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Conserved domains on  [gi|558611330|ref|NP_001273875|]
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thioredoxin domain-containing protein 8 isoform b [Homo sapiens]

Protein Classification

thioredoxin family protein( domain architecture ID 10121244)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 10-66 3.30e-11

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: 54.49  E-value: 3.30e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558611330 10 EFKTFLTAAghKLAVVQFSSKRCGPCKRMFPVFHELAET--------------------CHIKTIPTFQMFKKSQKV 66
Cdd:cd02947   2 EFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEypkvkfvkvdvdenpelaeeYGVRSIPTFLFFKNGKEV 76
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 10-66 3.30e-11

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: 54.49  E-value: 3.30e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558611330 10 EFKTFLTAAghKLAVVQFSSKRCGPCKRMFPVFHELAET--------------------CHIKTIPTFQMFKKSQKV 66
Cdd:cd02947   2 EFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEypkvkfvkvdvdenpelaeeYGVRSIPTFLFFKNGKEV 76
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 1-70 3.83e-09

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: 49.43  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611330   1 MVQIIKDTNeFKTFLTAAgHKLAVVQFSSKRCGPCKRMFPVFHELAETC---------------------HIKTIPTFQM 59
Cdd:COG3118    1 AVVELTDEN-FEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYggkvkfvkvdvdenpelaaqfGVRSIPTLLL 78

                         90
                 ....*....|.
gi 558611330  60 FKKSQKVTLFS 70
Cdd:COG3118   79 FKDGQPVDRFV 89
PTZ00051 PTZ00051
thioredoxin; Provisional
 1-69 2.16e-08

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 47.18  E-value: 2.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611330  1 MVQIIKDTNEFKTFLTaaGHKLAVVQFSSKRCGPCKRMFPVFH--------------------ELAETCHIKTIPTFQMF 60
Cdd:PTZ00051  1 MVHIVTSQAEFESTLS--QNELVIVDFYAEWCGPCKRIAPFYEecskeytkmvfvkvdvdelsEVAEKENITSMPTFKVF 78


                ....*....
gi 558611330 61 KKSQKVTLF 69
Cdd:PTZ00051 79 KNGSVVDTL 87
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 9-66 2.39e-08

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: 47.23  E-value: 2.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558611330    9 NEFKTFLtAAGHKLAVVQFSSKRCGPCKRMFPVFHELAET---------------------CHIKTIPTFQMFKKSQKV 66
Cdd:pfam00085   8 ANFDEVV-QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEykgnvvfakvdvdenpdlaskYGVRGYPTLIFFKNGQPV 85
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 10-66 1.17e-05

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: 40.35  E-value: 1.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558611330   10 EFKTFLtAAGHKLAVVQFSSKRCGPCKRMFPVFHELAETCH---------------------IKTIPTFQMFKKSQKV 66
Cdd:TIGR01068   5 NFDETI-ASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEgkvkfvklnvdenpdiaakygIRSIPTLLLFKNGKEV 81
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 10-66 3.30e-11

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: 54.49  E-value: 3.30e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558611330 10 EFKTFLTAAghKLAVVQFSSKRCGPCKRMFPVFHELAET--------------------CHIKTIPTFQMFKKSQKV 66
Cdd:cd02947   2 EFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEypkvkfvkvdvdenpelaeeYGVRSIPTFLFFKNGKEV 76
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 1-70 3.83e-09

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: 49.43  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611330   1 MVQIIKDTNeFKTFLTAAgHKLAVVQFSSKRCGPCKRMFPVFHELAETC---------------------HIKTIPTFQM 59
Cdd:COG3118    1 AVVELTDEN-FEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYggkvkfvkvdvdenpelaaqfGVRSIPTLLL 78

                         90
                 ....*....|.
gi 558611330  60 FKKSQKVTLFS 70
Cdd:COG3118   79 FKDGQPVDRFV 89
PTZ00051 PTZ00051
thioredoxin; Provisional
 1-69 2.16e-08

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 47.18  E-value: 2.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558611330  1 MVQIIKDTNEFKTFLTaaGHKLAVVQFSSKRCGPCKRMFPVFH--------------------ELAETCHIKTIPTFQMF 60
Cdd:PTZ00051  1 MVHIVTSQAEFESTLS--QNELVIVDFYAEWCGPCKRIAPFYEecskeytkmvfvkvdvdelsEVAEKENITSMPTFKVF 78


                ....*....
gi 558611330 61 KKSQKVTLF 69
Cdd:PTZ00051 79 KNGSVVDTL 87
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 9-66 2.39e-08

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: 47.23  E-value: 2.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558611330    9 NEFKTFLtAAGHKLAVVQFSSKRCGPCKRMFPVFHELAET---------------------CHIKTIPTFQMFKKSQKV 66
Cdd:pfam00085   8 ANFDEVV-QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEykgnvvfakvdvdenpdlaskYGVRGYPTLIFFKNGQPV 85
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 10-66 1.65e-06

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: 42.26  E-value: 1.65e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558611330 10 EFKTFLTAAGHKLAVVQFSSKRCGPCKRMFPVFHELAETCH---------------------IKTIPTFQMFKKSQKV 66
Cdd:cd02984   4 EFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFpsvlflsieaeelpeisekfeITAVPTFVFFRNGTIV 81
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 7-49 5.15e-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: 41.32  E-value: 5.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 558611330   7 DTNEFKTFLTAAGHKLAVVQFSSKRCGPCKRMFPVFHELAETC 49
Cdd:cd02985    2 SVEELDEALKKAKGRLVVLEFALKHSGPSVKIYPTMVKLSRTC 44
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 10-66 1.17e-05

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: 40.35  E-value: 1.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558611330   10 EFKTFLtAAGHKLAVVQFSSKRCGPCKRMFPVFHELAETCH---------------------IKTIPTFQMFKKSQKV 66
Cdd:TIGR01068   5 NFDETI-ASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEgkvkfvklnvdenpdiaakygIRSIPTLLLFKNGKEV 81
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 7-47 7.52e-04

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: 35.28  E-value: 7.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 558611330   7 DTNEFKTFLtaAGHKLAVVQFSSKRCGPCKRMFPVFHELAE 47
Cdd:cd02961    4 TDDNFDELV--KDSKDVLVEFYAPWCGHCKALAPEYEKLAK 42
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 21-47 1.03e-03

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 35.82  E-value: 1.03e-03
                         10        20
                 ....*....|....*....|....*..
gi 558611330  21 KLAVVQFSSKRCGPCKRMFPVFHELAE 47
Cdd:COG0526   29 KPVLVNFWATWCPPCRAEMPVLKELAE 55
PRK10996 PRK10996
thioredoxin 2; Provisional
 24-66 3.05e-03

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 34.27  E-value: 3.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558611330  24 VVQFSSKRCGPCKRMFPVFH---------------------ELAETCHIKTIPTFQMFKKSQKV 66
Cdd:PRK10996  56 VIDFWAPWCGPCRNFAPIFEdvaaersgkvrfvkvnteaerELSARFRIRSIPTIMIFKNGQVV 119
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 21-73 7.82e-03

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: 32.86  E-value: 7.82e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558611330 21 KLAVVQFSSKRCGPCKRMFPVFH---------------------ELAETCHIKTIPTFQMFKKSQKVTLFSRIK 73
Cdd:cd02949  14 RLILVLYTSPTCGPCRTLKPILNkvidefdgavhfveididedqEIAEAAGIMGTPTVQFFKDKELVKEISGVK 87
 
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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