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Conserved domains on  [gi|499646106|ref|WP_011326840|]
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MULTISPECIES: thioredoxin TrxA [Pseudoalteromonas]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 1-108 4.89e-57

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


The actual alignment was detected with superfamily member PRK09381:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 109  Bit Score: 171.79  E-value: 4.89e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   1 MSEKIIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLL 80
Cdd:PRK09381   1 MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLL 80

                         90       100
                 ....*....|....*....|....*...
gi 499646106  81 LFKDGQVAATKVGALSKTQLIEFLENNL 108
Cdd:PRK09381  81 LFKNGEVAATKVGALSKGQLKEFLDANL 108
 
Name Accession Description Interval E-value
trxA PRK09381
thioredoxin TrxA;
1-108 4.89e-57

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 171.79  E-value: 4.89e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   1 MSEKIIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLL 80
Cdd:PRK09381   1 MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLL 80

                         90       100
                 ....*....|....*....|....*...
gi 499646106  81 LFKDGQVAATKVGALSKTQLIEFLENNL 108
Cdd:PRK09381  81 LFKNGEVAATKVGALSKGQLKEFLDANL 108
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 4-108 3.38e-56

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: 169.23  E-value: 3.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   4 KIIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFK 83
Cdd:COG3118    1 AVVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFK 80

                         90       100
                 ....*....|....*....|....*
gi 499646106  84 DGQVAATKVGALSKTQLIEFLENNL 108
Cdd:COG3118   81 DGQPVDRFVGALPKEQLREFLDKVL 105
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 8-108 3.24e-51

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: 156.68  E-value: 3.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106    8 ITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKDGQV 87
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                          90       100
                  ....*....|....*....|.
gi 499646106   88 AATKVGALSKTQLIEFLENNL 108
Cdd:TIGR01068  81 VDRSVGALPKAALKQLINKNL 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 5-105 1.12e-43

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: 137.36  E-value: 1.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106    5 IIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKD 84
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|.
gi 499646106   85 GQVAATKVGALSKTQLIEFLE 105
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAFLK 102
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 11-105 9.91e-38

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: 122.28  E-value: 9.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  11 DSFEADVLQSdKPVLVDFWAEWCGPCKMIAPILSEVAEEFdGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKDGQVAAT 90
Cdd:cd02947    1 EEFEELIKSA-KPVVVDFWAPWCGPCKAIAPVLEELAEEY-PKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....*
gi 499646106  91 KVGALSKTQLIEFLE 105
Cdd:cd02947   79 VVGADPKEELEEFLE 93
 
Name Accession Description Interval E-value
trxA PRK09381
thioredoxin TrxA;
1-108 4.89e-57

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 171.79  E-value: 4.89e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   1 MSEKIIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLL 80
Cdd:PRK09381   1 MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLL 80

                         90       100
                 ....*....|....*....|....*...
gi 499646106  81 LFKDGQVAATKVGALSKTQLIEFLENNL 108
Cdd:PRK09381  81 LFKNGEVAATKVGALSKGQLKEFLDANL 108
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 4-108 3.38e-56

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: 169.23  E-value: 3.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   4 KIIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFK 83
Cdd:COG3118    1 AVVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFK 80

                         90       100
                 ....*....|....*....|....*
gi 499646106  84 DGQVAATKVGALSKTQLIEFLENNL 108
Cdd:COG3118   81 DGQPVDRFVGALPKEQLREFLDKVL 105
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 8-108 3.24e-51

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: 156.68  E-value: 3.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106    8 ITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKDGQV 87
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                          90       100
                  ....*....|....*....|.
gi 499646106   88 AATKVGALSKTQLIEFLENNL 108
Cdd:TIGR01068  81 VDRSVGALPKAALKQLINKNL 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 5-105 1.12e-43

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: 137.36  E-value: 1.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106    5 IIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKD 84
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|.
gi 499646106   85 GQVAATKVGALSKTQLIEFLE 105
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAFLK 102
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 11-105 9.91e-38

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: 122.28  E-value: 9.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  11 DSFEADVLQSdKPVLVDFWAEWCGPCKMIAPILSEVAEEFdGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKDGQVAAT 90
Cdd:cd02947    1 EEFEELIKSA-KPVVVDFWAPWCGPCKAIAPVLEELAEEY-PKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....*
gi 499646106  91 KVGALSKTQLIEFLE 105
Cdd:cd02947   79 VVGADPKEELEEFLE 93
PRK10996 PRK10996
thioredoxin 2; Provisional
 4-108 2.21e-30

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 105.15  E-value: 2.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   4 KIIQITDDSFEAdVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFK 83
Cdd:PRK10996  36 EVINATGETLDK-LLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFK 114

                         90       100
                 ....*....|....*....|....*
gi 499646106  84 DGQVAATKVGALSKTQLIEFLENNL 108
Cdd:PRK10996 115 NGQVVDMLNGAVPKAPFDSWLNEAL 139
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 6-104 2.77e-27

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: 96.14  E-value: 2.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   6 IQITDDSFEaDVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEF--DGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFK 83
Cdd:cd02961    1 VELTDDNFD-ELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                         90       100
                 ....*....|....*....|..
gi 499646106  84 DGQVAATK-VGALSKTQLIEFL 104
Cdd:cd02961   80 NGSKEPVKyEGPRTLESLVEFI 101
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 20-108 1.42e-24

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 90.13  E-value: 1.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  20 SDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGrVTIAKLNIDQNAGTPPKF----------------------GIRGIP 77
Cdd:COG0526   27 KGKPVLVNFWATWCPPCRAEMPVLKELAEEYGG-VVFVGVDVDENPEAVKAFlkelglpypvlldpdgelakayGVRGIP 105

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499646106  78 TLLLF-KDGQVAATKVGALSKTQLIEFLENNL 108
Cdd:COG0526  106 TTVLIdKDGKIVARHVGPLSPEELEEALEKLL 137
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 5-90 1.67e-23

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: 86.57  E-value: 1.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   5 IIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKD 84
Cdd:cd03001    2 VVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFGA 81


                 ....*.
gi 499646106  85 GQVAAT 90
Cdd:cd03001   82 GKNSPQ 87
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 11-105 1.81e-23

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: 86.17  E-value: 1.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  11 DSFEADVLQSD-KPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKDGQVAA 89
Cdd:cd02956    1 QNFQQVLQESTqVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                         90
                 ....*....|....*.
gi 499646106  90 TKVGALSKTQLIEFLE 105
Cdd:cd02956   81 GFQGAQPEEQLRQMLD 96
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 5-104 5.32e-20

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: 77.68  E-value: 5.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   5 IIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGR--VTIAKLNIDQ-NAGTPPKFGIRGIPTLLL 81
Cdd:cd02998    2 VVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEddVVIAKVDADEaNKDLAKKYGVSGFPTLKF 81

                         90       100
                 ....*....|....*....|....
gi 499646106  82 FKDGQVAATKV-GALSKTQLIEFL 104
Cdd:cd02998   82 FPKGSTEPVKYeGGRDLEDLVKFV 105
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 8-103 2.06e-19

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: 76.06  E-value: 2.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   8 ITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGR--VTIAKLNIDQNAgTPPKFGIRGIPTLLLFKdg 85
Cdd:cd02995    5 VVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDdnVVIAKMDATAND-VPSEFVVDGFPTILFFP-- 81

                         90
                 ....*....|....*...
gi 499646106  86 qvaatkvgALSKTQLIEF 103
Cdd:cd02995   82 --------AGDKSNPIKY 91
PTZ00051 PTZ00051
thioredoxin; Provisional
 9-94 7.08e-19

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 74.53  E-value: 7.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   9 TDDSFEAdVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFdGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKDGQVA 88
Cdd:PTZ00051   7 SQAEFES-TLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEY-TKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSVV 84


                 ....*.
gi 499646106  89 ATKVGA 94
Cdd:PTZ00051  85 DTLLGA 90
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 3-104 4.57e-18

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: 77.79  E-value: 4.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106    3 EKIIQITDDSFEaDVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEF---DGRVTIAKLNIDQNAGTPPKFGIRGIPTL 79
Cdd:TIGR01130   1 EDVLVLTKDNFD-DFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELkkkGPPIKLAKVDATEEKDLAQKYGVSGYPTL 79

                          90       100
                  ....*....|....*....|....*.
gi 499646106   80 LLFKDGQVAATKV-GALSKTQLIEFL 104
Cdd:TIGR01130  80 KIFRNGEDSVSDYnGPRDADGIVKYM 105
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 5-104 7.52e-18

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: 71.97  E-value: 7.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   5 IIQITDDSFEaDVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEF--DGRVTIAKLNI--DQNAGTPPKFGIRGIPTLL 80
Cdd:cd02997    2 VVHLTDEDFR-KFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELkeDGKGVLAAVDCtkPEHDALKEEYNVKGFPTFK 80

                         90       100
                 ....*....|....*....|....
gi 499646106  81 LFKDGQVAATKVGALSKTQLIEFL 104
Cdd:cd02997   81 YFENGKFVEKYEGERTAEDIIEFM 104
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 19-105 9.52e-18

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: 71.76  E-value: 9.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  19 QSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKDGQVAATKVGALSKT 98
Cdd:cd02949   11 ESDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVKMKS 90


                 ....*..
gi 499646106  99 QLIEFLE 105
Cdd:cd02949   91 EYREFIE 97
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 5-107 8.57e-17

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 72.35  E-value: 8.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   5 IIQITDDSFE----ADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLL 80
Cdd:PTZ00443  32 LVLLNDKNFEkltqASTGATTGPWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLL 111

                         90       100
                 ....*....|....*....|....*..
gi 499646106  81 LFKDGQVAATKVGALSKTQLIEFLENN 107
Cdd:PTZ00443 112 LFDKGKMYQYEGGDRSTEKLAAFALGD 138
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 4-86 9.01e-17

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: 69.24  E-value: 9.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   4 KIIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFK 83
Cdd:cd03004    2 SVITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYP 81


                 ...
gi 499646106  84 DGQ 86
Cdd:cd03004   82 GNA 84
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 11-85 1.46e-16

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: 73.56  E-value: 1.46e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499646106   11 DSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEF---DGRVTIAKLNIDQNagTPPKFGIRGIPTLLLFKDG 85
Cdd:TIGR01130 354 KNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYkdaESDVVIAKMDATAN--DVPPFEVEGFPTIKFVPAG 429
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 7-86 2.34e-16

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: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   7 QITDDSFEADVlqSDKPVLVDFWAEWCGPCKMIAPILSEVAEEF---DGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFK 83
Cdd:cd03005    4 ELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFnneNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFK 81


                 ...
gi 499646106  84 DGQ 86
Cdd:cd03005   82 DGE 84
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 12-107 6.79e-16

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 71.71  E-value: 6.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  12 SFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEF--DGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKDGQVAA 89
Cdd:PTZ00102 366 TFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYkdNDSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGERTP 445

                         90
                 ....*....|....*....
gi 499646106  90 TKV-GALSKTQLIEFLENN 107
Cdd:PTZ00102 446 IPYeGERTVEGFKEFVNKH 464
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 22-93 1.15e-14

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: 64.18  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  22 KPVLVDFWAEWCGPCKMIAPILSEVAEEFDGR----VTIA--------------KLNI------DQNAGTPPKFGIRGIP 77
Cdd:cd02966   20 KVVLVNFWASWCPPCRAEMPELEALAKEYKDDgvevVGVNvddddpaavkaflkKYGItfpvllDPDGELAKAYGVRGLP 99

                         90
                 ....*....|....*..
gi 499646106  78 TLLLF-KDGQVAATKVG 93
Cdd:cd02966  100 TTFLIdRDGRIRARHVG 116
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 10-103 1.21e-14

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: 64.01  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  10 DDSFEaDVLQSDKpVLVDFWAEWCGPCKMIAPILSEVAEEFDGR---VTIAKLNIDQNAGTPPKFGIRGIPTLLLFKdGQ 86
Cdd:cd03000    6 DDSFK-DVRKEDI-WLVDFYAPWCGHCKKLEPVWNEVGAELKSSgspVRVGKLDATAYSSIASEFGVRGYPTIKLLK-GD 82

                         90
                 ....*....|....*..
gi 499646106  87 VAATKVGALSKTQLIEF 103
Cdd:cd03000   83 LAYNYRGPRTKDDIVEF 99
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 4-88 1.80e-14

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: 63.54  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   4 KIIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTP--PKFGIRGIPTLLL 81
Cdd:cd03002    1 PVYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKNKPlcGKYGVQGFPTLKV 80


                 ....*..
gi 499646106  82 FKDGQVA 88
Cdd:cd03002   81 FRPPKKA 87
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 5-104 2.81e-14

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: 63.18  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   5 IIQITDDSFEaDVLQSDKPVLVDFWAEWCGPCKMIAPILSEVA----EEF--DGRVTIAKLNIDQNAGTPPKFGIRGIPT 78
Cdd:cd02996    3 IVSLTSGNID-DILQSAELVLVNFYADWCRFSQMLHPIFEEAAakikEEFpdAGKVVWGKVDCDKESDIADRYRINKYPT 81

                         90       100
                 ....*....|....*....|....*..
gi 499646106  79 LLLFKDGQVAATKV-GALSKTQLIEFL 104
Cdd:cd02996   82 LKLFRNGMMMKREYrGQRSVEALAEFV 108
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 2-85 2.92e-14

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 67.08  E-value: 2.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   2 SEKIIQITDDSFEaDVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFD---GRVTIAKLNIDQNAGTPPKFGIRGIPT 78
Cdd:PTZ00102  31 SEHVTVLTDSTFD-KFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkSEIVLASVDATEEMELAQEFGVRGYPT 109


                 ....*..
gi 499646106  79 LLLFKDG 85
Cdd:PTZ00102 110 IKFFNKG 116
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 18-106 3.44e-13

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: 61.20  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  18 LQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPP--KFGIRGIPTLLLF-KDGQVAATKVGA 94
Cdd:cd02950   17 LSNGKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVDNPKWLPEidRYRVDGIPHFVFLdREGNEEGQSIGL 96

                         90
                 ....*....|..
gi 499646106  95 LSKTQLIEFLEN 106
Cdd:cd02950   97 QPKQVLAQNLDA 108
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 19-94 7.07e-13

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: 59.21  E-value: 7.07e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499646106  19 QSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKDGQVAATKVGA 94
Cdd:cd02984   12 DASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDRVSGA 87
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 3-83 6.78e-12

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: 57.28  E-value: 6.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   3 EKIIQITDDSFEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFD---GRVTIAKLN--IDQNAGTPPKFGIRGIP 77
Cdd:cd02992    1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDcaDEENVALCRDFGVTGYP 80


                 ....*.
gi 499646106  78 TLLLFK 83
Cdd:cd02992   81 TLRYFP 86
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 19-105 1.27e-11

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 57.22  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  19 QSDKPVLVDFWAEWCGPC-KMIAPILS--EVAEEFDGRVTIAKLNIDQNAG--TPP-----------KFGIRGIPTLLLF 82
Cdd:COG2143   38 AEGKPILLFFESDWCPYCkKLHKEVFSdpEVAAYLKENFVVVQLDAEGDKEvtDFDgetltekelarKYGVRGTPTLVFF 117

                         90       100
                 ....*....|....*....|....
gi 499646106  83 -KDGQVAATKVGALSKTQLIEFLE 105
Cdd:COG2143  118 dAEGKEIARIPGYLKPETFLALLK 141
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 18-105 3.94e-11

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


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 54.92  E-value: 3.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  18 LQSDKPVLVDFWAEWCGPCKMIAPIL---SEVAEEFDGRVTIAKLNI----DQNAGTPPKFGIRGIPTLLLF--KDGQVA 88
Cdd:cd02953    8 LAQGKPVFVDFTADWCVTCKVNEKVVfsdPEVQAALKKDVVLLRADWtkndPEITALLKRFGVFGPPTYLFYgpGGEPEP 87

                         90
                 ....*....|....*..
gi 499646106  89 ATKVGALSKTQLIEFLE 105
Cdd:cd02953   88 LRLPGFLTADEFLEALE 104
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 25-87 4.22e-11

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: 53.86  E-value: 4.22e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499646106  25 LVDFWAEWCGPCKMIAPILSEVAEEFDGrVTIAKLNIDQNAGTPP---KFGIRGIPTLLLFKDGQV 87
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKG-VKFEAVDVDEDPALEKelkRYGVGGVPTLVVFGPGIG 65
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
21-108 4.75e-11

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 55.26  E-value: 4.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  21 DKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGR-VTI---------------AKLNI------DQNAGTPPKFGIRGIPT 78
Cdd:COG1225   21 GKPVVLYFYATWCPGCTAELPELRDLYEEFKDKgVEVlgvssdsdeahkkfaEKYGLpfpllsDPDGEVAKAYGVRGTPT 100

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499646106  79 LLLF-KDGQVAATKVGALS-KTQLIEFLENNL 108
Cdd:COG1225  101 TFLIdPDGKIRYVWVGPVDpRPHLEEVLEALL 132
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 15-106 8.19e-11

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 57.12  E-value: 8.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  15 ADVLQSDKPVLVDFWAEWCGPCK-MIAPILS--EVAEEFDGRVTIAKLNIDQNagTPP------KFGIRGIPTLLLF-KD 84
Cdd:COG4232  314 AEARAEGKPVFVDFTADWCVTCKeNERTVFSdpEVQAALADDVVLLKADVTDN--DPEitallkRFGRFGVPTYVFYdPD 391

                         90       100
                 ....*....|....*....|..
gi 499646106  85 GQVAATKVGALSKTQLIEFLEN 106
Cdd:COG4232  392 GEELPRLGFMLTADEFLAALEK 413
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 19-96 1.21e-10

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 54.23  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  19 QSDKPVLVDFWAEWCGPCKMIAPILSEVAEEF-----------DGRVT--IAK-------LNiDQNAGTPPKFGIRGIPT 78
Cdd:cd03011   18 LSGKPVLVYFWATWCPVCRFTSPTVNQLAADYpvvsvalrsgdDGAVArfMQKkgygfpvIN-DPDGVISARWGVSVTPA 96

                         90
                 ....*....|....*...
gi 499646106  79 LLLFKDGQVAATKVGALS 96
Cdd:cd03011   97 IVIVDPGGIVFVTTGVTS 114
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 8-106 1.53e-09

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 50.84  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   8 ITDDSFEADVL-QS-DKPVLVDFWAEWCGPCKMIAPILSEVAEEFDG-RVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKD 84
Cdd:cd02963    9 LTFSQYENEIVpKSfKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPlGVGIATVNAGHERRLARKLGAHSVPAIVGIIN 88

                         90       100
                 ....*....|....*....|..
gi 499646106  85 GQVAATKVGALSKTQLIEFLEN 106
Cdd:cd02963   89 GQVTFYHDSSFTKQHVVDFVRK 110
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 21-87 7.06e-09

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


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 48.84  E-value: 7.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   21 DKPVLVDFWAEWCGPCKMIAPILSEVAEEF--DGRVTIAKLNIDQNA-------------------GTPP------KFGI 73
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLkkKKNVEIVFVSLDRDLeefkdylkkmpkdwlsvpfDDDErnelkrKYGV 80

                          90
                  ....*....|....*
gi 499646106   74 RGIPTLLLF-KDGQV 87
Cdd:pfam13905  81 NAIPTLVLLdPNGEV 95
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 7-95 1.50e-08

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 48.73  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   7 QITDDSFEadvlqsDKPVLVDFWAEWCGPCKMIAPILSEVAEEfdGRVTIAKLNI-DQNA---------GTP-------- 68
Cdd:cd03010   17 TLTSADLK------GKPYLLNVWASWCAPCREEHPVLMALARQ--GRVPIYGINYkDNPEnalawlarhGNPyaavgfdp 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499646106  69 -----PKFGIRGIP-TLLLFKDGQVAATKVGAL 95
Cdd:cd03010   89 dgrvgIDLGVYGVPeTFLIDGDGIIRYKHVGPL 121
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 4-105 1.78e-08

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


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 48.14  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   4 KIIQITDDSFEaDVLQSDKpvLVDFWAEWCGPCKMIAPILSEVAEEFDG-RVTIAKLNIDQNAGTPPKFGIRGIPTLLLF 82
Cdd:cd02994    2 NVVELTDSNWT-LVLEGEW--MIEFYAPWCPACQQLQPEWEEFADWSDDlGINVAKVDVTQEPGLSGRFFVTALPTIYHA 78

                         90       100
                 ....*....|....*....|...
gi 499646106  83 KDGqVAATKVGALSKTQLIEFLE 105
Cdd:cd02994   79 KDG-VFRRYQGPRDKEDLISFIE 100
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
22-104 3.45e-08

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 47.42  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   22 KPVLVDFWAEWCGPCKMIAPILSE---VAEEFDGRVTIAKLNIDQNAGTP-------------PKFGIRGIPTLLLFKDG 85
Cdd:pfam13098   5 KPVLVVFTDPDCPYCKKLKKELLEdpdVTVYLGPNFVFIAVNIWCAKEVAkaftdilenkelgRKYGVRGTPTIVFFDGK 84

                          90
                  ....*....|....*....
gi 499646106   86 QVAATKVGALSKTQLIEFL 104
Cdd:pfam13098  85 GELLRLPGYVPAEEFLALL 103
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 13-85 1.37e-07

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 47.08  E-value: 1.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499646106   13 FEADVLQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEfdgRVTIAKLNIDQNAGTPPKF-GIRGIPTLLLFKDG 85
Cdd:TIGR00385  55 YTADVLTQGKPVLLNVWASWCPPCRAEHPYLNELAKQ---GLPIVGVDYKDDRQNAIKFlKELGNPYQLSLFDP 125
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 2-108 2.92e-07

TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail.


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 45.84  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   2 SEKIIQITDDSFEaDVLQSDKPV--LVDFWAEWCGPCKMIAPILSEVAEEFDGR-VTIAKLNIDQNAGTPPKFGI----- 73
Cdd:cd02962   27 PEHIKYFTPKTLE-EELERDKRVtwLVEFFTTWSPECVNFAPVFAELSLKYNNNnLKFGKIDIGRFPNVAEKFRVstspl 105

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499646106  74 -RGIPTLLLFKDGQVAA---TKVGALSKTQLIEFLENNL 108
Cdd:cd02962  106 sKQLPTIILFQGGKEVArrpYYNDSKGRAVPFTFSKENV 144
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
22-105 2.14e-06

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 43.84  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  22 KPVLVDFWAEWCGPCKMIAPILSEVAEEF-DGRVTIAKLNIDQNAGTPPKF----------------------GIRGIPT 78
Cdd:PRK03147  62 KGVFLNFWGTWCKPCEKEMPYMNELYPKYkEKGVEIIAVNVDETELAVKNFvnrygltfpvaidkgrqvidayGVGPLPT 141

                         90       100
                 ....*....|....*....|....*...
gi 499646106  79 LLLF-KDGQVAATKVGALSKTQLIEFLE 105
Cdd:PRK03147 142 TFLIdKDGKVVKVITGEMTEEQLEEYLE 169
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 4-103 2.44e-06

PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 42.51  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   4 KIIQITDDSFEADVlQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFK 83
Cdd:cd03003    2 EIVTLDRGDFDAAV-NSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFP 80

                         90       100
                 ....*....|....*....|
gi 499646106  84 DGQVAATKVGALSKTQLIEF 103
Cdd:cd03003   81 SGMNPEKYYGDRSKESLVKF 100
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 24-82 3.57e-06

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


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 41.96  E-value: 3.57e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499646106  24 VLVDFWAEWCGPCKMIAPILSEVAEEFDgrvTIAKLNIDQNAGTP---PKFGIRGIPTLLLF 82
Cdd:cd02999   21 TAVLFYASWCPFSASFRPHFNALSSMFP---QIRHLAIEESSIKPsllSRYGVVGFPTILLF 79
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 22-92 1.18e-05

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 41.06  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  22 KPVLVDFWAEWCGPCKMIAPILSEVAEEFdgRVTIAKLNI-----DQN--------AGTPP-----------------KF 71
Cdd:cd02964   18 KTVGLYFSASWCPPCRAFTPKLVEFYEKL--KEEGKNFEIvfvsrDRSeesfneyfSEMPPwlavpfedeelrellekQF 95

                         90       100
                 ....*....|....*....|..
gi 499646106  72 GIRGIPTLLLFK-DGQVAATKV 92
Cdd:cd02964   96 KVEGIPTLVVLKpDGDVVTTNA 117
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 6-106 2.18e-05

bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide reductase MsrB;


Pssm-ID: 184456 [Multi-domain]  Cd Length: 521  Bit Score: 41.78  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   6 IQITDDSFEADVLQSDKPVLVDFWAEWCGPCkmiapiLSEVAE--------EFDGR--VTIA------------------ 57
Cdd:PRK14018  41 LKTADNRPASVYLKKDKPTLIKFWASWCPLC------LSELGEtekwaqdaKFSSAnlITVAspgflhekkdgdfqkwya 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499646106  58 -------KLNIDQNAGTPPKFGIRGIPT-LLLFKDGQVAATKVGALSKTQLIEFLEN 106
Cdd:PRK14018 115 gldypklPVLTDNGGTLAQSLNISVYPSwAIIGKDGDVQRIVKGSISEAQALALIRN 171
PHA02125 PHA02125
thioredoxin-like protein
 28-80 2.91e-05

thioredoxin-like protein


Pssm-ID: 133998 [Multi-domain]  Cd Length: 75  Bit Score: 39.19  E-value: 2.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499646106  28 FWAEWCGPCKMIAPILSEVaeefdgRVTIAKLNIDQNAGTPPKFGIRGIPTLL 80
Cdd:PHA02125   5 FGAEWCANCKMVKPMLANV------EYTYVDVDTDEGVELTAKHHIRSLPTLV 51
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 4-93 3.45e-05

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: 39.46  E-value: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   4 KIIQITDDSFEADVLQSDK--PVLVDFWAEWCGPCKMIAPILSEVAEEFdgrVTIAKLNID-QNAGTPPKFGIRGIPTLL 80
Cdd:cd02957    5 EVREISSKEFLEEVTKASKgtRVVVHFYEPGFPRCKILDSHLEELAAKY---PETKFVKINaEKAFLVNYLDIKVLPTLL 81

                         90
                 ....*....|...
gi 499646106  81 LFKDGQVAATKVG 93
Cdd:cd02957   82 VYKNGELIDNIVG 94
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 22-92 3.47e-05

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 39.96  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  22 KPVLVDFWAEWCGPCKMIAPILSEVAEEFdgRVTIAKLNI-----DQN--------AGTP----P------------KFG 72
Cdd:cd03009   19 KTVGLYFSASWCPPCRAFTPKLVEFYEKL--KESGKNFEIvfiswDRDeesfndyfSKMPwlavPfsdrerrsrlnrTFK 96

                         90       100
                 ....*....|....*....|.
gi 499646106  73 IRGIPTLLLFK-DGQVAATKV 92
Cdd:cd03009   97 IEGIPTLIILDaDGEVVTTDA 117
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 13-37 4.14e-05

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 40.36  E-value: 4.14e-05
                         10        20
                 ....*....|....*....|....*
gi 499646106  13 FEADVLQSDKPVLVDFWAEWCGPCK 37
Cdd:PRK15412  60 YQADVLTQGKPVLLNVWATWCPTCR 84
dipZ PRK00293
thiol:disulfide interchange protein precursor; Provisional
 19-86 1.74e-04

thiol:disulfide interchange protein precursor; Provisional


Pssm-ID: 234717 [Multi-domain]  Cd Length: 571  Bit Score: 39.04  E-value: 1.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499646106  19 QSDKPVLVDFWAEWCGPCKMIAPIL---SEVAEEFDGRVTiakLNIDQNAGTP------PKFGIRGIPTLLLF-KDGQ 86
Cdd:PRK00293 472 GKGKPVMLDLYADWCVACKEFEKYTfsdPQVQQALADTVL---LQADVTANNAedvallKHYNVLGLPTILFFdAQGQ 546
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 19-82 2.97e-04

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


Pssm-ID: 433567 [Multi-domain]  Cd Length: 84  Bit Score: 36.57  E-value: 2.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499646106   19 QSDKPVLVDFWAEWCGPCKMIAPIL---SEVAEEFDGRVTIAKLNIDQ-NAGTPPKFGIRGIPTLLLF 82
Cdd:pfam13899  15 ERGKPVLVDFGADWCFTCQVLERDFlshEEVKAALAKNFVLLRLDWTSrDANITRAFDGQGVPHIAFL 82
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
 2-82 3.32e-04

OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of eight ER proteins that transfers core oligosaccharide from dolichol carrier to Asn-X-Ser/Thr motifs. This family includes both OST3 and OST6, each of which contains four predicted transmembrane helices. Disruption of OST3 and OST6 leads to a defect in the assembly of the complex. Hence, the function of these genes seems to be essential for recruiting a fully active complex necessary for efficient N-glycosylation. These proteins are also thought to be novel Mg2+ transporters.


Pssm-ID: 461420  Cd Length: 294  Bit Score: 38.00  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106    2 SEKIIQITDDSFEaDVLQSDKP--VLVDFWAEW----CGPCKMIAPILSEVA-------EEFDGRVTIAKLNIDQNAGTP 68
Cdd:pfam04756  10 SNGVIKLNDSNYK-RLLSGPRDysVVVLLTALDprfgCQLCREFQPEFELVAkswfkdhKAGSSKLFFATLDFDDGKDVF 88

                          90
                  ....*....|....
gi 499646106   69 PKFGIRGIPTLLLF 82
Cdd:pfam04756  89 QSLGLQTAPHLLLF 102
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 25-102 4.73e-04

F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor.


Pssm-ID: 433436 [Multi-domain]  Cd Length: 224  Bit Score: 37.67  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106   25 LVDFWAEWCGPCKMIAPILSEVAEEF---------DGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLF--KDGQVAATKVG 93
Cdd:pfam13728 133 LIFFYRGDCPYCEAQAPILQAFADKYgwtvrpvsvDGRPLPGFPNYRVDNGQAARLGVKRTPALFLVnpPSGDVVPVAAG 212


                  ....*....
gi 499646106   94 ALSKTQLIE 102
Cdd:pfam13728 213 VLSLDELEE 221
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 20-82 1.16e-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: 35.51  E-value: 1.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499646106  20 SDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGR-VTIAKLNID--QNAGTPPKFGIRGIPTLLLF 82
Cdd:cd02993   20 RNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSnVKVAKFNADgeQREFAKEELQLKSFPTILFF 85
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 22-101 1.22e-03

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: 35.54  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  22 KPVLVDFWAEWCGPCKMIAPILSEVAEEFDgRVTIAKLNIDQNAGTPP---KFGIRGIPTLLLFKDGQVAATKVGaLSKT 98
Cdd:cd02985   16 RLVVLEFALKHSGPSVKIYPTMVKLSRTCN-DVVFLLVNGDENDSTMElcrREKIIEVPHFLFYKDGEKIHEEEG-IGPD 93


                 ...
gi 499646106  99 QLI 101
Cdd:cd02985   94 ELI 96
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 21-62 1.27e-03

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 35.66  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 499646106   21 DKPVLVDFWAE-WCGPCKMIAPILSEVAEEFDGR-VTIAKLNID 62
Cdd:pfam00578  25 GKWVVLFFYPAdWTPVCTTELPALADLYEEFKKLgVEVLGVSVD 68
PLN02309 PLN02309
5'-adenylylsulfate reductase
 21-82 1.46e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 36.31  E-value: 1.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499646106  21 DKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGR-VTIAKLNID--QNAGTPPKFGIRGIPTLLLF 82
Cdd:PLN02309 365 KEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSgVKVAKFRADgdQKEFAKQELQLGSFPTILLF 429
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 18-94 3.20e-03

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: 34.23  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499646106  18 LQSDKPVLVDFWAEWCGPCKMIAPILSEVAEEFDGRV----TIAKLNIDqnagTPPKFGIRGIPTLLLFKDGQVAATKVG 93
Cdd:cd02948   14 LSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELGDDLlhfaTAEADTID----TLKRYRGKCEPTFLFYKNGELVAVIRG 89


                 .
gi 499646106  94 A 94
Cdd:cd02948   90 A 90
HyaE cd02965
HyaE family; HyaE is also called HupG and HoxO. They are proteins serving a critical role in ...
 39-97 4.64e-03

HyaE family; HyaE is also called HupG and HoxO. They are proteins serving a critical role in the assembly of multimeric [NiFe] hydrogenases, the enzymes that catalyze the oxidation of molecular hydrogen to enable microorganisms to utilize hydrogen as the sole energy source. The E. coli HyaE protein is a chaperone that specifically interacts with the twin-arginine translocation (Tat) signal peptide of the [NiFe] hydrogenase-1 beta subunit precursor. Tat signal peptides target precursor proteins to the Tat protein export system, which facilitates the transport of fully folded proteins across the inner membrane. HyaE may be involved in regulating the traffic of [NiFe] hydrogenase-1 on the Tat transport pathway.


Pssm-ID: 239263  Cd Length: 111  Bit Score: 33.82  E-value: 4.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499646106  39 IAPILSEVAEEFDGRVTIAKLNIDQNAGTPPKFGIRGIPTLLLFKDGQVaatkVGALSK 97
Cdd:cd02965   47 VAVVLPELLKAFPGRFRAAVVGRADEQALAARFGVLRTPALLFFRDGRY----VGVLAG 101
 
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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