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Conserved domains on  [gi|225579141|ref|NP_001139476|]
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thioredoxin domain-containing protein 2 isoform 1 [Rattus norvegicus]

Protein Classification

thioredoxin family protein( domain architecture ID 10121244)

thioredoxin family protein may function as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015035
PubMed:  11441809|15558583|12074972|30367780

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 454-547 2.32e-27

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: 105.33  E-value: 2.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 454 EEFEEVLKDAgeKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVGE 533
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....*
gi 225579141 534 FSGAL-VEKLEKSIA 547
Cdd:cd02947   79 VVGADpKEELEEFLE 93
PTZ00121 super family cl31754
MAEBL; Provisional
 151-466 1.82e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  151 REAEKPKSSEDLI----QSKKGDIFKPSEDsiQSKKGDMPKSSEDPIQSKKDDTAKSLEdtiQSKNGDMPKSSEdpiQSK 226
Cdd:PTZ00121 1451 KKAEEAKKAEEAKkkaeEAKKADEAKKKAE--EAKKADEAKKKAEEAKKKADEAKKAAE---AKKKADEAKKAE---EAK 1522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  227 KDDTARSLEdsiQSKKGDMPKSSDTIQSKESetpkfLQDTIQSKGGKINKQVKDSMKSKESKIRKPLKDSI--QSKENKI 304
Cdd:PTZ00121 1523 KADEAKKAE---EAKKADEAKKAEEKKKADE-----LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARI 1594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  305 PKSSQDSAQPKEGKIHKPLKDSLPSKEGDISKPSEDTIQAKEEITVSPEDTIQAKEEITMSPEDTIQAKEEITVSPEDTI 384
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  385 QAKEEITVSPEDTMQSKEEITVSPEDTVQSQEGDIKSSEDVQPSENEIFPFEAEIETLEEGMVRVIKDKEEFEEVLKDAG 464
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754


                  ..
gi 225579141  465 EK 466
Cdd:PTZ00121 1755 EK 1756
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 454-547 2.32e-27

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: 105.33  E-value: 2.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 454 EEFEEVLKDAgeKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVGE 533
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....*
gi 225579141 534 FSGAL-VEKLEKSIA 547
Cdd:cd02947   79 VVGADpKEELEEFLE 93
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 452-549 8.12e-23

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: 92.96  E-value: 8.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 452 DKEEFEE-VLKdaGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHED-VIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEE 529
Cdd:COG3118    6 TDENFEEeVLE--SDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQ 83

                         90       100
                 ....*....|....*....|.
gi 225579141 530 KVGEFSGAL-VEKLEKSIAEL 549
Cdd:COG3118   84 PVDRFVGALpKEQLREFLDKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 449-548 1.51e-21

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: 89.60  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  449 VIKDKEEFEEVLKDAgEKLVAVDFSAPWCGPCRKMRPHFHSLSLKH-EDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKN 527
Cdd:pfam00085   3 VVLTDANFDEVVQKS-SKPVLVDFYAPWCGPCKMLAPEYEELAQEYkGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|..
gi 225579141  528 EEKVGEFSGAL-VEKLEKSIAE 548
Cdd:pfam00085  82 GQPVDDYVGARpKDALAAFLKA 103
PTZ00051 PTZ00051
thioredoxin; Provisional
 446-543 6.85e-20

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 84.54  E-value: 6.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 446 MVRVIKDKEEFEEVLkdAGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFY 525
Cdd:PTZ00051   1 MVHIVTSQAEFESTL--SQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVF 78

                         90
                 ....*....|....*...
gi 225579141 526 KNEEKVGEFSGALVEKLE 543
Cdd:PTZ00051  79 KNGSVVDTLLGANDEALK 96
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 451-538 3.46e-13

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 65.77  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  451 KDKEEFEEVLKDaGEKLVAVDFSAPWCGPCRKMRPHFHSLSLK-HEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEE 529
Cdd:TIGR01068   1 LTDANFDETIAS-SDKPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGK 79


                  ....*....
gi 225579141  530 KVGEFSGAL 538
Cdd:TIGR01068  80 EVDRSVGAL 88
PTZ00121 PTZ00121
MAEBL; Provisional
 151-466 1.82e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  151 REAEKPKSSEDLI----QSKKGDIFKPSEDsiQSKKGDMPKSSEDPIQSKKDDTAKSLEdtiQSKNGDMPKSSEdpiQSK 226
Cdd:PTZ00121 1451 KKAEEAKKAEEAKkkaeEAKKADEAKKKAE--EAKKADEAKKKAEEAKKKADEAKKAAE---AKKKADEAKKAE---EAK 1522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  227 KDDTARSLEdsiQSKKGDMPKSSDTIQSKESetpkfLQDTIQSKGGKINKQVKDSMKSKESKIRKPLKDSI--QSKENKI 304
Cdd:PTZ00121 1523 KADEAKKAE---EAKKADEAKKAEEKKKADE-----LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARI 1594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  305 PKSSQDSAQPKEGKIHKPLKDSLPSKEGDISKPSEDTIQAKEEITVSPEDTIQAKEEITMSPEDTIQAKEEITVSPEDTI 384
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  385 QAKEEITVSPEDTMQSKEEITVSPEDTVQSQEGDIKSSEDVQPSENEIFPFEAEIETLEEGMVRVIKDKEEFEEVLKDAG 464
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754


                  ..
gi 225579141  465 EK 466
Cdd:PTZ00121 1755 EK 1756
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 454-547 2.32e-27

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: 105.33  E-value: 2.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 454 EEFEEVLKDAgeKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVGE 533
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....*
gi 225579141 534 FSGAL-VEKLEKSIA 547
Cdd:cd02947   79 VVGADpKEELEEFLE 93
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 452-549 8.12e-23

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: 92.96  E-value: 8.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 452 DKEEFEE-VLKdaGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHED-VIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEE 529
Cdd:COG3118    6 TDENFEEeVLE--SDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQ 83

                         90       100
                 ....*....|....*....|.
gi 225579141 530 KVGEFSGAL-VEKLEKSIAEL 549
Cdd:COG3118   84 PVDRFVGALpKEQLREFLDKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 449-548 1.51e-21

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: 89.60  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  449 VIKDKEEFEEVLKDAgEKLVAVDFSAPWCGPCRKMRPHFHSLSLKH-EDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKN 527
Cdd:pfam00085   3 VVLTDANFDEVVQKS-SKPVLVDFYAPWCGPCKMLAPEYEELAQEYkGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|..
gi 225579141  528 EEKVGEFSGAL-VEKLEKSIAE 548
Cdd:pfam00085  82 GQPVDDYVGARpKDALAAFLKA 103
PTZ00051 PTZ00051
thioredoxin; Provisional
 446-543 6.85e-20

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 84.54  E-value: 6.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 446 MVRVIKDKEEFEEVLkdAGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFY 525
Cdd:PTZ00051   1 MVHIVTSQAEFESTL--SQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVF 78

                         90
                 ....*....|....*...
gi 225579141 526 KNEEKVGEFSGALVEKLE 543
Cdd:PTZ00051  79 KNGSVVDTLLGANDEALK 96
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 452-536 1.53e-14

TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed of two TRX domains, a C-terminal TRX domain which contains a redox active CXXC motif and an N-terminal TRX-like domain which contains an SXXS sequence instead of the redox active motif. CDSP32 is a stress-inducible TRX, i.e., it acts as a TRX by reducing protein disulfides and is induced by environmental and oxidative stress conditions. It plays a critical role in plastid defense against oxidative damage, a role related to its function as a physiological electron donor to BAS1, a plastidic 2-cys peroxiredoxin. Plants lacking CDSP32 exhibit decreased photosystem II photochemical efficiencies and chlorophyll retention compared to WT controls, as well as an increased proportion of BAS1 in its overoxidized monomeric form.


Pssm-ID: 239283  Cd Length: 103  Bit Score: 69.44  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 452 DKEEFEEVLKDAGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEV---DTEDCEQLVQDCEVFHLPTFQFYKNE 528
Cdd:cd02985    2 SVEELDEALKKAKGRLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVngdENDSTMELCRREKIIEVPHFLFYKDG 81


                 ....*...
gi 225579141 529 EKVGEFSG 536
Cdd:cd02985   82 EKIHEEEG 89
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 452-536 9.09e-14

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: 67.25  E-value: 9.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 452 DKEEFEEVLKDagEKLVAVDFSAPWCGPCRKMRPHFHSLSLK---HEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKN- 527
Cdd:cd02961    4 TDDNFDELVKD--SKDVLVEFYAPWCGHCKALAPEYEKLAKElkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNg 81


                 ....*....
gi 225579141 528 EEKVGEFSG 536
Cdd:cd02961   82 SKEPVKYEG 90
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 451-538 3.46e-13

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 65.77  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  451 KDKEEFEEVLKDaGEKLVAVDFSAPWCGPCRKMRPHFHSLSLK-HEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEE 529
Cdd:TIGR01068   1 LTDANFDETIAS-SDKPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGK 79


                  ....*....
gi 225579141  530 KVGEFSGAL 538
Cdd:TIGR01068  80 EVDRSVGAL 88
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 453-547 1.70e-12

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


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 63.44  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 453 KEEFEEVLKDAGEKLVAVDFSAPWCGPCRKMRPHFHSLS-LKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKV 531
Cdd:cd02984    2 EEEFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAkEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIV 81

                         90
                 ....*....|....*.
gi 225579141 532 GEFSGALVEKLEKSIA 547
Cdd:cd02984   82 DRVSGADPKELAKKVE 97
PRK10996 PRK10996
thioredoxin 2; Provisional
 454-538 4.06e-11

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 60.85  E-value: 4.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 454 EEFEEVLKDagEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVI-FLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVG 532
Cdd:PRK10996  43 ETLDKLLQD--DLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVrFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVD 120


                 ....*.
gi 225579141 533 EFSGAL 538
Cdd:PRK10996 121 MLNGAV 126
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 460-549 1.42e-10

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 59.32  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 460 LKDAGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTED----------------------CEQLVQDCEVF 517
Cdd:COG0526   23 LADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDEnpeavkaflkelglpypvlldpDGELAKAYGVR 102

                         90       100       110
                 ....*....|....*....|....*....|....
gi 225579141 518 HLPTFQFY-KNEEKVGEFSGAL-VEKLEKSIAEL 549
Cdd:COG0526  103 GIPTTVLIdKDGKIVARHVGPLsPEELEEALEKL 136
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 470-531 5.63e-09

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 52.70  E-value: 5.63e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225579141 470 VDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDC---EQLVQDCEVFHLPTFQFYKNEEKV 531
Cdd:cd01659    2 VLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDpalEKELKRYGVGGVPTLVVFGPGIGV 66
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 452-548 2.39e-08

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: 51.93  E-value: 2.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 452 DKEEFEEVLKDagEKLVAVDFSAPWCGPCRKMRPHFH--SLSLKHE-DVIFLEVD-TEDCEQLVqdCEVFHL---PTFQF 524
Cdd:cd02997    6 TDEDFRKFLKK--EKHVLVMFYAPWCGHCKKMKPEFTkaATELKEDgKGVLAAVDcTKPEHDAL--KEEYNVkgfPTFKY 81

                         90       100
                 ....*....|....*....|....
gi 225579141 525 YKNEEKVGEFSGalvEKLEKSIAE 548
Cdd:cd02997   82 FENGKFVEKYEG---ERTAEDIIE 102
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 466-536 2.59e-08

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 51.73  E-value: 2.59e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225579141 466 KLVAVDFSAPWCGPCRKMRPHFHSLSLKH-EDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVGEFSG 536
Cdd:cd02949   14 RLILVLYTSPTCGPCRTLKPILNKVIDEFdGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISG 85
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 450-549 7.52e-08

TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are fusion proteins which contain one redox active TRX domain containing a CXXC motif and three NDPK domains, and are characterized as intermediate chains (ICs) of axonemal outer arm dynein. Dyneins are molecular motors that generate force against microtubules to produce cellular movement, and are divided into two classes: axonemal and cytoplasmic. They are supramolecular complexes consisting of three protein groups classified according to size: dynein heavy, intermediate and light chains. Axonemal dyneins form two structures, the inner and outer arms, which are attached to doublet microtubules throughout the cilia and flagella. The human homolog is the sperm-specific Sptrx-2, presumed to be a component of the human sperm axoneme architecture. Included in this group is another human protein, TRX-like protein 2, a smaller fusion protein containing one TRX and one NDPK domain, which is also associated with microtubular structures. The other members of this group are hypothetical insect proteins containing a TRX domain and outer arm dynein light chains (14 and 16kDa) of Chlamydomonas reinhardtii. Using standard assays, the fusion proteins have shown no TRX enzymatic activity.


Pssm-ID: 239246 [Multi-domain]  Cd Length: 102  Bit Score: 50.41  E-value: 7.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 450 IKDKEEFEEVLkdAGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFL----EVDT-EDCEQLVQDCEvfhlPTFQF 524
Cdd:cd02948    4 INNQEEWEELL--SNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELGDDLLHfataEADTiDTLKRYRGKCE----PTFLF 77

                         90       100
                 ....*....|....*....|....*
gi 225579141 525 YKNEEKVGEFSGALVEKLEKSIAEL 549
Cdd:cd02948   78 YKNGELVAVIRGANAPLLNKTITEL 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 470-537 1.28e-07

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: 49.98  E-value: 1.28e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225579141 470 VDFSAPWCGPCRKMRPHFHSLSLKHE----DVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVGEFSGA 537
Cdd:cd03005   21 VKFFAPWCGHCKRLAPTWEQLAKKFNnenpSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGT 92
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 435-537 5.24e-07

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 52.06  E-value: 5.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 435 FEAEIETLEEGMVRVIKDkEEFEEVLKDagEKLVAVDFSAPWCGPCRKMRPHFHS----LSLKHEDVIFLEVDTEDCEQL 510
Cdd:PTZ00102  22 FGSAEEHFISEHVTVLTD-STFDKFITE--NEIVLVKFYAPWCGHCKRLAPEYKKaakmLKEKKSEIVLASVDATEEMEL 98

                         90       100
                 ....*....|....*....|....*..
gi 225579141 511 VQDCEVFHLPTFQFYKNEEKVgEFSGA 537
Cdd:PTZ00102  99 AQEFGVRGYPTIKFFNKGNPV-NYSGG 124
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 452-537 1.93e-06

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: 46.47  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 452 DKEEFEEVLKDAGeKLVAVDFSAPWCGPCRKMRPHFHSLS---LKHEDVIFLEVDTEDCEQLVqdCEVFHL---PTFQFY 525
Cdd:cd02998    6 TDSNFDKVVGDDK-KDVLVEFYAPWCGHCKNLAPEYEKLAavfANEDDVVIAKVDADEANKDL--AKKYGVsgfPTLKFF 82

                         90
                 ....*....|...
gi 225579141 526 -KNEEKVGEFSGA 537
Cdd:cd02998   83 pKGSTEPVKYEGG 95
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 454-530 2.41e-06

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: 46.13  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 454 EEFEEVLKDAGEKLVaVDFSAPWCGPCRKMRPHFHSLS--LKHEdvifLEVDTEDC---EQLVQDCEVFHLPTFQFYKNE 528
Cdd:cd03004    9 EDFPELVLNRKEPWL-VDFYAPWCGPCQALLPELRKAAraLKGK----VKVGSVDCqkyESLCQQANIRAYPTIRLYPGN 83


                 ..
gi 225579141 529 EK 530
Cdd:cd03004   84 AS 85
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 445-536 6.58e-06

Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as cytosolic regulators of G protein functions. Phd and PhLPs specifically bind G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane and impeding G protein-mediated signal transduction by inhibiting the formation of a functional G protein trimer (G protein alphabetagamma). Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain. Also included in this family is a PhLP characterized as a viral inhibitor of apoptosis (IAP)-associated factor, named VIAF, that functions in caspase activation during apoptosis.


Pssm-ID: 239255 [Multi-domain]  Cd Length: 113  Bit Score: 45.24  E-value: 6.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 445 GMVRVIKDKEEFEEVLKDAGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEqLVQDCEVFHLPTFQF 524
Cdd:cd02957    4 GEVREISSKEFLEEVTKASKGTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKAF-LVNYLDIKVLPTLLV 82

                         90
                 ....*....|..
gi 225579141 525 YKNEEKVGEFSG 536
Cdd:cd02957   83 YKNGELIDNIVG 94
PTZ00121 PTZ00121
MAEBL; Provisional
 151-466 1.82e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  151 REAEKPKSSEDLI----QSKKGDIFKPSEDsiQSKKGDMPKSSEDPIQSKKDDTAKSLEdtiQSKNGDMPKSSEdpiQSK 226
Cdd:PTZ00121 1451 KKAEEAKKAEEAKkkaeEAKKADEAKKKAE--EAKKADEAKKKAEEAKKKADEAKKAAE---AKKKADEAKKAE---EAK 1522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  227 KDDTARSLEdsiQSKKGDMPKSSDTIQSKESetpkfLQDTIQSKGGKINKQVKDSMKSKESKIRKPLKDSI--QSKENKI 304
Cdd:PTZ00121 1523 KADEAKKAE---EAKKADEAKKAEEKKKADE-----LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARI 1594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  305 PKSSQDSAQPKEGKIHKPLKDSLPSKEGDISKPSEDTIQAKEEITVSPEDTIQAKEEITMSPEDTIQAKEEITVSPEDTI 384
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  385 QAKEEITVSPEDTMQSKEEITVSPEDTVQSQEGDIKSSEDVQPSENEIFPFEAEIETLEEGMVRVIKDKEEFEEVLKDAG 464
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754


                  ..
gi 225579141  465 EK 466
Cdd:PTZ00121 1755 EK 1756
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 456-538 3.14e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 44.12  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 456 FEEVLKDAGE--KLVAVDFSAPWCGPCRKM-RPHFHSLSLKH---EDVIFLEVD-------------TEDCEQLVQDCEV 516
Cdd:COG2143   29 LEEDLALAKAegKPILLFFESDWCPYCKKLhKEVFSDPEVAAylkENFVVVQLDaegdkevtdfdgeTLTEKELARKYGV 108

                         90       100
                 ....*....|....*....|...
gi 225579141 517 FHLPTFQFY-KNEEKVGEFSGAL 538
Cdd:COG2143  109 RGTPTLVFFdAEGKEIARIPGYL 131
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 456-530 7.73e-05

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: 41.77  E-value: 7.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225579141 456 FEEVLKDaGEKLVAVDFSAPWCGPCRKMRPHFHSL--SLK-HEDVIFLEVDTEDCEqlVQDCEVFH-LPTFQFYKNEEK 530
Cdd:cd02995   10 FDEVVLD-SDKDVLVEFYAPWCGHCKALAPIYEELaeKLKgDDNVVIAKMDATAND--VPSEFVVDgFPTILFFPAGDK 85
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 91-399 8.41e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.45  E-value: 8.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  91 KHEGSPKS-----------STKNTQLKQEDISKTSSYSKQTNSSNIPKSLAITTYPKQGSTLKPAANGTHDREAEKPKSS 159
Cdd:PTZ00449 506 KHDEPPEGpeasglppkapGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDP 585

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 160 edliqskkgdifKPSEDSIQSKKGDMPKSSEDPIQSKKDDTAKSLedtiqskngDMPKSSEDPIQSKKDDTARSLEDSIQ 239
Cdd:PTZ00449 586 ------------KHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELL---------DIPKSPKRPESPKSPKRPPPPQRPSS 644

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 240 SKKGDMPKSSDTIQSKESETPKFlqdTIQSKGGKINKQVKDSMKSKESKIRKPLKDSIQSkenkIPKSSQDSAQPKEGKI 319
Cdd:PTZ00449 645 PERPEGPKIIKSPKPPKSPKPPF---DPKFKEKFYDDYLDAAAKSKETKTTVVLDESFES----ILKETLPETPGTPFTT 717

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 320 HKPLKDSLPSKE-------GDISKPSEDTIqakEEITVSPEDTIQAKEEITMSPEDTIQAKEeitVSPEDtIQAKeeiTV 392
Cdd:PTZ00449 718 PRPLPPKLPRDEefpfepiGDPDAEQPDDI---EFFTPPEEERTFFHETPADTPLPDILAEE---FKEED-IHAE---TG 787


                 ....*..
gi 225579141 393 SPEDTMQ 399
Cdd:PTZ00449 788 EPDEAMK 794
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 453-537 8.84e-05

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 45.05  E-value: 8.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  453 KEEFEEVLKDAgeKLVAVDFSAPWCGPCRKMRPHFHS----LSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKN- 527
Cdd:TIGR01130   8 KDNFDDFIKSH--EFVLVEFYAPWCGHCKSLAPEYEKaadeLKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNg 85

                          90
                  ....*....|
gi 225579141  528 EEKVGEFSGA 537
Cdd:TIGR01130  86 EDSVSDYNGP 95
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 470-538 2.06e-04

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 41.55  E-value: 2.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225579141 470 VDFSAPWCGPCRKMRPHFHSLSLKHED---VIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNE-EKVGEFSGAL 538
Cdd:cd02950   25 VEFYADWCTVCQEMAPDVAKLKQKYGDqvnFVMLNVDNPKWLPEIDRYRVDGIPHFVFLDREgNEEGQSIGLQ 97
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 454-540 3.10e-04

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 39.95  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 454 EEFEEVLKDAGEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHED-VIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEEKVG 532
Cdd:cd02956    1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGqFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80


                 ....*...
gi 225579141 533 EFSGALVE 540
Cdd:cd02956   81 GFQGAQPE 88
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 460-506 6.93e-04

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 39.53  E-value: 6.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 225579141 460 LKDAGEKLVAVDFSAPWCGPCRKMRPHFHSLS--LKHEDVIFLEVDTED 506
Cdd:cd02966   14 LSDLKGKVVLVNFWASWCPPCRAEMPELEALAkeYKDDGVEVVGVNVDD 62
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 469-548 1.37e-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: 38.79  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 469 AVDFSAPWCGPCRKMRPHFHSLS---LKHEDVIFLEVdtEDC-----EQLVQDCEVFHLPTFQFYK---NEEKVG---EF 534
Cdd:cd02992   23 LVEFYASWCGHCRAFAPTWKKLArdlRKWRPVVRVAA--VDCadeenVALCRDFGVTGYPTLRYFPpfsKEATDGlkqEG 100

                         90
                 ....*....|....
gi 225579141 535 SGALVEKLEKSIAE 548
Cdd:cd02992  101 PERDVNELREALIL 114
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 452-491 1.53e-03

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: 38.50  E-value: 1.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 225579141 452 DKEEFEEVLKDAGeKLVAVDFSAPWCGPCRKMRPHFHSLS 491
Cdd:cd03002    6 TPKNFDKVVHNTN-YTTLVEFYAPWCGHCKNLKPEYAKAA 44
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
465-538 2.23e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.79  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  465 EKLVAVDFSAPWCGPCRKMR------PHFHSLSLKHEDVIFLEV-----------DTEDCEQLVQDCEVFHLPTFQFYKN 527
Cdd:pfam13098   4 GKPVLVVFTDPDCPYCKKLKkelledPDVTVYLGPNFVFIAVNIwcakevakaftDILENKELGRKYGVRGTPTIVFFDG 83

                          90
                  ....*....|.
gi 225579141  528 EEKVGEFSGAL 538
Cdd:pfam13098  84 KGELLRLPGYV 94
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 438-548 3.29e-03

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: 40.04  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141  438 EIETLEEGMVRVIKDKEeFEEVLKDAGeKLVAVDFSAPWCGPCRKMRPHFHSLSLKH----EDVIFLEVDTEDCEqlVQD 513
Cdd:TIGR01130 339 PIPEDDEGPVKVLVGKN-FDEIVLDET-KDVLVEFYAPWCGHCKNLAPIYEELAEKYkdaeSDVVIAKMDATAND--VPP 414

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 225579141  514 CEVFHLPTFQFYK---NEEKVGEFSGALVEKLEKSIAE 548
Cdd:TIGR01130 415 FEVEGFPTIKFVPagkKSEPVPYDGDRTLEDFSKFIAK 452
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 449-547 6.82e-03

Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; composed of predominantly uncharacterized eukaryotic proteins, containing a TRX-like domain without the redox active CXXC motif. The gene name for the human protein is TxnDC9. The two characterized members are described as Phd-like proteins, PLP1 of Saccharomyces cerevisiae and PhLP3 of Dictyostelium discoideum. Gene disruption experiments show that both PLP1 and PhLP3 are non-essential proteins. Unlike Phd and most Phd-like proteins, members of this group do not contain the Phd N-terminal helical domain which is implicated in binding to the G protein betagamma subunit.


Pssm-ID: 239287  Cd Length: 113  Bit Score: 36.78  E-value: 6.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 449 VIKDKEEFEEVLKdagEKLVAVDFSAPWCGPCRKMRPHFHSLSLKHEDVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNE 528
Cdd:cd02989    9 VSDEKEFFEIVKS---SERVVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVILFKNG 85

                         90       100       110
                 ....*....|....*....|....*....|.
gi 225579141 529 ---------EKVG---EFSgalVEKLEKSIA 547
Cdd:cd02989   86 ktvdrivgfEELGgkdDFS---TETLEKRLA 113
trxA PRK09381
thioredoxin TrxA;
458-547 9.80e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 36.20  E-value: 9.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579141 458 EVLKDAGekLVAVDFSAPWCGPCRKMRPHFHSLSLKHE-DVIFLEVDTEDCEQLVQDCEVFHLPTFQFYKNEE----KVG 532
Cdd:PRK09381  16 DVLKADG--AILVDFWAEWCGPCKMIAPILDEIADEYQgKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEvaatKVG 93

                         90
                 ....*....|....*.
gi 225579141 533 EFS-GALVEKLEKSIA 547
Cdd:PRK09381  94 ALSkGQLKEFLDANLA 109
 
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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