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Conserved domains on  [gi|957949417|gb|ALQ33531|]
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fumarate hydratase isoform 4 [Homo sapiens]

Protein Classification

lyase family protein( domain architecture ID 97)

lyase family protein belongs to a superfamily of enzymes that catalyze beta-elimination reactions in which a C-N or C-O bond is cleaved and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits

CATH:  1.20.200.10
EC:  4.-.-.-
SCOP:  3001572

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FumC super family cl43028
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ...
 49-161 3.97e-72

Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle


The actual alignment was detected with superfamily member COG0114:

Pssm-ID: 439884 [Multi-domain]  Cd Length: 461  Bit Score: 223.75  E-value: 3.97e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 127
Cdd:COG0114    3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGG--ERMPREFIRALALIKKAAARANAELGlLDAEKADAIVAAADEV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 957949417 128 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:COG0114   81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRA 114
 
Name Accession Description Interval E-value
FumC COG0114
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ...
 49-161 3.97e-72

Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439884 [Multi-domain]  Cd Length: 461  Bit Score: 223.75  E-value: 3.97e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 127
Cdd:COG0114    3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGG--ERMPREFIRALALIKKAAARANAELGlLDAEKADAIVAAADEV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 957949417 128 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:COG0114   81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRA 114
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 51-161 5.63e-72

Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176465 [Multi-domain]  Cd Length: 455  Bit Score: 223.15  E-value: 5.63e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:cd01362    1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALGLLKKAAAQANAELGlLDEEKADAIVQAADEVIA 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 957949417 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:cd01362   79 GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRA 110
fumC PRK00485
fumarate hydratase; Reviewed
 49-161 2.61e-70

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 219.19  E-value: 2.61e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 127
Cdd:PRK00485   3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALALLKKAAARVNAELGlLDAEKADAIVAAADEV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 957949417 128 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:PRK00485  81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRA 114
fumC_II TIGR00979
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ...
 50-162 1.25e-63

fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium tuberculosis, Streptomyces coelicolor, Pseudomonas aeruginosa) branch deeply, although within the same branch of a phylogenetic tree rooted by aspartate ammonia-lyase sequences, and score between the trusted and noise cutoffs. [Energy metabolism, TCA cycle]


Pssm-ID: 130052 [Multi-domain]  Cd Length: 458  Bit Score: 201.88  E-value: 1.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417   50 FRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGgvTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVA 128
Cdd:TIGR00979   1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIG--TEKMPLELIHAFAILKKAAAIVNEDLGkLDAKKADAIVQAADEIL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 957949417  129 EGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAV 162
Cdd:TIGR00979  79 AGKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAI 112
Lyase_1 pfam00206
Lyase;
58-158 6.69e-34

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 120.94  E-value: 6.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417   58 GELKVPNDKYYGAQTVRSTMNFKIGGVTermptpvIKAFGILKRAAAEVNQDYgldPKIANAIMKAADEVAE-GKLNDHF 136
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEED-------IKGLAALKKAAAKANVIL---KEEAAAIIKALDEVAEeGKLDDQF 70

                          90       100
                  ....*....|....*....|..
gi 957949417  137 PLVVWQTGSGTQTNMNVNEVIS 158
Cdd:pfam00206  71 PLKVWQEGSGTAVNMNLNEVIG 92
 
Name Accession Description Interval E-value
FumC COG0114
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ...
 49-161 3.97e-72

Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439884 [Multi-domain]  Cd Length: 461  Bit Score: 223.75  E-value: 3.97e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 127
Cdd:COG0114    3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGG--ERMPREFIRALALIKKAAARANAELGlLDAEKADAIVAAADEV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 957949417 128 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:COG0114   81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRA 114
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 51-161 5.63e-72

Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176465 [Multi-domain]  Cd Length: 455  Bit Score: 223.15  E-value: 5.63e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:cd01362    1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALGLLKKAAAQANAELGlLDEEKADAIVQAADEVIA 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 957949417 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:cd01362   79 GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRA 110
fumC PRK00485
fumarate hydratase; Reviewed
 49-161 2.61e-70

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 219.19  E-value: 2.61e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 127
Cdd:PRK00485   3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALALLKKAAARVNAELGlLDAEKADAIVAAADEV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 957949417 128 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:PRK00485  81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRA 114
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 51-161 3.62e-68

aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176468 [Multi-domain]  Cd Length: 450  Bit Score: 213.05  E-value: 3.62e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:cd01596    1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISG--ERMPPELIRALALVKKAAALANAELGlLDEEKADAIVQACDEVIA 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 957949417 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:cd01596   79 GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRA 110
PLN00134 PLN00134
fumarate hydratase; Provisional
 57-161 4.94e-64

fumarate hydratase; Provisional


Pssm-ID: 215069 [Multi-domain]  Cd Length: 458  Bit Score: 202.61  E-value: 4.94e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  57 FGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDH 135
Cdd:PLN00134   1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGlLDPDIGKAIMQAADEVAEGKLDDH 80

                         90       100
                 ....*....|....*....|....*.
gi 957949417 136 FPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:PLN00134  81 FPLVVWQTGSGTQTNMNANEVIANRA 106
fumC_II TIGR00979
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ...
 50-162 1.25e-63

fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium tuberculosis, Streptomyces coelicolor, Pseudomonas aeruginosa) branch deeply, although within the same branch of a phylogenetic tree rooted by aspartate ammonia-lyase sequences, and score between the trusted and noise cutoffs. [Energy metabolism, TCA cycle]


Pssm-ID: 130052 [Multi-domain]  Cd Length: 458  Bit Score: 201.88  E-value: 1.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417   50 FRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGgvTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVA 128
Cdd:TIGR00979   1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIG--TEKMPLELIHAFAILKKAAAIVNEDLGkLDAKKADAIVQAADEIL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 957949417  129 EGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAV 162
Cdd:TIGR00979  79 AGKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAI 112
AspA COG1027
Aspartate ammonia-lyase [Amino acid transport and metabolism];
51-161 3.28e-45

Aspartate ammonia-lyase [Amino acid transport and metabolism];


Pssm-ID: 440650 [Multi-domain]  Cd Length: 460  Bit Score: 153.67  E-value: 3.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:COG1027    1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGlLDKEKADAIVAACDEIIA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 957949417 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:COG1027   81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRA 112
aspA PRK12273
aspartate ammonia-lyase; Provisional
 48-161 3.70e-45

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 153.74  E-value: 3.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  48 NSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADE 126
Cdd:PRK12273   3 MNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGlLDEEKADAIVAACDE 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 957949417 127 VAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:PRK12273  83 ILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRA 117
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 51-161 5.86e-44

Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.


Pssm-ID: 176462 [Multi-domain]  Cd Length: 450  Bit Score: 150.37  E-value: 5.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:cd01357    1 RIEHDLLGEREVPADAYYGIQTLRALENFPISG--LKIHPELIRALAMVKKAAALANAELGlLDEEKAEAIVKACDEIIA 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 957949417 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:cd01357   79 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRA 110
PRK12425 PRK12425
class II fumarate hydratase;
51-161 1.45e-42

class II fumarate hydratase;


Pssm-ID: 171490 [Multi-domain]  Cd Length: 464  Bit Score: 146.99  E-value: 1.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:PRK12425   3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGK--ERMPLAVLHALALIKKAAARVNDRNGdLPADIARLIEQAADEVLD 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 957949417 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:PRK12425  81 GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRA 112
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 47-161 4.51e-42

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 145.51  E-value: 4.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  47 QNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAAD 125
Cdd:PRK13353   2 NKNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGY--KIHPELIRAFAQVKKAAALANADLGlLPRRIAEAIVQACD 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 957949417 126 EVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRA 161
Cdd:PRK13353  80 EILAGKLHDQFIVDPIQGGAGTSTNMNANEVIANRA 115
Lyase_1 pfam00206
Lyase;
58-158 6.69e-34

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 120.94  E-value: 6.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417   58 GELKVPNDKYYGAQTVRSTMNFKIGGVTermptpvIKAFGILKRAAAEVNQDYgldPKIANAIMKAADEVAE-GKLNDHF 136
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEED-------IKGLAALKKAAAKANVIL---KEEAAAIIKALDEVAEeGKLDDQF 70

                          90       100
                  ....*....|....*....|..
gi 957949417  137 PLVVWQTGSGTQTNMNVNEVIS 158
Cdd:pfam00206  71 PLKVWQEGSGTAVNMNLNEVIG 92
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 47-162 3.84e-31

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 116.64  E-value: 3.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957949417  47 QNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAAD 125
Cdd:PRK14515   8 KNGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGY--KIHEGLIKAFAIVKKAAALANTDVGrLELNKGGAIAEAAQ 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 957949417 126 EVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAV 162
Cdd:PRK14515  86 EILDGKWHDHFIVDPIQGGAGTSMNMNANEVIANRAL 122
 
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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