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Conserved domains on  [gi|490320746|ref|WP_004210231|]
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MULTISPECIES: HAD family hydrolase [Enterobacteriaceae]

Protein Classification

HAD family hydrolase( domain architecture ID 11552400)

HAD (haloacid dehalogenase) family hydrolase similar to Pseudomonas aeruginosa histidinol-phosphatase that catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine; the HAD (haloacid dehalogenase) family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.1.3.-
Gene Ontology:  GO:0046872|GO:0016791|GO:0016311
PubMed:  16889794|15337123
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 9-201 1.67e-57

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 180.19  E-value: 1.67e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   9 LSVFDFDGTLTRHDSFIPFLRFAfgNRAFSRRIVSMA----LPTLRCMGKQMTrdELKETLITTFLTGVEEkWVSSKAEE 84
Cdd:cd02612    1 LAFFDLDGTLIAGDSFFAFLRFK--GIAERRAPLEELlllrLMALYALGRLDG--AGMEALLGFATAGLAG-ELAALVEE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746  85 FCELYWHRLMRPAGLIAVANEVTSGAIVTLCSASPEIVLRPFAEKLRI-KLIGTQLETKDGILTGRISGHNCRCSQKIIR 163
Cdd:cd02612   76 FVEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIdNVLGTQLETEDGRYTGRIIGPPCYGEGKVKR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 490320746 164 LEKEYGP--LTDYHLRAWGDTRGDYELLSAATEPHWRHFH 201
Cdd:cd02612  156 LREWLAEegIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
 
Name Accession Description Interval E-value
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 9-201 1.67e-57

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 180.19  E-value: 1.67e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   9 LSVFDFDGTLTRHDSFIPFLRFAfgNRAFSRRIVSMA----LPTLRCMGKQMTrdELKETLITTFLTGVEEkWVSSKAEE 84
Cdd:cd02612    1 LAFFDLDGTLIAGDSFFAFLRFK--GIAERRAPLEELlllrLMALYALGRLDG--AGMEALLGFATAGLAG-ELAALVEE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746  85 FCELYWHRLMRPAGLIAVANEVTSGAIVTLCSASPEIVLRPFAEKLRI-KLIGTQLETKDGILTGRISGHNCRCSQKIIR 163
Cdd:cd02612   76 FVEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIdNVLGTQLETEDGRYTGRIIGPPCYGEGKVKR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 490320746 164 LEKEYGP--LTDYHLRAWGDTRGDYELLSAATEPHWRHFH 201
Cdd:cd02612  156 LREWLAEegIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 9-200 5.35e-29

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 107.43  E-value: 5.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746    9 LSVFDFDGTLTRHDSFIPFLRFAFGNR-AFSRRIVSMALPTLRC-MGKQMTRDELKETLITTFLTGVEEKWVSSKAEEFC 86
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNiLFEELRLPKVLARFEFfLNRGLDYMAYYRAFALDALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   87 ELYWHRLMRPAGLIAVANEVTSGAIVTLCSASPEIVLRPFAEKLRIK-LIGTQLET-KDGILTGRISGHNCRCSQKIIRL 164
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDnAIGTRLEEsEDGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 490320746  165 ----EKEYGPLTDYHlrAWGDTRGDYELLSAATEPHWRHF 200
Cdd:TIGR01490 161 aellAEEQIDLKDSY--AYGDSISDLPLLSLVGHPYVVNP 198
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 6-196 9.63e-25

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 96.83  E-value: 9.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   6 PRMLSVFDFDGTLTRHDSFIPFLRFAFGNRAFSRRIV--SMALPTLRCMGKQMTRDELKETLITTfLTGVEEKWVSSKAE 83
Cdd:COG0560    2 KMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVleEVAAITERAMAGELDFEESLRFRVAL-LAGLPEEELEELAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746  84 EFCELywHRLMRPAGLIAVANEVTSGAIVTLCSASPEIVLRPFAEKLRIK-LIGTQLETKDGILTGRISGHNCRCSQKII 162
Cdd:COG0560   81 RLFEE--VPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDhVIANELEVEDGRLTGEVVGPIVDGEGKAE 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490320746 163 RLE---KEYGpLTDYHLRAWGDTRGDYELLSAATEPH 196
Cdd:COG0560  159 ALRelaAELG-IDLEQSYAYGDSANDLPMLEAAGLPV 194
HAD pfam12710
haloacid dehalogenase-like hydrolase;
11-190 1.84e-18

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 79.50  E-value: 1.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   11 VFDFDGTLTRHDSFIPFLRFAFGNRAFS--RRIVSMALPTLRCMGKQMTRDELKEtLITTFLTGVEEKWVSSKAEEFCEL 88
Cdd:pfam12710   2 LFDLDGTLLDGDSLFLLIRALLRRGGPDlwRALLVLLLLALLRLLGRLSRAGARE-LLRALLAGLPEEDAAELERFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   89 YwHRLMRPAGLIAVANEVTSGAIVTLCSASPEIVLRPFAEKL-RIKLIGTQLETKDGILTGR--ISGHNCRCSQKIIRLE 165
Cdd:pfam12710  81 A-LPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELgFDEVLATELEVDDGRFTGElrLIGPPCAGEGKVRRLR 159

                         170       180
                  ....*....|....*....|....*....
gi 490320746  166 K----EYGPLTDYHLRAWGDTRGDYELLS 190
Cdd:pfam12710 160 AwlaaRGLGLDLADSVAYGDSPSDLPMLR 188
 
Name Accession Description Interval E-value
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 9-201 1.67e-57

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 180.19  E-value: 1.67e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   9 LSVFDFDGTLTRHDSFIPFLRFAfgNRAFSRRIVSMA----LPTLRCMGKQMTrdELKETLITTFLTGVEEkWVSSKAEE 84
Cdd:cd02612    1 LAFFDLDGTLIAGDSFFAFLRFK--GIAERRAPLEELlllrLMALYALGRLDG--AGMEALLGFATAGLAG-ELAALVEE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746  85 FCELYWHRLMRPAGLIAVANEVTSGAIVTLCSASPEIVLRPFAEKLRI-KLIGTQLETKDGILTGRISGHNCRCSQKIIR 163
Cdd:cd02612   76 FVEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIdNVLGTQLETEDGRYTGRIIGPPCYGEGKVKR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 490320746 164 LEKEYGP--LTDYHLRAWGDTRGDYELLSAATEPHWRHFH 201
Cdd:cd02612  156 LREWLAEegIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 9-200 5.35e-29

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 107.43  E-value: 5.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746    9 LSVFDFDGTLTRHDSFIPFLRFAFGNR-AFSRRIVSMALPTLRC-MGKQMTRDELKETLITTFLTGVEEKWVSSKAEEFC 86
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNiLFEELRLPKVLARFEFfLNRGLDYMAYYRAFALDALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   87 ELYWHRLMRPAGLIAVANEVTSGAIVTLCSASPEIVLRPFAEKLRIK-LIGTQLET-KDGILTGRISGHNCRCSQKIIRL 164
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDnAIGTRLEEsEDGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 490320746  165 ----EKEYGPLTDYHlrAWGDTRGDYELLSAATEPHWRHF 200
Cdd:TIGR01490 161 aellAEEQIDLKDSY--AYGDSISDLPLLSLVGHPYVVNP 198
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 6-196 9.63e-25

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 96.83  E-value: 9.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   6 PRMLSVFDFDGTLTRHDSFIPFLRFAFGNRAFSRRIV--SMALPTLRCMGKQMTRDELKETLITTfLTGVEEKWVSSKAE 83
Cdd:COG0560    2 KMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVleEVAAITERAMAGELDFEESLRFRVAL-LAGLPEEELEELAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746  84 EFCELywHRLMRPAGLIAVANEVTSGAIVTLCSASPEIVLRPFAEKLRIK-LIGTQLETKDGILTGRISGHNCRCSQKII 162
Cdd:COG0560   81 RLFEE--VPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDhVIANELEVEDGRLTGEVVGPIVDGEGKAE 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490320746 163 RLE---KEYGpLTDYHLRAWGDTRGDYELLSAATEPH 196
Cdd:COG0560  159 ALRelaAELG-IDLEQSYAYGDSANDLPMLEAAGLPV 194
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 9-192 3.62e-21

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 86.25  E-value: 3.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746    9 LSVFDFDGTLTRHDSFIPFLRFAFGNR---------AFSRRIVSMALPTLRCMGKQMTRDElketlittfltgveekwvs 79
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLAKLLGTNdevieltrlAPSGRISFEDALGRRLALLHRSRSE------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   80 SKAEEFcelYWHRLMRPAG---LIAVANEvtSGAIVTLCSASPEIVLRPFAEKLRI-KLIGTQLETKD-GILTGRISG-- 152
Cdd:TIGR01488  62 EVAKEF---LARQVALRPGareLISWLKE--RGIDTVIVSGGFDFFVEPVAEKLGIdDVFANRLEFDDnGLLTGPIEGqv 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 490320746  153 -HNCRCSQKIIRLEKEYGPLTDYHLRAWGDTRGDYELLSAA 192
Cdd:TIGR01488 137 nPEGECKGKVLKELLEESKITLKKIIAVGDSVNDLPMLKLA 177
HAD pfam12710
haloacid dehalogenase-like hydrolase;
11-190 1.84e-18

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 79.50  E-value: 1.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   11 VFDFDGTLTRHDSFIPFLRFAFGNRAFS--RRIVSMALPTLRCMGKQMTRDELKEtLITTFLTGVEEKWVSSKAEEFCEL 88
Cdd:pfam12710   2 LFDLDGTLLDGDSLFLLIRALLRRGGPDlwRALLVLLLLALLRLLGRLSRAGARE-LLRALLAGLPEEDAAELERFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320746   89 YwHRLMRPAGLIAVANEVTSGAIVTLCSASPEIVLRPFAEKL-RIKLIGTQLETKDGILTGR--ISGHNCRCSQKIIRLE 165
Cdd:pfam12710  81 A-LPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELgFDEVLATELEVDDGRFTGElrLIGPPCAGEGKVRRLR 159

                         170       180
                  ....*....|....*....|....*....
gi 490320746  166 K----EYGPLTDYHLRAWGDTRGDYELLS 190
Cdd:pfam12710 160 AwlaaRGLGLDLADSVAYGDSPSDLPMLR 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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