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Conserved domains on  [gi|646531364|ref|WP_025551223|]
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thiol:disulfide interchange protein DsbA/DsbL [Vibrio parahaemolyticus]

Protein Classification

thiol:disulfide interchange protein DsbA/DsbL( domain architecture ID 10122479)

thiol:disulfide interchange protein DsbA/DsbL is involved in disulfide bond formation and it functions by transferring its disulfide bond to other proteins

Gene Ontology:  GO:0015035
PubMed:  12524212|15558583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 24-195 3.86e-64

DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.


:

Pssm-ID: 239317 [Multi-domain]  Cd Length: 178  Bit Score: 195.97  E-value: 3.86e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  24 EGEHYKVLDLEV-SKKPLVTEFFSFYCPHCNTFEPVIQQLKKQLPEGTKLQKNHVSFMGGnMGPSMSKAFATMVAMKIED 102
Cdd:cd03019    1 EGKDYTVLSPPIpSGKPEVIEFFSYGCPHCYNFEPILEAWVKKLPKDVKFEKVPVVFGGG-EGEPLARAFYAAEALGLED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364 103 QMVPVMFNRIHNMRKPPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFENSGLTGVPAVIVNNKYLVQAQS 182
Cdd:cd03019   80 KLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNPSA 159

                        170
                 ....*....|....*....
gi 646531364 183 IKSM------DEYFALVNY 195
Cdd:cd03019  160 IGGDdtlqvlDELIEKVRY 178
 
Name Accession Description Interval E-value
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 24-195 3.86e-64

DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.


Pssm-ID: 239317 [Multi-domain]  Cd Length: 178  Bit Score: 195.97  E-value: 3.86e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  24 EGEHYKVLDLEV-SKKPLVTEFFSFYCPHCNTFEPVIQQLKKQLPEGTKLQKNHVSFMGGnMGPSMSKAFATMVAMKIED 102
Cdd:cd03019    1 EGKDYTVLSPPIpSGKPEVIEFFSYGCPHCYNFEPILEAWVKKLPKDVKFEKVPVVFGGG-EGEPLARAFYAAEALGLED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364 103 QMVPVMFNRIHNMRKPPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFENSGLTGVPAVIVNNKYLVQAQS 182
Cdd:cd03019   80 KLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNPSA 159

                        170
                 ....*....|....*....
gi 646531364 183 IKSM------DEYFALVNY 195
Cdd:cd03019  160 IGGDdtlqvlDELIEKVRY 178
PRK10954 PRK10954
thiol:disulfide interchange protein DsbA;
1-200 2.22e-56

thiol:disulfide interchange protein DsbA;


Pssm-ID: 182863 [Multi-domain]  Cd Length: 207  Bit Score: 177.21  E-value: 2.22e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364   1 MKKLFALFSMLMLSLSAHAAQFKEGEHYKVLDLEVSKKPLVTEFFSFYCPHCNTFEPVI---QQLKKQLPEGTKLQKNHV 77
Cdd:PRK10954   1 MKKIWLALAGMVLAFSASAAQFTDGKQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYhvsDNVKKKLPEGTKMTKYHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  78 SFMgGNMGPSMSKAFATMVAMKIEDQMVPVMFNRIHNMRKpPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDK 157
Cdd:PRK10954  81 EFL-GPLGKELTQAWAVAMALGVEDKVTPPLFEGVQKTQT-IQSAADIRDVFIKAGVKGEDYDAAWNSFVVKSLVAQQEK 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 646531364 158 QFENSGLTGVPAVIVNNKYLVQAQ--SIKSMDEYFA----LVNYLLTLK 200
Cdd:PRK10954 159 AAADLQLRGVPAMFVNGKYMVNNQgmDTSSMDVYVQqyadVVKFLLEKK 207
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 41-191 2.66e-30

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 109.83  E-value: 2.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364   41 VTEFFSFYCPHCNTFEPVIQQLKKQLPeGTKLQKNHVSFMG----GNMGPSMSKAFATMVAMKIE--------------- 101
Cdd:pfam01323   2 VDEFFDFLCPFCYLAKERLEKLAARYG-DVKVVYRPFPLAGakkiGNVGPSNLPVKLKYMMADLErwaalygiplrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  102 ---------------------DQMVPVMFNRIHNMRKPPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFE 160
Cdd:pfam01323  81 flgnstranrlalaagaeglaEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTAAAI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 646531364  161 NSGLTGVPAVIVNNKYLVQAQSIKSMDEYFA 191
Cdd:pfam01323 161 SLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 38-188 6.78e-28

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 102.38  E-value: 6.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  38 KPLVTEFFSFYCPHCNTFEPVIQQLKKQLPEGT-KLQKNHVSFMGGNmgpSMSKAFATMVAMKIE--DQMVPVMFNRihn 114
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKYVDGKvRVVYRPFPLLHPD---SLRAARAALCAADQGkfWAFHDALFAN--- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 646531364 115 mrKPPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFENSGLTGVPAVIVNNKYLVQAQSIKSMDE 188
Cdd:COG1651   75 --QPALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEA 146
 
Name Accession Description Interval E-value
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 24-195 3.86e-64

DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.


Pssm-ID: 239317 [Multi-domain]  Cd Length: 178  Bit Score: 195.97  E-value: 3.86e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  24 EGEHYKVLDLEV-SKKPLVTEFFSFYCPHCNTFEPVIQQLKKQLPEGTKLQKNHVSFMGGnMGPSMSKAFATMVAMKIED 102
Cdd:cd03019    1 EGKDYTVLSPPIpSGKPEVIEFFSYGCPHCYNFEPILEAWVKKLPKDVKFEKVPVVFGGG-EGEPLARAFYAAEALGLED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364 103 QMVPVMFNRIHNMRKPPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFENSGLTGVPAVIVNNKYLVQAQS 182
Cdd:cd03019   80 KLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNPSA 159

                        170
                 ....*....|....*....
gi 646531364 183 IKSM------DEYFALVNY 195
Cdd:cd03019  160 IGGDdtlqvlDELIEKVRY 178
PRK10954 PRK10954
thiol:disulfide interchange protein DsbA;
1-200 2.22e-56

thiol:disulfide interchange protein DsbA;


Pssm-ID: 182863 [Multi-domain]  Cd Length: 207  Bit Score: 177.21  E-value: 2.22e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364   1 MKKLFALFSMLMLSLSAHAAQFKEGEHYKVLDLEVSKKPLVTEFFSFYCPHCNTFEPVI---QQLKKQLPEGTKLQKNHV 77
Cdd:PRK10954   1 MKKIWLALAGMVLAFSASAAQFTDGKQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYhvsDNVKKKLPEGTKMTKYHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  78 SFMgGNMGPSMSKAFATMVAMKIEDQMVPVMFNRIHNMRKpPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDK 157
Cdd:PRK10954  81 EFL-GPLGKELTQAWAVAMALGVEDKVTPPLFEGVQKTQT-IQSAADIRDVFIKAGVKGEDYDAAWNSFVVKSLVAQQEK 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 646531364 158 QFENSGLTGVPAVIVNNKYLVQAQ--SIKSMDEYFA----LVNYLLTLK 200
Cdd:PRK10954 159 AAADLQLRGVPAMFVNGKYMVNNQgmDTSSMDVYVQqyadVVKFLLEKK 207
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 41-191 2.66e-30

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 109.83  E-value: 2.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364   41 VTEFFSFYCPHCNTFEPVIQQLKKQLPeGTKLQKNHVSFMG----GNMGPSMSKAFATMVAMKIE--------------- 101
Cdd:pfam01323   2 VDEFFDFLCPFCYLAKERLEKLAARYG-DVKVVYRPFPLAGakkiGNVGPSNLPVKLKYMMADLErwaalygiplrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  102 ---------------------DQMVPVMFNRIHNMRKPPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFE 160
Cdd:pfam01323  81 flgnstranrlalaagaeglaEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTAAAI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 646531364  161 NSGLTGVPAVIVNNKYLVQAQSIKSMDEYFA 191
Cdd:pfam01323 161 SLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 38-188 6.78e-28

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 102.38  E-value: 6.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  38 KPLVTEFFSFYCPHCNTFEPVIQQLKKQLPEGT-KLQKNHVSFMGGNmgpSMSKAFATMVAMKIE--DQMVPVMFNRihn 114
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKYVDGKvRVVYRPFPLLHPD---SLRAARAALCAADQGkfWAFHDALFAN--- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 646531364 115 mrKPPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFENSGLTGVPAVIVNNKYLVQAQSIKSMDE 188
Cdd:COG1651   75 --QPALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEA 146
Thioredoxin_4 pfam13462
Thioredoxin;
38-189 1.04e-10

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 57.74  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364   38 KPLVTEFFSFYCPHCNTFEPVIQQLKKQlpegtKLQKNHVSFMGGNM---GPSMSKAfATMVAMKIEDQMVPVMFNRIHN 114
Cdd:pfam13462  13 PVTVVEYADLRCPHCAKFHEEVLKLLEE-----YIDTGKVRFIIRDFpldGEGESLL-AAMAARCAGDQSPEYFLVIDKL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 646531364  115 MRKPPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFENSGLTGVPAVIVNNKYLVQAQSIKSMDEY 189
Cdd:pfam13462  87 LYSQQEEWAQDLELAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGKKVDGPLTYEELKKL 161
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 41-181 7.72e-10

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 53.95  E-value: 7.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  41 VTEFFSFYCPHCNTFEPVIQQLKKQLPEGTKLQKNHVSFMGGNMGPSMSKAFATMVAMKIEdqmvpvmfnrihnmrkppr 120
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDGGVRVVYRPFPLLGGMPPNSLAAARAALAAAAQG------------------- 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 646531364 121 ddaelrqifldegidakKFDAAYNGFAVDSMVRRMdkqfensGLTGVPAVIVNNKYLVQAQ 181
Cdd:cd02972   62 -----------------KFEALHEALADTALARAL-------GVTGTPTFVVNGEKYSGAG 98
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 41-175 7.69e-08

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.


Pssm-ID: 239321 [Multi-domain]  Cd Length: 154  Bit Score: 49.51  E-value: 7.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646531364  41 VTEFFSFYCPHCNTFEPVIQQLKKQLPEgTKLQKNHVSFMGGnmgpsmSKAFATMVAMKIEDQMvPVMFNRIHN--MRKP 118
Cdd:cd03023    9 IVEFFDYNCGYCKKLAPELEKLLKEDPD-VRVVFKEFPILGE------SSVLAARVALAVWKNG-PGKYLEFHNalMATR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 646531364 119 PR-DDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFENSGLTGVPAVIVNNK 175
Cdd:cd03023   81 GRlNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDT 138
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 121-182 6.23e-06

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 44.87  E-value: 6.23e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 646531364 121 DDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFENSGLTGVPAVIVNNKYLVQ-AQS 182
Cdd:COG2761  130 DREVLLDLAAEVGLDAEEFRADLESDEAAAAVRADEAEARELGVTGVPTFVFDGKYAVSgAQP 192
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 117-182 3.90e-04

DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239322 [Multi-domain]  Cd Length: 201  Bit Score: 39.87  E-value: 3.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 646531364 117 KPPRDDAELRQIFLDEGIDAKKFDAAYNGFAVDSMVRRMDKQFENSGLTGVPAVIVNNKYLVQ-AQS 182
Cdd:cd03024  126 KDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADEVRADEARARQLGISGVPFFVFNGKYAVSgAQP 192
 
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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