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Conserved domains on  [gi|124263658|gb|ABM97548|]
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Kruppel-like factor 5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KLF5_N cd21579
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ...
 1-279 2.36e-91

N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. It belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF5.


:

Pssm-ID: 410335  Cd Length: 273  Bit Score: 274.86  E-value: 2.36e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658   1 MEKYLTPQLPPVPIiPEHKKYRRDSASVVDQFFTDTEGLPYSINMNVFLPDITHLRTGLYKSQRPCVTHIKTEPVAIFSH 80
Cdd:cd21579   59 MDKYLSPQPPPPPA-PEDKKYRRESASVVDEFFSEDKGSPYSVNMNVFLPDVTYLRTGLCRPVRPIKTEPKHEPPPPTSF 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658  81 QSettaPPPAPTQALPEFTSIFSSHQTAapeVNNIFIKQELPTPDLHlsvptQQGHLYQLLNTPDLDmpsstnqtaamdt 160
Cdd:cd21579  138 CS----SSNGTTQALPEFTSVFSAPQSA---VNNVFIKQEMPSFDDQ-----QQGPLFQLLNSDLDQ------------- 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658 161 lnvsmsaamaglnthtsavpqtavkqfqgmppctytmpsqflPQQATYFPPSPPSSEPGSPDRQAEMLQNLTPPPSYAAT 240
Cdd:cd21579  193 ------------------------------------------QQQPTYLPPSPPNSEPGSPDRQKELLHNLSPPPSYAAS 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 124263658 241 IASKLAIHNPNLP----TTLPVNSQNIQPVRYNRRSNPDLEKR 279
Cdd:cd21579  231 IASKLAGQTPGLPppgvGPLSPGQAQSAPVRYNRRNNPDLEKR 273
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 342-364 1.16e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.82  E-value: 1.16e-04
                          10        20
                  ....*....|....*....|...
gi 124263658  342 FQCGVCNRSFSRSDHLALHMKRH 364
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-353 5.02e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 5.02e-04
                          10        20
                  ....*....|....*....|....*.
gi 124263658  328 ELTRHYRKHTGAKPFQCGVCNRSFSR 353
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
268-342 1.29e-03

FOG: Zn-finger [General function prediction only];


The actual alignment was detected with superfamily member COG5048:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124263658 268 YNRRSNPDLEKRRIHYCdyPGCTKVYTKSSHLKAHLRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPF 342
Cdd:COG5048   20 PKSTLKSLSNAPRPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
 
Name Accession Description Interval E-value
KLF5_N cd21579
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ...
 1-279 2.36e-91

N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. It belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF5.


Pssm-ID: 410335  Cd Length: 273  Bit Score: 274.86  E-value: 2.36e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658   1 MEKYLTPQLPPVPIiPEHKKYRRDSASVVDQFFTDTEGLPYSINMNVFLPDITHLRTGLYKSQRPCVTHIKTEPVAIFSH 80
Cdd:cd21579   59 MDKYLSPQPPPPPA-PEDKKYRRESASVVDEFFSEDKGSPYSVNMNVFLPDVTYLRTGLCRPVRPIKTEPKHEPPPPTSF 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658  81 QSettaPPPAPTQALPEFTSIFSSHQTAapeVNNIFIKQELPTPDLHlsvptQQGHLYQLLNTPDLDmpsstnqtaamdt 160
Cdd:cd21579  138 CS----SSNGTTQALPEFTSVFSAPQSA---VNNVFIKQEMPSFDDQ-----QQGPLFQLLNSDLDQ------------- 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658 161 lnvsmsaamaglnthtsavpqtavkqfqgmppctytmpsqflPQQATYFPPSPPSSEPGSPDRQAEMLQNLTPPPSYAAT 240
Cdd:cd21579  193 ------------------------------------------QQQPTYLPPSPPNSEPGSPDRQKELLHNLSPPPSYAAS 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 124263658 241 IASKLAIHNPNLP----TTLPVNSQNIQPVRYNRRSNPDLEKR 279
Cdd:cd21579  231 IASKLAGQTPGLPppgvGPLSPGQAQSAPVRYNRRNNPDLEKR 273
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 342-364 1.16e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.82  E-value: 1.16e-04
                          10        20
                  ....*....|....*....|...
gi 124263658  342 FQCGVCNRSFSRSDHLALHMKRH 364
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-353 5.02e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 5.02e-04
                          10        20
                  ....*....|....*....|....*.
gi 124263658  328 ELTRHYRKHTGAKPFQCGVCNRSFSR 353
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
268-342 1.29e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124263658 268 YNRRSNPDLEKRRIHYCdyPGCTKVYTKSSHLKAHLRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPF 342
Cdd:COG5048   20 PKSTLKSLSNAPRPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
zf-H2C2_2 pfam13465
Zinc-finger double domain;
298-325 2.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 2.12e-03
                          10        20
                  ....*....|....*....|....*...
gi 124263658  298 HLKAHLRTHTGEKPYKCtwEGCDWRFAR 325
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
 
Name Accession Description Interval E-value
KLF5_N cd21579
N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also ...
 1-279 2.36e-91

N-terminal domain of Kruppel-like factor 5; Kruppel-like factor 5 (KLF5; also known as also known as Krueppel-like factor 5; intestinal enriched Kruppel-like factor/IKLF; basic transcription element binding protein 2/BTEB2) a protein that in humans is encoded by the KLF5 gene. KLF5 is involved in numerous functions in eukaryotic cells, such as proliferation, migration, and differentiation. The loss of KLF5 expression is associated with tumors of the breast, cervix, endometrium, ovary, and prostate. KLF5 mediates the expression of several genes essential for proper cardiac structure and function, and plays a role in familial dilated cardiomyopathy. It functions as a transcriptional activator. KLF5 exhibits both transcriptional activation activity as well as trans-activating function. It belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF5.


Pssm-ID: 410335  Cd Length: 273  Bit Score: 274.86  E-value: 2.36e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658   1 MEKYLTPQLPPVPIiPEHKKYRRDSASVVDQFFTDTEGLPYSINMNVFLPDITHLRTGLYKSQRPCVTHIKTEPVAIFSH 80
Cdd:cd21579   59 MDKYLSPQPPPPPA-PEDKKYRRESASVVDEFFSEDKGSPYSVNMNVFLPDVTYLRTGLCRPVRPIKTEPKHEPPPPTSF 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658  81 QSettaPPPAPTQALPEFTSIFSSHQTAapeVNNIFIKQELPTPDLHlsvptQQGHLYQLLNTPDLDmpsstnqtaamdt 160
Cdd:cd21579  138 CS----SSNGTTQALPEFTSVFSAPQSA---VNNVFIKQEMPSFDDQ-----QQGPLFQLLNSDLDQ------------- 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658 161 lnvsmsaamaglnthtsavpqtavkqfqgmppctytmpsqflPQQATYFPPSPPSSEPGSPDRQAEMLQNLTPPPSYAAT 240
Cdd:cd21579  193 ------------------------------------------QQQPTYLPPSPPNSEPGSPDRQKELLHNLSPPPSYAAS 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 124263658 241 IASKLAIHNPNLP----TTLPVNSQNIQPVRYNRRSNPDLEKR 279
Cdd:cd21579  231 IASKLAGQTPGLPppgvGPLSPGQAQSAPVRYNRRNNPDLEKR 273
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 342-364 1.16e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.82  E-value: 1.16e-04
                          10        20
                  ....*....|....*....|...
gi 124263658  342 FQCGVCNRSFSRSDHLALHMKRH 364
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
328-353 5.02e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 5.02e-04
                          10        20
                  ....*....|....*....|....*.
gi 124263658  328 ELTRHYRKHTGAKPFQCGVCNRSFSR 353
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
268-342 1.29e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 1.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124263658 268 YNRRSNPDLEKRRIHYCdyPGCTKVYTKSSHLKAHLRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPF 342
Cdd:COG5048   20 PKSTLKSLSNAPRPDSC--PNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSD 92
zf-H2C2_2 pfam13465
Zinc-finger double domain;
298-325 2.12e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 2.12e-03
                          10        20
                  ....*....|....*....|....*...
gi 124263658  298 HLKAHLRTHTGEKPYKCtwEGCDWRFAR 325
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKC--PECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
240-360 2.91e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.29  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658 240 TIASKLAIHNPNLPTTLPVNSQNIQPVRYNRRSNPDLEKRRIHYCDYPGCTKVYTKSSHLKAHLRTHTGEKPYKCTWEGC 319
Cdd:COG5048  345 LHTSISPAKEKLLNSSSKFSPLLNNEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPC 424

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 124263658 320 DWRFARSDELTRHYRKHTGAKPFQCgVCNRSFSRSDHLALH 360
Cdd:COG5048  425 SKSFNRHYNLIPHKKIHTNHAPLLC-SILKSFRRDLDLSNH 464
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 312-336 6.75e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 6.75e-03
                          10        20
                  ....*....|....*....|....*
gi 124263658  312 YKCTweGCDWRFARSDELTRHYRKH 336
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 269-362 9.65e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 37.78  E-value: 9.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124263658 269 NRRSNPDLEKRRIHYCDYPGcTKVYTKsshlkahlrthtGEKPYKCTWEGCDWRFARSDELTRHyRKH------------ 336
Cdd:COG5189  320 NSSSNGKLAHGGERNIDTPS-RMLKVK------------DGKPYKCPVEGCNKKYKNQNGLKYH-MLHghqnqklhenps 385

                         90       100       110
                 ....*....|....*....|....*....|....
gi 124263658 337 --------TGAKPFQCGVCNRSFSRSDHLALHMK 362
Cdd:COG5189  386 pekmnifsAKDKPYRCEVCDKRYKNLNGLKYHRK 419
 
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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