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Conserved domains on  [gi|2532338551|ref|WP_289859927|]
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DUF4369 domain-containing protein [uncultured Muribaculum sp.]

Protein Classification

glutathione S-transferase; glutathione S-transferase family protein( domain architecture ID 10626247)

glutathione S-transferase (GST) catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress; similar to class-delta/epsilon GSTs which play major roles in insecticide resistance| glutathione S-transferase (GST) family protein similar to human failed axon connections homolog, which may play a role in axonal development

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
235-363 7.68e-13

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 64.89  E-value: 7.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 235 DITLTDNKGKPHNLEEVTknNKVVVLNFTIYSAEGSPAFNLDLAKVYEKRHNQGLEIYQVAVDNDEfQWKQSAR--NLPW 312
Cdd:COG1225     3 DFTLPDLDGKTVSLSDLR--GKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDE-AHKKFAEkyGLPF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2532338551 313 ITVYNPpstGSQILLNYNVGTLPTTYII-ANGELVER----VDDITKLDSAVAPYL 363
Cdd:COG1225    80 PLLSDP---DGEVAKAYGVRGTPTTFLIdPDGKIRYVwvgpVDPRPHLEEVLEALL 132
DUF4369 pfam14289
Domain of unknown function (DUF4369); This domain family is found in bacteria, and is ...
 27-118 4.71e-10

Domain of unknown function (DUF4369); This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with pfam00578. LPAM signal peptide sequence is found in some family members.


:

Pssm-ID: 433842  Cd Length: 92  Bit Score: 55.81  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551  27 NVNGSIEGADSKTMILQASDNGRWYTLDSITTdKNGNFKYSHDpIGYPDIFRLVLDGKSIYFPIdSVETVNITSTADAFD 106
Cdd:pfam14289   2 TIEGTIKGLKDGTKVYLSYDGGGLVKLDSAVV-KNGKFTFKGK-VDEPPMAYLLIDDKSGALPF-FLENGTITIKLDPGD 78

                          90
                  ....*....|..
gi 2532338551 107 SDYELSGSTAAE 118
Cdd:pfam14289  79 FIAKVKGSPLND 90
 
Name Accession Description Interval E-value
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
235-363 7.68e-13

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 64.89  E-value: 7.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 235 DITLTDNKGKPHNLEEVTknNKVVVLNFTIYSAEGSPAFNLDLAKVYEKRHNQGLEIYQVAVDNDEfQWKQSAR--NLPW 312
Cdd:COG1225     3 DFTLPDLDGKTVSLSDLR--GKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDE-AHKKFAEkyGLPF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2532338551 313 ITVYNPpstGSQILLNYNVGTLPTTYII-ANGELVER----VDDITKLDSAVAPYL 363
Cdd:COG1225    80 PLLSDP---DGEVAKAYGVRGTPTTFLIdPDGKIRYVwvgpVDPRPHLEEVLEALL 132
DUF4369 pfam14289
Domain of unknown function (DUF4369); This domain family is found in bacteria, and is ...
 27-118 4.71e-10

Domain of unknown function (DUF4369); This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with pfam00578. LPAM signal peptide sequence is found in some family members.


Pssm-ID: 433842  Cd Length: 92  Bit Score: 55.81  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551  27 NVNGSIEGADSKTMILQASDNGRWYTLDSITTdKNGNFKYSHDpIGYPDIFRLVLDGKSIYFPIdSVETVNITSTADAFD 106
Cdd:pfam14289   2 TIEGTIKGLKDGTKVYLSYDGGGLVKLDSAVV-KNGKFTFKGK-VDEPPMAYLLIDDKSGALPF-FLENGTITIKLDPGD 78

                          90
                  ....*....|..
gi 2532338551 107 SDYELSGSTAAE 118
Cdd:pfam14289  79 FIAKVKGSPLND 90
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 235-349 7.91e-09

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 53.01  E-value: 7.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 235 DITLTDNKGKPHNLEEVTknNKVVVLNFT----IYSAEGSPafnlDLAKVYEKRHNQGLEIYQVAVDNDEfqwKQSARNl 310
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLK--GKVVLVNFWaswcPPCRAEMP----ELEALAKEYKDDGVEVVGVNVDDDD---PAAVKA- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2532338551 311 pWITVYNPP-----STGSQILLNYNVGTLPTTYII-ANGELVERV 349
Cdd:cd02966    71 -FLKKYGITfpvllDPDGELAKAYGVRGLPTTFLIdRDGRIRARH 114
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 235-348 6.30e-05

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 42.21  E-value: 6.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 235 DITLTDNKGKPHNLEEVtkNNKVVVLNFtiYSAEGSPAFNL---DLAKVYEKRHNQGLEIYQVAVDNDE--FQWKQsARN 309
Cdd:pfam00578   7 DFELPDGDGGTVSLSDY--RGKWVVLFF--YPADWTPVCTTelpALADLYEEFKKLGVEVLGVSVDSPEshKAFAE-KYG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2532338551 310 LPWITVYNPpstGSQILLNYNV------GTLPTTYII-ANGELVER 348
Cdd:pfam00578  82 LPFPLLSDP---DGEVARAYGVlneeegGALRATFVIdPDGKVRYI 124
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
235-349 1.45e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 41.91  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 235 DITLTDNKGKPHNLEEVtkNNKVVVLNFTIYSAEGSPAFNLDLAKVYEKRHNQGLEIyqVAVDNDEfqwkqsarnlPWIT 314
Cdd:PRK03147   43 NFVLTDLEGKKIELKDL--KGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEI--IAVNVDE----------TELA 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2532338551 315 VYN-----------PPSTGSQILLNYNVGTLPTTYII-ANGELVERV 349
Cdd:PRK03147  109 VKNfvnrygltfpvAIDKGRQVIDAYGVGPLPTTFLIdKDGKVVKVI 155
 
Name Accession Description Interval E-value
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
235-363 7.68e-13

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 64.89  E-value: 7.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 235 DITLTDNKGKPHNLEEVTknNKVVVLNFTIYSAEGSPAFNLDLAKVYEKRHNQGLEIYQVAVDNDEfQWKQSAR--NLPW 312
Cdd:COG1225     3 DFTLPDLDGKTVSLSDLR--GKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDE-AHKKFAEkyGLPF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2532338551 313 ITVYNPpstGSQILLNYNVGTLPTTYII-ANGELVER----VDDITKLDSAVAPYL 363
Cdd:COG1225    80 PLLSDP---DGEVAKAYGVRGTPTTFLIdPDGKIRYVwvgpVDPRPHLEEVLEALL 132
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 226-363 1.01e-11

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 62.01  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 226 MLVNEIKLFDITLTDNKGKPHNLEEVtkNNKVVVLNFtiySAEGSP---AFNLDLAKVYEKrhNQGLEIYQVAVDNDEFQ 302
Cdd:COG0526     1 MKAVGKPAPDFTLTDLDGKPLSLADL--KGKPVLVNF---WATWCPpcrAEMPVLKELAEE--YGGVVFVGVDVDENPEA 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2532338551 303 WKQSAR--NLPWITVYNPpstGSQILLNYNVGTLPTTYII-ANGELVERV---DDITKLDSAVAPYL 363
Cdd:COG0526    74 VKAFLKelGLPYPVLLDP---DGELAKAYGVRGIPTTVLIdKDGKIVARHvgpLSPEELEEALEKLL 137
DUF4369 pfam14289
Domain of unknown function (DUF4369); This domain family is found in bacteria, and is ...
 27-118 4.71e-10

Domain of unknown function (DUF4369); This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with pfam00578. LPAM signal peptide sequence is found in some family members.


Pssm-ID: 433842  Cd Length: 92  Bit Score: 55.81  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551  27 NVNGSIEGADSKTMILQASDNGRWYTLDSITTdKNGNFKYSHDpIGYPDIFRLVLDGKSIYFPIdSVETVNITSTADAFD 106
Cdd:pfam14289   2 TIEGTIKGLKDGTKVYLSYDGGGLVKLDSAVV-KNGKFTFKGK-VDEPPMAYLLIDDKSGALPF-FLENGTITIKLDPGD 78

                          90
                  ....*....|..
gi 2532338551 107 SDYELSGSTAAE 118
Cdd:pfam14289  79 FIAKVKGSPLND 90
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 235-349 7.91e-09

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 53.01  E-value: 7.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 235 DITLTDNKGKPHNLEEVTknNKVVVLNFT----IYSAEGSPafnlDLAKVYEKRHNQGLEIYQVAVDNDEfqwKQSARNl 310
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLK--GKVVLVNFWaswcPPCRAEMP----ELEALAKEYKDDGVEVVGVNVDDDD---PAAVKA- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2532338551 311 pWITVYNPP-----STGSQILLNYNVGTLPTTYII-ANGELVERV 349
Cdd:cd02966    71 -FLKKYGITfpvllDPDGELAKAYGVRGLPTTFLIdRDGRIRARH 114
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 235-348 6.30e-05

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 42.21  E-value: 6.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 235 DITLTDNKGKPHNLEEVtkNNKVVVLNFtiYSAEGSPAFNL---DLAKVYEKRHNQGLEIYQVAVDNDE--FQWKQsARN 309
Cdd:pfam00578   7 DFELPDGDGGTVSLSDY--RGKWVVLFF--YPADWTPVCTTelpALADLYEEFKKLGVEVLGVSVDSPEshKAFAE-KYG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2532338551 310 LPWITVYNPpstGSQILLNYNV------GTLPTTYII-ANGELVER 348
Cdd:pfam00578  82 LPFPLLSDP---DGEVARAYGVlneeegGALRATFVIdPDGKVRYI 124
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 272-348 9.24e-05

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 41.89  E-value: 9.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 272 AFNLDLAKVYEKRHNQG--LEIYQVAVDNDEFQWKQSARNLPWITV-YNPPSTGSQILLNYNVGTLPTTYII-ANGELVE 347
Cdd:cd03009    35 AFTPKLVEFYEKLKESGknFEIVFISWDRDEESFNDYFSKMPWLAVpFSDRERRSRLNRTFKIEGIPTLIILdADGEVVT 114


                  .
gi 2532338551 348 R 348
Cdd:cd03009   115 T 115
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
235-349 1.45e-04

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 41.91  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 235 DITLTDNKGKPHNLEEVtkNNKVVVLNFTIYSAEGSPAFNLDLAKVYEKRHNQGLEIyqVAVDNDEfqwkqsarnlPWIT 314
Cdd:PRK03147   43 NFVLTDLEGKKIELKDL--KGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEI--IAVNVDE----------TELA 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2532338551 315 VYN-----------PPSTGSQILLNYNVGTLPTTYII-ANGELVERV 349
Cdd:PRK03147  109 VKNfvnrygltfpvAIDKGRQVIDAYGVGPLPTTFLIdKDGKVVKVI 155
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 255-340 1.46e-04

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 40.37  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532338551 255 NKVVVLNFTIYSAEGSPAFNLDLAKVYEK-RHNQGLEIYQVAVDNDEFQWKQSARNLP--WITVYNPPSTGSQILLNYNV 331
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKlKKKKNVEIVFVSLDRDLEEFKDYLKKMPkdWLSVPFDDDERNELKRKYGV 80


                  ....*....
gi 2532338551 332 GTLPTTYII 340
Cdd:pfam13905  81 NAIPTLVLL 89
 
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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