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Conserved domains on  [gi|241666446|ref|NP_001155894|]
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protein C-ets-1 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ets1_N_flank super family cl44939
Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of ...
 26-118 4.64e-54

Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of transcription factors in which the DNA-binding activity is in an autoinhibited state. The autoinhibition of Ets1 is mediated by structural coupling of the regions flanking the Ets domain. The inhibitory regions are folded as helices HI1 and HI2 N-terminal to the ETS domain and as H4 C-terminal to the ETS domain, which are packed together to form an inhibitory module. This domain represents the N-terminal flanking region of Ets domain which contains the residues forming HI1 and HI2 helices and additional residues(244-301) N-terminal to HI1. HI1 and HI2 exert the autoinhibitory function by directing the inhibitory residues N-terminal to HI1 to mask the Ets domain DNA-binding surface. These residues are flexible and function by masking the DNA-binding surface of the Ets domain. Phosphorylation of serine residues present in this region enhances autoinhibition dramatically. These inhibitory sequences are required for cooperative DNA binding.


The actual alignment was detected with superfamily member pfam19525:

Pssm-ID: 466113  Cd Length: 188  Bit Score: 171.71  E-value: 4.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241666446   26 SPGKLGGQDSFESIESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVI 105
Cdd:pfam19525  96 SRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFQSLQRVPSYDSFDSEDYPAALPSHKPKGTFKDYVRDRADLNKDKPVI 175

                          90
                  ....*....|...
gi 241666446  106 PAAALAGYTGSGP 118
Cdd:pfam19525 176 PAAALAGYTGRMM 188
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
 118-202 1.24e-49

erythroblast transformation specific domain; variation of the helix-turn-helix motif


:

Pssm-ID: 197710  Cd Length: 87  Bit Score: 156.66  E-value: 1.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241666446   118 PIQLWQFLLELLTDKSCQSFISWTG-DGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVY 196
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDrDEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80


                   ....*.
gi 241666446   197 RFVCDL 202
Cdd:smart00413  81 KFVKNP 86
 
Name Accession Description Interval E-value
Ets1_N_flank pfam19525
Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of ...
 26-118 4.64e-54

Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of transcription factors in which the DNA-binding activity is in an autoinhibited state. The autoinhibition of Ets1 is mediated by structural coupling of the regions flanking the Ets domain. The inhibitory regions are folded as helices HI1 and HI2 N-terminal to the ETS domain and as H4 C-terminal to the ETS domain, which are packed together to form an inhibitory module. This domain represents the N-terminal flanking region of Ets domain which contains the residues forming HI1 and HI2 helices and additional residues(244-301) N-terminal to HI1. HI1 and HI2 exert the autoinhibitory function by directing the inhibitory residues N-terminal to HI1 to mask the Ets domain DNA-binding surface. These residues are flexible and function by masking the DNA-binding surface of the Ets domain. Phosphorylation of serine residues present in this region enhances autoinhibition dramatically. These inhibitory sequences are required for cooperative DNA binding.


Pssm-ID: 466113  Cd Length: 188  Bit Score: 171.71  E-value: 4.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241666446   26 SPGKLGGQDSFESIESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVI 105
Cdd:pfam19525  96 SRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFQSLQRVPSYDSFDSEDYPAALPSHKPKGTFKDYVRDRADLNKDKPVI 175

                          90
                  ....*....|...
gi 241666446  106 PAAALAGYTGSGP 118
Cdd:pfam19525 176 PAAALAGYTGRMM 188
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
 118-202 1.24e-49

erythroblast transformation specific domain; variation of the helix-turn-helix motif


Pssm-ID: 197710  Cd Length: 87  Bit Score: 156.66  E-value: 1.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241666446   118 PIQLWQFLLELLTDKSCQSFISWTG-DGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVY 196
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDrDEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80


                   ....*.
gi 241666446   197 RFVCDL 202
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
120-198 4.25e-46

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 147.64  E-value: 4.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241666446  120 QLWQFLLELLTDKSCQSFISWT-GDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRF 198
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTdKEEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
 
Name Accession Description Interval E-value
Ets1_N_flank pfam19525
Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of ...
 26-118 4.64e-54

Ets1 N-terminal flanking region of Ets domain; Ets1 is a member of the Ets family of transcription factors in which the DNA-binding activity is in an autoinhibited state. The autoinhibition of Ets1 is mediated by structural coupling of the regions flanking the Ets domain. The inhibitory regions are folded as helices HI1 and HI2 N-terminal to the ETS domain and as H4 C-terminal to the ETS domain, which are packed together to form an inhibitory module. This domain represents the N-terminal flanking region of Ets domain which contains the residues forming HI1 and HI2 helices and additional residues(244-301) N-terminal to HI1. HI1 and HI2 exert the autoinhibitory function by directing the inhibitory residues N-terminal to HI1 to mask the Ets domain DNA-binding surface. These residues are flexible and function by masking the DNA-binding surface of the Ets domain. Phosphorylation of serine residues present in this region enhances autoinhibition dramatically. These inhibitory sequences are required for cooperative DNA binding.


Pssm-ID: 466113  Cd Length: 188  Bit Score: 171.71  E-value: 4.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241666446   26 SPGKLGGQDSFESIESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVI 105
Cdd:pfam19525  96 SRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFQSLQRVPSYDSFDSEDYPAALPSHKPKGTFKDYVRDRADLNKDKPVI 175

                          90
                  ....*....|...
gi 241666446  106 PAAALAGYTGSGP 118
Cdd:pfam19525 176 PAAALAGYTGRMM 188
ETS smart00413
erythroblast transformation specific domain; variation of the helix-turn-helix motif
 118-202 1.24e-49

erythroblast transformation specific domain; variation of the helix-turn-helix motif


Pssm-ID: 197710  Cd Length: 87  Bit Score: 156.66  E-value: 1.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241666446   118 PIQLWQFLLELLTDKSCQSFISWTG-DGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVY 196
Cdd:smart00413   1 GIQLWQFLLDLLLDPENSDIIKWTDrDEGEFKLVDPEEVARLWGQRKNKPNMNYEKLSRALRYYYKKNILEKVPGKRLVY 80


                   ....*.
gi 241666446   197 RFVCDL 202
Cdd:smart00413  81 KFVKNP 86
Ets pfam00178
Ets-domain;
120-198 4.25e-46

Ets-domain;


Pssm-ID: 459700  Cd Length: 80  Bit Score: 147.64  E-value: 4.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241666446  120 QLWQFLLELLTDKSCQSFISWT-GDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRF 198
Cdd:pfam00178   1 QLWQFLLDLLTDPEYSDIIKWTdKEEGEFRLVDPEAVARLWGKRKGNPKMTYEKLSRALRYYYKKGILEKVPGKRLTYRF 80
 
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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