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Conserved domains on  [gi|672750161|gb|AIJ82053|]
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DSBA-like thioredoxin domain protein [Brucella canis]

Protein Classification

DsbA family protein( domain architecture ID 16062126)

DsbA family protein such as Proteus mirabilis suppressor of copper sensitivity protein C ScaC (PmScsC), a homotrimeric disulfide isomerase that plays a role in copper tolerance

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  9099998|10049365|15558583|12524212|12074972|30367780
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 104-257 1.41e-73

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: 221.31  E-value: 1.41e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 104 GNPNGDVTVYEFFDYNCGYCKRALPDMEAILKKDPNVRYVLKEFPILGPDSMRAHVVSQAFKALMPEKYPEFHEMLLGGH 183
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGESSVLAARVALAVWKNGPGKYLEFHNALMATR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672750161 184 GRATEESAIADAVKLGADEAKLREKMKDPAITGAFQRTYQLAQQLNITGTPSYVIGDELVPGAIGIDGLRQRIA 257
Cdd:cd03023   81 GRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPGAVPADTLKEAID 154
ScsC_N pfam18312
Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in ...
 47-78 2.37e-06

Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in Copper resistance protein ScsS present in Proteus mirabilis. ScsC is a powerful disulfide isomerase that is able to refold and reactivate the scrambled disulfide form of the model substrate RNase A. The protein has a thioredoxin 4 domain (pfam13462) but, unlike other characterized proteins in this family, it is trimeric. The N-terminal domain is responsible for trimerization of ScsC which is needed for isomerase activity.


:

Pssm-ID: 465704  Cd Length: 34  Bit Score: 43.15  E-value: 2.37e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 672750161   47 KAVENIVRNYLLQNPELMLEVQTALETKQAHA 78
Cdd:pfam18312   3 AAIEAIVRDYLLENPEILVEALTALQKRQAAA 34
 
Name Accession Description Interval E-value
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 104-257 1.41e-73

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: 221.31  E-value: 1.41e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 104 GNPNGDVTVYEFFDYNCGYCKRALPDMEAILKKDPNVRYVLKEFPILGPDSMRAHVVSQAFKALMPEKYPEFHEMLLGGH 183
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGESSVLAARVALAVWKNGPGKYLEFHNALMATR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672750161 184 GRATEESAIADAVKLGADEAKLREKMKDPAITGAFQRTYQLAQQLNITGTPSYVIGDELVPGAIGIDGLRQRIA 257
Cdd:cd03023   81 GRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPGAVPADTLKEAID 154
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 109-260 1.44e-47

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 155.16  E-value: 1.44e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 109 DVTVYEFFDYNCGYCKRALPDMEAILKK--DPNVRYVLKEFPILGPDSMRAHVVSQAfkALMPEKYPEFHEMLLGGHGRA 186
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKyvDGKVRVVYRPFPLLHPDSLRAARAALC--AADQGKFWAFHDALFANQPAL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672750161 187 TEESAIADAVKLGADEAKLREKMKDPAITGAFQRTYQLAQQLNITGTPSYVIGDELVPGAIGIDGLRQRIAAAR 260
Cdd:COG1651   79 TDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 111-257 2.38e-29

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: 109.44  E-value: 2.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161  111 TVYEFFDYNCGYCKRALPDMEAILKKDPNVRYVLKEFPILGP-------------------------------------- 152
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVKVVYRPFPLAGAkkignvgpsnlpvklkymmadlerwaalygiplrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161  153 ---DSMRAHVVSQAFKA--LMPEKYPEFHEMLLGGHGRATEESAIAD-AVKLGADEAKLREKMKDPAITGAFQRTYQLAQ 226
Cdd:pfam01323  81 flgNSTRANRLALAAGAegLAEKVVRELFNALWGEGAAITDDSVLREvAEKAGLDAEEFDEFLDSPAVKEAVRENTAAAI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 672750161  227 QLNITGTPSYVIGDELVPGAIGIDGLRQRIA 257
Cdd:pfam01323 161 SLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
ScsC_N pfam18312
Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in ...
 47-78 2.37e-06

Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in Copper resistance protein ScsS present in Proteus mirabilis. ScsC is a powerful disulfide isomerase that is able to refold and reactivate the scrambled disulfide form of the model substrate RNase A. The protein has a thioredoxin 4 domain (pfam13462) but, unlike other characterized proteins in this family, it is trimeric. The N-terminal domain is responsible for trimerization of ScsC which is needed for isomerase activity.


Pssm-ID: 465704  Cd Length: 34  Bit Score: 43.15  E-value: 2.37e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 672750161   47 KAVENIVRNYLLQNPELMLEVQTALETKQAHA 78
Cdd:pfam18312   3 AAIEAIVRDYLLENPEILVEALTALQKRQAAA 34
 
Name Accession Description Interval E-value
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 104-257 1.41e-73

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: 221.31  E-value: 1.41e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 104 GNPNGDVTVYEFFDYNCGYCKRALPDMEAILKKDPNVRYVLKEFPILGPDSMRAHVVSQAFKALMPEKYPEFHEMLLGGH 183
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILGESSVLAARVALAVWKNGPGKYLEFHNALMATR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672750161 184 GRATEESAIADAVKLGADEAKLREKMKDPAITGAFQRTYQLAQQLNITGTPSYVIGDELVPGAIGIDGLRQRIA 257
Cdd:cd03023   81 GRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPGAVPADTLKEAID 154
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 109-260 1.44e-47

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 155.16  E-value: 1.44e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 109 DVTVYEFFDYNCGYCKRALPDMEAILKK--DPNVRYVLKEFPILGPDSMRAHVVSQAfkALMPEKYPEFHEMLLGGHGRA 186
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKyvDGKVRVVYRPFPLLHPDSLRAARAALC--AADQGKFWAFHDALFANQPAL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672750161 187 TEESAIADAVKLGADEAKLREKMKDPAITGAFQRTYQLAQQLNITGTPSYVIGDELVPGAIGIDGLRQRIAAAR 260
Cdd:COG1651   79 TDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 111-257 2.38e-29

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: 109.44  E-value: 2.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161  111 TVYEFFDYNCGYCKRALPDMEAILKKDPNVRYVLKEFPILGP-------------------------------------- 152
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVKVVYRPFPLAGAkkignvgpsnlpvklkymmadlerwaalygiplrfpan 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161  153 ---DSMRAHVVSQAFKA--LMPEKYPEFHEMLLGGHGRATEESAIAD-AVKLGADEAKLREKMKDPAITGAFQRTYQLAQ 226
Cdd:pfam01323  81 flgNSTRANRLALAAGAegLAEKVVRELFNALWGEGAAITDDSVLREvAEKAGLDAEEFDEFLDSPAVKEAVRENTAAAI 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 672750161  227 QLNITGTPSYVIGDELVPGAIGIDGLRQRIA 257
Cdd:pfam01323 161 SLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
Thioredoxin_4 pfam13462
Thioredoxin;
102-256 7.98e-19

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 80.85  E-value: 7.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161  102 VFGNPNGDVTVYEFFDYNCGYCKRALPDMEAILKK---DPNVRYVLKEFPILGP-DSMRAHVVSQAFKALMPEKYPEFHE 177
Cdd:pfam13462   6 VIGNPDAPVTVVEYADLRCPHCAKFHEEVLKLLEEyidTGKVRFIIRDFPLDGEgESLLAAMAARCAGDQSPEYFLVIDK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161  178 ML--LGGHGRATEESAIADAVKLGADEAKLREKMKDPAITGAFQRtyqlAQQLNITGTPSYVIGDELVPGAIGIDGLRQR 255
Cdd:pfam13462  86 LLysQQEEWAQDLELAALAGLKDEEFEACLEEEDFLALVMADVKE----ARAAGINFTPTFIINGKKVDGPLTYEELKKL 161


                  .
gi 672750161  256 I 256
Cdd:pfam13462 162 I 162
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 112-246 1.61e-17

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: 75.52  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 112 VYEFFDYNCGYCKRALPDMEAILKKDP-NVRYVLKEFPILG---PDSMRAHVVSQAfkALMPEKYPEFHEmllgghgrat 187
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDgGVRVVYRPFPLLGgmpPNSLAAARAALA--AAAQGKFEALHE---------- 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672750161 188 eesAIADavklgadeaklrekmkdpaitgafqrtYQLAQQLNITGTPSYVIGDELVPGA 246
Cdd:cd02972   69 ---ALAD---------------------------TALARALGVTGTPTFVVNGEKYSGA 97
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 70-256 1.56e-16

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: 75.43  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161  70 ALETKQAHAAQEQVKQVLAANQSVLfDPKHDAVFGNPNGDVTVYEFFDYNCGYCKRALPDMEAiLKKDPNVRYVLkeFPI 149
Cdd:cd03020   40 DAKGRKDDLTEARLAQLNAIDLSAL-PLDDAIVYGKGNGKRVVYVFTDPDCPYCRKLEKELKP-NADGVTVRIFP--VPI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 150 LG-PDSMRAhvVSQAFKAlmPEKYPEFHEMLLGGHGRATEESAIADAvklgadeaklrekmkdpaitgafQRTYQLAQQL 228
Cdd:cd03020  116 LGlPDSTAK--AAAIWCA--KDRAKAWTDAMSGGKVPPPAASCDNPV-----------------------AANLALGRQL 168

                        170       180
                 ....*....|....*....|....*....
gi 672750161 229 NITGTPSYVIGD-ELVPGAIGIDGLRQRI 256
Cdd:cd03020  169 GVNGTPTIVLADgRVVPGAPPAAQLEALL 197
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 106-239 1.63e-12

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: 64.23  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 106 PNGDVTVYEFFDYNCGYCKRALPDMEAILKKDP-NVRYvlKEFPI-----LGPDSMRAHVVSQAF---KALMPEKYPEFH 176
Cdd:cd03019   13 PSGKPEVIEFFSYGCPHCYNFEPILEAWVKKLPkDVKF--EKVPVvfgggEGEPLARAFYAAEALgleDKLHAALFEAIH 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672750161 177 EmllgGHGRATEESAIAD-AVKLGADEAKLREKMKDPAITGAFQRTYQLAQQLNITGTPSYVIG 239
Cdd:cd03019   91 E----KRKRLLDPDDIRKiFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVN 150
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 148-259 1.23e-07

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: 50.65  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 148 PILGPDSMRAHVVSQAfkALMPEKYPEFHEMLLgghgRA--TEESAIAD-------AVKLGADEAKLREKMKDPAITGAF 218
Cdd:COG2761   88 RIKPPNTFDAHRLLKA--AELQGKQDALLEALF----EAyfTEGRDIGDrevlldlAAEVGLDAEEFRADLESDEAAAAV 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 672750161 219 QRTYQLAQQLNITGTPSYVIGDE-LVPGAIGIDGLRQRIAAA 259
Cdd:COG2761  162 RADEAEARELGVTGVPTFVFDGKyAVSGAQPYEVFEQALRQA 203
ScsC_N pfam18312
Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in ...
 47-78 2.37e-06

Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in Copper resistance protein ScsS present in Proteus mirabilis. ScsC is a powerful disulfide isomerase that is able to refold and reactivate the scrambled disulfide form of the model substrate RNase A. The protein has a thioredoxin 4 domain (pfam13462) but, unlike other characterized proteins in this family, it is trimeric. The N-terminal domain is responsible for trimerization of ScsC which is needed for isomerase activity.


Pssm-ID: 465704  Cd Length: 34  Bit Score: 43.15  E-value: 2.37e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 672750161   47 KAVENIVRNYLLQNPELMLEVQTALETKQAHA 78
Cdd:pfam18312   3 AAIEAIVRDYLLENPEILVEALTALQKRQAAA 34
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
 152-251 3.03e-05

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: 43.85  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 152 PDSMRAHVVSQAFKA---LMPEKYPEFHEMLLGGH---GR--ATEESAIADAVKLGADEAKLREKMKDPAITGAFQRTYQ 223
Cdd:cd03025   81 LFDLDSAPASRAIKAarlQGPERLLEMLKAIQRAHyveGRdlADTEVLRELAIELGLDVEEFLEDFQSDEAKQAIQEDQK 160

                         90       100
                 ....*....|....*....|....*...
gi 672750161 224 LAQQLNITGTPSYVIGDELVPGAIGIDG 251
Cdd:cd03025  161 LARELGINGFPTLVLEDDNGEGILLTGY 188
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
 163-259 2.63e-04

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


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 41.00  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 163 AFKALMPEKYPEFHEMLLGGH---GR-ATEESAIAD-AVKLGADEAKLREKMKDPAITGAFQRTYQLAQQLNITGTPSYV 237
Cdd:COG3531  100 AARELAPERELAMLHAIQRAFyveGRdISDPEVLAElAAELGLDAEAFAAALASEETRQHIQQEFALARQLGVQGFPTLV 179

                         90       100
                 ....*....|....*....|....*..
gi 672750161 238 I--GDELVPGAIG---IDGLRQRIAAA 259
Cdd:COG3531  180 LeqGGQLYLLPRGygdPEALLAALEQL 206
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 149-246 3.90e-03

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: 37.56  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672750161 149 ILGPDSMRAHVVSQAfkALMPEKYPEFHEMLLgghgRA--TEESAIAD-------AVKLGADEAKLREKMKDPAITGAFQ 219
Cdd:cd03024   89 VRPPNTFDAHRLIHL--AKEQGKQDALVEALF----RAyfTEGKDIGDrdvlvdlAEEAGLDAAEARAVLASDEYADEVR 162

                         90       100
                 ....*....|....*....|....*...
gi 672750161 220 RTYQLAQQLNITGTPSYVI-GDELVPGA 246
Cdd:cd03024  163 ADEARARQLGISGVPFFVFnGKYAVSGA 190
 
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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