIIAKIDITANDI--QLANPEQYPFFRL 462
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKG--NVVFAKVDVDENPDlaSKYGVRGYPTLIF 78

                          90       100
                  ....*....|....*....|....*.
gi 568951425  463 FPtDSQEAVMYKGEHTMKGFCDFLES 488
Cdd:pfam00085  79 FK-NGQPVDDYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 386-490 4.63e-10

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: 56.75  E-value: 4.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 386 VKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHstVIIAKIDITANDiQLAnpEQY-----PFF 460
Cdd:COG3118    2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK--VKFVKVDVDENP-ELA--AQFgvrsiPTL 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 568951425 461 RLFpTDSQEAVMYKGEHTMKGFCDFLESHV 490
Cdd:COG3118   77 LLF-KDGQPVDRFVGALPKEQLREFLDKVL 105
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 44-126 6.33e-09

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: 53.38  E-value: 6.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  44 VLTPAGLTQTLNETRFLMVIFHNPSLKQSRKLAKELGKAAEIFgKGKNGLGFGKVDITKETELQQEFDITHAPELKLFFE 123
Cdd:cd02961    2 ELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKEL-KGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80


                 ...
gi 568951425 124 GNR 126
Cdd:cd02961   81 GSK 83
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 156-248 1.34e-06

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: 46.95  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 156 FNNSDEVADFVKSRPLVIVGFFQDLEEEVAELFYDTIKDFPE-LTFGAIQIKNSFGRFHVILDSVLVFKKGkiVKRQELI 234
Cdd:cd02981    4 LTSKEELEKFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRDdYGFGHTSDKEVAKKLKVKPGSVVLFKPF--EEEPVEY 81

                         90
                 ....*....|....
gi 568951425 235 NDSTNKDHLNQVIK 248
Cdd:cd02981   82 DGEFTEESLVEFIK 95
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 385-485 2.51e-06

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: 46.13  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 385 PVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQnhSTVIIAKIDITANDiQLANP---EQYPFFR 461
Cdd:cd03001    1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALK--GIVKVGAVDADVHQ-SLAQQygvRGFPTIK 77

                         90       100
                 ....*....|....*....|....
gi 568951425 462 LFPTDSQEAVMYKGEHTMKGFCDF 485
Cdd:cd03001   78 VFGAGKNSPQDYQGGRTAKAIVSA 101
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 400-485 5.77e-06

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


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 45.14  E-value: 5.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 400 DKEKDV------FVMFYAPWSEKCRVLLPLLEELGIKYQNH-STVIIAKIDIT-----ANDIQLanpEQYPFFRLFPTDS 467
Cdd:cd03000    7 DSFKDVrkediwLVDFYAPWCGHCKKLEPVWNEVGAELKSSgSPVRVGKLDATayssiASEFGV---RGYPTIKLLKGDL 83

                         90
                 ....*....|....*...
gi 568951425 468 qeAVMYKGEHTMKGFCDF 485
Cdd:cd03000   84 --AYNYRGPRTKDDIVEF 99
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 385-485 1.30e-05

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: 44.28  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 385 PVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGikYQNHSTVIIAKIDITAN---------DIQlanpe 455
Cdd:cd03002    1 PVYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAA--KELDGLVQVAAVDCDEDknkplcgkyGVQ----- 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568951425 456 QYPFFRLFPT---DSQEAVM-YKGEHTMKGFCDF 485
Cdd:cd03002   74 GFPTLKVFRPpkkASKHAVEdYNGERSAKAIVDF 107
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 398-447 2.63e-05

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: 42.93  E-value: 2.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568951425 398 VLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNhstVIIAKIDITAN 447
Cdd:cd02947    6 LIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK---VKFVKVDVDEN 52
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 392-477 3.04e-05

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


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 43.05  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 392 KNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGiKYQNHsTVIIAKIDITAND--IQLANPEQYPFFRLFPTDSQE 469
Cdd:cd03004    9 EDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAA-RALKG-KVKVGSVDCQKYEslCQQANIRAYPTIRLYPGNASK 86


                 ....*...
gi 568951425 470 AVMYKGEH 477
Cdd:cd03004   87 YHSYNGWH 94
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 393-447 4.13e-05

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: 42.64  E-value: 4.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568951425 393 NFN-VVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQnhSTVIIAKIDITAN 447
Cdd:cd02956    2 NFQqVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQ--GQFVLAKVNCDAQ 55
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 41-124 1.24e-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: 41.61  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425  41 NLMVLTPAGLTQTLNETRFLMVIFHNPSLKQSRKLAKELGKAAEIFGK---GKNGLGFGKVDITKETELQQEFDITHAPE 117
Cdd:cd02996    2 EIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEefpDAGKVVWGKVDCDKESDIADRYRINKYPT 81


                 ....*..
gi 568951425 118 LKLFFEG 124
Cdd:cd02996   82 LKLFRNG 88
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 399-486 2.21e-04

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: 40.76  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 399 LDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHSTVIIAKIDIT--ANDI--QLANPEQYPFFRLFpTDSQEAVMYK 474
Cdd:cd02997   14 LKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAAVDCTkpEHDAlkEEYNVKGFPTFKYF-ENGKFVEKYE 92

                         90
                 ....*....|..
gi 568951425 475 GEHTMKGFCDFL 486
Cdd:cd02997   93 GERTAEDIIEFM 104
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 385-470 2.83e-03

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: 37.63  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 385 PVKKLVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHS-TVIIAKIDiTAND--IQLANP---EQYP 458
Cdd:cd02992    2 PVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRpVVRVAAVD-CADEenVALCRDfgvTGYP 80

                         90
                 ....*....|..
gi 568951425 459 FFRLFPTDSQEA 470
Cdd:cd02992   81 TLRYFPPFSKEA 92
trxA PRK09381
thioredoxin TrxA;
389-447 3.11e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 37.74  E-value: 3.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568951425 389 LVGKNFNVVVLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHSTViiAKIDITAN 447
Cdd:PRK09381   8 LTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTV--AKLNIDQN 64
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 398-486 4.46e-03

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: 36.98  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 398 VLDKEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQN----HSTVIIAKIDITANDI--QLANPEQYPFFRLFPTDSQEAV 471
Cdd:cd02996   14 ILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEefpdAGKVVWGKVDCDKESDiaDRYRINKYPTLKLFRNGMMMKR 93

                         90
                 ....*....|....*
gi 568951425 472 MYKGEHTMKGFCDFL 486
Cdd:cd02996   94 EYRGQRSVEALAEFV 108
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 401-476 5.66e-03

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: 37.05  E-value: 5.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951425 401 KEKDVFVMFYAPWSEKCRVLLPLLEELGIKYQNHStVIIAKIDITANDIQLANPE----QYPFFRLFPTDSQEAVMYKGE 476
Cdd:cd02993   20 RNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSN-VKVAKFNADGEQREFAKEElqlkSFPTILFFPKNSRQPIKYPSE 98
 
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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