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Conserved domains on  [gi|440459721|gb|AGC06988|]
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WASP, partial [Anopheles gambiae]

Protein Classification

WASP family protein( domain architecture ID 10100405)

WASP (wiskott-Aldrich syndrome protein) family protein similar to Schizosaccharomyces pombe Wiskott-Aldrich syndrome protein homolog 1 (WSP1) that has a role in regulating actin assembly, so regulating polarized growth

Gene Ontology:  GO:0034315|GO:0003779|GO:0071933
PubMed:  9883880

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EVH1_WASP-like cd01205
WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called ...
 1-83 4.01e-37

WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called Bee1p) and its homolog N (neuronal)-WASP are signal transduction proteins that promote actin polymerization in response to upstream intracellular signals. WAS is an X-linked recessive disease, characterized by eczema, immunodeficiency, and thrombocytopenia. The majority of patients with WAS, or a milder version of the disorder, X-linked thrombocytopenia (XLT), have point mutations in the EVH1 domain of WASP. WASP is an actin regulatory protein consisting of an N-terminal EVH1 domain called WH1 which binds LPPPEP peptides, a basic region (B), a GTP binding domain (GBP), a proline rich region, a WH2 domain, and a verprolin-cofilin-acidic motif (VCA) which activates the actin-related protein (Arp)2/3 actin nucleating complex. The B, GBD, and the proline-rich region are involved in autoinhibitory interactions that repress or block the activity of the VCA. Yeast members lack the GTP binding domain. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


:

Pssm-ID: 269916  Cd Length: 101  Bit Score: 119.94  E-value: 4.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440459721   1 VQLYTTQsPAHASWVKR-CTGALCFIKDNIRKSYYFRLYCLKANQMVWEQELYEKIEVTQPKPYLITFEGQDGIVAFNFA 79
Cdd:cd01205    7 ARLYYAE-PDPDSWSYTgLTGALCFVKDNAKRSYFFRLVDLKTRGVVWEQELYEGFEYNQDRPFFHTFEGDECMIGLNFA 85


                 ....
gi 440459721  80 TEDE 83
Cdd:cd01205   86 DEDE 89
 
Name Accession Description Interval E-value
EVH1_WASP-like cd01205
WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called ...
 1-83 4.01e-37

WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called Bee1p) and its homolog N (neuronal)-WASP are signal transduction proteins that promote actin polymerization in response to upstream intracellular signals. WAS is an X-linked recessive disease, characterized by eczema, immunodeficiency, and thrombocytopenia. The majority of patients with WAS, or a milder version of the disorder, X-linked thrombocytopenia (XLT), have point mutations in the EVH1 domain of WASP. WASP is an actin regulatory protein consisting of an N-terminal EVH1 domain called WH1 which binds LPPPEP peptides, a basic region (B), a GTP binding domain (GBP), a proline rich region, a WH2 domain, and a verprolin-cofilin-acidic motif (VCA) which activates the actin-related protein (Arp)2/3 actin nucleating complex. The B, GBD, and the proline-rich region are involved in autoinhibitory interactions that repress or block the activity of the VCA. Yeast members lack the GTP binding domain. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269916  Cd Length: 101  Bit Score: 119.94  E-value: 4.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440459721   1 VQLYTTQsPAHASWVKR-CTGALCFIKDNIRKSYYFRLYCLKANQMVWEQELYEKIEVTQPKPYLITFEGQDGIVAFNFA 79
Cdd:cd01205    7 ARLYYAE-PDPDSWSYTgLTGALCFVKDNAKRSYFFRLVDLKTRGVVWEQELYEGFEYNQDRPFFHTFEGDECMIGLNFA 85


                 ....
gi 440459721  80 TEDE 83
Cdd:cd01205   86 DEDE 89
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 1-83 2.57e-25

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


Pssm-ID: 395450  Cd Length: 111  Bit Score: 90.20  E-value: 2.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440459721    1 VQLYTTQSPAHASWVK-RCTGALCFIKDNIRKSYYFRLYCLKANQMVWEQELYEKIEVTQPKPYLITFEGQDGIVAFNFA 79
Cdd:pfam00568  16 AQVYLADPDNKRHWIKaKHSGVVCFVKDSPQNSYFIRLVDIQDGKVIWNQEIYPNMEYNQARPFFHTFADSRCVYGLNFA 95


                  ....
gi 440459721   80 TEDE 83
Cdd:pfam00568  96 SEEE 99
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-83 2.73e-12

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 56.98  E-value: 2.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440459721     1 VQLYTTQSPAhasWVKRCTG-ALCFIKDNIRKSYYFRLYCLKAN-QMVWEQELYEKIEVTQPKPYLITFEGQDGIVAFNF 78
Cdd:smart00461  13 VQLYDADTKK---WVPTGEGgAANLVIDKNQRSYFFRIVGIKGQdKVIWNQELYKNFKYNQATPTFHQWADDKCVYGLNF 89


                   ....*
gi 440459721    79 ATEDE 83
Cdd:smart00461  90 ASEEE 94
 
Name Accession Description Interval E-value
EVH1_WASP-like cd01205
WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called ...
 1-83 4.01e-37

WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called Bee1p) and its homolog N (neuronal)-WASP are signal transduction proteins that promote actin polymerization in response to upstream intracellular signals. WAS is an X-linked recessive disease, characterized by eczema, immunodeficiency, and thrombocytopenia. The majority of patients with WAS, or a milder version of the disorder, X-linked thrombocytopenia (XLT), have point mutations in the EVH1 domain of WASP. WASP is an actin regulatory protein consisting of an N-terminal EVH1 domain called WH1 which binds LPPPEP peptides, a basic region (B), a GTP binding domain (GBP), a proline rich region, a WH2 domain, and a verprolin-cofilin-acidic motif (VCA) which activates the actin-related protein (Arp)2/3 actin nucleating complex. The B, GBD, and the proline-rich region are involved in autoinhibitory interactions that repress or block the activity of the VCA. Yeast members lack the GTP binding domain. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269916  Cd Length: 101  Bit Score: 119.94  E-value: 4.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440459721   1 VQLYTTQsPAHASWVKR-CTGALCFIKDNIRKSYYFRLYCLKANQMVWEQELYEKIEVTQPKPYLITFEGQDGIVAFNFA 79
Cdd:cd01205    7 ARLYYAE-PDPDSWSYTgLTGALCFVKDNAKRSYFFRLVDLKTRGVVWEQELYEGFEYNQDRPFFHTFEGDECMIGLNFA 85


                 ....
gi 440459721  80 TEDE 83
Cdd:cd01205   86 DEDE 89
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 1-83 2.57e-25

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


Pssm-ID: 395450  Cd Length: 111  Bit Score: 90.20  E-value: 2.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440459721    1 VQLYTTQSPAHASWVK-RCTGALCFIKDNIRKSYYFRLYCLKANQMVWEQELYEKIEVTQPKPYLITFEGQDGIVAFNFA 79
Cdd:pfam00568  16 AQVYLADPDNKRHWIKaKHSGVVCFVKDSPQNSYFIRLVDIQDGKVIWNQEIYPNMEYNQARPFFHTFADSRCVYGLNFA 95


                  ....
gi 440459721   80 TEDE 83
Cdd:pfam00568  96 SEEE 99
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-83 2.73e-12

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 56.98  E-value: 2.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440459721     1 VQLYTTQSPAhasWVKRCTG-ALCFIKDNIRKSYYFRLYCLKAN-QMVWEQELYEKIEVTQPKPYLITFEGQDGIVAFNF 78
Cdd:smart00461  13 VQLYDADTKK---WVPTGEGgAANLVIDKNQRSYFFRIVGIKGQdKVIWNQELYKNFKYNQATPTFHQWADDKCVYGLNF 89


                   ....*
gi 440459721    79 ATEDE 83
Cdd:smart00461  90 ASEEE 94
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 1-83 2.06e-08

EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; The EVH1 domains are part of the PH domain superfamily. EVH1 subfamilies include Enables/VASP, Homer/Vesl, WASP, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269909  Cd Length: 103  Bit Score: 47.07  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440459721   1 VQLYTtQSPAHASWVK---RCTGALCFIKDNIRKSYYFRLYCLKANQMVWEQELYEKIEVTQPKPYLITFEGQDGIVAFN 77
Cdd:cd00837    7 AHVMQ-IDDSNKNWVPaggKGASRVSYFKDTTRNSFRIIGVDIKDKKVVINCTITKNLVYNKATQTFHQWADDRTVFGLN 85


                 ....*.
gi 440459721  78 FATEDE 83
Cdd:cd00837   86 FASEED 91
 
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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