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Conserved domains on  [gi|31543902|ref|NP_058072|]
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thioredoxin-like protein 1 [Mus musculus]

Protein Classification

thioredoxin-like protein 1( domain architecture ID 10121417)

thioredoxin-like protein 1 (TXNL1) has a variety of functions, including cell signal transduction, cell cycle regulation, protein synthesis, modification and degradation, vesicle transport, transcriptional regulation, cell apoptosis, virus replication and oxidative stress regulation, etc., and plays an important role in the occurrence and development of human diseases.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PITH pfam06201
PITH domain; This family was formerly known as DUF1000. The full-length, Txnl1, protein which ...
 126-268 4.12e-58

PITH domain; This family was formerly known as DUF1000. The full-length, Txnl1, protein which is a probable component of the 26S proteasome, uses its C-terminal, PITH, domain to associate specifically with the 26S proteasome. PITH derives from proteasome-interacting thioredoxin domain.


:

Pssm-ID: 461848  Cd Length: 148  Bit Score: 182.80  E-value: 4.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902   126 LMPFINKAGCECLNESDEHGFDN----CLRKDMS-FLESDCDEQLLITVAFNQPVKLYSMKF---QGPDNGQGPKYVKIF 197
Cdd:pfam06201   1 LYSYIDLDKVECLNEDDEGSGKRfkpwDERLDDDkYLESDADEQLLIHIPFTGPVKLHSILIrtgTSSEEGSAPKTIKLF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543902   198 INLPRSMDFEEAErsePTQALELTEDDIKEDGIVPLRYVKFQNVNSVTLFVQSNQGEEETTRISYFTFIGT 268
Cdd:pfam06201  81 INRRDNLDFDDAE---PTQEIELTEEDDDGVVEYPLRFVKFQNVSSLTLFFEDNNGGDDVTRIYYIGLRGE 148
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 12-104 1.87e-22

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: 88.77  E-value: 1.87e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902  12 DFQPELSGAGsrLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQY 91
Cdd:cd02947   2 EFEELIKSAK--PVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                        90
                ....*....|....
gi 31543902  92 QGADAVG-LEEKIK 104
Cdd:cd02947  80 VGADPKEeLEEFLE 93
 
Name Accession Description Interval E-value
PITH pfam06201
PITH domain; This family was formerly known as DUF1000. The full-length, Txnl1, protein which ...
 126-268 4.12e-58

PITH domain; This family was formerly known as DUF1000. The full-length, Txnl1, protein which is a probable component of the 26S proteasome, uses its C-terminal, PITH, domain to associate specifically with the 26S proteasome. PITH derives from proteasome-interacting thioredoxin domain.


Pssm-ID: 461848  Cd Length: 148  Bit Score: 182.80  E-value: 4.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902   126 LMPFINKAGCECLNESDEHGFDN----CLRKDMS-FLESDCDEQLLITVAFNQPVKLYSMKF---QGPDNGQGPKYVKIF 197
Cdd:pfam06201   1 LYSYIDLDKVECLNEDDEGSGKRfkpwDERLDDDkYLESDADEQLLIHIPFTGPVKLHSILIrtgTSSEEGSAPKTIKLF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543902   198 INLPRSMDFEEAErsePTQALELTEDDIKEDGIVPLRYVKFQNVNSVTLFVQSNQGEEETTRISYFTFIGT 268
Cdd:pfam06201  81 INRRDNLDFDDAE---PTQEIELTEEDDDGVVEYPLRFVKFQNVSSLTLFFEDNNGGDDVTRIYYIGLRGE 148
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 12-104 1.87e-22

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: 88.77  E-value: 1.87e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902  12 DFQPELSGAGsrLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQY 91
Cdd:cd02947   2 EFEELIKSAK--PVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                        90
                ....*....|....
gi 31543902  92 QGADAVG-LEEKIK 104
Cdd:cd02947  80 VGADPKEeLEEFLE 93
PTZ00051 PTZ00051
thioredoxin; Provisional
 4-101 1.71e-19

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 81.46  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902    4 VKPVGSDPDFQPELSGagSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFR 83
Cdd:PTZ00051   2 VHIVTSQAEFESTLSQ--NELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFK 79

                         90
                 ....*....|....*...
gi 31543902   84 NKVRIDQYQGADAVGLEE 101
Cdd:PTZ00051  80 NGSVVDTLLGANDEALKQ 97
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 9-107 4.63e-15

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: 69.46  E-value: 4.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902   9 SDPDFQPELSGAGsRLAVVKFTMRGCGPCLRIAPAFSSMSNKY-PQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVR 87
Cdd:COG3118   6 TDENFEEEVLESD-KPVLVDFWAPWCGPCKMLAPVLEELAAEYgGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                        90       100
                ....*....|....*....|.
gi 31543902  88 IDQYQGA-DAVGLEEKIKQHL 107
Cdd:COG3118  85 VDRFVGAlPKEQLREFLDKVL 105
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 9-104 9.94e-15

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: 68.41  E-value: 9.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902     9 SDPDFQPELSgAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYP-QAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVR 87
Cdd:pfam00085   6 TDANFDEVVQ-KSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQP 84

                          90
                  ....*....|....*...
gi 31543902    88 IDQYQGA-DAVGLEEKIK 104
Cdd:pfam00085  85 VDDYVGArPKDALAAFLK 102
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 16-107 6.50e-12

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: 60.77  E-value: 6.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902    16 ELSGAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYP-QAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQYQGA 94
Cdd:TIGR01068   8 ETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEgKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGA 87

                          90
                  ....*....|....
gi 31543902    95 -DAVGLEEKIKQHL 107
Cdd:TIGR01068  88 lPKAALKQLINKNL 101
 
Name Accession Description Interval E-value
PITH pfam06201
PITH domain; This family was formerly known as DUF1000. The full-length, Txnl1, protein which ...
 126-268 4.12e-58

PITH domain; This family was formerly known as DUF1000. The full-length, Txnl1, protein which is a probable component of the 26S proteasome, uses its C-terminal, PITH, domain to associate specifically with the 26S proteasome. PITH derives from proteasome-interacting thioredoxin domain.


Pssm-ID: 461848  Cd Length: 148  Bit Score: 182.80  E-value: 4.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902   126 LMPFINKAGCECLNESDEHGFDN----CLRKDMS-FLESDCDEQLLITVAFNQPVKLYSMKF---QGPDNGQGPKYVKIF 197
Cdd:pfam06201   1 LYSYIDLDKVECLNEDDEGSGKRfkpwDERLDDDkYLESDADEQLLIHIPFTGPVKLHSILIrtgTSSEEGSAPKTIKLF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31543902   198 INLPRSMDFEEAErsePTQALELTEDDIKEDGIVPLRYVKFQNVNSVTLFVQSNQGEEETTRISYFTFIGT 268
Cdd:pfam06201  81 INRRDNLDFDDAE---PTQEIELTEEDDDGVVEYPLRFVKFQNVSSLTLFFEDNNGGDDVTRIYYIGLRGE 148
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 12-104 1.87e-22

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: 88.77  E-value: 1.87e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902  12 DFQPELSGAGsrLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQY 91
Cdd:cd02947   2 EFEELIKSAK--PVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                        90
                ....*....|....
gi 31543902  92 QGADAVG-LEEKIK 104
Cdd:cd02947  80 VGADPKEeLEEFLE 93
PTZ00051 PTZ00051
thioredoxin; Provisional
 4-101 1.71e-19

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 81.46  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902    4 VKPVGSDPDFQPELSGagSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFR 83
Cdd:PTZ00051   2 VHIVTSQAEFESTLSQ--NELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFK 79

                         90
                 ....*....|....*...
gi 31543902   84 NKVRIDQYQGADAVGLEE 101
Cdd:PTZ00051  80 NGSVVDTLLGANDEALKQ 97
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 9-107 4.63e-15

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: 69.46  E-value: 4.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902   9 SDPDFQPELSGAGsRLAVVKFTMRGCGPCLRIAPAFSSMSNKY-PQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVR 87
Cdd:COG3118   6 TDENFEEEVLESD-KPVLVDFWAPWCGPCKMLAPVLEELAAEYgGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                        90       100
                ....*....|....*....|.
gi 31543902  88 IDQYQGA-DAVGLEEKIKQHL 107
Cdd:COG3118  85 VDRFVGAlPKEQLREFLDKVL 105
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 9-104 9.94e-15

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: 68.41  E-value: 9.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902     9 SDPDFQPELSgAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYP-QAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVR 87
Cdd:pfam00085   6 TDANFDEVVQ-KSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQP 84

                          90
                  ....*....|....*...
gi 31543902    88 IDQYQGA-DAVGLEEKIK 104
Cdd:pfam00085  85 VDDYVGArPKDALAAFLK 102
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 16-107 6.50e-12

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: 60.77  E-value: 6.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902    16 ELSGAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYP-QAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQYQGA 94
Cdd:TIGR01068   8 ETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEgKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGA 87

                          90
                  ....*....|....
gi 31543902    95 -DAVGLEEKIKQHL 107
Cdd:TIGR01068  88 lPKAALKQLINKNL 101
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 9-104 1.42e-10

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: 56.90  E-value: 1.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902   9 SDPDFQPELSGAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNK-YPQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVR 87
Cdd:cd02984   1 SEEEFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80

                        90
                ....*....|....*..
gi 31543902  88 IDQYQGADAVGLEEKIK 104
Cdd:cd02984  81 VDRVSGADPKELAKKVE 97
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 23-93 7.12e-10

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: 55.20  E-value: 7.12e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543902  23 RLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAV-FLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQYQG 93
Cdd:cd02949  14 RLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVhFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISG 85
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 16-93 1.36e-06

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: 45.94  E-value: 1.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902  16 ELSGAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEV---DVHQCQGTAATNNISATPTFLFFRNKVRIDQYQ 92
Cdd:cd02985   9 ALKKAKGRLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVngdENDSTMELCRREKIIEVPHFLFYKDGEKIHEEE 88


                .
gi 31543902  93 G 93
Cdd:cd02985  89 G 89
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 20-93 1.74e-06

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: 45.68  E-value: 1.74e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543902  20 AGSRLAVVKFTMRGCGPCLRIAPAFSSMSNKY---PQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVR-IDQYQG 93
Cdd:cd02961  13 KDSKDVLVEFYAPWCGHCKALAPEYEKLAKELkgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNGSKePVKYEG 90
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 27-94 2.78e-06

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: 44.97  E-value: 2.78e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543902  27 VKFTMRGCGPCLRIAPAFSSMSNKY----PQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQYQGA 94
Cdd:cd03005  21 VKFFAPWCGHCKRLAPTWEQLAKKFnnenPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGT 92
PRK10996 PRK10996
thioredoxin 2; Provisional
 26-94 3.68e-05

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 42.75  E-value: 3.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902   26 VVKFTMRGCGPCLRIAPAFSSMS-NKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQYQGA 94
Cdd:PRK10996  56 VIDFWAPWCGPCRNFAPIFEDVAaERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNGA 125
trxA PRK09381
thioredoxin TrxA;
24-84 4.54e-05

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 41.97  E-value: 4.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543902   24 LAVVKFTMRGCGPCLRIAPAFSSMSNKYP-QAVFLEVDVHQCQGTAATNNISATPTFLFFRN 84
Cdd:PRK09381  23 AILVDFWAEWCGPCKMIAPILDEIADEYQgKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKN 84
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 24-105 1.84e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 42.82  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902   24 LAVVKFTMRGCGPCLRIAPAFSS----MSNKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQYQGADAVGL 99
Cdd:PTZ00102  51 IVLVKFYAPWCGHCKRLAPEYKKaakmLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGNPVNYSGGRTADGI 130


                 ....*.
gi 31543902  100 EEKIKQ 105
Cdd:PTZ00102 131 VSWIKK 136
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 26-91 8.36e-04

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: 37.29  E-value: 8.36e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902  26 VVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEVDV----HQCQgTAATNNISATPTFLFFRNKVRIDQY 91
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVdedpALEK-ELKRYGVGGVPTLVVFGPGIGVKYG 69
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 12-93 7.44e-03

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: 35.35  E-value: 7.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543902  12 DFqPELSGAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNK-YPQAVFLEVDVHQCQGTAATNNISATPTF-LFFRNKVRID 89
Cdd:cd03004  10 DF-PELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARAlKGKVKVGSVDCQKYESLCQQANIRAYPTIrLYPGNASKYH 88


                ....
gi 31543902  90 QYQG 93
Cdd:cd03004  89 SYNG 92
 
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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