Cytoplasmic Fragile-X interacting family; This entry includes Cytoplasmic fragile X mental ...
389-500
2.69e-56
Cytoplasmic Fragile-X interacting family; This entry includes Cytoplasmic fragile X mental retardation interacting proteins 1/2 (CYFIP1/2) from humans and their homologs, such as Sra-1 (specifically Rac1-associated protein 1) from Drosophila and PIROGI from Arabidopsis. CYFIP1/2 interact with FMRP (fragile X mental retardation protein) which is responsible for pathologic manifestations in the Fragile X Syndrome. CYFIP1 interacts with the small GTPase Rac1. CYFIP1 represses cap-dependent translation of mRNA by interacting with the initiation factor eIF4E. CYFIP1 and CYFIP2 are part of the Wiskott-Aldrich syndrome protein-family verprolin-homologous protein (WAVE) complex that regulates actin polymerization at synapses. Drosophila Sra-1 interacts with the Kette and Wasp. It is required for neuronal and bristle development in Drosophila. PIROGI is part of a WAVE complex that activates the ARP2/3 complex and is Involved in regulation of actin organization.
The actual alignment was detected with superfamily member pfam05994:
Pssm-ID: 461799 Cd Length: 842 Bit Score: 201.36 E-value: 2.69e-56
Cytoplasmic Fragile-X interacting family; This entry includes Cytoplasmic fragile X mental ...
389-500
2.69e-56
Cytoplasmic Fragile-X interacting family; This entry includes Cytoplasmic fragile X mental retardation interacting proteins 1/2 (CYFIP1/2) from humans and their homologs, such as Sra-1 (specifically Rac1-associated protein 1) from Drosophila and PIROGI from Arabidopsis. CYFIP1/2 interact with FMRP (fragile X mental retardation protein) which is responsible for pathologic manifestations in the Fragile X Syndrome. CYFIP1 interacts with the small GTPase Rac1. CYFIP1 represses cap-dependent translation of mRNA by interacting with the initiation factor eIF4E. CYFIP1 and CYFIP2 are part of the Wiskott-Aldrich syndrome protein-family verprolin-homologous protein (WAVE) complex that regulates actin polymerization at synapses. Drosophila Sra-1 interacts with the Kette and Wasp. It is required for neuronal and bristle development in Drosophila. PIROGI is part of a WAVE complex that activates the ARP2/3 complex and is Involved in regulation of actin organization.
Pssm-ID: 461799 Cd Length: 842 Bit Score: 201.36 E-value: 2.69e-56
Cytoplasmic Fragile-X interacting family; This entry includes Cytoplasmic fragile X mental ...
389-500
2.69e-56
Cytoplasmic Fragile-X interacting family; This entry includes Cytoplasmic fragile X mental retardation interacting proteins 1/2 (CYFIP1/2) from humans and their homologs, such as Sra-1 (specifically Rac1-associated protein 1) from Drosophila and PIROGI from Arabidopsis. CYFIP1/2 interact with FMRP (fragile X mental retardation protein) which is responsible for pathologic manifestations in the Fragile X Syndrome. CYFIP1 interacts with the small GTPase Rac1. CYFIP1 represses cap-dependent translation of mRNA by interacting with the initiation factor eIF4E. CYFIP1 and CYFIP2 are part of the Wiskott-Aldrich syndrome protein-family verprolin-homologous protein (WAVE) complex that regulates actin polymerization at synapses. Drosophila Sra-1 interacts with the Kette and Wasp. It is required for neuronal and bristle development in Drosophila. PIROGI is part of a WAVE complex that activates the ARP2/3 complex and is Involved in regulation of actin organization.
Pssm-ID: 461799 Cd Length: 842 Bit Score: 201.36 E-value: 2.69e-56
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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