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Conserved domains on  [gi|1585518102|gb|TBU28470|]
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hypothetical protein BD311DRAFT_663345 [Dichomitus squalens]

Protein Classification

Wiskott-Aldrich syndrome protein( domain architecture ID 10100414)

Wiskott-Aldrich syndrome protein (WASp) acts as an effector protein for Rho-type GTPases that regulates actin filament reorganization via its interaction with the Arp2/3 complex

Gene Ontology:  GO:0003779|GO:0031267|GO:0030695|GO:0030048|GO:2000601
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 ...
 26-126 2.89e-57

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: 181.19  E-value: 2.89e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585518102  26 ILTAALARIYYAHPNPNEWSYTGLQGALAFVRD-QQGVYNLKLVDLTgTRGIIWEHELYEGFEYFQDRPFFHSFAGDECM 104
Cdd:cd01205     1 ILAAAVARLYYAEPDPDSWSYTGLTGALCFVKDnAKRSYFFRLVDLK-TRGVVWEQELYEGFEYNQDRPFFHTFEGDECM 79

                          90       100
                  ....*....|....*....|..
gi 1585518102 105 IGIVFSDESEAKTFNKKVTTRK 126
Cdd:cd01205    80 IGLNFADEDEAAAFYKKVQEKL 101
CRIB super family cl00113
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 153-207 8.06e-07

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. CRIB-containing effector proteins are functionally diverse and include serine/threonine kinases, tyrosine kinases, actin-binding proteins, and adapter molecules.


The actual alignment was detected with superfamily member pfam00786:

Pssm-ID: 412170  Cd Length: 59  Bit Score: 45.77  E-value: 8.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1585518102 153 MISGPTagSFKHVAHMGYDSEKGFtSTNVDPSWEAFLSnleGQGVSREVLEQNMD 207
Cdd:pfam00786   1 MISAPT--NFKHTVHVGFDPDTGF-FTGLPPEWAKLLD---SSGITEDEQKENPK 49
 
Name Accession Description Interval E-value
EVH1_WASP-like cd01205
WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called ...
 26-126 2.89e-57

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: 181.19  E-value: 2.89e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585518102  26 ILTAALARIYYAHPNPNEWSYTGLQGALAFVRD-QQGVYNLKLVDLTgTRGIIWEHELYEGFEYFQDRPFFHSFAGDECM 104
Cdd:cd01205     1 ILAAAVARLYYAEPDPDSWSYTGLTGALCFVKDnAKRSYFFRLVDLK-TRGVVWEQELYEGFEYNQDRPFFHTFEGDECM 79

                          90       100
                  ....*....|....*....|..
gi 1585518102 105 IGIVFSDESEAKTFNKKVTTRK 126
Cdd:cd01205    80 IGLNFADEDEAAAFYKKVQEKL 101
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 24-126 3.15e-25

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: 98.20  E-value: 3.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585518102   24 NKILTAALARIYYAhpNPNEWSYTGLQGALAFVRDQ-QGVYNLKLVDLTGTRGIIWEHELYEGFEYFQDRPFFHSFAGDE 102
Cdd:smart00461   5 CIILARAVVQLYDA--DTKKWVPTGEGGAANLVIDKnQRSYFFRIVGIKGQDKVIWNQELYKNFKYNQATPTFHQWADDK 82

                           90       100
                   ....*....|....*....|....
gi 1585518102  103 CMIGIVFSDESEAKTFNKKVTTRK 126
Cdd:smart00461  83 CVYGLNFASEEEAKKFRKKVLKAL 106
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 23-126 4.68e-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: 97.91  E-value: 4.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585518102  23 ANKILTAALARIYYAHPNPNE-WSYTGLQGALAFVRDQ-QGVYNLKLVDLTGtRGIIWEHELYEGFEYFQDRPFFHSFAG 100
Cdd:pfam00568   7 KCQTICTAVAQVYLADPDNKRhWIKAKHSGVVCFVKDSpQNSYFIRLVDIQD-GKVIWNQEIYPNMEYNQARPFFHTFAD 85

                          90       100
                  ....*....|....*....|....*.
gi 1585518102 101 DECMIGIVFSDESEAKTFNKKVTTRK 126
Cdd:pfam00568  86 SRCVYGLNFASEEEATKFAKAVQEAL 111
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 153-207 8.06e-07

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 45.77  E-value: 8.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1585518102 153 MISGPTagSFKHVAHMGYDSEKGFtSTNVDPSWEAFLSnleGQGVSREVLEQNMD 207
Cdd:pfam00786   1 MISAPT--NFKHTVHVGFDPDTGF-FTGLPPEWAKLLD---SSGITEDEQKENPK 49
CRIB cd00132
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 152-198 2.34e-05

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. CRIB-containing effector proteins are functionally diverse and include serine/threonine kinases, tyrosine kinases, actin-binding proteins, and adapter molecules.


Pssm-ID: 238077  Cd Length: 42  Bit Score: 40.88  E-value: 2.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1585518102 152 SMISGPTagSFKHVAHMGYDSEkGFTSTNVDPSWEaflSNLEGQGVS 198
Cdd:cd00132     1 MEISTPT--DFKHISHVGWDGV-GFDGANLPPDLQ---SLFQTAGIS 41
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 154-192 4.77e-03

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 34.49  E-value: 4.77e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1585518102  154 ISGPTagSFKHVAHMGYDSeKGFTSTNVDPSWEAFLSNL 192
Cdd:smart00285   1 ISTPT--NFKHIAHVGFDG-QTGGFTGLPTEWKSLLKTS 36
 
Name Accession Description Interval E-value
EVH1_WASP-like cd01205
WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called ...
 26-126 2.89e-57

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: 181.19  E-value: 2.89e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585518102  26 ILTAALARIYYAHPNPNEWSYTGLQGALAFVRD-QQGVYNLKLVDLTgTRGIIWEHELYEGFEYFQDRPFFHSFAGDECM 104
Cdd:cd01205     1 ILAAAVARLYYAEPDPDSWSYTGLTGALCFVKDnAKRSYFFRLVDLK-TRGVVWEQELYEGFEYNQDRPFFHTFEGDECM 79

                          90       100
                  ....*....|....*....|..
gi 1585518102 105 IGIVFSDESEAKTFNKKVTTRK 126
Cdd:cd01205    80 IGLNFADEDEAAAFYKKVQEKL 101
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 24-126 3.15e-25

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: 98.20  E-value: 3.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585518102   24 NKILTAALARIYYAhpNPNEWSYTGLQGALAFVRDQ-QGVYNLKLVDLTGTRGIIWEHELYEGFEYFQDRPFFHSFAGDE 102
Cdd:smart00461   5 CIILARAVVQLYDA--DTKKWVPTGEGGAANLVIDKnQRSYFFRIVGIKGQDKVIWNQELYKNFKYNQATPTFHQWADDK 82

                           90       100
                   ....*....|....*....|....
gi 1585518102  103 CMIGIVFSDESEAKTFNKKVTTRK 126
Cdd:smart00461  83 CVYGLNFASEEEAKKFRKKVLKAL 106
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 23-126 4.68e-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: 97.91  E-value: 4.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585518102  23 ANKILTAALARIYYAHPNPNE-WSYTGLQGALAFVRDQ-QGVYNLKLVDLTGtRGIIWEHELYEGFEYFQDRPFFHSFAG 100
Cdd:pfam00568   7 KCQTICTAVAQVYLADPDNKRhWIKAKHSGVVCFVKDSpQNSYFIRLVDIQD-GKVIWNQEIYPNMEYNQARPFFHTFAD 85

                          90       100
                  ....*....|....*....|....*.
gi 1585518102 101 DECMIGIVFSDESEAKTFNKKVTTRK 126
Cdd:pfam00568  86 SRCVYGLNFASEEEATKFAKAVQEAL 111
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 30-123 2.54e-10

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: 57.09  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585518102  30 ALARIYYAHPNPNEWSYTGLQGA--LAFVRD-QQGVYNLKLVDLTGTRgIIWEHELYEGFEYFQDRPFFHSFAGDECMIG 106
Cdd:cd00837     5 ARAHVMQIDDSNKNWVPAGGKGAsrVSYFKDtTRNSFRIIGVDIKDKK-VVINCTITKNLVYNKATQTFHQWADDRTVFG 83

                          90
                  ....*....|....*..
gi 1585518102 107 IVFSDESEAKTFNKKVT 123
Cdd:cd00837    84 LNFASEEDATKFAEAVQ 100
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 153-207 8.06e-07

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 45.77  E-value: 8.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1585518102 153 MISGPTagSFKHVAHMGYDSEKGFtSTNVDPSWEAFLSnleGQGVSREVLEQNMD 207
Cdd:pfam00786   1 MISAPT--NFKHTVHVGFDPDTGF-FTGLPPEWAKLLD---SSGITEDEQKENPK 49
CRIB cd00132
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 152-198 2.34e-05

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. CRIB-containing effector proteins are functionally diverse and include serine/threonine kinases, tyrosine kinases, actin-binding proteins, and adapter molecules.


Pssm-ID: 238077  Cd Length: 42  Bit Score: 40.88  E-value: 2.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1585518102 152 SMISGPTagSFKHVAHMGYDSEkGFTSTNVDPSWEaflSNLEGQGVS 198
Cdd:cd00132     1 MEISTPT--DFKHISHVGWDGV-GFDGANLPPDLQ---SLFQTAGIS 41
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 154-192 4.77e-03

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 34.49  E-value: 4.77e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1585518102  154 ISGPTagSFKHVAHMGYDSeKGFTSTNVDPSWEAFLSNL 192
Cdd:smart00285   1 ISTPT--NFKHIAHVGFDG-QTGGFTGLPTEWKSLLKTS 36
 
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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