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Conserved domains on  [gi|516232603|ref|WP_017636566|]
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MULTISPECIES: thioredoxin family protein [Staphylococcus]

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 ...
 9-101 1.46e-17

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: 71.05  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232603   9 AQFKTFINQHPLVVVHVMRDHCSVCHAVLPQVKDLLQEtFPQVKLAIINQNEVTDIAGELSIFTVPVDLIFMNGKEMHRQ 88
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                         90
                 ....*....|...
gi 516232603  89 GRFIDLQKFERQL 101
Cdd:cd02947   80 VGADPKEELEEFL 92
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 9-101 1.46e-17

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: 71.05  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232603   9 AQFKTFINQHPLVVVHVMRDHCSVCHAVLPQVKDLLQEtFPQVKLAIINQNEVTDIAGELSIFTVPVDLIFMNGKEMHRQ 88
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                         90
                 ....*....|...
gi 516232603  89 GRFIDLQKFERQL 101
Cdd:cd02947   80 VGADPKEELEEFL 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 12-101 1.21e-12

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: 59.06  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232603  12 KTFINQHPLVVVHVMRDHCSVCHAVLPQVKDLLQETFPQVKLAIINQNEVTDIAGELSIFTVPVDLIFMNGKEMHRQGRF 91
Cdd:COG3118   12 EEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGA 91

                         90
                 ....*....|
gi 516232603  92 IDLQKFERQL 101
Cdd:COG3118   92 LPKEQLREFL 101
PTZ00051 PTZ00051
thioredoxin; Provisional
 1-83 9.61e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 43.71  E-value: 9.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232603   1 MTETIRDVAQFKTFINQHPLVVVHVMRDHCSVCHAVLPQVkDLLQETFPQVKLAIINQNEVTDIAGELSIFTVPVDLIFM 80
Cdd:PTZ00051   1 MVHIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFY-EECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFK 79


                 ...
gi 516232603  81 NGK 83
Cdd:PTZ00051  80 NGS 82
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 11-83 6.45e-05

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: 40.43  E-value: 6.45e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516232603   11 FKTFINQHPLVVVHVMRDHCSVCHAVLPQVK---DLLQETFPQVKLAIINQNEVTDIAGELSIFTVPVDLIFMNGK 83
Cdd:TIGR01130  11 FDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEkaaDELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNGE 86
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 9-101 1.46e-17

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: 71.05  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232603   9 AQFKTFINQHPLVVVHVMRDHCSVCHAVLPQVKDLLQEtFPQVKLAIINQNEVTDIAGELSIFTVPVDLIFMNGKEMHRQ 88
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                         90
                 ....*....|...
gi 516232603  89 GRFIDLQKFERQL 101
Cdd:cd02947   80 VGADPKEELEEFL 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 12-101 1.21e-12

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: 59.06  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232603  12 KTFINQHPLVVVHVMRDHCSVCHAVLPQVKDLLQETFPQVKLAIINQNEVTDIAGELSIFTVPVDLIFMNGKEMHRQGRF 91
Cdd:COG3118   12 EEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGA 91

                         90
                 ....*....|
gi 516232603  92 IDLQKFERQL 101
Cdd:COG3118   92 LPKEQLREFL 101
PTZ00051 PTZ00051
thioredoxin; Provisional
 1-83 9.61e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 43.71  E-value: 9.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232603   1 MTETIRDVAQFKTFINQHPLVVVHVMRDHCSVCHAVLPQVkDLLQETFPQVKLAIINQNEVTDIAGELSIFTVPVDLIFM 80
Cdd:PTZ00051   1 MVHIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFY-EECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFK 79


                 ...
gi 516232603  81 NGK 83
Cdd:PTZ00051  80 NGS 82
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 11-83 6.45e-05

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: 40.43  E-value: 6.45e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516232603   11 FKTFINQHPLVVVHVMRDHCSVCHAVLPQVK---DLLQETFPQVKLAIINQNEVTDIAGELSIFTVPVDLIFMNGK 83
Cdd:TIGR01130  11 FDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEkaaDELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNGE 86
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 9-87 2.44e-04

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: 37.25  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232603   9 AQFKTFINQHP--LVVVHVMRDHCSVCHAVLPQVKDLLQETFPQVKLAIINQNEVTDIAGELSIFTVPVDLIFMNGKEMH 86
Cdd:cd02984    3 EEFEELLKSDAskLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVD 82


                 .
gi 516232603  87 R 87
Cdd:cd02984   83 R 83
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 21-107 1.05e-03

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 36.21  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232603  21 VVVHVMRDHCSVCHAVLPQVKDlLQETFPQVKLAIINQNE------------------VTD----IAGELSIFTVPVDLI 78
Cdd:COG0526   31 VLVNFWATWCPPCRAEMPVLKE-LAEEYGGVVFVGVDVDEnpeavkaflkelglpypvLLDpdgeLAKAYGVRGIPTTVL 109

                         90       100       110
                 ....*....|....*....|....*....|
gi 516232603  79 FM-NGKEMHRQGRFIDLQKFERQLTPMYEK 107
Cdd:COG0526  110 IDkDGKIVARHVGPLSPEELEEALEKLLAK 139
 
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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