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Conserved domains on  [gi|1246803562|ref|WP_096388262|]
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DsbA family protein [Hafnia sp. CBA7124]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
5-213 5.42e-90

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member PRK10954:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 207  Bit Score: 263.11  E-value: 5.42e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562   5 MKKyLLLALLSTfsLFSFASHAADYQEGEQYVKLKNKVPNAPAVVEFFSFYCPPCNQFANVYKVSEAVNERLPQNDKVVK 84
Cdd:PRK10954    1 MKK-IWLALAGM--VLAFSASAAQFTDGKQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYHVSDNVKKKLPEGTKMTK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  85 YHVSAMGSMGEELTEAWSVAIALGIENKVEKPLFDAVQKEQSIKNKEDIRQVFIKAGIPAEEYDGALHSFMVKSITAKQQ 164
Cdd:PRK10954   78 YHVEFLGPLGKELTQAWAVAMALGVEDKVTPPLFEGVQKTQTIQSAADIRDVFIKAGVKGEDYDAAWNSFVVKSLVAQQE 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1246803562 165 NATEAFGVRGTPSFYVGGQYQIKNDGMQSKTIDGYRTEFADVVKFLVDQ 213
Cdd:PRK10954  158 KAAADLQLRGVPAMFVNGKYMVNNQGMDTSSMDVYVQQYADVVKFLLEK 206
 
Name Accession Description Interval E-value
PRK10954 PRK10954
thiol:disulfide interchange protein DsbA;
5-213 5.42e-90

thiol:disulfide interchange protein DsbA;


Pssm-ID: 182863 [Multi-domain]  Cd Length: 207  Bit Score: 263.11  E-value: 5.42e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562   5 MKKyLLLALLSTfsLFSFASHAADYQEGEQYVKLKNKVPNAPAVVEFFSFYCPPCNQFANVYKVSEAVNERLPQNDKVVK 84
Cdd:PRK10954    1 MKK-IWLALAGM--VLAFSASAAQFTDGKQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYHVSDNVKKKLPEGTKMTK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  85 YHVSAMGSMGEELTEAWSVAIALGIENKVEKPLFDAVQKEQSIKNKEDIRQVFIKAGIPAEEYDGALHSFMVKSITAKQQ 164
Cdd:PRK10954   78 YHVEFLGPLGKELTQAWAVAMALGVEDKVTPPLFEGVQKTQTIQSAADIRDVFIKAGVKGEDYDAAWNSFVVKSLVAQQE 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1246803562 165 NATEAFGVRGTPSFYVGGQYQIKNDGMQSKTIDGYRTEFADVVKFLVDQ 213
Cdd:PRK10954  158 KAAADLQLRGVPAMFVNGKYMVNNQGMDTSSMDVYVQQYADVVKFLLEK 206
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
31-213 1.03e-48

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: 157.07  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  31 EGEQYVKLKNKVPNA-PAVVEFFSFYCPPCNQFANVYKVSEAvneRLPQNDKVVKYHVSAMGSMGEELTEAWSVAIALGI 109
Cdd:cd03019     1 EGKDYTVLSPPIPSGkPEVIEFFSYGCPHCYNFEPILEAWVK---KLPKDVKFEKVPVVFGGGEGEPLARAFYAAEALGL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562 110 ENKVEKPLFDAVQKEQSIKNKED-IRQVFIKAGIPAEEYDGALHSFMVKSITAKQQNATEAFGVRGTPSFYVGGQYQIKN 188
Cdd:cd03019    78 EDKLHAALFEAIHEKRKRLLDPDdIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNP 157
                         170       180
                  ....*....|....*....|....*
gi 1246803562 189 DGMQSktidgyrTEFADVVKFLVDQ 213
Cdd:cd03019   158 SAIGG-------DDTLQVLDELIEK 175
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
47-183 1.92e-20

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: 84.79  E-value: 1.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  47 AVVEFFSFYCPPCNQFANVYKVSEAVNERLpqndKVVKYHVSAMGSM--------------------------------- 93
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDV----KVVYRPFPLAGAKkignvgpsnlpvklkymmadlerwaalygiplr 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  94 -----GEELTEAWSVAIALGIENKVEK---PLFDAVQKE-QSIKNKEDIRQVFIKAGIPAEEYDGALHSFMVKSITAKQQ 164
Cdd:pfam01323  77 fpanfLGNSTRANRLALAAGAEGLAEKvvrELFNALWGEgAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENT 156
                         170
                  ....*....|....*....
gi 1246803562 165 NATEAFGVRGTPSFYVGGQ 183
Cdd:pfam01323 157 AAAISLGVFGVPTFVVGGK 175
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
48-183 3.03e-20

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 83.12  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  48 VVEFFSFYCPPCNQFANVYKvseAVNERLPQND-KVVKYHVSAMGSMGEELTEAwsvAIALGIENKVEkPLFDAVQKEQS 126
Cdd:COG1651     4 VVEFFDYQCPYCARFHPELP---ELLKKYVDGKvRVVYRPFPLLHPDSLRAARA---ALCAADQGKFW-AFHDALFANQP 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246803562 127 IKNKEDIRQVFIKAGIPAEEYDGALHSFMVKSITAKQQNATEAFGVRGTPSFYVGGQ 183
Cdd:COG1651    77 ALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGK 133
 
Name Accession Description Interval E-value
PRK10954 PRK10954
thiol:disulfide interchange protein DsbA;
5-213 5.42e-90

thiol:disulfide interchange protein DsbA;


Pssm-ID: 182863 [Multi-domain]  Cd Length: 207  Bit Score: 263.11  E-value: 5.42e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562   5 MKKyLLLALLSTfsLFSFASHAADYQEGEQYVKLKNKVPNAPAVVEFFSFYCPPCNQFANVYKVSEAVNERLPQNDKVVK 84
Cdd:PRK10954    1 MKK-IWLALAGM--VLAFSASAAQFTDGKQYTTLDKPVAGEPQVLEFFSFYCPHCYQFEEVYHVSDNVKKKLPEGTKMTK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  85 YHVSAMGSMGEELTEAWSVAIALGIENKVEKPLFDAVQKEQSIKNKEDIRQVFIKAGIPAEEYDGALHSFMVKSITAKQQ 164
Cdd:PRK10954   78 YHVEFLGPLGKELTQAWAVAMALGVEDKVTPPLFEGVQKTQTIQSAADIRDVFIKAGVKGEDYDAAWNSFVVKSLVAQQE 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1246803562 165 NATEAFGVRGTPSFYVGGQYQIKNDGMQSKTIDGYRTEFADVVKFLVDQ 213
Cdd:PRK10954  158 KAAADLQLRGVPAMFVNGKYMVNNQGMDTSSMDVYVQQYADVVKFLLEK 206
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
31-213 1.03e-48

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: 157.07  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  31 EGEQYVKLKNKVPNA-PAVVEFFSFYCPPCNQFANVYKVSEAvneRLPQNDKVVKYHVSAMGSMGEELTEAWSVAIALGI 109
Cdd:cd03019     1 EGKDYTVLSPPIPSGkPEVIEFFSYGCPHCYNFEPILEAWVK---KLPKDVKFEKVPVVFGGGEGEPLARAFYAAEALGL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562 110 ENKVEKPLFDAVQKEQSIKNKED-IRQVFIKAGIPAEEYDGALHSFMVKSITAKQQNATEAFGVRGTPSFYVGGQYQIKN 188
Cdd:cd03019    78 EDKLHAALFEAIHEKRKRLLDPDdIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNGKYVVNP 157
                         170       180
                  ....*....|....*....|....*
gi 1246803562 189 DGMQSktidgyrTEFADVVKFLVDQ 213
Cdd:cd03019   158 SAIGG-------DDTLQVLDELIEK 175
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
47-183 1.92e-20

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: 84.79  E-value: 1.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  47 AVVEFFSFYCPPCNQFANVYKVSEAVNERLpqndKVVKYHVSAMGSM--------------------------------- 93
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDV----KVVYRPFPLAGAKkignvgpsnlpvklkymmadlerwaalygiplr 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  94 -----GEELTEAWSVAIALGIENKVEK---PLFDAVQKE-QSIKNKEDIRQVFIKAGIPAEEYDGALHSFMVKSITAKQQ 164
Cdd:pfam01323  77 fpanfLGNSTRANRLALAAGAEGLAEKvvrELFNALWGEgAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENT 156
                         170
                  ....*....|....*....
gi 1246803562 165 NATEAFGVRGTPSFYVGGQ 183
Cdd:pfam01323 157 AAAISLGVFGVPTFVVGGK 175
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
48-183 3.03e-20

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 83.12  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  48 VVEFFSFYCPPCNQFANVYKvseAVNERLPQND-KVVKYHVSAMGSMGEELTEAwsvAIALGIENKVEkPLFDAVQKEQS 126
Cdd:COG1651     4 VVEFFDYQCPYCARFHPELP---ELLKKYVDGKvRVVYRPFPLLHPDSLRAARA---ALCAADQGKFW-AFHDALFANQP 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246803562 127 IKNKEDIRQVFIKAGIPAEEYDGALHSFMVKSITAKQQNATEAFGVRGTPSFYVGGQ 183
Cdd:COG1651    77 ALTDDDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGK 133
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
48-183 2.75e-05

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: 41.62  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  48 VVEFFSFYCPPCNQFanvYKVSEAVNERLPQNDKVVKYHVSAMGSMGEElTEAWSVAIALGIENKVEKPLFDAVqkeqsi 127
Cdd:cd02972     1 IVEFFDPLCPYCYLF---EPELEKLLYADDGGVRVVYRPFPLLGGMPPN-SLAAARAALAAAAQGKFEALHEAL------ 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1246803562 128 knkedirqvfikagipaeeydgalhsfmvksitaKQQNATEAFGVRGTPSFYVGGQ 183
Cdd:cd02972    71 ----------------------------------ADTALARALGVTGTPTFVVNGE 92
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
43-183 2.08e-04

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: 40.27  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  43 PNAPA-VVEFFSFYCPPCnqfanvyKVSEAVNERLPQNDKVVKYHVSAMGSMGEELTEAWSVAIALGIEN--KVEKpLFD 119
Cdd:cd03023     3 PNGDVtIVEFFDYNCGYC-------KKLAPELEKLLKEDPDVRVVFKEFPILGESSVLAARVALAVWKNGpgKYLE-FHN 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246803562 120 AVQKEQSIKNKEDIRQVFIKAGIPAEEYDGALHSFMVKSITAKQQNATEAFGVRGTPSFYVGGQ 183
Cdd:cd03023    75 ALMATRGRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDT 138
Thioredoxin_4 pfam13462
Thioredoxin;
43-183 3.82e-04

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 39.63  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562  43 PNAPA-VVEFFSFYCPPCNQFanvYKVSEAVNERLPQNDKV--------------VKYHVSAMGSMGEELTEAWSVAIAL 107
Cdd:pfam13462  10 PDAPVtVVEYADLRCPHCAKF---HEEVLKLLEEYIDTGKVrfiirdfpldgegeSLLAAMAARCAGDQSPEYFLVIDKL 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246803562 108 GIENKVEKPLFDAVQKEQSIKNKEDirqvfiKAGIPAEEYDGALhsfmvksitAKQQNATEAFGVRGTPSFYVGGQ 183
Cdd:pfam13462  87 LYSQQEEWAQDLELAALAGLKDEEF------EACLEEEDFLALV---------MADVKEARAAGINFTPTFIINGK 147
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
114-186 1.87e-03

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


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 37.92  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246803562 114 EKPLFDAVQKE-----QSIKNKEDIRQVFIKAGIPAEEYDGALHSFMVKSITAKQQNATEAFGVRGTPSFYV--GGQYQI 186
Cdd:COG3531   109 ELAMLHAIQRAfyvegRDISDPEVLAELAAELGLDAEAFAAALASEETRQHIQQEFALARQLGVQGFPTLVLeqGGQLYL 188
 
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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