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Conserved domains on  [gi|14249348|ref|NP_116120|]
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thioredoxin domain-containing protein 17 [Homo sapiens]

Protein Classification

TRP14_like domain-containing protein( domain architecture ID 10121469)

TRP14_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRP14_like cd02952
Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a ...
 4-121 3.55e-71

Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a 14kD cytosolic protein that shows disulfide reductase activity in vitro with a different substrate specificity compared with another human cytosolic protein, TRX1. TRP14 catalyzes the reduction of small disulfide-containing peptides but does not reduce disulfides of ribonucleotide reductase, peroxiredoxin and methionine sulfoxide reductase, which are TRX1 substrates. TRP14 also plays a role in tumor necrosis factor (TNF)-alpha signaling pathways, distinct from that of TRX1. Its depletion promoted TNF-alpha induced activation of c-Jun N-terminal kinase and mitogen-activated protein kinases.


:

Pssm-ID: 239250  Cd Length: 119  Bit Score: 208.35  E-value: 3.55e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249348   4 YEEVSVSGFEEFHRAVEQHNGKTIFAYFTGSKDAGGKSWCPDCVQAEPVVREGLKHISEGCVFIYCQVGEKPYWKDPNND 83
Cdd:cd02952   1 PLETAVRGYEEFLKLLKSHEGKPIFILFYGDKDPDGQSWCPDCVKAEPVVREALKAAPEDCVFIYCDVGDRPYWRDPNNP 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 14249348  84 FRKNLKVT-AVPTLLKYGTPQKLVESECLQANLVEMLFS 121
Cdd:cd02952  81 FRTDPKLTtGVPTLLRWKTPQRLVEDECLQADLVEMFFE 119
 
Name Accession Description Interval E-value
TRP14_like cd02952
Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a ...
 4-121 3.55e-71

Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a 14kD cytosolic protein that shows disulfide reductase activity in vitro with a different substrate specificity compared with another human cytosolic protein, TRX1. TRP14 catalyzes the reduction of small disulfide-containing peptides but does not reduce disulfides of ribonucleotide reductase, peroxiredoxin and methionine sulfoxide reductase, which are TRX1 substrates. TRP14 also plays a role in tumor necrosis factor (TNF)-alpha signaling pathways, distinct from that of TRX1. Its depletion promoted TNF-alpha induced activation of c-Jun N-terminal kinase and mitogen-activated protein kinases.


Pssm-ID: 239250  Cd Length: 119  Bit Score: 208.35  E-value: 3.55e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249348   4 YEEVSVSGFEEFHRAVEQHNGKTIFAYFTGSKDAGGKSWCPDCVQAEPVVREGLKHISEGCVFIYCQVGEKPYWKDPNND 83
Cdd:cd02952   1 PLETAVRGYEEFLKLLKSHEGKPIFILFYGDKDPDGQSWCPDCVKAEPVVREALKAAPEDCVFIYCDVGDRPYWRDPNNP 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 14249348  84 FRKNLKVT-AVPTLLKYGTPQKLVESECLQANLVEMLFS 121
Cdd:cd02952  81 FRTDPKLTtGVPTLLRWKTPQRLVEDECLQADLVEMFFE 119
DUF953 pfam06110
Eukaryotic protein of unknown function (DUF953); This family consists of several hypothetical ...
 8-122 2.96e-55

Eukaryotic protein of unknown function (DUF953); This family consists of several hypothetical eukaryotic proteins of unknown function.


Pssm-ID: 399247  Cd Length: 119  Bit Score: 168.04  E-value: 2.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249348     8 SVSGFEEFHRAVEQ--HNGKTIFAYFTGSKDAGGKSWCPDCVQAEPVVREGLKHISEGCVFIYCQVGEKPYWKDPNNDFR 85
Cdd:pfam06110   1 MALGFEEFNKSTKEseNGSKPIFILFSGSKDTTGESWCPDCVRAEPVIYEALKEAPEDVHFIRVDVGDRPYWRDPANPFR 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 14249348    86 K--NLKVTAVPTLLKYGTPQKLVESECLQANLVEMLFSE 122
Cdd:pfam06110  81 KdpRLKLTGVPTLLRWKGPQRLDGHQCHNSHLVEMFFEE 119
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 18-97 5.95e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 39.67  E-value: 5.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249348  18 AVEQHNGKTIFAYFTGSkdaggksWCPDCVQAEPVVREgLKHISEGCVFIYCQVGEK---------------PYWKDPNN 82
Cdd:COG0526  22 SLADLKGKPVLVNFWAT-------WCPPCRAEMPVLKE-LAEEYGGVVFVGVDVDENpeavkaflkelglpyPVLLDPDG 93

                        90
                ....*....|....*
gi 14249348  83 DFRKNLKVTAVPTLL 97
Cdd:COG0526  94 ELAKAYGVRGIPTTV 108
 
Name Accession Description Interval E-value
TRP14_like cd02952
Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a ...
 4-121 3.55e-71

Human TRX-related protein 14 (TRP14)-like family; composed of proteins similar to TRP14, a 14kD cytosolic protein that shows disulfide reductase activity in vitro with a different substrate specificity compared with another human cytosolic protein, TRX1. TRP14 catalyzes the reduction of small disulfide-containing peptides but does not reduce disulfides of ribonucleotide reductase, peroxiredoxin and methionine sulfoxide reductase, which are TRX1 substrates. TRP14 also plays a role in tumor necrosis factor (TNF)-alpha signaling pathways, distinct from that of TRX1. Its depletion promoted TNF-alpha induced activation of c-Jun N-terminal kinase and mitogen-activated protein kinases.


Pssm-ID: 239250  Cd Length: 119  Bit Score: 208.35  E-value: 3.55e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249348   4 YEEVSVSGFEEFHRAVEQHNGKTIFAYFTGSKDAGGKSWCPDCVQAEPVVREGLKHISEGCVFIYCQVGEKPYWKDPNND 83
Cdd:cd02952   1 PLETAVRGYEEFLKLLKSHEGKPIFILFYGDKDPDGQSWCPDCVKAEPVVREALKAAPEDCVFIYCDVGDRPYWRDPNNP 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 14249348  84 FRKNLKVT-AVPTLLKYGTPQKLVESECLQANLVEMLFS 121
Cdd:cd02952  81 FRTDPKLTtGVPTLLRWKTPQRLVEDECLQADLVEMFFE 119
DUF953 pfam06110
Eukaryotic protein of unknown function (DUF953); This family consists of several hypothetical ...
 8-122 2.96e-55

Eukaryotic protein of unknown function (DUF953); This family consists of several hypothetical eukaryotic proteins of unknown function.


Pssm-ID: 399247  Cd Length: 119  Bit Score: 168.04  E-value: 2.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249348     8 SVSGFEEFHRAVEQ--HNGKTIFAYFTGSKDAGGKSWCPDCVQAEPVVREGLKHISEGCVFIYCQVGEKPYWKDPNNDFR 85
Cdd:pfam06110   1 MALGFEEFNKSTKEseNGSKPIFILFSGSKDTTGESWCPDCVRAEPVIYEALKEAPEDVHFIRVDVGDRPYWRDPANPFR 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 14249348    86 K--NLKVTAVPTLLKYGTPQKLVESECLQANLVEMLFSE 122
Cdd:pfam06110  81 KdpRLKLTGVPTLLRWKGPQRLDGHQCHNSHLVEMFFEE 119
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 18-97 5.95e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 39.67  E-value: 5.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249348  18 AVEQHNGKTIFAYFTGSkdaggksWCPDCVQAEPVVREgLKHISEGCVFIYCQVGEK---------------PYWKDPNN 82
Cdd:COG0526  22 SLADLKGKPVLVNFWAT-------WCPPCRAEMPVLKE-LAEEYGGVVFVGVDVDENpeavkaflkelglpyPVLLDPDG 93

                        90
                ....*....|....*
gi 14249348  83 DFRKNLKVTAVPTLL 97
Cdd:COG0526  94 ELAKAYGVRGIPTTV 108
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 13-99 4.25e-04

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: 36.77  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249348  13 EEFHRAVEQHngKTIFAYFtgskdagGKSWCPDCVQAEPVVREgLKHISEGCVFIYCQVgekpywkDPNNDFRKNLKVTA 92
Cdd:cd02947   1 EEFEELIKSA--KPVVVDF-------WAPWCGPCKAIAPVLEE-LAEEYPKVKFVKVDV-------DENPELAEEYGVRS 63


                ....*..
gi 14249348  93 VPTLLKY 99
Cdd:cd02947  64 IPTFLFF 70
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 39-106 5.40e-03

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: 33.44  E-value: 5.40e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14249348  39 GKSWCPDCVQAEPVVREgLKHISEGCVFIYCQVGEKPYWKdpnnDFRKNLKVTAVPTLLKYGTPQKLV 106
Cdd:cd01659   5 YAPWCPFCQALRPVLAE-LALLNKGVKFEAVDVDEDPALE----KELKRYGVGGVPTLVVFGPGIGVK 67
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
23-97 9.04e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 33.55  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249348    23 NGKTIFAYFTgskdaggKSWCPDCVQAEPVVRE---GLKHISEGCVF----IYCQVGEKPYWKD--PNNDFRKNLKVTAV 93
Cdd:pfam13098   3 NGKPVLVVFT-------DPDCPYCKKLKKELLEdpdVTVYLGPNFVFiavnIWCAKEVAKAFTDilENKELGRKYGVRGT 75


                  ....
gi 14249348    94 PTLL 97
Cdd:pfam13098  76 PTIV 79
 
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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