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Conserved domains on  [gi|447037817|ref|WP_001115073|]
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MULTISPECIES: DsbA family protein [Gammaproteobacteria]

Protein Classification

DsbA family protein( domain architecture ID 11447254)

DsbA family protein belongs to the thioredoxin superfamily of proteins containing a redox active CXXC motif, similar to DsbA that is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  11967064|9099998|10049365|15558583|12524212
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 114-273 7.85e-35

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


:

Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 123.18  E-value: 7.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 114 TLVEFSDMECPFCKQFHDTPKQIVDA-SKGNVNWQWKHMPLDfhNPTAHREALAAECIAEQKGnrgFWVFVNDIFhhSQG 192
Cdd:COG1651    3 TVVEFFDYQCPYCARFHPELPELLKKyVDGKVRVVYRPFPLL--HPDSLRAARAALCAADQGK---FWAFHDALF--ANQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 193 NGAGVADLASVVTGVGADLDEFRDCLGSGKHEDKVEADIQKAKSYGVNGTPaTFVVDNqtgksQLLGGAQPAQAIMAVMR 272
Cdd:COG1651   76 PALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTP-TFVVNG-----KLVSGAVPYEELEAALD 149


                 .
gi 447037817 273 K 273
Cdd:COG1651  150 A 150
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 114-273 7.85e-35

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 123.18  E-value: 7.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 114 TLVEFSDMECPFCKQFHDTPKQIVDA-SKGNVNWQWKHMPLDfhNPTAHREALAAECIAEQKGnrgFWVFVNDIFhhSQG 192
Cdd:COG1651    3 TVVEFFDYQCPYCARFHPELPELLKKyVDGKVRVVYRPFPLL--HPDSLRAARAALCAADQGK---FWAFHDALF--ANQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 193 NGAGVADLASVVTGVGADLDEFRDCLGSGKHEDKVEADIQKAKSYGVNGTPaTFVVDNqtgksQLLGGAQPAQAIMAVMR 272
Cdd:COG1651   76 PALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTP-TFVVNG-----KLVSGAVPYEELEAALD 149


                 .
gi 447037817 273 K 273
Cdd:COG1651  150 A 150
Thioredoxin_4 pfam13462
Thioredoxin;
104-249 2.83e-14

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 68.91  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817  104 HIYGAPGARFTLVEFSDMECPFCKQFHDTPKQIVDA--SKGNVNWQWKHMPLDFHNPtAHREALAAECIAEQkgNRGFWV 181
Cdd:pfam13462   5 PVIGNPDAPVTVVEYADLRCPHCAKFHEEVLKLLEEyiDTGKVRFIIRDFPLDGEGE-SLLAAMAARCAGDQ--SPEYFL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447037817  182 FVNDIFHHSQGNGAGVADLASVvtgVGADLDEFRDCLGSGKHEDKVEADIQKAKSYGVNGTPaTFVVD 249
Cdd:pfam13462  82 VIDKLLYSQQEEWAQDLELAAL---AGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTP-TFIIN 145
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 115-251 3.20e-13

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: 64.35  E-value: 3.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 115 LVEFSDMECPFCKQFHDTPKQIVDASKGNVNWQWKHMPLDFHNPT-AHREALAAECIAEQKgnrGFWVFVNDIfhhsqgn 193
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDGGVRVVYRPFPLLGGMPPnSLAAARAALAAAAQG---KFEALHEAL------- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 447037817 194 gagvadlasvvtgvgadldefrdclgsgkhedkveADIQKAKSYGVNGTPaTFVVDNQ 251
Cdd:cd02972   71 -----------------------------------ADTALARALGVTGTP-TFVVNGE 92
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 114-273 7.85e-35

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 123.18  E-value: 7.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 114 TLVEFSDMECPFCKQFHDTPKQIVDA-SKGNVNWQWKHMPLDfhNPTAHREALAAECIAEQKGnrgFWVFVNDIFhhSQG 192
Cdd:COG1651    3 TVVEFFDYQCPYCARFHPELPELLKKyVDGKVRVVYRPFPLL--HPDSLRAARAALCAADQGK---FWAFHDALF--ANQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 193 NGAGVADLASVVTGVGADLDEFRDCLGSGKHEDKVEADIQKAKSYGVNGTPaTFVVDNqtgksQLLGGAQPAQAIMAVMR 272
Cdd:COG1651   76 PALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTP-TFVVNG-----KLVSGAVPYEELEAALD 149


                 .
gi 447037817 273 K 273
Cdd:COG1651  150 A 150
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 150-275 9.45e-15

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: 71.07  E-value: 9.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 150 HMPLDFHNPT------AHReALAAeciAEQKGnrGFWVFVNDIFHHSQGNGAGVAD---LASVVTGVGADLDEFRDCLGS 220
Cdd:COG2761   81 GLPFDFDRIKppntfdAHR-LLKA---AELQG--KQDALLEALFEAYFTEGRDIGDrevLLDLAAEVGLDAEEFRADLES 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447037817 221 GKHEDKVEADIQKAKSYGVNGTPaTFVVDNQtgksQLLGGAQPAQAIMAVMRKMM 275
Cdd:COG2761  155 DEAAAAVRADEAEARELGVTGVP-TFVFDGK----YAVSGAQPYEVFEQALRQAL 204
Thioredoxin_4 pfam13462
Thioredoxin;
104-249 2.83e-14

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 68.91  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817  104 HIYGAPGARFTLVEFSDMECPFCKQFHDTPKQIVDA--SKGNVNWQWKHMPLDFHNPtAHREALAAECIAEQkgNRGFWV 181
Cdd:pfam13462   5 PVIGNPDAPVTVVEYADLRCPHCAKFHEEVLKLLEEyiDTGKVRFIIRDFPLDGEGE-SLLAAMAARCAGDQ--SPEYFL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447037817  182 FVNDIFHHSQGNGAGVADLASVvtgVGADLDEFRDCLGSGKHEDKVEADIQKAKSYGVNGTPaTFVVD 249
Cdd:pfam13462  82 VIDKLLYSQQEEWAQDLELAAL---AGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTP-TFIIN 145
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 115-251 3.20e-13

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: 64.35  E-value: 3.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 115 LVEFSDMECPFCKQFHDTPKQIVDASKGNVNWQWKHMPLDFHNPT-AHREALAAECIAEQKgnrGFWVFVNDIfhhsqgn 193
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDGGVRVVYRPFPLLGGMPPnSLAAARAALAAAAQG---KFEALHEAL------- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 447037817 194 gagvadlasvvtgvgadldefrdclgsgkhedkveADIQKAKSYGVNGTPaTFVVDNQ 251
Cdd:cd02972   71 -----------------------------------ADTALARALGVTGTP-TFVVNGE 92
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 114-253 7.27e-12

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: 62.83  E-value: 7.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817  114 TLVEFSDMECPFCKQFHDTPKQIVdASKGNVNWQWKHMPLDFHNPT---------------------------------- 159
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLA-ARYGDVKVVYRPFPLAGAKKIgnvgpsnlpvklkymmadlerwaalygiplrfpa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817  160 --------AHREALAAEciAEQKGNRgfwvFVNDIFHHSQGNGAGVAD---LASVVTGVGADLDEFRDCLGSGKHEDKVE 228
Cdd:pfam01323  80 nflgnstrANRLALAAG--AEGLAEK----VVRELFNALWGEGAAITDdsvLREVAEKAGLDAEEFDEFLDSPAVKEAVR 153

                         170       180
                  ....*....|....*....|....*
gi 447037817  229 ADIQKAKSYGVNGTPaTFVVDNQTG 253
Cdd:pfam01323 154 ENTAAAISLGVFGVP-TFVVGGKMV 177
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 160-272 9.42e-11

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: 59.90  E-value: 9.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 160 AHREALAAEciAEQKGNRgfwvFVNDIF--HHSQG-NgagVAD---LASVVTGVGADLDEFRDCLGSGKHEDKVEADIQK 233
Cdd:cd03024   97 AHRLIHLAK--EQGKQDA----LVEALFraYFTEGkD---IGDrdvLVDLAEEAGLDAAEARAVLASDEYADEVRADEAR 167

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 447037817 234 AKSYGVNGTPaTFVVDNQtgksQLLGGAQPAQAIMAVMR 272
Cdd:cd03024  168 ARQLGISGVP-FFVFNGK----YAVSGAQPPEVFLQALR 201
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 107-271 4.34e-10

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: 57.22  E-value: 4.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 107 GAPGARFTLVEFSDMECPFCKQFHDTPKQIVDASkGNVNWQWKHMPLdFHNP--TAHREALAAECIAEQKgnrgFWVFVN 184
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKED-PDVRVVFKEFPI-LGESsvLAARVALAVWKNGPGK----YLEFHN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 185 DIFHHSQG-NGAGVADLAsvvTGVGADLDEFRDCLGSGKHEDKVEADIQKAKSYGVNGTPAtFVVDnqtgkSQLLGGAQP 263
Cdd:cd03023   75 ALMATRGRlNEESLLRIA---KKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPA-FIIG-----DTVIPGAVP 145


                 ....*...
gi 447037817 264 AQAIMAVM 271
Cdd:cd03023  146 ADTLKEAI 153
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 106-271 9.28e-05

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 42.30  E-value: 9.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 106 YGAPGARFTLVEFSDMECPFCKQFHDTpkqiVDASKGNVNWQWKHMPLDFHnPTAHREALAAECiAEQKgnrgfwvfvND 185
Cdd:cd03020   72 YGKGNGKRVVYVFTDPDCPYCRKLEKE----LKPNADGVTVRIFPVPILGL-PDSTAKAAAIWC-AKDR---------AK 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 186 IFH-HSQGNGAGVADlasvvtgvgadldefRDClgsgkhEDKVEADIQKAKSYGVNGTPATFVVDnqtGksQLLGGAQPA 264
Cdd:cd03020  137 AWTdAMSGGKVPPPA---------------ASC------DNPVAANLALGRQLGVNGTPTIVLAD---G--RVVPGAPPA 190


                 ....*..
gi 447037817 265 QAIMAVM 271
Cdd:cd03020  191 AQLEALL 197
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 150-251 4.70e-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: 40.30  E-value: 4.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 150 HMPLDFHNPT--AHREALAAeciaeqkGNRGFWV--FVNDIFHHSQGNGAGVAD---LASVVTGVGADLDEFRDCLGSGK 222
Cdd:cd03022   76 RFPPRFPPNTlrAMRAALAA-------QAEGDAAeaFARAVFRALWGEGLDIADpavLAAVAAAAGLDADELLAAADDPA 148

                         90       100
                 ....*....|....*....|....*....
gi 447037817 223 HEDKVEADIQKAKSYGVNGTPaTFVVDNQ 251
Cdd:cd03022  149 VKAALRANTEEAIARGVFGVP-TFVVDGE 176
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
 200-274 4.76e-04

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


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 40.23  E-value: 4.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447037817 200 LASVVTGVGADLDEFRDCLGSGKHEDKVEADIQKAKSYGVNGTPaTFVVDNQTGKSQLLGGAQPAQAIMAVMRKM 274
Cdd:COG3531  133 LAELAAELGLDAEAFAAALASEETRQHIQQEFALARQLGVQGFP-TLVLEQGGQLYLLPRGYGDPEALLAALEQL 206
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 115-274 1.71e-03

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: 38.42  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 115 LVEFSDMECPFCKQFHDTPKQIVDASKGNVNWqwKHMPLDFHNP--TAHREALAAeciAEQKGNrgFWVFVNDIFHHSQG 192
Cdd:cd03019   19 VIEFFSYGCPHCYNFEPILEAWVKKLPKDVKF--EKVPVVFGGGegEPLARAFYA---AEALGL--EDKLHAALFEAIHE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 193 NG---AGVADLASVVTGVGADLDEFRDCLGSGKHEDKVEADIQKAKSYGVNGTPAtFVVDnqtGKSQLLGGAQPAQAIMA 269
Cdd:cd03019   92 KRkrlLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPA-FVVN---GKYVVNPSAIGGDDTLQ 167


                 ....*
gi 447037817 270 VMRKM 274
Cdd:cd03019  168 VLDEL 172
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
 164-265 3.74e-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: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447037817 164 ALAAECIAEQKGNRGFWVFVNDIFHHSQGNGAGVAD---LASVVTGVGADLDEFRDCLGSGKHEDKVEADIQKAKSYGVN 240
Cdd:cd03025   89 ASRAIKAARLQGPERLLEMLKAIQRAHYVEGRDLADtevLRELAIELGLDVEEFLEDFQSDEAKQAIQEDQKLARELGIN 168

                         90       100
                 ....*....|....*....|....*
gi 447037817 241 GTPaTFVVDNQTGKSQLLGGAQPAQ 265
Cdd:cd03025  169 GFP-TLVLEDDNGEGILLTGYYPYE 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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