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Conserved domains on  [gi|610992087|gb|EZI97740|]
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DSBA-like thioredoxin domain protein [Acinetobacter baumannii 44298_1]

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
PubMed:  12524212|9099998|10049365|15558583
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 ...
 3-204 1.57e-85

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: 252.50  E-value: 1.57e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087   3 VDVWSDVVCPFCYIGKKRLEHVAAEAG--IELDIHWHSFELDPDAPaKHDTSNTERLAKKYGRTYEEMEEMeRNIAAMAA 80
Cdd:cd03024    1 IDIWSDVVCPWCYIGKRRLEKALAELGdeVDVEIEWRPFELNPDMP-PEGEDRREYLARKYGSTAEQAAAM-RRVEAAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087  81 SEGIDFQWQKANSGNSFNAHRIIHLAQSKGLGNEAKEAFFHAYMTEGLAIGEREVVEEIASRIGLDNAEVEYVLDTNELA 160
Cdd:cd03024   79 AEGLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 610992087 161 DFVRHDEKIAHeQLNVTGVPFFVFDQRIALAGAQPREVFLQVLE 204
Cdd:cd03024  159 DEVRADEARAR-QLGISGVPFFVFNGKYAVSGAQPPEVFLQALR 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 ...
 3-204 1.57e-85

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: 252.50  E-value: 1.57e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087   3 VDVWSDVVCPFCYIGKKRLEHVAAEAG--IELDIHWHSFELDPDAPaKHDTSNTERLAKKYGRTYEEMEEMeRNIAAMAA 80
Cdd:cd03024    1 IDIWSDVVCPWCYIGKRRLEKALAELGdeVDVEIEWRPFELNPDMP-PEGEDRREYLARKYGSTAEQAAAM-RRVEAAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087  81 SEGIDFQWQKANSGNSFNAHRIIHLAQSKGLGNEAKEAFFHAYMTEGLAIGEREVVEEIASRIGLDNAEVEYVLDTNELA 160
Cdd:cd03024   79 AEGLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 610992087 161 DFVRHDEKIAHeQLNVTGVPFFVFDQRIALAGAQPREVFLQVLE 204
Cdd:cd03024  159 DEVRADEARAR-QLGISGVPFFVFNGKYAVSGAQPPEVFLQALR 201
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 1-206 2.09e-84

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: 249.80  E-value: 2.09e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087   1 MRVDVWSDVVCPFCYIGKKRLEHVAAEAGIELDIHWHSFELDPDAPAKHDTSNTERLAKKygrTYEEMEEMERNIAAMAA 80
Cdd:COG2761    2 LKIDIFSDVVCPWCYIGKRRLEKALAEFGDDVEIRWRPFELNPDMPPEGEDRREYLLAKG---SPEQAEQMRAHVEEAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087  81 SEGIDFQWQKANSGNSFNAHRIIHLAQSKGLGNEAKEAFFHAYMTEGLAIGEREVVEEIASRIGLDNAEVEYVLDTNELA 160
Cdd:COG2761   79 EEGLPFDFDRIKPPNTFDAHRLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDEAA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 610992087 161 DFVRHDEKIAHeQLNVTGVPFFVFDQRIALAGAQPREVFLQVLEQA 206
Cdd:COG2761  159 AAVRADEAEAR-ELGVTGVPTFVFDGKYAVSGAQPYEVFEQALRQA 203
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 2-204 4.82e-39

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: 133.71  E-value: 4.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087    2 RVDVWSDVVCPFCYIGKKRLEHVAAEAGiELDIHWHSFELDPDAPakhdtSNTERLAKKYGRTYEEMEEMERniaaMAAS 81
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYG-DVKVVYRPFPLAGAKK-----IGNVGPSNLPVKLKYMMADLER----WAAL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087   82 EGIDFQWQKANSGNSFNAHRIIHLAQSKGLGNEAKEAFFHAYMTEGLAIGEREVVEEIASRIGLDNAEVEYVLDTNELAD 161
Cdd:pfam01323  71 YGIPLRFPANFLGNSTRANRLALAAGAEGLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKE 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 610992087  162 FVRHDEKIAhEQLNVTGVPFFVFDQRiALAGAQPREVFLQVLE 204
Cdd:pfam01323 151 AVRENTAAA-ISLGVFGVPTFVVGGK-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 ...
 3-204 1.57e-85

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: 252.50  E-value: 1.57e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087   3 VDVWSDVVCPFCYIGKKRLEHVAAEAG--IELDIHWHSFELDPDAPaKHDTSNTERLAKKYGRTYEEMEEMeRNIAAMAA 80
Cdd:cd03024    1 IDIWSDVVCPWCYIGKRRLEKALAELGdeVDVEIEWRPFELNPDMP-PEGEDRREYLARKYGSTAEQAAAM-RRVEAAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087  81 SEGIDFQWQKANSGNSFNAHRIIHLAQSKGLGNEAKEAFFHAYMTEGLAIGEREVVEEIASRIGLDNAEVEYVLDTNELA 160
Cdd:cd03024   79 AEGLEFDFDRVRPPNTFDAHRLIHLAKEQGKQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARAVLASDEYA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 610992087 161 DFVRHDEKIAHeQLNVTGVPFFVFDQRIALAGAQPREVFLQVLE 204
Cdd:cd03024  159 DEVRADEARAR-QLGISGVPFFVFNGKYAVSGAQPPEVFLQALR 201
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 1-206 2.09e-84

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: 249.80  E-value: 2.09e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087   1 MRVDVWSDVVCPFCYIGKKRLEHVAAEAGIELDIHWHSFELDPDAPAKHDTSNTERLAKKygrTYEEMEEMERNIAAMAA 80
Cdd:COG2761    2 LKIDIFSDVVCPWCYIGKRRLEKALAEFGDDVEIRWRPFELNPDMPPEGEDRREYLLAKG---SPEQAEQMRAHVEEAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087  81 SEGIDFQWQKANSGNSFNAHRIIHLAQSKGLGNEAKEAFFHAYMTEGLAIGEREVVEEIASRIGLDNAEVEYVLDTNELA 160
Cdd:COG2761   79 EEGLPFDFDRIKPPNTFDAHRLLKAAELQGKQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLESDEAA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 610992087 161 DFVRHDEKIAHeQLNVTGVPFFVFDQRIALAGAQPREVFLQVLEQA 206
Cdd:COG2761  159 AAVRADEAEAR-ELGVTGVPTFVFDGKYAVSGAQPYEVFEQALRQA 203
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 2-204 4.82e-39

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: 133.71  E-value: 4.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087    2 RVDVWSDVVCPFCYIGKKRLEHVAAEAGiELDIHWHSFELDPDAPakhdtSNTERLAKKYGRTYEEMEEMERniaaMAAS 81
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYG-DVKVVYRPFPLAGAKK-----IGNVGPSNLPVKLKYMMADLER----WAAL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087   82 EGIDFQWQKANSGNSFNAHRIIHLAQSKGLGNEAKEAFFHAYMTEGLAIGEREVVEEIASRIGLDNAEVEYVLDTNELAD 161
Cdd:pfam01323  71 YGIPLRFPANFLGNSTRANRLALAAGAEGLAEKVVRELFNALWGEGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKE 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 610992087  162 FVRHDEKIAhEQLNVTGVPFFVFDQRiALAGAQPREVFLQVLE 204
Cdd:pfam01323 151 AVRENTAAA-ISLGVFGVPTFVVGGK-MVFGADRLDTLADALA 191
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 3-185 7.15e-18

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: 78.44  E-value: 7.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087   3 VDVWSDVVCPFCYIGKKRLEHVAAEAGieLDIHWHSFELDPDAPAKHDTSNTERLAKKygRTYEeMEEMERniaaMAASE 82
Cdd:cd03022    1 IDFYFDFSSPYSYLAHERLPALAARHG--ATVRYRPILLGGVFKATGNVPPANRPPAK--GRYR-LRDLER----WARRY 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087  83 GIDFQWQKANSGNSFNAHRIIHLAQSKGLGNEA-KEAFFHAYMTEGLAIGEREVVEEIASRIGLDNAEVEYVLDTNELAD 161
Cdd:cd03022   72 GIPLRFPPRFPPNTLRAMRAALAAQAEGDAAEAfARAVFRALWGEGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKA 151

                        170       180
                 ....*....|....*....|....
gi 610992087 162 FVRHDEKIAHEqLNVTGVPFFVFD 185
Cdd:cd03022  152 ALRANTEEAIA-RGVFGVPTFVVD 174
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 94-206 3.15e-09

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 53.85  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087  94 GNSFNAHRIIHLAQSKGlgneAKEAFFHAYMTEGLAIGErEVVEEIASRIGLDNAEVEYVLDTNELADFVRHDEKIAhEQ 173
Cdd:COG1651   46 PDSLRAARAALCAADQG----KFWAFHDALFANQPALTD-DDLREIAKEAGLDAAKFDACLNSGAVAAKVEADTALA-QA 119

                         90       100       110
                 ....*....|....*....|....*....|...
gi 610992087 174 LNVTGVPFFVFDQRIaLAGAQPREVFLQVLEQA 206
Cdd:COG1651  120 LGVTGTPTFVVNGKL-VSGAVPYEELEAALDAA 151
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 3-80 5.41e-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: 52.02  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087   3 VDVWSDVVCPFCYIGKKRLEHVAAEAGIELDIHWHSFELDPDAPakhdtSNTERLAKKYGRTYEE--MEEMERNIAAMAA 80
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDGGVRVVYRPFPLLGGMP-----PNSLAAARAALAAAAQgkFEALHEALADTAL 75
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
 121-206 7.64e-07

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


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 48.32  E-value: 7.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087 121 HAYMTEGLAIGEREVVEEIASRIGLDNAEVEYVLDTNELADFVRHDEKIAHeQLNVTGVPFFVF---DQRIALA-GAQPR 196
Cdd:COG3531  118 RAFYVEGRDISDPEVLAELAAELGLDAEAFAAALASEETRQHIQQEFALAR-QLGVQGFPTLVLeqgGQLYLLPrGYGDP 196

                         90
                 ....*....|
gi 610992087 197 EVFLQVLEQA 206
Cdd:COG3531  197 EALLAALEQL 206
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
 106-186 9.30e-07

DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif with similarity to DsbA and FrnE. FrnE is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239323 [Multi-domain]  Cd Length: 193  Bit Score: 47.70  E-value: 9.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087 106 AQSKGLGNEAKEAFFHAYMTEGLAIGEREVVEEIASRIGLDNAEVEYVLDTNELADFVRHDEKIAHeQLNVTGVPFFVFD 185
Cdd:cd03025   98 LQGPERLLEMLKAIQRAHYVEGRDLADTEVLRELAIELGLDVEEFLEDFQSDEAKQAIQEDQKLAR-ELGINGFPTLVLE 176


                 .
gi 610992087 186 Q 186
Cdd:cd03025  177 D 177
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 94-204 1.25e-03

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: 37.96  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610992087  94 GNSFNAHRIIhLAqSKGLGNEAKEAFFHAYMTEGLAIGErEVVEEIASRIGLDNAEVEYVLDTNELADFVRHDEKIAhEQ 173
Cdd:cd03023   49 ESSVLAARVA-LA-VWKNGPGKYLEFHNALMATRGRLNE-ESLLRIAKKAGLDEAKLKKDMDDPEIEATIDKNRQLA-RA 124

                         90       100       110
                 ....*....|....*....|....*....|.
gi 610992087 174 LNVTGVPFFVFDQRIaLAGAQPREVFLQVLE 204
Cdd:cd03023  125 LGITGTPAFIIGDTV-IPGAVPADTLKEAID 154
 
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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