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Conserved domains on  [gi|1370450555|gb|AVQ09948|]
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putative thioredoxin [Salmonella phage vB_SenS_PHB06]

Protein Classification

thioredoxin family protein( domain architecture ID 11459707)

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
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 11-66 4.31e-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: 49.05  E-value: 4.31e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370450555  11 STCNPCKMFEPVFDKVVSDYN--LEIHK-ETD-NTELMQKFGVRQVPVVVLadrLPNGRV 66
Cdd:COG3118    28 PWCGPCKMLAPVLEELAAEYGgkVKFVKvDVDeNPELAAQFGVRSIPTLLL---FKDGQP 84
 
Name Accession Description Interval E-value
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 11-66 4.31e-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: 49.05  E-value: 4.31e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370450555  11 STCNPCKMFEPVFDKVVSDYN--LEIHK-ETD-NTELMQKFGVRQVPVVVLadrLPNGRV 66
Cdd:COG3118    28 PWCGPCKMLAPVLEELAAEYGgkVKFVKvDVDeNPELAAQFGVRSIPTLLL---FKDGQP 84
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 13-93 1.89e-08

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: 47.67  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370450555  13 CNPCKMFEPVFDKVVSDYN--LEIHK-ETD-NTELMQKFGVRQVPVVVLadrLPNGRVEANhiLIGRQLRketmhEAIKN 88
Cdd:TIGR01068  26 CGPCKMIAPILEELAKEYEgkVKFVKlNVDeNPDIAAKYGIRSIPTLLL---FKNGKEVDR--SVGALPK-----AALKQ 95


                  ....*
gi 1370450555  89 FLDDN 93
Cdd:TIGR01068  96 LINKN 100
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 11-57 2.81e-06

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: 41.77  E-value: 2.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1370450555 11 STCNPCKMFEPVFDKVVSDY-NLEIHK-ETD-NTELMQKFGVRQVPVVVL 57
Cdd:cd02947   20 PWCGPCKAIAPVLEELAEEYpKVKFVKvDVDeNPELAEEYGVRSIPTFLF 69
trxA PRK09381
thioredoxin TrxA;
13-93 8.73e-05

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 38.12  E-value: 8.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370450555  13 CNPCKMFEPVFDKVVSDYN--LEIHKET--DNTELMQKFGVRQVPVVVLadrLPNGRVEANHIligRQLRKETMheaiKN 88
Cdd:PRK09381   33 CGPCKMIAPILDEIADEYQgkLTVAKLNidQNPGTAPKYGIRGIPTLLL---FKNGEVAATKV---GALSKGQL----KE 102


                  ....*
gi 1370450555  89 FLDDN 93
Cdd:PRK09381  103 FLDAN 107
Thioredoxin_3 pfam13192
Thioredoxin domain;
10-61 1.53e-04

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 36.81  E-value: 1.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1370450555 10 GSTCNPCKMFEPVFDKVVSDYNL--EIHKETDNTELMqKFGVRQVPVVVLADRL 61
Cdd:pfam13192  2 GPGCPKCPQLEKAVKEAAAELGIdaEVEKVTDFPEIA-KYGVMSTPALVINGKV 54
 
Name Accession Description Interval E-value
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 11-66 4.31e-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: 49.05  E-value: 4.31e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370450555  11 STCNPCKMFEPVFDKVVSDYN--LEIHK-ETD-NTELMQKFGVRQVPVVVLadrLPNGRV 66
Cdd:COG3118    28 PWCGPCKMLAPVLEELAAEYGgkVKFVKvDVDeNPELAAQFGVRSIPTLLL---FKDGQP 84
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 13-93 1.89e-08

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: 47.67  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370450555  13 CNPCKMFEPVFDKVVSDYN--LEIHK-ETD-NTELMQKFGVRQVPVVVLadrLPNGRVEANhiLIGRQLRketmhEAIKN 88
Cdd:TIGR01068  26 CGPCKMIAPILEELAKEYEgkVKFVKlNVDeNPDIAAKYGIRSIPTLLL---FKNGKEVDR--SVGALPK-----AALKQ 95


                  ....*
gi 1370450555  89 FLDDN 93
Cdd:TIGR01068  96 LINKN 100
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 11-57 2.81e-06

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: 41.77  E-value: 2.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1370450555 11 STCNPCKMFEPVFDKVVSDY-NLEIHK-ETD-NTELMQKFGVRQVPVVVL 57
Cdd:cd02947   20 PWCGPCKAIAPVLEELAEEYpKVKFVKvDVDeNPELAEEYGVRSIPTFLF 69
trxA PRK09381
thioredoxin TrxA;
13-93 8.73e-05

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 38.12  E-value: 8.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370450555  13 CNPCKMFEPVFDKVVSDYN--LEIHKET--DNTELMQKFGVRQVPVVVLadrLPNGRVEANHIligRQLRKETMheaiKN 88
Cdd:PRK09381   33 CGPCKMIAPILDEIADEYQgkLTVAKLNidQNPGTAPKYGIRGIPTLLL---FKNGEVAATKV---GALSKGQL----KE 102


                  ....*
gi 1370450555  89 FLDDN 93
Cdd:PRK09381  103 FLDAN 107
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 10-90 1.32e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 38.13  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370450555  10 GSTCNPCKMFEPVFDKVVSDYN----LEIHKETD---------------------NTELMQKFGVRQVPVVVLADrlPNG 64
Cdd:COG0526    37 ATWCPPCRAEMPVLKELAEEYGgvvfVGVDVDENpeavkaflkelglpypvlldpDGELAKAYGVRGIPTTVLID--KDG 114

                          90       100
                  ....*....|....*....|....*.
gi 1370450555  65 RVEANHIligRQLRKETMHEAIKNFL 90
Cdd:COG0526   115 KIVARHV---GPLSPEELEEALEKLL 137
Thioredoxin_3 pfam13192
Thioredoxin domain;
10-61 1.53e-04

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 36.81  E-value: 1.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1370450555 10 GSTCNPCKMFEPVFDKVVSDYNL--EIHKETDNTELMqKFGVRQVPVVVLADRL 61
Cdd:pfam13192  2 GPGCPKCPQLEKAVKEAAAELGIdaEVEKVTDFPEIA-KYGVMSTPALVINGKV 54
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 13-92 2.17e-04

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: 36.83  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370450555  13 CNPCKMFEPVFDKVVSDY--NLEIHK--ETDNTELMQKFGVRQVPVVVLadrLPNGRVEANhiLIGRqlRKEtmhEAIKN 88
Cdd:pfam00085  30 CGPCKMLAPEYEELAQEYkgNVVFAKvdVDENPDLASKYGVRGYPTLIF---FKNGQPVDD--YVGA--RPK---DALAA 99


                  ....
gi 1370450555  89 FLDD 92
Cdd:pfam00085 100 FLKA 103
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
 13-57 3.66e-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: 37.61  E-value: 3.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370450555  13 CNPCKMFEPVFDKVVSDYNLEIHKET-----------DNTELMQKFGVRQVPVVVL 57
Cdd:pfam04756  46 CQLCREFQPEFELVAKSWFKDHKAGSsklffatldfdDGKDVFQSLGLQTAPHLLL 101
PRK10996 PRK10996
thioredoxin 2; Provisional
 13-57 1.12e-03

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 35.43  E-value: 1.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370450555  13 CNPCKMFEPVFDKVVSDYNLEIHKETDNTE----LMQKFGVRQVPVVVL 57
Cdd:PRK10996   64 CGPCRNFAPIFEDVAAERSGKVRFVKVNTEaereLSARFRIRSIPTIMI 112
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 13-57 2.87e-03

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: 34.12  E-value: 2.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370450555  13 CNPCKMFEPVFDKVVSDY----NLEIHK--ETDNTELMQKFGVRQVPVVVL 57
Cdd:cd02961    27 CGHCKALAPEYEKLAKELkgdgKVVVAKvdCTANNDLCSEYGVRGYPTIKL 77
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 4-57 9.48e-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: 32.47  E-value: 9.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370450555  4 LVYLLKGSTCNPCKMFEPVFDKVVSDYNLEIH-KETD---NTELMQKFGVRQVPVVVL 57
Cdd:cd02949   16 ILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHfVEIDideDQEIAEAAGIMGTPTVQF 73
 
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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