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Conserved domains on  [gi|495777649|ref|WP_008502228|]
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MULTISPECIES: DsbA family oxidoreductase [Enterobacteriaceae]

Protein Classification

DsbA family oxidoreductase( domain architecture ID 10122494)

DsbA family oxidoreductase belonging to the thioredoxin superfamily, similar to Deinococcus radiodurans FrnE, a cadmium-inducible disulfide isomerase chaperone that functions in oxidative stress tolerance

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015036
PubMed:  12524212|9099998|10049365|15558583
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 10-208 9.53e-76

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: 227.46  E-value: 9.53e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  10 IDIWSDLVCPWCWIAKKRFEQGLNRFEFRDQVVIRHHSYRLAGGTPA--MPFKDAIVKKLGSQHSAELMMNQVGTAGKSE 87
Cdd:cd03024    1 IDIWSDVVCPWCYIGKRRLEKALAELGDEVDVEIEWRPFELNPDMPPegEDRREYLARKYGSTAEQAAAMRRVEAAAAAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  88 GLIYNFDGMMFGDTEDAHTLLVAARKAGIADAVEERFYHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFRAT 167
Cdd:cd03024   81 GLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 495777649 168 VSDDEAHAQSIGLSGVPVFVMNEKYAISGAQGADNFLNALR 208
Cdd:cd03024  161 VRADEARARQLGISGVPFFVFNGKYAVSGAQPPEVFLQALR 201
 
Name Accession Description Interval E-value
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 10-208 9.53e-76

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: 227.46  E-value: 9.53e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  10 IDIWSDLVCPWCWIAKKRFEQGLNRFEFRDQVVIRHHSYRLAGGTPA--MPFKDAIVKKLGSQHSAELMMNQVGTAGKSE 87
Cdd:cd03024    1 IDIWSDVVCPWCYIGKRRLEKALAELGDEVDVEIEWRPFELNPDMPPegEDRREYLARKYGSTAEQAAAMRRVEAAAAAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  88 GLIYNFDGMMFGDTEDAHTLLVAARKAGIADAVEERFYHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFRAT 167
Cdd:cd03024   81 GLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 495777649 168 VSDDEAHAQSIGLSGVPVFVMNEKYAISGAQGADNFLNALR 208
Cdd:cd03024  161 VRADEARARQLGISGVPFFVFNGKYAVSGAQPPEVFLQALR 201
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 7-212 1.65e-69

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: 211.67  E-value: 1.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649   7 TLTIDIWSDLVCPWCWIAKKRFEQGLNRFEfrDQVVIRHHSYRLAGGTPAMPFK-DAIVKKLGSQHSAELMMNQVGTAGK 85
Cdd:COG2761    1 PLKIDIFSDVVCPWCYIGKRRLEKALAEFG--DDVEIRWRPFELNPDMPPEGEDrREYLLAKGSPEQAEQMRAHVEEAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  86 SEGLIYNFDGMMFGDTEDAHTLLVAARKAGIADAVEERFYHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFR 165
Cdd:COG2761   79 EEGLPFDFDRIKPPNTFDAHRLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDEAA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495777649 166 ATVSDDEAHAQSIGLSGVPVFVMNEKYAISGAQGADNFLNALRQVWD 212
Cdd:COG2761  159 AAVRADEAEARELGVTGVPTFVFDGKYAVSGAQPYEVFEQALRQALA 205
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 9-208 9.42e-39

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: 132.94  E-value: 9.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649    9 TIDIWSDLVCPWCWIAKKRFEQGLNRfefRDQVVIRHHSYRLAGGTPAMPFKDAIVKklgsqHSAELMMNQVGTAGKSEG 88
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAAR---YGDVKVVYRPFPLAGAKKIGNVGPSNLP-----VKLKYMMADLERWAALYG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649   89 LIYNFDGMMFGDTEDAHTLLVAARKAGIADAVEERFYHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFRATV 168
Cdd:pfam01323  73 IPLRFPANFLGNSTRANRLALAAGAEGLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 495777649  169 SDDEAHAQSIGLSGVPVFVMNEKyAISGAQGADNFLNALR 208
Cdd:pfam01323 153 RENTAAAISLGVFGVPTFVVGGK-MVFGADRLDTLADALA 191
 
Name Accession Description Interval E-value
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 10-208 9.53e-76

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: 227.46  E-value: 9.53e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  10 IDIWSDLVCPWCWIAKKRFEQGLNRFEFRDQVVIRHHSYRLAGGTPA--MPFKDAIVKKLGSQHSAELMMNQVGTAGKSE 87
Cdd:cd03024    1 IDIWSDVVCPWCYIGKRRLEKALAELGDEVDVEIEWRPFELNPDMPPegEDRREYLARKYGSTAEQAAAMRRVEAAAAAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  88 GLIYNFDGMMFGDTEDAHTLLVAARKAGIADAVEERFYHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFRAT 167
Cdd:cd03024   81 GLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 495777649 168 VSDDEAHAQSIGLSGVPVFVMNEKYAISGAQGADNFLNALR 208
Cdd:cd03024  161 VRADEARARQLGISGVPFFVFNGKYAVSGAQPPEVFLQALR 201
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 7-212 1.65e-69

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: 211.67  E-value: 1.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649   7 TLTIDIWSDLVCPWCWIAKKRFEQGLNRFEfrDQVVIRHHSYRLAGGTPAMPFK-DAIVKKLGSQHSAELMMNQVGTAGK 85
Cdd:COG2761    1 PLKIDIFSDVVCPWCYIGKRRLEKALAEFG--DDVEIRWRPFELNPDMPPEGEDrREYLLAKGSPEQAEQMRAHVEEAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  86 SEGLIYNFDGMMFGDTEDAHTLLVAARKAGIADAVEERFYHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFR 165
Cdd:COG2761   79 EEGLPFDFDRIKPPNTFDAHRLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDEAA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495777649 166 ATVSDDEAHAQSIGLSGVPVFVMNEKYAISGAQGADNFLNALRQVWD 212
Cdd:COG2761  159 AAVRADEAEARELGVTGVPTFVFDGKYAVSGAQPYEVFEQALRQALA 205
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 9-208 9.42e-39

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: 132.94  E-value: 9.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649    9 TIDIWSDLVCPWCWIAKKRFEQGLNRfefRDQVVIRHHSYRLAGGTPAMPFKDAIVKklgsqHSAELMMNQVGTAGKSEG 88
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAAR---YGDVKVVYRPFPLAGAKKIGNVGPSNLP-----VKLKYMMADLERWAALYG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649   89 LIYNFDGMMFGDTEDAHTLLVAARKAGIADAVEERFYHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFRATV 168
Cdd:pfam01323  73 IPLRFPANFLGNSTRANRLALAAGAEGLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 495777649  169 SDDEAHAQSIGLSGVPVFVMNEKyAISGAQGADNFLNALR 208
Cdd:pfam01323 153 RENTAAAISLGVFGVPTFVVGGK-MVFGADRLDTLADALA 191
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 110-210 1.27e-11

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 60.40  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649 110 AARkAGIADAVEERF--YHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFRATVSDDEAHAQSIGLSGVPVFV 187
Cdd:COG1651   51 AAR-AALCAADQGKFwaFHDALFANQPALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFV 129

                         90       100
                 ....*....|....*....|...
gi 495777649 188 MNEKYaISGAQGADNFLNALRQV 210
Cdd:COG1651  130 VNGKL-VSGAVPYEELEAALDAA 151
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 10-64 6.00e-07

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: 46.24  E-value: 6.00e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495777649  10 IDIWSDLVCPWCWIAKKRFEQGLnrFEFRDQVVIRHHSYRLAGGTPAMPFKDAIV 64
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLL--YADDGGVRVVYRPFPLLGGMPPNSLAAARA 53
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 110-207 8.60e-07

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: 47.67  E-value: 8.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649 110 AARKAGIADAVEERFYHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFRATVSDDEAHAQSIGLSGVPVFVMN 189
Cdd:cd03019   71 AAEALGLEDKLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVN 150

                         90       100
                 ....*....|....*....|..
gi 495777649 190 EKYAIS----GAQGADNFLNAL 207
Cdd:cd03019  151 GKYVVNpsaiGGDDTLQVLDEL 172
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 99-206 1.39e-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: 43.74  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  99 GDTEDAHTLLVAARKAGiADAVEErfYHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFRATVSDDEAHAQSI 178
Cdd:cd03023   49 ESSVLAARVALAVWKNG-PGKYLE--FHNALMATRGRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARAL 125

                         90       100
                 ....*....|....*....|....*...
gi 495777649 179 GLSGVPVFVMNEKyAISGAQGADNFLNA 206
Cdd:cd03023  126 GITGTPAFIIGDT-VIPGAVPADTLKEA 152
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 10-190 9.23e-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: 41.84  E-value: 9.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  10 IDIWSDLVCPWCWIAKKRFEQGLNRFEFRdqvvIRHHSYRL------AGGTPamPFKDAIVK----KLGSQHSAELMmnq 79
Cdd:cd03022    1 IDFYFDFSSPYSYLAHERLPALAARHGAT----VRYRPILLggvfkaTGNVP--PANRPPAKgryrLRDLERWARRY--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  80 vgtagkseGLIYNFDGMMFGDTEDAHTLLVAARKAG-----IADAVeerfYHGSITEGRSLFDRQQLVAMAVEAGMEKAD 154
Cdd:cd03022   72 --------GIPLRFPPRFPPNTLRAMRAALAAQAEGdaaeaFARAV----FRALWGEGLDIADPAVLAAVAAAAGLDADE 139

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495777649 155 AEAALENDDFRATVSDDEAHAQSIGLSGVPVFVMNE 190
Cdd:cd03022  140 LLAAADDPAVKAALRANTEEAIARGVFGVPTFVVDG 175
Thioredoxin_4 pfam13462
Thioredoxin;
135-207 3.36e-04

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 40.02  E-value: 3.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495777649  135 LFDRQQLVA----MAVEAGMEKADAEAALENDDFRATVSDDEAHAQSIGLSGVPVFVMNEKyAISGAQGADNFLNAL 207
Cdd:pfam13462  87 LYSQQEEWAqdleLAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGK-KVDGPLTYEELKKLI 162
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
 18-188 5.59e-04

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: 39.61  E-value: 5.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  18 CPWCWIAK---KRFEQglnrfEFRDQVVIRHHsyrlAGGTPAMPFKDAIVKKLGSQHSAELMMNQvgTAGKSEGLiYNFD 94
Cdd:cd03025   11 CGWCYGFEpllEKLKE-----EYGGGIEVELH----LGGLLPGNNARQITKQWRIYVHWHKARIA--LTGQPFGE-DYLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777649  95 GMMFG-DTEDAHTLLVAARKAGIADAVE--ERFYHGSITEGRSLFDRQQLVAMAVEAGMEKADAEAALENDDFRATVSDD 171
Cdd:cd03025   79 LLLFDlDSAPASRAIKAARLQGPERLLEmlKAIQRAHYVEGRDLADTEVLRELAIELGLDVEEFLEDFQSDEAKQAIQED 158

                        170
                 ....*....|....*..
gi 495777649 172 EAHAQSIGLSGVPVFVM 188
Cdd:cd03025  159 QKLARELGINGFPTLVL 175
 
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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