NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|134133290|ref|NP_001077039|]
View 

ERBB receptor feedback inhibitor 1a [Danio rerio]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Inhibitor_Mig-6 super family cl13070
EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen ...
324-366 5.00e-05

EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen induced gene 6 (Mig-6), EGFR becomes inactive due to the conformation it adopts which is Src/CDK like. The binding of the two proteins prevents EGFR acting as a cyclin-like activator for other kinase domains.The structure of Mig-6(1) consists of alpha helices-G and -H with a polar surface and hydrophobic residues for interactions with EGFR. A critical step for the activation of EGFR is the formation of an asymmetric dimer involving the kinase domains of the protein. Since Mig-6 binds to the kinase domain it blocks this process and EGFR becomes inactive.


The actual alignment was detected with superfamily member pfam11555:

Pssm-ID: 463294 [Multi-domain]  Cd Length: 74  Bit Score: 41.52  E-value: 5.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134133290  324 RPPKVPPREPLS-ACPRTPSPKSLPI---------YYNG--------IMPPTQSFAPDPKY 366
Cdd:pfam11555   1 RPPQIPPRDPLSqPGSRTPSPMGLVVgspqqpathSYSSylstspgkLMPTTQSFASDPKY 61
 
Name Accession Description Interval E-value
Inhibitor_Mig-6 pfam11555
EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen ...
324-366 5.00e-05

EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen induced gene 6 (Mig-6), EGFR becomes inactive due to the conformation it adopts which is Src/CDK like. The binding of the two proteins prevents EGFR acting as a cyclin-like activator for other kinase domains.The structure of Mig-6(1) consists of alpha helices-G and -H with a polar surface and hydrophobic residues for interactions with EGFR. A critical step for the activation of EGFR is the formation of an asymmetric dimer involving the kinase domains of the protein. Since Mig-6 binds to the kinase domain it blocks this process and EGFR becomes inactive.


Pssm-ID: 463294 [Multi-domain]  Cd Length: 74  Bit Score: 41.52  E-value: 5.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134133290  324 RPPKVPPREPLS-ACPRTPSPKSLPI---------YYNG--------IMPPTQSFAPDPKY 366
Cdd:pfam11555   1 RPPQIPPRDPLSqPGSRTPSPMGLVVgspqqpathSYSSylstspgkLMPTTQSFASDPKY 61
 
Name Accession Description Interval E-value
Inhibitor_Mig-6 pfam11555
EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen ...
324-366 5.00e-05

EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen induced gene 6 (Mig-6), EGFR becomes inactive due to the conformation it adopts which is Src/CDK like. The binding of the two proteins prevents EGFR acting as a cyclin-like activator for other kinase domains.The structure of Mig-6(1) consists of alpha helices-G and -H with a polar surface and hydrophobic residues for interactions with EGFR. A critical step for the activation of EGFR is the formation of an asymmetric dimer involving the kinase domains of the protein. Since Mig-6 binds to the kinase domain it blocks this process and EGFR becomes inactive.


Pssm-ID: 463294 [Multi-domain]  Cd Length: 74  Bit Score: 41.52  E-value: 5.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134133290  324 RPPKVPPREPLS-ACPRTPSPKSLPI---------YYNG--------IMPPTQSFAPDPKY 366
Cdd:pfam11555   1 RPPQIPPRDPLSqPGSRTPSPMGLVVgspqqpathSYSSylstspgkLMPTTQSFASDPKY 61
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH