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Conserved domains on  [gi|1085076452|gb|OGS75679|]
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hypothetical protein A2063_01145 [Gallionellales bacterium GWA2_60_142]

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 ...
 27-201 9.16e-58

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: 179.79  E-value: 9.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  27 KGYTLLVPAQPTAtqKIEVLEFFSYGCSHCFHLHHDLSIWAKKMPKDVELVYVPVIFRDSA-EPLARTYYALESMPNFEK 105
Cdd:cd03019     3 KDYTVLSPPIPSG--KPEVIEFFSYGCPHCYNFEPILEAWVKKLPKDVKFEKVPVVFGGGEgEPLARAFYAAEALGLEDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452 106 MHDAIYRGMNVENAELFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVDGKYVITG--L 183
Cdd:cd03019    81 LHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNPsaI 160

                         170
                  ....*....|....*...
gi 1085076452 184 QPADTIRVLDAVIAKARK 201
Cdd:cd03019   161 GGDDTLQVLDELIEKVRY 178
 
Name Accession Description Interval E-value
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 27-201 9.16e-58

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: 179.79  E-value: 9.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  27 KGYTLLVPAQPTAtqKIEVLEFFSYGCSHCFHLHHDLSIWAKKMPKDVELVYVPVIFRDSA-EPLARTYYALESMPNFEK 105
Cdd:cd03019     3 KDYTVLSPPIPSG--KPEVIEFFSYGCPHCYNFEPILEAWVKKLPKDVKFEKVPVVFGGGEgEPLARAFYAAEALGLEDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452 106 MHDAIYRGMNVENAELFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVDGKYVITG--L 183
Cdd:cd03019    81 LHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNPsaI 160

                         170
                  ....*....|....*...
gi 1085076452 184 QPADTIRVLDAVIAKARK 201
Cdd:cd03019   161 GGDDTLQVLDELIEKVRY 178
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 42-200 7.68e-33

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 115.48  E-value: 7.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  42 KIEVLEFFSYGCSHCFHLHHDLSIWAKKMPK-DVELVYVPV-IFRDSAEPLARTYYALESMPNFEKMHDAIYrgmnvENA 119
Cdd:COG1651     1 KVTVVEFFDYQCPYCARFHPELPELLKKYVDgKVRVVYRPFpLLHPDSLRAARAALCAADQGKFWAFHDALF-----ANQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452 120 ELFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVDGKyVITGLQPADTirvLDAVIAKA 199
Cdd:COG1651    76 PALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGK-LVSGAVPYEE---LEAALDAA 151


                  .
gi 1085076452 200 R 200
Cdd:COG1651   152 L 152
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 58-190 5.23e-11

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: 59.36  E-value: 5.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  58 HLHHDLSIWAKKmpKDVELVYVPVIFRDSAEPLARTYYALESMP---NFEKMHDAIYrgmnVENAELFDLDSIAAYVAKQ 134
Cdd:pfam01323  59 YMMADLERWAAL--YGIPLRFPANFLGNSTRANRLALAAGAEGLaekVVRELFNALW----GEGAAITDDSVLREVAEKA 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085076452 135 GADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVDGKyVITGLQPADTIR 190
Cdd:pfam01323 133 GLDAEEFDEFLDSPAVKEAVRENTAAAISLGVFGVPTFVVGGK-MVFGADRLDTLA 187
PRK10954 PRK10954
thiol:disulfide interchange protein DsbA;
1-180 2.32e-10

thiol:disulfide interchange protein DsbA;


Pssm-ID: 182863 [Multi-domain]  Cd Length: 207  Bit Score: 57.80  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452   1 MKNVIKSLVVAAaLLFGSTACSEEANKGYTLL---VPAQPtatqkiEVLEFFSYGCSHCF---HLHHDLSIWAKKMPKDV 74
Cdd:PRK10954    1 MKKIWLALAGMV-LAFSASAAQFTDGKQYTTLdkpVAGEP------QVLEFFSFYCPHCYqfeEVYHVSDNVKKKLPEGT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  75 ELVYVPVIFR-DSAEPLARTYYALESMPNFEKMHDAIYRGMNvENAELFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSR 153
Cdd:PRK10954   74 KMTKYHVEFLgPLGKELTQAWAVAMALGVEDKVTPPLFEGVQ-KTQTIQSAADIRDVFIKAGVKGEDYDAAWNSFVVKSL 152

                         170       180
                  ....*....|....*....|....*..
gi 1085076452 154 VTRAKQMIRSYAIQGTPTLVVDGKYVI 180
Cdd:PRK10954  153 VAQQEKAAADLQLRGVPAMFVNGKYMV 179
 
Name Accession Description Interval E-value
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 27-201 9.16e-58

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: 179.79  E-value: 9.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  27 KGYTLLVPAQPTAtqKIEVLEFFSYGCSHCFHLHHDLSIWAKKMPKDVELVYVPVIFRDSA-EPLARTYYALESMPNFEK 105
Cdd:cd03019     3 KDYTVLSPPIPSG--KPEVIEFFSYGCPHCYNFEPILEAWVKKLPKDVKFEKVPVVFGGGEgEPLARAFYAAEALGLEDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452 106 MHDAIYRGMNVENAELFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVDGKYVITG--L 183
Cdd:cd03019    81 LHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNPsaI 160

                         170
                  ....*....|....*...
gi 1085076452 184 QPADTIRVLDAVIAKARK 201
Cdd:cd03019   161 GGDDTLQVLDELIEKVRY 178
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 42-200 7.68e-33

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 115.48  E-value: 7.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  42 KIEVLEFFSYGCSHCFHLHHDLSIWAKKMPK-DVELVYVPV-IFRDSAEPLARTYYALESMPNFEKMHDAIYrgmnvENA 119
Cdd:COG1651     1 KVTVVEFFDYQCPYCARFHPELPELLKKYVDgKVRVVYRPFpLLHPDSLRAARAALCAADQGKFWAFHDALF-----ANQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452 120 ELFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVDGKyVITGLQPADTirvLDAVIAKA 199
Cdd:COG1651    76 PALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGK-LVSGAVPYEE---LEAALDAA 151


                  .
gi 1085076452 200 R 200
Cdd:COG1651   152 L 152
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 42-190 4.17e-14

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: 66.85  E-value: 4.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  42 KIEVLEFFSYGCSHCFHLHHDLSIWAKKMPkDVELVYVPV-IFRDSAEPLARTYYA-LESMPN-FEKMHDAIY--RGMnv 116
Cdd:cd03023     6 DVTIVEFFDYNCGYCKKLAPELEKLLKEDP-DVRVVFKEFpILGESSVLAARVALAvWKNGPGkYLEFHNALMatRGR-- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085076452 117 enaelFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVdGKYVITGLQPADTIR 190
Cdd:cd03023    83 -----LNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFII-GDTVIPGAVPADTLK 150
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 45-179 1.68e-12

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: 60.88  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  45 VLEFFSYGCSHCFHLHHDLSIWAKKMPKDVELVYVPVIFRD----SAEPLARTYYALESMPNFEKMHDAIyrgmnvenae 120
Cdd:cd02972     1 IVEFFDPLCPYCYLFEPELEKLLYADDGGVRVVYRPFPLLGgmppNSLAAARAALAAAAQGKFEALHEAL---------- 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1085076452 121 lfdldsiaayvakqgadrakftaaynsfsmssrvtRAKQMIRSYAIQGTPTLVVDGKYV 179
Cdd:cd02972    71 -----------------------------------ADTALARALGVTGTPTFVVNGEKY 94
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 104-197 1.72e-12

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: 63.36  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452 104 EKMHDAIYRGMNVENAELFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVDGKYVITGL 183
Cdd:COG2761   111 DALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDEAAAAVRADEAEARELGVTGVPTFVFDGKYAVSGA 190

                          90
                  ....*....|....*
gi 1085076452 184 QPADTI-RVLDAVIA 197
Cdd:COG2761   191 QPYEVFeQALRQALA 205
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 58-190 5.23e-11

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: 59.36  E-value: 5.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  58 HLHHDLSIWAKKmpKDVELVYVPVIFRDSAEPLARTYYALESMP---NFEKMHDAIYrgmnVENAELFDLDSIAAYVAKQ 134
Cdd:pfam01323  59 YMMADLERWAAL--YGIPLRFPANFLGNSTRANRLALAAGAEGLaekVVRELFNALW----GEGAAITDDSVLREVAEKA 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085076452 135 GADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVDGKyVITGLQPADTIR 190
Cdd:pfam01323 133 GLDAEEFDEFLDSPAVKEAVRENTAAAISLGVFGVPTFVVGGK-MVFGADRLDTLA 187
Thioredoxin_4 pfam13462
Thioredoxin;
42-190 6.80e-11

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 58.51  E-value: 6.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  42 KIEVLEFFSYGCSHCFHLHHDLS-IWAKKMPK-DVELVYVPVIFRDSAEPLARTYYAL----ESMPNFEKMHDAIYR-GM 114
Cdd:pfam13462  13 PVTVVEYADLRCPHCAKFHEEVLkLLEEYIDTgKVRFIIRDFPLDGEGESLLAAMAARcagdQSPEYFLVIDKLLYSqQE 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085076452 115 NVENAELFDldsiaayvAKQGADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVDGKyVITGLQPADTIR 190
Cdd:pfam13462  93 EWAQDLELA--------ALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGK-KVDGPLTYEELK 159
PRK10954 PRK10954
thiol:disulfide interchange protein DsbA;
1-180 2.32e-10

thiol:disulfide interchange protein DsbA;


Pssm-ID: 182863 [Multi-domain]  Cd Length: 207  Bit Score: 57.80  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452   1 MKNVIKSLVVAAaLLFGSTACSEEANKGYTLL---VPAQPtatqkiEVLEFFSYGCSHCF---HLHHDLSIWAKKMPKDV 74
Cdd:PRK10954    1 MKKIWLALAGMV-LAFSASAAQFTDGKQYTTLdkpVAGEP------QVLEFFSFYCPHCYqfeEVYHVSDNVKKKLPEGT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  75 ELVYVPVIFR-DSAEPLARTYYALESMPNFEKMHDAIYRGMNvENAELFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSR 153
Cdd:PRK10954   74 KMTKYHVEFLgPLGKELTQAWAVAMALGVEDKVTPPLFEGVQ-KTQTIQSAADIRDVFIKAGVKGEDYDAAWNSFVVKSL 152

                         170       180
                  ....*....|....*....|....*..
gi 1085076452 154 VTRAKQMIRSYAIQGTPTLVVDGKYVI 180
Cdd:PRK10954  153 VAQQEKAAADLQLRGVPAMFVNGKYMV 179
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 104-193 2.92e-08

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: 51.81  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452 104 EKMHDAIYRGMNVENAELFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSRVTRAKQMIRSYAIQGTPTLVVDGKYVITGL 183
Cdd:cd03024   111 DALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADEVRADEARARQLGISGVPFFVFNGKYAVSGA 190

                          90
                  ....*....|.
gi 1085076452 184 QPADTI-RVLD 193
Cdd:cd03024   191 QPPEVFlQALR 201
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
 84-190 1.70e-06

Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 46.78  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  84 RDSaEPLARTYYALESM-PNFE-KMHDAIYRGMNVENAELFDLDSIAAYVAKQGADRAKFTAAYNSFSMSSRVTRAKQMI 161
Cdd:COG3531    89 LDS-EPACRAVLAARELaPERElAMLHAIQRAFYVEGRDISDPEVLAELAAELGLDAEAFAAALASEETRQHIQQEFALA 167

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1085076452 162 RSYAIQGTPTLVV---DGKYVIT-GLQPADTIR 190
Cdd:COG3531   168 RQLGVQGFPTLVLeqgGQLYLLPrGYGDPEALL 200
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 58-176 4.25e-04

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: 39.53  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085076452  58 HLHHDLSIWAKKMpkDVELVYVPVIFRDSAEPLARTYYALESMPNFEKMHDAIYRGMNVENAELFDLDSIAAYVAKQGAD 137
Cdd:cd03022    59 YRLRDLERWARRY--GIPLRFPPRFPPNTLRAMRAALAAQAEGDAAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLD 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1085076452 138 RAKFTAAYNSfsmssrvTRAKQMIRS---YAIQ----GTPTLVVDG 176
Cdd:cd03022   137 ADELLAAADD-------PAVKAALRAnteEAIArgvfGVPTFVVDG 175
Thioredoxin_3 pfam13192
Thioredoxin domain;
161-185 7.03e-04

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 36.81  E-value: 7.03e-04
                          10        20
                  ....*....|....*....|....*
gi 1085076452 161 IRSYAIQGTPTLVVDGKYVITGLQP 185
Cdd:pfam13192  37 IAKYGVMSTPALVINGKVVSSGKVP 61
 
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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