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Conserved domains on  [gi|62471737|ref|NP_001014536|]
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enabled, isoform E [Drosophila melanogaster]

Protein Classification

Ena/VASP family protein( domain architecture ID 10100512)

Ena/VASP family proteins are implicated in a diverse range of signaling, nuclear transport and cytoskeletal events

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: ...
 5-112 7.53e-68

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: 217.18  E-value: 7.53e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737   5 SIIGARASVMVYDDNQKKWVPSGSSSGLSKVQIYHHQQNNTFRVVGRKLQDHEVVINCSILKGLKYNQATATFHQWRDSK 84
Cdd:cd01207   1 SVASARASVMVYDDENKRWVPSGGSQGLSRVQIYHNTRNNTFRVVGRKLQDHEVVINCAILKGLKYNQATPTFHQWRDAR 80

                        90       100
                ....*....|....*....|....*...
gi 62471737  85 FVYGLNFSSQNDAENFARAMMHALEVLS 112
Cdd:cd01207  81 QVYGLNFASKEEATEFAQAMLLALERLN 108
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 650-683 1.32e-12

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: 62.28  E-value: 1.32e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 62471737   650 DLDTLKAEIVREMRLEIQKVKNEIIDAIKSEFNR 683
Cdd:pfam08776   2 DLERLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
 
Name Accession Description Interval E-value
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 5-112 7.53e-68

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: 217.18  E-value: 7.53e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737   5 SIIGARASVMVYDDNQKKWVPSGSSSGLSKVQIYHHQQNNTFRVVGRKLQDHEVVINCSILKGLKYNQATATFHQWRDSK 84
Cdd:cd01207   1 SVASARASVMVYDDENKRWVPSGGSQGLSRVQIYHNTRNNTFRVVGRKLQDHEVVINCAILKGLKYNQATPTFHQWRDAR 80

                        90       100
                ....*....|....*....|....*...
gi 62471737  85 FVYGLNFSSQNDAENFARAMMHALEVLS 112
Cdd:cd01207  81 QVYGLNFASKEEATEFAQAMLLALERLN 108
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-108 2.71e-43

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: 151.35  E-value: 2.71e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737      1 MTEQSIIGARASVMVYDDNQKKWVPSGSSsGLSKVQIYHHQQNNTFRVVGRKLQDhEVVINCSILKGLKYNQATATFHQW 80
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKKWVPTGEG-GAANLVIDKNQRSYFFRIVGIKGQD-KVIWNQELYKNFKYNQATPTFHQW 78

                           90       100
                   ....*....|....*....|....*...
gi 62471737     81 RDSKFVYGLNFSSQNDAENFARAMMHAL 108
Cdd:smart00461  79 ADDKCVYGLNFASEEEAKKFRKKVLKAL 106
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-108 9.10e-33

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: 122.17  E-value: 9.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737     4 QSIIGARASVMVYD-DNQKKWVPSGSSSglsKVQIYHHQQNNTFRVVGRKLQDHEVVINCSILKGLKYNQATATFHQWRD 82
Cdd:pfam00568   9 QTICTAVAQVYLADpDNKRHWIKAKHSG---VVCFVKDSPQNSYFIRLVDIQDGKVIWNQEIYPNMEYNQARPFFHTFAD 85

                          90       100
                  ....*....|....*....|....*.
gi 62471737    83 SKFVYGLNFSSQNDAENFARAMMHAL 108
Cdd:pfam00568  86 SRCVYGLNFASEEEATKFAKAVQEAL 111
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 650-683 1.32e-12

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: 62.28  E-value: 1.32e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 62471737   650 DLDTLKAEIVREMRLEIQKVKNEIIDAIKSEFNR 683
Cdd:pfam08776   2 DLERLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
 
Name Accession Description Interval E-value
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 5-112 7.53e-68

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: 217.18  E-value: 7.53e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737   5 SIIGARASVMVYDDNQKKWVPSGSSSGLSKVQIYHHQQNNTFRVVGRKLQDHEVVINCSILKGLKYNQATATFHQWRDSK 84
Cdd:cd01207   1 SVASARASVMVYDDENKRWVPSGGSQGLSRVQIYHNTRNNTFRVVGRKLQDHEVVINCAILKGLKYNQATPTFHQWRDAR 80

                        90       100
                ....*....|....*....|....*...
gi 62471737  85 FVYGLNFSSQNDAENFARAMMHALEVLS 112
Cdd:cd01207  81 QVYGLNFASKEEATEFAQAMLLALERLN 108
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-108 2.71e-43

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: 151.35  E-value: 2.71e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737      1 MTEQSIIGARASVMVYDDNQKKWVPSGSSsGLSKVQIYHHQQNNTFRVVGRKLQDhEVVINCSILKGLKYNQATATFHQW 80
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKKWVPTGEG-GAANLVIDKNQRSYFFRIVGIKGQD-KVIWNQELYKNFKYNQATPTFHQW 78

                           90       100
                   ....*....|....*....|....*...
gi 62471737     81 RDSKFVYGLNFSSQNDAENFARAMMHAL 108
Cdd:smart00461  79 ADDKCVYGLNFASEEEAKKFRKKVLKAL 106
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 5-108 1.04e-41

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: 146.84  E-value: 1.04e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737   5 SIIGARASVMVYDDNQKKWVPSGSSsGLSKVQIYHHQQNNTFRVVGRKLQDHEVVINCSILKGLKYNQATATFHQWRDSK 84
Cdd:cd00837   1 SIFSARAHVMQIDDSNKNWVPAGGK-GASRVSYFKDTTRNSFRIIGVDIKDKKVVINCTITKNLVYNKATQTFHQWADDR 79

                        90       100
                ....*....|....*....|....
gi 62471737  85 FVYGLNFSSQNDAENFARAMMHAL 108
Cdd:cd00837  80 TVFGLNFASEEDATKFAEAVQEAL 103
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-108 9.10e-33

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: 122.17  E-value: 9.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737     4 QSIIGARASVMVYD-DNQKKWVPSGSSSglsKVQIYHHQQNNTFRVVGRKLQDHEVVINCSILKGLKYNQATATFHQWRD 82
Cdd:pfam00568   9 QTICTAVAQVYLADpDNKRHWIKAKHSG---VVCFVKDSPQNSYFIRLVDIQDGKVIWNQEIYPNMEYNQARPFFHTFAD 85

                          90       100
                  ....*....|....*....|....*.
gi 62471737    83 SKFVYGLNFSSQNDAENFARAMMHAL 108
Cdd:pfam00568  86 SRCVYGLNFASEEEATKFAKAVQEAL 111
EVH1_SPRED-like cd10574
Sprouty-related EVH1 domain-containing-like proteins EVH1 domain; The Spred family has the ...
 5-112 8.89e-22

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: 90.84  E-value: 8.89e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737   5 SIIGARASVMVYDDNQKKWVPSGSSsGLSKVQIYHHQQ-----NNTFRVVGRKLQDHEVVINCSILKGLKYNQATATFHQ 79
Cdd:cd10574   1 CLVRVRAVVMTRDDSSGGWLPLGGG-GLSIVSVCKVMPeegapRTEYVIHGERIRDKTVVLECTLRKDLVYNKVMPTFHH 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 62471737  80 WRDSKFVYGLNFSSQNDAENFARAMMHALEVLS 112
Cdd:cd10574  80 WRIGEKKFGLTFQSPADARAFDRGVRRALEDLS 112
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-109 5.20e-14

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: 68.53  E-value: 5.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737   3 EQSIIGARASVMVYDDNQKK-WVPSgSSSGLSkVQIYHHQQNNTFRVVGrkLQDHEVVINCSILKGLKYNQATATFHQWR 81
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKsWIPA-SKQAVT-VSFFYDSTRNTYRIIS--VEGSKAIINSTITPNMTFTKTSQKFGQWA 76

                        90       100       110
                ....*....|....*....|....*....|
gi 62471737  82 DSK--FVYGLNFSSQNDAENFARAMMHALE 109
Cdd:cd01206  77 DSRanTVYGLGFASEAELTKFAEKFQEAKE 106
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 650-683 1.32e-12

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: 62.28  E-value: 1.32e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 62471737   650 DLDTLKAEIVREMRLEIQKVKNEIIDAIKSEFNR 683
Cdd:pfam08776   2 DLERLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 3-117 8.24e-06

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: 45.48  E-value: 8.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737   3 EQSIIGARASVMVYDDNQKKWvpsgSSSGLSKVQIYHHQQNNTFRVVGRKLQDHEVVINCSILKGLKYNQATATfhqwrD 82
Cdd:cd13174   6 ETKLFGERAKLYRFDADTKEW----KERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTS-----D 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 62471737  83 SKFVYGlnfssqndAENFARAMMHALEVLSGRVAN 117
Cdd:cd13174  77 KSFTWG--------GMNYAEDAEPEVETLAVRFKN 103
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 3-72 3.46e-04

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: 41.22  E-value: 3.46e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471737      3 EQSIIGARASVMVYDDNQKKWvpsgSSSGLSKVQIYHHQQNNT-FRVVGRKLQDHEVVINCSILKGLKYNQ 72
Cdd:smart00160  19 EEVIFSARAKLYRFANDKKEW----KERGVGDLKILKSKDNGGkVRIVMRRDGVLKVCANHPIFKSMTLKP 85
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 9-108 9.98e-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: 39.50  E-value: 9.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737   9 ARASVMVYDDNQKKWVpsgsSSGLSKVQIYHHQQNNTFRVVGRKLQDHEVVINCSILKGLKYNQATATFHQWR------- 81
Cdd:cd00835  12 KRAKLFRFDKETKEWK----ERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWVwtamdds 87

                        90       100       110
                ....*....|....*....|....*....|.
gi 62471737  82 ---DSKFV-YGLNFSSQNDAENFARAMMHAL 108
Cdd:cd00835  88 edgEGKPEtFAVRFKTAEDAEEFKKAFEEAQ 118
EVH1_WASP-like cd01205
WASP family proteins EVH1 domain; The Wiskott-Aldrich Syndrome Protein (WASP; also called ...
 46-105 1.22e-03

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: 38.66  E-value: 1.22e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471737  46 FRVVGrkLQDHEVVINCSILKGLKYNQATATFHQWRDSKFVYGLNFSSQNDAENFARAMM 105
Cdd:cd01205  41 FRLVD--LKTRGVVWEQELYEGFEYNQDRPFFHTFEGDECMIGLNFADEDEAAAFYKKVQ 98
 
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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