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Conserved domains on  [gi|2524968384|ref|WP_286911454|]
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thiol:disulfide interchange protein DsbA/DsbL [Idiomarina sp. UBA4520]

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 ...
 25-203 1.10e-45

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: 148.98  E-value: 1.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  25 ENEHFEVVDTKATSE-PEIIEYFSFYCIACYRFEPIAKELASTYPS--AFKKSHtsgLSPKPGMGKKMTQAYALALMLNK 101
Cdd:cd03019     1 EGKDYTVLSPPIPSGkPEVIEFFSYGCPHCYNFEPILEAWVKKLPKdvKFEKVP---VVFGGGEGEPLARAFYAAEALGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384 102 EQAISESIFKQQFGQRQSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDARDKNITGTPTLIVNGKYKILI 181
Cdd:cd03019    78 EDKLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNP 157

                         170       180
                  ....*....|....*....|..
gi 2524968384 182 NGFrDSDDLIGDLKLAIGQLMK 203
Cdd:cd03019   158 SAI-GGDDTLQVLDELIEKVRY 178
 
Name Accession Description Interval E-value
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 25-203 1.10e-45

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: 148.98  E-value: 1.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  25 ENEHFEVVDTKATSE-PEIIEYFSFYCIACYRFEPIAKELASTYPS--AFKKSHtsgLSPKPGMGKKMTQAYALALMLNK 101
Cdd:cd03019     1 EGKDYTVLSPPIPSGkPEVIEFFSYGCPHCYNFEPILEAWVKKLPKdvKFEKVP---VVFGGGEGEPLARAFYAAEALGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384 102 EQAISESIFKQQFGQRQSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDARDKNITGTPTLIVNGKYKILI 181
Cdd:cd03019    78 EDKLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNP 157

                         170       180
                  ....*....|....*....|..
gi 2524968384 182 NGFrDSDDLIGDLKLAIGQLMK 203
Cdd:cd03019   158 SAI-GGDDTLQVLDELIEKVRY 178
PRK10954 PRK10954
thiol:disulfide interchange protein DsbA;
8-179 2.01e-33

thiol:disulfide interchange protein DsbA;


Pssm-ID: 182863 [Multi-domain]  Cd Length: 207  Bit Score: 118.66  E-value: 2.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384   8 VLFVTLMATTAQAKELIENEHFEVVDTKATSEPEIIEYFSFYCIACYRFEPIAKelastYPSAFKKS----------HTS 77
Cdd:PRK10954    7 ALAGMVLAFSASAAQFTDGKQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYH-----VSDNVKKKlpegtkmtkyHVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  78 GLSPkpgMGKKMTQAYALALMLNKEQAISESIFKQqFGQRQSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMD 157
Cdd:PRK10954   82 FLGP---LGKELTQAWAVAMALGVEDKVTPPLFEG-VQKTQTIQSAADIRDVFIKAGVKGEDYDAAWNSFVVKSLVAQQE 157

                         170       180
                  ....*....|....*....|..
gi 2524968384 158 KDARDKNITGTPTLIVNGKYKI 179
Cdd:PRK10954  158 KAAADLQLRGVPAMFVNGKYMV 179
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 40-190 2.23e-22

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 88.52  E-value: 2.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  40 PEIIEYFSFYCIACYRFEPIAKELASTYPS---AFKKSHTSGLSPKpgmGKKMTQAYALALMLNKEQAISESIFKQQFGq 116
Cdd:COG1651     2 VTVVEFFDYQCPYCARFHPELPELLKKYVDgkvRVVYRPFPLLHPD---SLRAARAALCAADQGKFWAFHDALFANQPA- 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524968384 117 rqsiDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDARDKNITGTPTLIVNGKykiLINGFRDSDDL 190
Cdd:COG1651    78 ----LTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGK---LVSGAVPYEEL 144
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 41-176 1.68e-13

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: 65.91  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  41 EIIEYFSFYCIACYRFEPIAKELASTYPSA------F-----KKSHTSGLSPKPGMGKKM-------------------- 89
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVkvvyrpFplagaKKIGNVGPSNLPVKLKYMmadlerwaalygiplrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  90 -----TQAYALALMLNKE---QAISESIFKQQFGQRQSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDAR 161
Cdd:pfam01323  81 flgnsTRANRLALAAGAEglaEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTAAAI 160

                         170
                  ....*....|....*
gi 2524968384 162 DKNITGTPTLIVNGK 176
Cdd:pfam01323 161 SLGVFGVPTFVVGGK 175
 
Name Accession Description Interval E-value
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 25-203 1.10e-45

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: 148.98  E-value: 1.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  25 ENEHFEVVDTKATSE-PEIIEYFSFYCIACYRFEPIAKELASTYPS--AFKKSHtsgLSPKPGMGKKMTQAYALALMLNK 101
Cdd:cd03019     1 EGKDYTVLSPPIPSGkPEVIEFFSYGCPHCYNFEPILEAWVKKLPKdvKFEKVP---VVFGGGEGEPLARAFYAAEALGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384 102 EQAISESIFKQQFGQRQSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDARDKNITGTPTLIVNGKYKILI 181
Cdd:cd03019    78 EDKLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNP 157

                         170       180
                  ....*....|....*....|..
gi 2524968384 182 NGFrDSDDLIGDLKLAIGQLMK 203
Cdd:cd03019   158 SAI-GGDDTLQVLDELIEKVRY 178
PRK10954 PRK10954
thiol:disulfide interchange protein DsbA;
8-179 2.01e-33

thiol:disulfide interchange protein DsbA;


Pssm-ID: 182863 [Multi-domain]  Cd Length: 207  Bit Score: 118.66  E-value: 2.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384   8 VLFVTLMATTAQAKELIENEHFEVVDTKATSEPEIIEYFSFYCIACYRFEPIAKelastYPSAFKKS----------HTS 77
Cdd:PRK10954    7 ALAGMVLAFSASAAQFTDGKQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYH-----VSDNVKKKlpegtkmtkyHVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  78 GLSPkpgMGKKMTQAYALALMLNKEQAISESIFKQqFGQRQSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMD 157
Cdd:PRK10954   82 FLGP---LGKELTQAWAVAMALGVEDKVTPPLFEG-VQKTQTIQSAADIRDVFIKAGVKGEDYDAAWNSFVVKSLVAQQE 157

                         170       180
                  ....*....|....*....|..
gi 2524968384 158 KDARDKNITGTPTLIVNGKYKI 179
Cdd:PRK10954  158 KAAADLQLRGVPAMFVNGKYMV 179
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 40-190 2.23e-22

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 88.52  E-value: 2.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  40 PEIIEYFSFYCIACYRFEPIAKELASTYPS---AFKKSHTSGLSPKpgmGKKMTQAYALALMLNKEQAISESIFKQQFGq 116
Cdd:COG1651     2 VTVVEFFDYQCPYCARFHPELPELLKKYVDgkvRVVYRPFPLLHPD---SLRAARAALCAADQGKFWAFHDALFANQPA- 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524968384 117 rqsiDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDARDKNITGTPTLIVNGKykiLINGFRDSDDL 190
Cdd:COG1651    78 ----LTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGK---LVSGAVPYEEL 144
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 41-176 1.68e-13

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: 65.91  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  41 EIIEYFSFYCIACYRFEPIAKELASTYPSA------F-----KKSHTSGLSPKPGMGKKM-------------------- 89
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVkvvyrpFplagaKKIGNVGPSNLPVKLKYMmadlerwaalygiplrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  90 -----TQAYALALMLNKE---QAISESIFKQQFGQRQSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDAR 161
Cdd:pfam01323  81 flgnsTRANRLALAAGAEglaEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTAAAI 160

                         170
                  ....*....|....*
gi 2524968384 162 DKNITGTPTLIVNGK 176
Cdd:pfam01323 161 SLGVFGVPTFVVGGK 175
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 91-179 1.75e-11

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: 60.67  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  91 QAYALALMLNKEQAISESIFKQQFGQRQSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDARDKNITGTPT 170
Cdd:COG2761    99 RLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDEAAAAVRADEAEARELGVTGVPT 178


                  ....*....
gi 2524968384 171 LIVNGKYKI 179
Cdd:COG2761   179 FVFDGKYAV 187
Thioredoxin_4 pfam13462
Thioredoxin;
42-176 8.08e-11

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 58.12  E-value: 8.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  42 IIEYFSFYCIACYRFEPIAKELASTYPSAFKKSHTSGLSPKPGmGKKMTQAYALALMLNKEQAISESIFKQQFGQRQSID 121
Cdd:pfam13462  16 VVEYADLRCPHCAKFHEEVLKLLEEYIDTGKVRFIIRDFPLDG-EGESLLAAMAARCAGDQSPEYFLVIDKLLYSQQEEW 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2524968384 122 TQDKlkDIFVQAGVSEKDFERGYNSFSVKARARQMDKDARDKNITGTPTLIVNGK 176
Cdd:pfam13462  95 AQDL--ELAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGK 147
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 95-179 3.36e-06

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: 45.65  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  95 LALMLNKEQAISESIFKQQFGQRQSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDARDKNITGTPTLIVN 174
Cdd:cd03024   103 LAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADEVRADEARARQLGISGVPFFVFN 182


                  ....*
gi 2524968384 175 GKYKI 179
Cdd:cd03024   183 GKYAV 187
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 42-176 3.84e-06

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: 43.93  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  42 IIEYFSFYCIACYRFEPIAKELASTYPS--AFKKSHTSGLSPKPGMGKKMTQAYALALMLNKEQAIsesifkqqfgqrqs 119
Cdd:cd02972     1 IVEFFDPLCPYCYLFEPELEKLLYADDGgvRVVYRPFPLLGGMPPNSLAAARAALAAAAQGKFEAL-------------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2524968384 120 idtQDKLKDIfvqagvsekdfergynsfsvkararqmdKDARDKNITGTPTLIVNGK 176
Cdd:cd02972    67 ---HEALADT----------------------------ALARALGVTGTPTFVVNGE 92
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 92-175 2.76e-05

DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK).


Pssm-ID: 239320 [Multi-domain]  Cd Length: 192  Bit Score: 43.00  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  92 AYALALMLNKEQAISESIFKQQFGQRQSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDARDKNITGTPTL 171
Cdd:cd03022    92 ALAAQAEGDAAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAALRANTEEAIARGVFGVPTF 171


                  ....
gi 2524968384 172 IVNG 175
Cdd:cd03022   172 VVDG 175
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 42-190 7.98e-05

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: 41.43  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  42 IIEYFSFYCIACYRFEPIAKELASTYPSA---FK----------KSHTSGLSPKPGMGKKMTQAYaLALMLNKEQAises 108
Cdd:cd03023     9 IVEFFDYNCGYCKKLAPELEKLLKEDPDVrvvFKefpilgessvLAARVALAVWKNGPGKYLEFH-NALMATRGRL---- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384 109 ifkqqfgqrqsidTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQMDKDARDKNITGTPTLIVNGKykiLINGFRDSD 188
Cdd:cd03023    84 -------------NEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDT---VIPGAVPAD 147


                  ..
gi 2524968384 189 DL 190
Cdd:cd03023   148 TL 149
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
 40-188 2.20e-03

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


Pssm-ID: 239323 [Multi-domain]  Cd Length: 193  Bit Score: 37.69  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384  40 PEIIEYFSFYCIACYRFEPIAKELASTYPSAFKKSHTSGLSPkPGMGKKMTQAYALALMLNKEQAISESifKQQFGQR-- 117
Cdd:cd03025     1 LELYYFIDPLCGWCYGFEPLLEKLKEEYGGGIEVELHLGGLL-PGNNARQITKQWRIYVHWHKARIALT--GQPFGEDyl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524968384 118 ------------------------------------------QSIDTQDKLKDIFVQAGVSEKDFERGYNSFSVKARARQ 155
Cdd:cd03025    78 elllfdldsapasraikaarlqgperllemlkaiqrahyvegRDLADTEVLRELAIELGLDVEEFLEDFQSDEAKQAIQE 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2524968384 156 MDKDARDKNITGTPTLIV--NGKYKILINGFRDSD 188
Cdd:cd03025   158 DQKLARELGINGFPTLVLedDNGEGILLTGYYPYE 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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