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Conserved domains on  [gi|1720353643|ref|XP_030102994|]
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protein enabled homolog isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 36-143 1.48e-72

Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: Vasodilator-stimulated phosphoprotein (VASP), enabled gene product from Drosophila (Ena), mammalian enabled (Mena) and Ena/VASP-Like protein (EVL) localize to focal adhesions and to sites of actin filament dynamics. These proteins share a common modular organization with a highly conserved N- and C-terminal domains, termed Ena/VASP homology domains 1 and 2 (EVH1 and EVH2), that are separated by a central proline-rich domain. The EVH1 domain binds to other proteins at proline rich sequences. The majority of Ena-VASP type EVH1 domains recognize FPPPP motifs such as in the focal adhesion proteins zyxin and vinculin, and the ActA surface protein of Listeria monocytogenes, however the LIM3 domain of Tes lacks the FPPPP motif but still binds the EVH1 domain of Mena. It has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains. EVH2 mediates oligomerization within the family. The proline-rich region binds SH3 and WW domains as well as profilin, a protein that regulates actin filament dynamics. 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: 269918  Cd Length: 108  Bit Score: 232.97  E-value: 1.48e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  36 SICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDAR 115
Cdd:cd01207     1 SVASARASVMVYDDENKRWVPSGGSQGLSRVQIYHNTRNNTFRVVGRKLQDHEVVINCAILKGLKYNQATPTFHQWRDAR 80

                          90       100
                  ....*....|....*....|....*...
gi 1720353643 116 QVYGLNFGSKEDANVFASAMMHALEVLN 143
Cdd:cd01207    81 QVYGLNFASKEEATEFAQAMLLALERLN 108
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 822-856 8.43e-15

VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This region corresponds to the tetramerization domain which forms a right handed alpha helical coiled coil structure.


:

Pssm-ID: 462599  Cd Length: 35  Bit Score: 68.83  E-value: 8.43e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720353643 822 LDYDRLKQDILDEMRKELAKLKEELIDAIRQELSK 856
Cdd:pfam08776   1 SDLERLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
WH2_hVASP-like cd22185
Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human ...
 654-680 1.09e-07

Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human Vasodilator-stimulated phosphoprotein and related proteins; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of Ena/VASP family members including Protein enabled homolog (also known as Mena, mammalian enabled), VASP (vasodilator-stimulated phosphoprotein) and EVL (Ena-VASP-like or Enabled VASP or Ena/VASP). These are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells, platelet activation and cell migration. Ena/VASP proteins processively elongate F-actin barbed ends, promoting dissociation of barbed end assembly antagonists (uncapping). WH2 domains are small, widespread intrinsically disordered actin-binding peptides displaying significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. WH2 domains are identified by a central consensus actin-binding motif LKKT/V flanked by variable N-terminal and C-terminal extensions.


:

Pssm-ID: 409225  Cd Length: 27  Bit Score: 48.44  E-value: 1.09e-07
                          10        20
                  ....*....|....*....|....*..
gi 1720353643 654 DNRPLTGLAAAIAGAKLRKVSRVEDGS 680
Cdd:cd22185     1 GGSGAPGLAAAIAGAKLRKVSKQEEAS 27
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 356-576 1.88e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  356 AATRFATSLGSAFHPVLPHYATVPRPLNKNSRPSSPvntPSSQPPAAKSCAWPTSNFSPLPPSPpimiSSPPGKATGPRP 435
Cdd:PHA03247  2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAA 2816

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  436 VLPVcVSSPVPQMPPSPTA-------PNGSLDSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPPPLPPPPLPPLASLSHC 508
Cdd:PHA03247  2817 ALPP-AASPAGPLPPPTSAqptapppPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRST 2895

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720353643  509 GSQASPPPGTPLASTPSSKPSVLPSPSAAAPASAETPLNPElgdsSASEPGLQAASQPAESPTPQGLV 576
Cdd:PHA03247  2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP----PRPQPPLAPTTDPAGAGEPSGAV 2959
 
Name Accession Description Interval E-value
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 36-143 1.48e-72

Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: Vasodilator-stimulated phosphoprotein (VASP), enabled gene product from Drosophila (Ena), mammalian enabled (Mena) and Ena/VASP-Like protein (EVL) localize to focal adhesions and to sites of actin filament dynamics. These proteins share a common modular organization with a highly conserved N- and C-terminal domains, termed Ena/VASP homology domains 1 and 2 (EVH1 and EVH2), that are separated by a central proline-rich domain. The EVH1 domain binds to other proteins at proline rich sequences. The majority of Ena-VASP type EVH1 domains recognize FPPPP motifs such as in the focal adhesion proteins zyxin and vinculin, and the ActA surface protein of Listeria monocytogenes, however the LIM3 domain of Tes lacks the FPPPP motif but still binds the EVH1 domain of Mena. It has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains. EVH2 mediates oligomerization within the family. The proline-rich region binds SH3 and WW domains as well as profilin, a protein that regulates actin filament dynamics. 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: 269918  Cd Length: 108  Bit Score: 232.97  E-value: 1.48e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  36 SICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDAR 115
Cdd:cd01207     1 SVASARASVMVYDDENKRWVPSGGSQGLSRVQIYHNTRNNTFRVVGRKLQDHEVVINCAILKGLKYNQATPTFHQWRDAR 80

                          90       100
                  ....*....|....*....|....*...
gi 1720353643 116 QVYGLNFGSKEDANVFASAMMHALEVLN 143
Cdd:cd01207    81 QVYGLNFASKEEATEFAQAMLLALERLN 108
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 35-139 9.63e-45

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: 156.46  E-value: 9.63e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  35 QSICQARAAVMVYDDANKK-WVPAGGstgFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRD 113
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRhWIKAKH---SGVVCFVKDSPQNSYFIRLVDIQDGKVIWNQEIYPNMEYNQARPFFHTFAD 85

                          90       100
                  ....*....|....*....|....*.
gi 1720353643 114 ARQVYGLNFGSKEDANVFASAMMHAL 139
Cdd:pfam00568  86 SRCVYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 33-139 1.98e-38

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: 138.26  E-value: 1.98e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643   33 SEQSICQARAAVMVYDDANKKWVPAGGStGFSRVHIYHHTGNNTFRVVGRKIQDhQVVINCAIPKGLKYNQATQTFHQWR 112
Cdd:smart00461   2 GSQCIILARAVVQLYDADTKKWVPTGEG-GAANLVIDKNQRSYFFRIVGIKGQD-KVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 1720353643  113 DARQVYGLNFGSKEDANVFASAMMHAL 139
Cdd:smart00461  80 DDKCVYGLNFASEEEAKKFRKKVLKAL 106
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 822-856 8.43e-15

VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This region corresponds to the tetramerization domain which forms a right handed alpha helical coiled coil structure.


Pssm-ID: 462599  Cd Length: 35  Bit Score: 68.83  E-value: 8.43e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720353643 822 LDYDRLKQDILDEMRKELAKLKEELIDAIRQELSK 856
Cdd:pfam08776   1 SDLERLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
WH2_hVASP-like cd22185
Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human ...
 654-680 1.09e-07

Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human Vasodilator-stimulated phosphoprotein and related proteins; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of Ena/VASP family members including Protein enabled homolog (also known as Mena, mammalian enabled), VASP (vasodilator-stimulated phosphoprotein) and EVL (Ena-VASP-like or Enabled VASP or Ena/VASP). These are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells, platelet activation and cell migration. Ena/VASP proteins processively elongate F-actin barbed ends, promoting dissociation of barbed end assembly antagonists (uncapping). WH2 domains are small, widespread intrinsically disordered actin-binding peptides displaying significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. WH2 domains are identified by a central consensus actin-binding motif LKKT/V flanked by variable N-terminal and C-terminal extensions.


Pssm-ID: 409225  Cd Length: 27  Bit Score: 48.44  E-value: 1.09e-07
                          10        20
                  ....*....|....*....|....*..
gi 1720353643 654 DNRPLTGLAAAIAGAKLRKVSRVEDGS 680
Cdd:cd22185     1 GGSGAPGLAAAIAGAKLRKVSKQEEAS 27
PHA03247 PHA03247
large tegument protein UL36; Provisional
 356-576 1.88e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  356 AATRFATSLGSAFHPVLPHYATVPRPLNKNSRPSSPvntPSSQPPAAKSCAWPTSNFSPLPPSPpimiSSPPGKATGPRP 435
Cdd:PHA03247  2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAA 2816

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  436 VLPVcVSSPVPQMPPSPTA-------PNGSLDSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPPPLPPPPLPPLASLSHC 508
Cdd:PHA03247  2817 ALPP-AASPAGPLPPPTSAqptapppPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRST 2895

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720353643  509 GSQASPPPGTPLASTPSSKPSVLPSPSAAAPASAETPLNPElgdsSASEPGLQAASQPAESPTPQGLV 576
Cdd:PHA03247  2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP----PRPQPPLAPTTDPAGAGEPSGAV 2959
 
Name Accession Description Interval E-value
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 36-143 1.48e-72

Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: Vasodilator-stimulated phosphoprotein (VASP), enabled gene product from Drosophila (Ena), mammalian enabled (Mena) and Ena/VASP-Like protein (EVL) localize to focal adhesions and to sites of actin filament dynamics. These proteins share a common modular organization with a highly conserved N- and C-terminal domains, termed Ena/VASP homology domains 1 and 2 (EVH1 and EVH2), that are separated by a central proline-rich domain. The EVH1 domain binds to other proteins at proline rich sequences. The majority of Ena-VASP type EVH1 domains recognize FPPPP motifs such as in the focal adhesion proteins zyxin and vinculin, and the ActA surface protein of Listeria monocytogenes, however the LIM3 domain of Tes lacks the FPPPP motif but still binds the EVH1 domain of Mena. It has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains. EVH2 mediates oligomerization within the family. The proline-rich region binds SH3 and WW domains as well as profilin, a protein that regulates actin filament dynamics. 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: 269918  Cd Length: 108  Bit Score: 232.97  E-value: 1.48e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  36 SICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDAR 115
Cdd:cd01207     1 SVASARASVMVYDDENKRWVPSGGSQGLSRVQIYHNTRNNTFRVVGRKLQDHEVVINCAILKGLKYNQATPTFHQWRDAR 80

                          90       100
                  ....*....|....*....|....*...
gi 1720353643 116 QVYGLNFGSKEDANVFASAMMHALEVLN 143
Cdd:cd01207    81 QVYGLNFASKEEATEFAQAMLLALERLN 108
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 36-139 7.60e-53

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: 178.81  E-value: 7.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  36 SICQARAAVMVYDDANKKWVPAGGsTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDAR 115
Cdd:cd00837     1 SIFSARAHVMQIDDSNKNWVPAGG-KGASRVSYFKDTTRNSFRIIGVDIKDKKVVINCTITKNLVYNKATQTFHQWADDR 79

                          90       100
                  ....*....|....*....|....
gi 1720353643 116 QVYGLNFGSKEDANVFASAMMHAL 139
Cdd:cd00837    80 TVFGLNFASEEDATKFAEAVQEAL 103
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 35-139 9.63e-45

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: 156.46  E-value: 9.63e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  35 QSICQARAAVMVYDDANKK-WVPAGGstgFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRD 113
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRhWIKAKH---SGVVCFVKDSPQNSYFIRLVDIQDGKVIWNQEIYPNMEYNQARPFFHTFAD 85

                          90       100
                  ....*....|....*....|....*.
gi 1720353643 114 ARQVYGLNFGSKEDANVFASAMMHAL 139
Cdd:pfam00568  86 SRCVYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 33-139 1.98e-38

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: 138.26  E-value: 1.98e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643   33 SEQSICQARAAVMVYDDANKKWVPAGGStGFSRVHIYHHTGNNTFRVVGRKIQDhQVVINCAIPKGLKYNQATQTFHQWR 112
Cdd:smart00461   2 GSQCIILARAVVQLYDADTKKWVPTGEG-GAANLVIDKNQRSYFFRIVGIKGQD-KVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 1720353643  113 DARQVYGLNFGSKEDANVFASAMMHAL 139
Cdd:smart00461  80 DDKCVYGLNFASEEEAKKFRKKVLKAL 106
EVH1_SPRED-like cd10574
Sprouty-related EVH1 domain-containing-like proteins EVH1 domain; The Spred family has the ...
 36-142 3.49e-23

Sprouty-related EVH1 domain-containing-like proteins EVH1 domain; The Spred family has the following domains: an N-terminal EVH1 domain, a unique KBD (c-Kit kinase binding) domain which that is phosphorylated by the stem cell factor receptor c-Kit, and a C-terminal cysteine-rich SPR (Sprouty-related) domain which is involved in membrane localization. There are 3 Spred proteins: Spred1 which interacts with both Ras and Raf through its SPR domain; Spred2 which is the most abundant isoform; and Spred3 which has a non-functional KBD and maintains the inhibitory action on Raf. Legius syndrome is caused by heterozygous mutations in Spred1. Both EVH1 and SPR domains are involved in the inhibition of the MAP kinase pathway by Spred proteins. The specific function of the Spred2 EVH1 domain is unknown and there are no known interacting proteins to date. It is thought that its EVH1 domain will have a fourth distinct peptide binding mechanism within the EVH1 family. 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: 269978  Cd Length: 113  Bit Score: 95.08  E-value: 3.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  36 SICQARAAVMVYDDANKKWVPAGGStGFSRVHIY-----HHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQ 110
Cdd:cd10574     1 CLVRVRAVVMTRDDSSGGWLPLGGG-GLSIVSVCkvmpeEGAPRTEYVIHGERIRDKTVVLECTLRKDLVYNKVMPTFHH 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720353643 111 WRDARQVYGLNFGSKEDANVFASAMMHALEVL 142
Cdd:cd10574    80 WRIGEKKFGLTFQSPADARAFDRGVRRALEDL 111
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 34-140 1.10e-15

Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. 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: 269917  Cd Length: 109  Bit Score: 73.54  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  34 EQSICQARAAVMVYDDANKK-WVPAggSTGFSRVHIYHHTGNNTFRVVGrkIQDHQVVINCAIPKGLKYNQATQTFHQWR 112
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKsWIPA--SKQAVTVSFFYDSTRNTYRIIS--VEGSKAIINSTITPNMTFTKTSQKFGQWA 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1720353643 113 DARQ--VYGLNFGSKEDANVFASAMMHALE 140
Cdd:cd01206    77 DSRAntVYGLGFASEAELTKFAEKFQEAKE 106
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 822-856 8.43e-15

VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This region corresponds to the tetramerization domain which forms a right handed alpha helical coiled coil structure.


Pssm-ID: 462599  Cd Length: 35  Bit Score: 68.83  E-value: 8.43e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720353643 822 LDYDRLKQDILDEMRKELAKLKEELIDAIRQELSK 856
Cdd:pfam08776   1 SDLERLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
WH2_hVASP-like cd22185
Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human ...
 654-680 1.09e-07

Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human Vasodilator-stimulated phosphoprotein and related proteins; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of Ena/VASP family members including Protein enabled homolog (also known as Mena, mammalian enabled), VASP (vasodilator-stimulated phosphoprotein) and EVL (Ena-VASP-like or Enabled VASP or Ena/VASP). These are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells, platelet activation and cell migration. Ena/VASP proteins processively elongate F-actin barbed ends, promoting dissociation of barbed end assembly antagonists (uncapping). WH2 domains are small, widespread intrinsically disordered actin-binding peptides displaying significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. WH2 domains are identified by a central consensus actin-binding motif LKKT/V flanked by variable N-terminal and C-terminal extensions.


Pssm-ID: 409225  Cd Length: 27  Bit Score: 48.44  E-value: 1.09e-07
                          10        20
                  ....*....|....*....|....*..
gi 1720353643 654 DNRPLTGLAAAIAGAKLRKVSRVEDGS 680
Cdd:cd22185     1 GGSGAPGLAAAIAGAKLRKVSKQEEAS 27
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 38-135 1.30e-06

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


Pssm-ID: 275390  Cd Length: 89  Bit Score: 47.01  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  38 CQARAAVMVYDDankkwvpagGSTGFSRVHIYHHtgnntfRVVGRKIQDHQVVINCAIPKGLKYNQATQT----FHQWR- 112
Cdd:cd00900     1 LKFRAVRVYREP---------TKRVEGTLYITSD------RLILRDKNDGGLELSIPISDIVNVNVSPQGpssrYLVLVl 65

                          90       100
                  ....*....|....*....|....
gi 1720353643 113 -DARQVYGLNFGSKEDANVFASAM 135
Cdd:cd00900    66 kDRGEFVGFSFPKEEDAIEISDAL 89
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 39-139 1.10e-04

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBP2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The RanBD proteins of the nuclear pore complex (NPC): nucleoporin 1 (NUP1), NUP2, NUP61, and Nuclear Pore complex Protein 9 (npp-9) are present in the parent, but specific models were not made due to lineage. To date there been no reports of inositol phosphate or phosphoinositide binding by Ran-binding proteins.


Pssm-ID: 269907 [Multi-domain]  Cd Length: 118  Bit Score: 42.58  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  39 QARAAVMVYDDANKKWVpaggSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWR------ 112
Cdd:cd00835    11 EKRAKLFRFDKETKEWK----ERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWVwtamdd 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720353643 113 -----DARQVYGLNFGSKEDANVFASAMMHAL 139
Cdd:cd00835    87 sedgeGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
PHA03247 PHA03247
large tegument protein UL36; Provisional
 356-576 1.88e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  356 AATRFATSLGSAFHPVLPHYATVPRPLNKNSRPSSPvntPSSQPPAAKSCAWPTSNFSPLPPSPpimiSSPPGKATGPRP 435
Cdd:PHA03247  2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAA 2816

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  436 VLPVcVSSPVPQMPPSPTA-------PNGSLDSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPPPLPPPPLPPLASLSHC 508
Cdd:PHA03247  2817 ALPP-AASPAGPLPPPTSAqptapppPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRST 2895

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720353643  509 GSQASPPPGTPLASTPSSKPSVLPSPSAAAPASAETPLNPElgdsSASEPGLQAASQPAESPTPQGLV 576
Cdd:PHA03247  2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP----PRPQPPLAPTTDPAGAGEPSGAV 2959
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 41-100 2.00e-04

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269995  Cd Length: 118  Bit Score: 41.62  E-value: 2.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  41 RAAVMVYDDANKKWVPAGgsTGfsRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLK 100
Cdd:cd13174    13 RAKLYRFDADTKEWKERG--VG--EMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQ 68
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 393-572 8.66e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.99  E-value: 8.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643 393 NTPSSQPPAAKSCAW------PTSNFSPLPPSPPIMISSPPGKATGPRPVLPVCV-------SSPVPQMPPSPTAPNGSL 459
Cdd:PLN03209  322 KIPSQRVPPKESDAAdgpkpvPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAyedlkppTSPIPTPPSSSPASSKSV 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643 460 DSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPPPLPPPPLPPLASLSHcGSQASPPPGTPLASTPSSKPSV-LPSPSAAA 538
Cdd:PLN03209  402 DAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKP-PTSPSPTAPTGVSPSVSSTSSVpAVPDTAPA 480

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720353643 539 PASAETPLNPELGDSSASEPGLQAASQPAESPTP 572
Cdd:PLN03209  481 TAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSP 514
PHA03247 PHA03247
large tegument protein UL36; Provisional
 318-572 2.48e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  318 PPSYakviSAPVSDATPDYAVVTALPPTSTPPTPPLRHAATRFATSLGSAFHPVLPHYATVPR-------PLNKNSRPSS 390
Cdd:PHA03247  2628 PPSP----SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRaarptvgSLTSLADPPP 2703

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  391 PVNTPSSQP------------PAAKSCAWPTSNFSPLPPSPPIMISSPPGKATGPRPvlpvcvssPVPQMPPSPTAPNGs 458
Cdd:PHA03247  2704 PPPTPEPAPhalvsatplppgPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP--------PTTAGPPAPAPPAA- 2774

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643  459 ldsvtyPVSPPPTSGPAAPPPPPPPPPPPPPPPPPLPPPPLPPLASLSHCGSQASPPPGTPLASTPSSKPSVLPSPSAAA 538
Cdd:PHA03247  2775 ------PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1720353643  539 PASAETPLNPElGDSSASEPGLQAASQPAESPTP 572
Cdd:PHA03247  2849 SLPLGGSVAPG-GDVRRRPPSRSPAAKPAAPARP 2881
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 33-138 2.86e-03

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase).


Pssm-ID: 197549  Cd Length: 130  Bit Score: 38.52  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720353643   33 SEQSICQARAAVMVYDDANKKWVPAGgsTGFSRVhIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWR 112
Cdd:smart00160  18 DEEVIFSARAKLYRFANDKKEWKERG--VGDLKI-LKSKDNGGKVRIVMRRDGVLKVCANHPIFKSMTLKPLAGSNRALK 94

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1720353643  113 DARQVYG----------LNFGSKEDANVFASAMMHA 138
Cdd:smart00160  95 WTPEDFAddipklvlyaVRFKTKEEADSFKNIFEEA 130
 
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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