Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
1013-1042
5.28e-15
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).
:
Pssm-ID: 409204 Cd Length: 30 Bit Score: 69.87 E-value: 5.28e-15
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
606-1000
6.16e-60
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.
Pssm-ID: 214697 [Multi-domain] Cd Length: 392 Bit Score: 211.44 E-value: 6.16e-60
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
1013-1042
5.28e-15
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).
Pssm-ID: 409204 Cd Length: 30 Bit Score: 69.87 E-value: 5.28e-15
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
606-1000
6.16e-60
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.
Pssm-ID: 214697 [Multi-domain] Cd Length: 392 Bit Score: 211.44 E-value: 6.16e-60
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
1013-1042
5.28e-15
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).
Pssm-ID: 409204 Cd Length: 30 Bit Score: 69.87 E-value: 5.28e-15
Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three ...
858-926
6.71e-03
Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. They are predominantly found in the enzyme alpha-mannosidase.
Pssm-ID: 462728 [Multi-domain] Cd Length: 98 Bit Score: 37.24 E-value: 6.71e-03
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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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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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