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Conserved domains on  [gi|568065225|ref|WP_024052886|]
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MULTISPECIES: hypothetical protein [Streptococcus]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 48-144 1.62e-09

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is 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 the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member TIGR01295:

Pssm-ID: 469754  Cd Length: 122  Bit Score: 52.25  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065225   48 ITVPELKEKQAQSENFYLYIGRGTCPHCRRFVKQLQRAKTKS---FYYLDSEKKTP-------ELVAFREAYKIKF-VPY 116
Cdd:TIGR01295  11 TTVVRALEALDKKETATFFIGRKTCPYCRKFSGTLSGVVAQTkapIYYIDSENNGSfemsslnDLTAFRSRFGIPTsFMG 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 568065225  117 FGKFTGLTEEKVLQIKA--NMTTKEIENFN 144
Cdd:TIGR01295  91 TPTFVHITDGKQVSVRCgsSTTAQELQDIA 120
 
Name Accession Description Interval E-value
PedC_BrcD TIGR01295
bacteriocin transport accessory protein, putative; This model describes a small family of ...
 48-144 1.62e-09

bacteriocin transport accessory protein, putative; This model describes a small family of proteins believed to aid in the export of various class II bacteriocins, which are ribosomally-synthesized, non-lantibiotic bacterial peptide antibiotics. Members of this family are found in operons for pediocin PA-1 from Pediococcus acidilactici and brochocin-C from Brochothrix campestris.


Pssm-ID: 273542  Cd Length: 122  Bit Score: 52.25  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065225   48 ITVPELKEKQAQSENFYLYIGRGTCPHCRRFVKQLQRAKTKS---FYYLDSEKKTP-------ELVAFREAYKIKF-VPY 116
Cdd:TIGR01295  11 TTVVRALEALDKKETATFFIGRKTCPYCRKFSGTLSGVVAQTkapIYYIDSENNGSfemsslnDLTAFRSRFGIPTsFMG 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 568065225  117 FGKFTGLTEEKVLQIKA--NMTTKEIENFN 144
Cdd:TIGR01295  91 TPTFVHITDGKQVSVRCgsSTTAQELQDIA 120
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 52-143 4.77e-03

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: 34.46  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065225  52 ELKEKQAQSENFYLYIGRGTCPHCRRFVKQLQRAKTKS----FYYLDSEkKTPELVafrEAYKIKFVPYFGKFTGltEEK 127
Cdd:cd02947    2 EFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYpkvkFVKVDVD-ENPELA---EEYGVRSIPTFLFFKN--GKE 75

                         90
                 ....*....|....*.
gi 568065225 128 VLQIKANMTTKEIENF 143
Cdd:cd02947   76 VDRVVGADPKEELEEF 91
 
Name Accession Description Interval E-value
PedC_BrcD TIGR01295
bacteriocin transport accessory protein, putative; This model describes a small family of ...
 48-144 1.62e-09

bacteriocin transport accessory protein, putative; This model describes a small family of proteins believed to aid in the export of various class II bacteriocins, which are ribosomally-synthesized, non-lantibiotic bacterial peptide antibiotics. Members of this family are found in operons for pediocin PA-1 from Pediococcus acidilactici and brochocin-C from Brochothrix campestris.


Pssm-ID: 273542  Cd Length: 122  Bit Score: 52.25  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065225   48 ITVPELKEKQAQSENFYLYIGRGTCPHCRRFVKQLQRAKTKS---FYYLDSEKKTP-------ELVAFREAYKIKF-VPY 116
Cdd:TIGR01295  11 TTVVRALEALDKKETATFFIGRKTCPYCRKFSGTLSGVVAQTkapIYYIDSENNGSfemsslnDLTAFRSRFGIPTsFMG 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 568065225  117 FGKFTGLTEEKVLQIKA--NMTTKEIENFN 144
Cdd:TIGR01295  91 TPTFVHITDGKQVSVRCgsSTTAQELQDIA 120
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 52-143 4.77e-03

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: 34.46  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065225  52 ELKEKQAQSENFYLYIGRGTCPHCRRFVKQLQRAKTKS----FYYLDSEkKTPELVafrEAYKIKFVPYFGKFTGltEEK 127
Cdd:cd02947    2 EFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYpkvkFVKVDVD-ENPELA---EEYGVRSIPTFLFFKN--GKE 75

                         90
                 ....*....|....*.
gi 568065225 128 VLQIKANMTTKEIENF 143
Cdd:cd02947   76 VDRVVGADPKEELEEF 91
 
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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