NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|763409439|ref|WP_044265959|]
View 

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
SCOP:  3000031

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
10-207 1.61e-75

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: 226.69  E-value: 1.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  10 IDIWSDLVCPWCWIAKKRFEQGLAAFEHKEQVVVRHHSFRISGDRPA--VPFRKALYKKFGGEHGAELMMNQVGTAGKAE 87
Cdd:cd03024    1 IDIWSDVVCPWCYIGKRRLEKALAELGDEVDVEIEWRPFELNPDMPPegEDRREYLARKYGSTAEQAAAMRRVEAAAAAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  88 GLQYNFDTMLFGDTEDAHTLLAAARHANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALANEAFRAS 167
Cdd:cd03024   81 GLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 763409439 168 VAEDEAHARSIGVSGVPLFLLNEKYAISGAQSADNFLNAL 207
Cdd:cd03024  161 VRADEARARQLGISGVPFFVFNGKYAVSGAQPPEVFLQAL 200
 
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 ...
10-207 1.61e-75

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: 226.69  E-value: 1.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  10 IDIWSDLVCPWCWIAKKRFEQGLAAFEHKEQVVVRHHSFRISGDRPA--VPFRKALYKKFGGEHGAELMMNQVGTAGKAE 87
Cdd:cd03024    1 IDIWSDVVCPWCYIGKRRLEKALAELGDEVDVEIEWRPFELNPDMPPegEDRREYLARKYGSTAEQAAAMRRVEAAAAAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  88 GLQYNFDTMLFGDTEDAHTLLAAARHANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALANEAFRAS 167
Cdd:cd03024   81 GLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 763409439 168 VAEDEAHARSIGVSGVPLFLLNEKYAISGAQSADNFLNAL 207
Cdd:cd03024  161 VRADEARARQLGISGVPFFVFNGKYAVSGAQPPEVFLQAL 200
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
8-212 1.95e-73

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: 221.68  E-value: 1.95e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439   8 ITIDIWSDLVCPWCWIAKKRFEQGLAAFEHkeQVVVRHHSFRISGDRPAVPF-RKALYKKFGGEHGAELMMNQVGTAGKA 86
Cdd:COG2761    2 LKIDIFSDVVCPWCYIGKRRLEKALAEFGD--DVEIRWRPFELNPDMPPEGEdRREYLLAKGSPEQAEQMRAHVEEAAAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  87 EGLQYNFDTMLFGDTEDAHTLLAAARHANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALANEAFRA 166
Cdd:COG2761   80 EGLPFDFDRIKPPNTFDAHRLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDEAAA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 763409439 167 SVAEDEAHARSIGVSGVPLFLLNEKYAISGAQSADNFLNALKQVWE 212
Cdd:COG2761  160 AVRADEAEARELGVTGVPTFVFDGKYAVSGAQPYEVFEQALRQALA 205
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
9-208 2.90e-37

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: 129.09  E-value: 2.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439    9 TIDIWSDLVCPWCWIAKKRFEQGLAAFEHkeqVVVRHHSFRISGDRPAVPFRKALYKKFGGEhgaelMMNQVGTAGKAEG 88
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGD---VKVVYRPFPLAGAKKIGNVGPSNLPVKLKY-----MMADLERWAALYG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439   89 LQYNFDTMLFGDTEDAHTLLAAARHANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALANEAFRASV 168
Cdd:pfam01323  73 IPLRFPANFLGNSTRANRLALAAGAEGLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAV 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 763409439  169 AEDEAHARSIGVSGVPLFLLNEKyAISGAQSADNFLNALK 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 ...
10-207 1.61e-75

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: 226.69  E-value: 1.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  10 IDIWSDLVCPWCWIAKKRFEQGLAAFEHKEQVVVRHHSFRISGDRPA--VPFRKALYKKFGGEHGAELMMNQVGTAGKAE 87
Cdd:cd03024    1 IDIWSDVVCPWCYIGKRRLEKALAELGDEVDVEIEWRPFELNPDMPPegEDRREYLARKYGSTAEQAAAMRRVEAAAAAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  88 GLQYNFDTMLFGDTEDAHTLLAAARHANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALANEAFRAS 167
Cdd:cd03024   81 GLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYADE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 763409439 168 VAEDEAHARSIGVSGVPLFLLNEKYAISGAQSADNFLNAL 207
Cdd:cd03024  161 VRADEARARQLGISGVPFFVFNGKYAVSGAQPPEVFLQAL 200
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
8-212 1.95e-73

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: 221.68  E-value: 1.95e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439   8 ITIDIWSDLVCPWCWIAKKRFEQGLAAFEHkeQVVVRHHSFRISGDRPAVPF-RKALYKKFGGEHGAELMMNQVGTAGKA 86
Cdd:COG2761    2 LKIDIFSDVVCPWCYIGKRRLEKALAEFGD--DVEIRWRPFELNPDMPPEGEdRREYLLAKGSPEQAEQMRAHVEEAAAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  87 EGLQYNFDTMLFGDTEDAHTLLAAARHANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALANEAFRA 166
Cdd:COG2761   80 EGLPFDFDRIKPPNTFDAHRLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDEAAA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 763409439 167 SVAEDEAHARSIGVSGVPLFLLNEKYAISGAQSADNFLNALKQVWE 212
Cdd:COG2761  160 AVRADEAEARELGVTGVPTFVFDGKYAVSGAQPYEVFEQALRQALA 205
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
9-208 2.90e-37

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: 129.09  E-value: 2.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439    9 TIDIWSDLVCPWCWIAKKRFEQGLAAFEHkeqVVVRHHSFRISGDRPAVPFRKALYKKFGGEhgaelMMNQVGTAGKAEG 88
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGD---VKVVYRPFPLAGAKKIGNVGPSNLPVKLKY-----MMADLERWAALYG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439   89 LQYNFDTMLFGDTEDAHTLLAAARHANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALANEAFRASV 168
Cdd:pfam01323  73 IPLRFPANFLGNSTRANRLALAAGAEGLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAV 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 763409439  169 AEDEAHARSIGVSGVPLFLLNEKyAISGAQSADNFLNALK 208
Cdd:pfam01323 153 RENTAAAISLGVFGVPTFVVGGK-MVFGADRLDTLADALA 191
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
8-210 4.51e-12

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 61.94  E-value: 4.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439   8 ITIDIWSDLVCPWCwiakKRFEQGLAAFEHK---EQVVVRHHsfrisgdrpAVPFrkalykkfggehgaelmmnqvgtag 84
Cdd:COG1651    2 VTVVEFFDYQCPYC----ARFHPELPELLKKyvdGKVRVVYR---------PFPL------------------------- 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  85 kaeglqynfdtmLFGDTEDAHTLLAAARHANIGDAMAERFYrasvtEGRSIFDPQELIALAAEVGMSRDDAESALANEAF 164
Cdd:COG1651   44 ------------LHPDSLRAARAALCAADQGKFWAFHDALF-----ANQPALTDDDLREIAKEAGLDAAKFDACLNSGAV 106
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 763409439 165 RASVAEDEAHARSIGVSGVPLFLLNEKYaISGAQSADNFLNALKQV 210
Cdd:COG1651  107 AAKVEADTALAQALGVTGTPTFVVNGKL-VSGAVPYEELEAALDAA 151
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
18-210 9.18e-12

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


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 62.19  E-value: 9.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  18 CPWCWIAKKRFEQgLAAfEHKEQVVVRHHS---FRISGDRPaVPFRKALYKKfGGEHGAELMMNQVGTAGKAEGLQYNfd 94
Cdd:COG3531   12 CGWCYGFAPVIEA-LAE-ALGDRLDVELLSgglFPGSNRRP-MDPEMRAYIQ-PHWQRIAQLTGQPFGEAYNDLLRDG-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  95 TMLFgDTEDAHTLLAAARH--ANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALANEAFRASVAEDE 172
Cdd:COG3531   86 TFVL-DSEPACRAVLAARElaPERELAMLHAIQRAFYVEGRDISDPEVLAELAAELGLDAEAFAAALASEETRQHIQQEF 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 763409439 173 AHARSIGVSGVPLFLL---NEKYAI-SGAQSADNFLNALKQV 210
Cdd:COG3531  165 ALARQLGVQGFPTLVLeqgGQLYLLpRGYGDPEALLAALEQL 206
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
10-190 4.88e-10

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: 56.87  E-value: 4.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  10 IDIWSDLVCPWCWIAKKRFEQgLAAfEHKEQVVVRhhsfrisgdrpavPFRKALYKKFGGEHGAELMMNQVGTAGKAE-- 87
Cdd:cd03022    1 IDFYFDFSSPYSYLAHERLPA-LAA-RHGATVRYR-------------PILLGGVFKATGNVPPANRPPAKGRYRLRDle 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  88 ------GLQYNFDTMLFGDTEDAHTL-LAAARHANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALA 160
Cdd:cd03022   66 rwarryGIPLRFPPRFPPNTLRAMRAaLAAQAEGDAAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAAD 145
                        170       180       190
                 ....*....|....*....|....*....|..
gi 763409439 161 NEAFRASVAE--DEAHARsiGVSGVPLFLLNE 190
Cdd:cd03022  146 DPAVKAALRAntEEAIAR--GVFGVPTFVVDG 175
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
10-74 9.78e-08

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: 48.56  E-value: 9.78e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 763409439  10 IDIWSDLVCPWCWIAKKRFEQGLAAFEHKeqVVVRHHSFRISGDRPAVPFRKALYKKFGGEHGAE 74
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDGG--VRVVYRPFPLLGGMPPNSLAAARAALAAAAQGKF 63
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
99-207 1.94e-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: 49.59  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  99 GDTEDAHTLL-AAARHANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALANEAFRASVAEDEAHARS 177
Cdd:cd03019   59 GGEGEPLARAfYAAEALGLEDKLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKK 138
                         90       100       110
                 ....*....|....*....|....*....|....
gi 763409439 178 IGVSGVPLFLLNEKYAIS----GAQSADNFLNAL 207
Cdd:cd03019  139 YKITGVPAFVVNGKYVVNpsaiGGDDTLQVLDEL 172
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
18-188 2.92e-07

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: 49.24  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  18 CPWCWIAKKRFEQglAAFEHKEQVVVRHHSF---RISGDRPAVPfRKALYKkfgGEHG-AELMMNQVGTAGKAEGLQYNF 93
Cdd:cd03025   11 CGWCYGFEPLLEK--LKEEYGGGIEVELHLGgllPGNNARQITK-QWRIYV---HWHKaRIALTGQPFGEDYLELLLFDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763409439  94 DTmlfgdtEDAHTLLAAAR--HANIGDAMAERFYRASVTEGRSIFDPQELIALAAEVGMSRDDAESALANEAFRASVAED 171
Cdd:cd03025   85 DS------APASRAIKAARlqGPERLLEMLKAIQRAHYVEGRDLADTEVLRELAIELGLDVEEFLEDFQSDEAKQAIQED 158
                        170
                 ....*....|....*..
gi 763409439 172 EAHARSIGVSGVPLFLL 188
Cdd:cd03025  159 QKLARELGINGFPTLVL 175
Thioredoxin_4 pfam13462
Thioredoxin;
137-209 9.87e-05

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 41.56  E-value: 9.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 763409439  137 DPQELIALAAEVGMSRDDAESALANEAFRASVAEDEAHARSIGVSGVPLFLLNEKyAISGAQSADNFLNALKQ 209
Cdd:pfam13462  93 EWAQDLELAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGK-KVDGPLTYEELKKLIDD 164
RPP1 COG1603
RNase P/RNase MRP subunit p30 [Translation, ribosomal structure and biogenesis];
133-160 2.73e-03

RNase P/RNase MRP subunit p30 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441211 [Multi-domain]  Cd Length: 231  Bit Score: 37.95  E-value: 2.73e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 763409439 133 RSIFD---PQELIALAAEVGMSRDDAESALA 160
Cdd:COG1603  177 RSHLDlraPRELIALGELFGFEEEEAEEGLS 207
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH