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Conserved domains on  [gi|2639432218|ref|WP_322789972|]
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thioredoxin domain-containing protein [Pseudokineococcus marinus]

Protein Classification

DsbA family protein( domain architecture ID 11447254)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 36-191 1.40e-35

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


:

Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 122.03  E-value: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  36 PVLVEFLDFECEACAAAYPLVEQIREEY-DGRLSVVARYFPLPgHANAENAAVAVEAAAGQGAFEAMYQRMYATQAQWGE 114
Cdd:COG1651     2 VTVVEFFDYQCPYCARFHPELPELLKKYvDGKVRVVYRPFPLL-HPDSLRAARAALCAADQGKFWAFHDALFANQPALTD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2639432218 115 QQqsqadlFRTFAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFLDGQRIE-PTSIEDFRAQVDAAL 191
Cdd:COG1651    81 DD------LREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSgAVPYEELEAALDAAL 152
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 36-191 1.40e-35

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 122.03  E-value: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  36 PVLVEFLDFECEACAAAYPLVEQIREEY-DGRLSVVARYFPLPgHANAENAAVAVEAAAGQGAFEAMYQRMYATQAQWGE 114
Cdd:COG1651     2 VTVVEFFDYQCPYCARFHPELPELLKKYvDGKVRVVYRPFPLL-HPDSLRAARAALCAADQGKFWAFHDALFANQPALTD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2639432218 115 QQqsqadlFRTFAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFLDGQRIE-PTSIEDFRAQVDAAL 191
Cdd:COG1651    81 DD------LREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSgAVPYEELEAALDAAL 152
Thioredoxin_4 pfam13462
Thioredoxin;
33-189 3.42e-25

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 95.87  E-value: 3.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  33 PDAPV-LVEFLDFECEACAAAYPLVEQIREEY--DGRLSVVARYFPLPGHANAENAAVAVEAAAGQG-AFEAMYQRMYAT 108
Cdd:pfam13462  10 PDAPVtVVEYADLRCPHCAKFHEEVLKLLEEYidTGKVRFIIRDFPLDGEGESLLAAMAARCAGDQSpEYFLVIDKLLYS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218 109 QAQWGEQQQSqadlfrtFAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFLDGQRIE-PTSIEDFRAQV 187
Cdd:pfam13462  90 QQEEWAQDLE-------LAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGKKVDgPLTYEELKKLI 162


                  ..
gi 2639432218 188 DA 189
Cdd:pfam13462 163 DD 164
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 33-188 3.02e-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: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  33 PDAPV-LVEFLDFECEACAAAYPLVEQIREEyDGRLSVVARYFPLPGHANAENAAVA-VEAAAGQGAFEAMYQRMYATQA 110
Cdd:cd03023     3 PNGDVtIVEFFDYNCGYCKKLAPELEKLLKE-DPDVRVVFKEFPILGESSVLAARVAlAVWKNGPGKYLEFHNALMATRG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2639432218 111 QWGEQQQSQAdlfrtfAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFLDGQRIE-PTSIEDFRAQVD 188
Cdd:cd03023    82 RLNEESLLRI------AKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPgAVPADTLKEAID 154
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 36-191 1.40e-35

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 122.03  E-value: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  36 PVLVEFLDFECEACAAAYPLVEQIREEY-DGRLSVVARYFPLPgHANAENAAVAVEAAAGQGAFEAMYQRMYATQAQWGE 114
Cdd:COG1651     2 VTVVEFFDYQCPYCARFHPELPELLKKYvDGKVRVVYRPFPLL-HPDSLRAARAALCAADQGKFWAFHDALFANQPALTD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2639432218 115 QQqsqadlFRTFAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFLDGQRIE-PTSIEDFRAQVDAAL 191
Cdd:COG1651    81 DD------LREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSgAVPYEELEAALDAAL 152
Thioredoxin_4 pfam13462
Thioredoxin;
33-189 3.42e-25

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 95.87  E-value: 3.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  33 PDAPV-LVEFLDFECEACAAAYPLVEQIREEY--DGRLSVVARYFPLPGHANAENAAVAVEAAAGQG-AFEAMYQRMYAT 108
Cdd:pfam13462  10 PDAPVtVVEYADLRCPHCAKFHEEVLKLLEEYidTGKVRFIIRDFPLDGEGESLLAAMAARCAGDQSpEYFLVIDKLLYS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218 109 QAQWGEQQQSqadlfrtFAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFLDGQRIE-PTSIEDFRAQV 187
Cdd:pfam13462  90 QQEEWAQDLE-------LAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGKKVDgPLTYEELKKLI 162


                  ..
gi 2639432218 188 DA 189
Cdd:pfam13462 163 DD 164
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 33-188 3.02e-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: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  33 PDAPV-LVEFLDFECEACAAAYPLVEQIREEyDGRLSVVARYFPLPGHANAENAAVA-VEAAAGQGAFEAMYQRMYATQA 110
Cdd:cd03023     3 PNGDVtIVEFFDYNCGYCKKLAPELEKLLKE-DPDVRVVFKEFPILGESSVLAARVAlAVWKNGPGKYLEFHNALMATRG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2639432218 111 QWGEQQQSQAdlfrtfAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFLDGQRIE-PTSIEDFRAQVD 188
Cdd:cd03023    82 RLNEESLLRI------AKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPgAVPADTLKEAID 154
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 38-175 6.12e-09

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: 51.25  E-value: 6.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  38 LVEFLDFECEACAAAYPLVEQIREEYDGRLSVVARYFPLPGHANAEnaavaveaaagqgAFEAMyqRMYAtqaqwgeqqq 117
Cdd:cd02972     1 IVEFFDPLCPYCYLFEPELEKLLYADDGGVRVVYRPFPLLGGMPPN-------------SLAAA--RAAL---------- 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2639432218 118 sqadlfrtFAADLGLDLAAYDAAvadpgtlsrvgRDLTDGQALGVQSTPTFFLDGQRI 175
Cdd:cd02972    56 --------AAAAQGKFEALHEAL-----------ADTALARALGVTGTPTFVVNGEKY 94
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 41-173 8.65e-08

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: 50.27  E-value: 8.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  41 FLDFECEACAAAYPLVEQIREEYDGRLSVVARYFPLPGH--ANAENAAVAVEAAAGQGAFEAMYQRMYATQA-------- 110
Cdd:COG2761     7 FSDVVCPWCYIGKRRLEKALAEFGDDVEIRWRPFELNPDmpPEGEDRREYLLAKGSPEQAEQMRAHVEEAAAeeglpfdf 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218 111 ---------------QWGEQQQSQADLFRTF--------------------AADLGLDLAAYDAAVADPGTLSRVGRDLT 155
Cdd:COG2761    87 drikppntfdahrllKAAELQGKQDALLEALfeayftegrdigdrevlldlAAEVGLDAEEFRADLESDEAAAAVRADEA 166

                         170
                  ....*....|....*...
gi 2639432218 156 DGQALGVQSTPTFFLDGQ 173
Cdd:COG2761   167 EARELGVTGVPTFVFDGK 184
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 26-183 3.11e-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: 48.44  E-value: 3.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  26 HY--LSDAGPDA-PVLVEFLDFECEACAAAYPLVEQIREEYDGrlSVVARYFPLpghanaenaavaveaAAGQGAFEAMy 102
Cdd:cd03019     4 DYtvLSPPIPSGkPEVIEFFSYGCPHCYNFEPILEAWVKKLPK--DVKFEKVPV---------------VFGGGEGEPL- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218 103 QRMYAT----------------QAQWGEQQQSQADLFRTFAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTP 166
Cdd:cd03019    66 ARAFYAaealgledklhaalfeAIHEKRKRLLDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVP 145

                         170
                  ....*....|....*...
gi 2639432218 167 TFFLDGQ-RIEPTSIEDF 183
Cdd:cd03019   146 AFVVNGKyVVNPSAIGGD 163
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 37-175 4.88e-07

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: 47.81  E-value: 4.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  37 VLVEFLDFECEACAAAYPLVEQIREEYdGRLSVVARYFPLPGHANAENAAVAVEAAAGQGAFEAMYQR------------ 104
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARY-GDVKVVYRPFPLAGAKKIGNVGPSNLPVKLKYMMADLERWaalygiplrfpa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218 105 ------------MYATQAQ--------------WGEQQQ-SQADLFRTFAADLGLDLAAYDAAVADPGTLSRVGRDLTDG 157
Cdd:pfam01323  80 nflgnstranrlALAAGAEglaekvvrelfnalWGEGAAiTDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTAAA 159

                         170
                  ....*....|....*...
gi 2639432218 158 QALGVQSTPTFFLDGQRI 175
Cdd:pfam01323 160 ISLGVFGVPTFVVGGKMV 177
NahD COG3917
2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and ...
 95-195 1.07e-05

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


Pssm-ID: 443122 [Multi-domain]  Cd Length: 196  Bit Score: 44.01  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  95 QGAFEAMYQRMYAtqAQWGEQQQ-SQADLFRTFAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFLDGQ 173
Cdd:COG3917    99 AGAAAAFVRAVFR--AVWAEGRDiADPAVLAAIAAAAGLDAAALLAAAQSPAVKARLRANTEEAVARGVFGAPTFVVDGE 176

                          90       100
                  ....*....|....*....|....*...
gi 2639432218 174 ------RIEptsiedfraQVDAALAQRR 195
Cdd:COG3917   177 lfwgqdRLD---------FLEAALAGGG 195
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 95-173 2.85e-04

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: 40.26  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2639432218  95 QGAFEAMYQRMYatQAQWGEQQQ-SQADLFRTFAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFLDGQ 173
Cdd:cd03024   107 QGKQDALVEALF--RAYFTEGKDiGDRDVLVDLAEEAGLDAAEARAVLASDEYADEVRADEARARQLGISGVPFFVFNGK 184
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 109-173 4.92e-04

DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK).


Pssm-ID: 239320 [Multi-domain]  Cd Length: 192  Bit Score: 39.15  E-value: 4.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2639432218 109 QAQWGEQQQ-SQADLFRTFAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFLDGQ 173
Cdd:cd03022   111 RALWGEGLDiADPAVLAAVAAAAGLDADELLAAADDPAVKAALRANTEEAIARGVFGVPTFVVDGE 176
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
 118-190 7.79e-03

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


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 35.99  E-value: 7.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2639432218 118 SQADLFRTFAADLGLDLAAYDAAVADPGTLSRVGRDLTDGQALGVQSTPTFFL-DGQRIEP-----TSIEDFRAQVDAA 190
Cdd:COG3531   128 SDPEVLAELAAELGLDAEAFAAALASEETRQHIQQEFALARQLGVQGFPTLVLeQGGQLYLlprgyGDPEALLAALEQL 206
 
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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