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Conserved domains on  [gi|2714218129|ref|WP_340903477|]
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MULTISPECIES: DsbA family oxidoreductase [unclassified Paenibacillus]

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

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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 ...
3-205 6.15e-95

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: 276.38  E-value: 6.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   3 IEIWSDFLCPFCYIGKRRLENVLEQFPHRDEVKLQFKSFELDPNAAlNPGKTNSEYLAAKYNMSAEQAKGMnAQMNANAR 82
Cdd:cd03024     1 IDIWSDVVCPWCYIGKRRLEKALAELGDEVDVEIEWRPFELNPDMP-PEGEDRREYLARKYGSTAEQAAAM-RRVEAAAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  83 TAGLEYNIDAMIPTNSFSAHRLTHWADTQGKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQFT 162
Cdd:cd03024    79 AEGLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYA 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2714218129 163 DNVRADQAEGEQLGIRGVPFFVFDRKFAVSGAQPDEVFLDAIQ 205
Cdd:cd03024   159 DEVRADEARARQLGISGVPFFVFNGKYAVSGAQPPEVFLQALR 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 ...
3-205 6.15e-95

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: 276.38  E-value: 6.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   3 IEIWSDFLCPFCYIGKRRLENVLEQFPHRDEVKLQFKSFELDPNAAlNPGKTNSEYLAAKYNMSAEQAKGMnAQMNANAR 82
Cdd:cd03024     1 IDIWSDVVCPWCYIGKRRLEKALAELGDEVDVEIEWRPFELNPDMP-PEGEDRREYLARKYGSTAEQAAAM-RRVEAAAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  83 TAGLEYNIDAMIPTNSFSAHRLTHWADTQGKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQFT 162
Cdd:cd03024    79 AEGLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYA 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2714218129 163 DNVRADQAEGEQLGIRGVPFFVFDRKFAVSGAQPDEVFLDAIQ 205
Cdd:cd03024   159 DEVRADEARARQLGISGVPFFVFNGKYAVSGAQPPEVFLQALR 201
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
1-209 7.66e-94

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: 273.68  E-value: 7.66e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   1 MNIEIWSDFLCPFCYIGKRRLENVLEQFPhrDEVKLQFKSFELDPNAALNPGKTNsEYLAAKynMSAEQAKGMNAQMNAN 80
Cdd:COG2761     2 LKIDIFSDVVCPWCYIGKRRLEKALAEFG--DDVEIRWRPFELNPDMPPEGEDRR-EYLLAK--GSPEQAEQMRAHVEEA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  81 ARTAGLEYNIDAMIPTNSFSAHRLTHWADTQGKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQ 160
Cdd:COG2761    77 AAEEGLPFDFDRIKPPNTFDAHRLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2714218129 161 FTDNVRADQAEGEQLGIRGVPFFVFDRKFAVSGAQPDEVFLDAIQKAWD 209
Cdd:COG2761   157 AAAAVRADEAEARELGVTGVPTFVFDGKYAVSGAQPYEVFEQALRQALA 205
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
3-205 1.32e-48

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: 158.36  E-value: 1.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   3 IEIWSDFLCPFCYIGKRRLENVLEQFPHrdeVKLQFKSFELDPNAALNPGKTNseylaakynMSAEQAKGMNAQMNANAR 82
Cdd:pfam01323   2 VDEFFDFLCPFCYLAKERLEKLAARYGD---VKVVYRPFPLAGAKKIGNVGPS---------NLPVKLKYMMADLERWAA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  83 TAGLEYNIDAMIPTNSFSAHRLTHWADTQGKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQFT 162
Cdd:pfam01323  70 LYGIPLRFPANFLGNSTRANRLALAAGAEGLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVK 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2714218129 163 DNVRADQAEGEQLGIRGVPFFVFDRKfAVSGAQPDEVFLDAIQ 205
Cdd:pfam01323 150 EAVRENTAAAISLGVFGVPTFVVGGK-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 ...
3-205 6.15e-95

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: 276.38  E-value: 6.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   3 IEIWSDFLCPFCYIGKRRLENVLEQFPHRDEVKLQFKSFELDPNAAlNPGKTNSEYLAAKYNMSAEQAKGMnAQMNANAR 82
Cdd:cd03024     1 IDIWSDVVCPWCYIGKRRLEKALAELGDEVDVEIEWRPFELNPDMP-PEGEDRREYLARKYGSTAEQAAAM-RRVEAAAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  83 TAGLEYNIDAMIPTNSFSAHRLTHWADTQGKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQFT 162
Cdd:cd03024    79 AEGLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYA 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2714218129 163 DNVRADQAEGEQLGIRGVPFFVFDRKFAVSGAQPDEVFLDAIQ 205
Cdd:cd03024   159 DEVRADEARARQLGISGVPFFVFNGKYAVSGAQPPEVFLQALR 201
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
1-209 7.66e-94

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: 273.68  E-value: 7.66e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   1 MNIEIWSDFLCPFCYIGKRRLENVLEQFPhrDEVKLQFKSFELDPNAALNPGKTNsEYLAAKynMSAEQAKGMNAQMNAN 80
Cdd:COG2761     2 LKIDIFSDVVCPWCYIGKRRLEKALAEFG--DDVEIRWRPFELNPDMPPEGEDRR-EYLLAK--GSPEQAEQMRAHVEEA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  81 ARTAGLEYNIDAMIPTNSFSAHRLTHWADTQGKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQ 160
Cdd:COG2761    77 AAEEGLPFDFDRIKPPNTFDAHRLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2714218129 161 FTDNVRADQAEGEQLGIRGVPFFVFDRKFAVSGAQPDEVFLDAIQKAWD 209
Cdd:COG2761   157 AAAAVRADEAEARELGVTGVPTFVFDGKYAVSGAQPYEVFEQALRQALA 205
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
3-205 1.32e-48

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: 158.36  E-value: 1.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   3 IEIWSDFLCPFCYIGKRRLENVLEQFPHrdeVKLQFKSFELDPNAALNPGKTNseylaakynMSAEQAKGMNAQMNANAR 82
Cdd:pfam01323   2 VDEFFDFLCPFCYLAKERLEKLAARYGD---VKVVYRPFPLAGAKKIGNVGPS---------NLPVKLKYMMADLERWAA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  83 TAGLEYNIDAMIPTNSFSAHRLTHWADTQGKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQFT 162
Cdd:pfam01323  70 LYGIPLRFPANFLGNSTRANRLALAAGAEGLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVK 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2714218129 163 DNVRADQAEGEQLGIRGVPFFVFDRKfAVSGAQPDEVFLDAIQ 205
Cdd:pfam01323 150 EAVRENTAAAISLGVFGVPTFVVGGK-MVFGADRLDTLADALA 191
NahD COG3917
2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and ...
3-186 1.18e-22

2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443122 [Multi-domain]  Cd Length: 196  Bit Score: 91.39  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   3 IEIWSDFLCPFCYIGKRRLENVLEQFphrdEVKLQFKSFELDPNAALNPGKTNSEYLAAK--YnmsaeqakgMNAQMNAN 80
Cdd:COG3917     2 IDFYFDFSSPYAYLAATRLEALAARH----GAEVRWRPVLLGAVFKATGGTPPAERIPAKgrY---------RLRDLARW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  81 ARTAGLEYNIDAMIPTNSFSAHRLTHWADTQGKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQ 160
Cdd:COG3917    69 ARKLGLPFRFPPHFPVNPLLAARAALAAQDAGAAAAFVRAVFRAVWAEGRDIADPAVLAAIAAAAGLDAAALLAAAQSPA 148
                         170       180
                  ....*....|....*....|....*.
gi 2714218129 161 FTDNVRADQAEGEQLGIRGVPFFVFD 186
Cdd:COG3917   149 VKARLRANTEEAVARGVFGAPTFVVD 174
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
3-186 2.92e-21

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: 87.68  E-value: 2.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   3 IEIWSDFLCPFCYIGKRRLENVLEQFPhrdeVKLQFKSFELDP--NAALNPGktnseylaakyNMSAEQAKG--MNAQMN 78
Cdd:cd03022     1 IDFYFDFSSPYSYLAHERLPALAARHG----ATVRYRPILLGGvfKATGNVP-----------PANRPPAKGryRLRDLE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  79 ANARTAGLEYNIDAMIPTNSFSAHRLTHWADTQG-KALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLS 157
Cdd:cd03022    66 RWARRYGIPLRFPPRFPPNTLRAMRAALAAQAEGdAAEAFARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAAD 145
                         170       180
                  ....*....|....*....|....*....
gi 2714218129 158 SDQFTDNVRADQAEGEQLGIRGVPFFVFD 186
Cdd:cd03022   146 DPAVKAALRANTEEAIARGVFGVPTFVVD 174
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
3-207 2.01e-19

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 81.58  E-value: 2.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   3 IEIWSDFLCPFCYIGKRRLENVLEQFPhRDEVKLQFKSFeldpnaalnpgktnseylaakynmsaeqakgmnaqmnanar 82
Cdd:COG1651     4 VVEFFDYQCPYCARFHPELPELLKKYV-DGKVRVVYRPF----------------------------------------- 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  83 tagleynidAMIPTNSFSAHRLTHWADTQGKALELSERIFqavfiEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQFT 162
Cdd:COG1651    42 ---------PLLHPDSLRAARAALCAADQGKFWAFHDALF-----ANQPALTDDDLREIAKEAGLDAAKFDACLNSGAVA 107
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2714218129 163 DNVRADQAEGEQLGIRGVPFFVFDRKFaVSGAQPDEVFLDAIQKA 207
Cdd:COG1651   108 AKVEADTALAQALGVTGTPTFVVNGKL-VSGAVPYEELEAALDAA 151
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
112-207 8.64e-14

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


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 67.96  E-value: 8.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129 112 GKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQFTDNVRADQAEGEQLGIRGVPFFVF--DRKF 189
Cdd:COG3531   107 ERELAMLHAIQRAFYVEGRDISDPEVLAELAAELGLDAEAFAAALASEETRQHIQQEFALARQLGVQGFPTLVLeqGGQL 186
                          90       100
                  ....*....|....*....|
gi 2714218129 190 AV--SGAQPDEVFLDAIQKA 207
Cdd:COG3531   187 YLlpRGYGDPEALLAALEQL 206
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
3-195 1.43e-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: 62.04  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   3 IEIWSDFLCPFCYIGKRRLENVLEQfpHRDEVKLQFKSFELDPNAalnpgktnseylaakynmsaeqakgmnaqmnanar 82
Cdd:cd02972     1 IVEFFDPLCPYCYLFEPELEKLLYA--DDGGVRVVYRPFPLLGGM----------------------------------- 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  83 tagleynidamiPTNSFSAHRLTHWADTQGKALELSERIfqavfiegkhsgdtevlaqlaeevgldrdaatavlssdqft 162
Cdd:cd02972    44 ------------PPNSLAAARAALAAAAQGKFEALHEAL----------------------------------------- 70
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2714218129 163 dnvrADQAEGEQLGIRGVPFFVFDRKfAVSGAQ 195
Cdd:cd02972    71 ----ADTALARALGVTGTPTFVVNGE-KYSGAG 98
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
3-187 1.75e-12

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: 63.88  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   3 IEIWS--DFLCPFCYigkrRLENVLEQFphRDEVKLQFKsFELDPNA-ALNPGKTNSEYLAAKYNMSAEQAKGMNAQMNA 79
Cdd:cd03025     1 LELYYfiDPLCGWCY----GFEPLLEKL--KEEYGGGIE-VELHLGGlLPGNNARQITKQWRIYVHWHKARIALTGQPFG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  80 NARTAGLEYNIDAMIPTNSFSAHRLThwadTQGKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSD 159
Cdd:cd03025    74 EDYLELLLFDLDSAPASRAIKAARLQ----GPERLLEMLKAIQRAHYVEGRDLADTEVLRELAIELGLDVEEFLEDFQSD 149
                         170       180
                  ....*....|....*....|....*...
gi 2714218129 160 QFTDNVRADQAEGEQLGIRGVPFFVFDR 187
Cdd:cd03025   150 EAKQAIQEDQKLARELGINGFPTLVLED 177
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
6-205 7.90e-12

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: 61.46  E-value: 7.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129   6 WSDFLCPFCyigkRRLENVLEQFPHRD-EVKLQFKSFeldpnaalnPGKTNSEYLAAKYNMSAeqakgmnaqmnanarta 84
Cdd:cd03023    12 FFDYNCGYC----KKLAPELEKLLKEDpDVRVVFKEF---------PILGESSVLAARVALAV----------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129  85 gleynidamiptnsfsahrlthWADTQGKALELSERIFQavfIEGKHsgDTEVLAQLAEEVGLDRDAATAVLSSDQFTDN 164
Cdd:cd03023    62 ----------------------WKNGPGKYLEFHNALMA---TRGRL--NEESLLRIAKKAGLDEAKLKKDMDDPEIEAT 114
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2714218129 165 VRADQAEGEQLGIRGVPFFVFDRKFaVSGAQPDEVFLDAIQ 205
Cdd:cd03023   115 IDKNRQLARALGITGTPAFIIGDTV-IPGAVPADTLKEAID 154
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
108-193 1.49e-06

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: 46.90  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129 108 ADTQGKALELSERIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQFTDNVRADQAEGEQLGIRGVPFFVFDR 187
Cdd:cd03019    72 AEALGLEDKLHAALFEAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNG 151

                  ....*.
gi 2714218129 188 KFAVSG 193
Cdd:cd03019   152 KYVVNP 157
Thioredoxin_5 pfam13743
Thioredoxin;
120-200 1.89e-06

Thioredoxin;


Pssm-ID: 404608 [Multi-domain]  Cd Length: 176  Bit Score: 46.84  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714218129 120 RIFQAVFIEGKHSGDTEVLAQLAEEVGLDRDAATAVLSSDQFTDNVRADQAEGEQLGIRGVPFFVF------DRKFAVSG 193
Cdd:pfam13743  88 KLQEAVFLEKQNISDEELLLECAEKAGLDVEEFKEDLHSDLAKKAFQCDQKLAAEMGVTEHPTLVFfnsnveEEGLKVEG 167

                  ....*..
gi 2714218129 194 AQPDEVF 200
Cdd:pfam13743 168 CYPYDVY 174
Thioredoxin_4 pfam13462
Thioredoxin;
139-206 1.93e-04

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 40.79  E-value: 1.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2714218129 139 AQLAEEVGLDRDAATAVLSSDQFTDNVRADQAEGEQLGIRGVP-FFVFDRKFAvsGAQPDEVFLDAIQK 206
Cdd:pfam13462  98 LELAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPtFIINGKKVD--GPLTYEELKKLIDD 164
 
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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