NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2318155607|ref|XP_050990597|]
View 

vasodilator-stimulated phosphoprotein isoform X1 [Labeo rohita]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: ...
 6-115 1.02e-65

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: 205.62  E-value: 1.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607   6 SICQARATVMIYDDGNKKWVPAGtGAQAFSRVQIYHNPSNNAFRVVGRKMQtDQQVVMNCPIVKGIKYNQATPNFHQWRD 85
Cdd:cd01207     1 SVASARASVMVYDDENKRWVPSG-GSQGLSRVQIYHNTRNNTFRVVGRKLQ-DHEVVINCAILKGLKYNQATPTFHQWRD 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 2318155607  86 ARQVWGLNFGSKEDAALFANGMMHALDVLN 115
Cdd:cd01207    79 ARQVYGLNFASKEEATEFAQAMLLALERLN 108
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 397-427 5.42e-11

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: 56.89  E-value: 5.42e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2318155607 397 RIKQELLEEVRKELQKVKDEIIRAFIQELQK 427
Cdd:pfam08776   5 RLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
 
Name Accession Description Interval E-value
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 6-115 1.02e-65

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: 205.62  E-value: 1.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607   6 SICQARATVMIYDDGNKKWVPAGtGAQAFSRVQIYHNPSNNAFRVVGRKMQtDQQVVMNCPIVKGIKYNQATPNFHQWRD 85
Cdd:cd01207     1 SVASARASVMVYDDENKRWVPSG-GSQGLSRVQIYHNTRNNTFRVVGRKLQ-DHEVVINCAILKGLKYNQATPTFHQWRD 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 2318155607  86 ARQVWGLNFGSKEDAALFANGMMHALDVLN 115
Cdd:cd01207    79 ARQVYGLNFASKEEATEFAQAMLLALERLN 108
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 6-111 1.07e-39

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: 137.97  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607   6 SICQARATVMIYDDGNKK-WVPAgtgaQAFSRVQIYHNPSNNAFRVVGRKMQtDQQVVMNCPIVKGIKYNQATPNFHQWR 84
Cdd:pfam00568  10 TICTAVAQVYLADPDNKRhWIKA----KHSGVVCFVKDSPQNSYFIRLVDIQ-DGKVIWNQEIYPNMEYNQARPFFHTFA 84

                          90       100
                  ....*....|....*....|....*..
gi 2318155607  85 DARQVWGLNFGSKEDAALFANGMMHAL 111
Cdd:pfam00568  85 DSRCVYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 3-111 5.62e-39

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: 135.95  E-value: 5.62e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607    3 SESSICQARATVMIYDDGNKKWVPAGTGAqaFSRVQIYHNPSNNAFRVVGRKMQTdqQVVMNCPIVKGIKYNQATPNFHQ 82
Cdd:smart00461   2 GSQCIILARAVVQLYDADTKKWVPTGEGG--AANLVIDKNQRSYFFRIVGIKGQD--KVIWNQELYKNFKYNQATPTFHQ 77

                           90       100
                   ....*....|....*....|....*....
gi 2318155607   83 WRDARQVWGLNFGSKEDAALFANGMMHAL 111
Cdd:smart00461  78 WADDKCVYGLNFASEEEAKKFRKKVLKAL 106
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 397-427 5.42e-11

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: 56.89  E-value: 5.42e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2318155607 397 RIKQELLEEVRKELQKVKDEIIRAFIQELQK 427
Cdd:pfam08776   5 RLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
 
Name Accession Description Interval E-value
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 6-115 1.02e-65

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: 205.62  E-value: 1.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607   6 SICQARATVMIYDDGNKKWVPAGtGAQAFSRVQIYHNPSNNAFRVVGRKMQtDQQVVMNCPIVKGIKYNQATPNFHQWRD 85
Cdd:cd01207     1 SVASARASVMVYDDENKRWVPSG-GSQGLSRVQIYHNTRNNTFRVVGRKLQ-DHEVVINCAILKGLKYNQATPTFHQWRD 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 2318155607  86 ARQVWGLNFGSKEDAALFANGMMHALDVLN 115
Cdd:cd01207    79 ARQVYGLNFASKEEATEFAQAMLLALERLN 108
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 6-111 1.01e-42

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: 145.68  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607   6 SICQARATVMIYDDGNKKWVPAGTGAqaFSRVQIYHNPSNNAFRVVGRKMQtDQQVVMNCPIVKGIKYNQATPNFHQWRD 85
Cdd:cd00837     1 SIFSARAHVMQIDDSNKNWVPAGGKG--ASRVSYFKDTTRNSFRIIGVDIK-DKKVVINCTITKNLVYNKATQTFHQWAD 77

                          90       100
                  ....*....|....*....|....*.
gi 2318155607  86 ARQVWGLNFGSKEDAALFANGMMHAL 111
Cdd:cd00837    78 DRTVFGLNFASEEDATKFAEAVQEAL 103
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 6-111 1.07e-39

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: 137.97  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607   6 SICQARATVMIYDDGNKK-WVPAgtgaQAFSRVQIYHNPSNNAFRVVGRKMQtDQQVVMNCPIVKGIKYNQATPNFHQWR 84
Cdd:pfam00568  10 TICTAVAQVYLADPDNKRhWIKA----KHSGVVCFVKDSPQNSYFIRLVDIQ-DGKVIWNQEIYPNMEYNQARPFFHTFA 84

                          90       100
                  ....*....|....*....|....*..
gi 2318155607  85 DARQVWGLNFGSKEDAALFANGMMHAL 111
Cdd:pfam00568  85 DSRCVYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 3-111 5.62e-39

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: 135.95  E-value: 5.62e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607    3 SESSICQARATVMIYDDGNKKWVPAGTGAqaFSRVQIYHNPSNNAFRVVGRKMQTdqQVVMNCPIVKGIKYNQATPNFHQ 82
Cdd:smart00461   2 GSQCIILARAVVQLYDADTKKWVPTGEGG--AANLVIDKNQRSYFFRIVGIKGQD--KVIWNQELYKNFKYNQATPTFHQ 77

                           90       100
                   ....*....|....*....|....*....
gi 2318155607   83 WRDARQVWGLNFGSKEDAALFANGMMHAL 111
Cdd:smart00461  78 WADDKCVYGLNFASEEEAKKFRKKVLKAL 106
EVH1_SPRED-like cd10574
Sprouty-related EVH1 domain-containing-like proteins EVH1 domain; The Spred family has the ...
 6-114 9.74e-20

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: 84.29  E-value: 9.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607   6 SICQARATVMIYDDGNKKWVPAGTGAqaFSRVQIY-----HNPSNNAFRVVGRKMQtDQQVVMNCPIVKGIKYNQATPNF 80
Cdd:cd10574     1 CLVRVRAVVMTRDDSSGGWLPLGGGG--LSIVSVCkvmpeEGAPRTEYVIHGERIR-DKTVVLECTLRKDLVYNKVMPTF 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2318155607  81 HQWRDARQVWGLNFGSKEDAALFANGMMHALDVL 114
Cdd:cd10574    78 HHWRIGEKKFGLTFQSPADARAFDRGVRRALEDL 111
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 4-112 4.42e-11

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: 59.67  E-value: 4.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607   4 ESSICQARATVMIYDDGNKK-WVPAGTGAqafSRVQIYHNPSNNAFRVVGRKmqtDQQVVMNCPIVKGIKYNQATPNFHQ 82
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKsWIPASKQA---VTVSFFYDSTRNTYRIISVE---GSKAIINSTITPNMTFTKTSQKFGQ 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2318155607  83 WRDAR--QVWGLNFGSKEDAALFANGMMHALD 112
Cdd:cd01206    75 WADSRanTVYGLGFASEAELTKFAEKFQEAKE 106
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 397-427 5.42e-11

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: 56.89  E-value: 5.42e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2318155607 397 RIKQELLEEVRKELQKVKDEIIRAFIQELQK 427
Cdd:pfam08776   5 RLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 9-103 1.26e-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: 41.43  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607   9 QARATVMIYDDGNKKWVPAGTGaqafsRVQIYHNPSNNAFRVVgrkMQTDQ--QVVMNCPIVKGIKYNQATPNFHQWR-- 84
Cdd:cd00835    11 EKRAKLFRFDKETKEWKERGVG-----DLKILKNKDTGKYRIV---MRRDQvlKLCCNHYILPDMKLTKMGNNDRAWVwt 82

                          90       100
                  ....*....|....*....|....*...
gi 2318155607  85 ---------DARQVWGLNFGSKEDAALF 103
Cdd:cd00835    83 amddsedgeGKPETFAVRFKTAEDAEEF 110
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 3-110 8.79e-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: 39.29  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318155607    3 SESSICQARATVMIYDDGNKKWVPAGTGaqafsRVQI-YHNPSNNAFRVVGRKMQTdQQVVMNCPIVKGIKYNQATPNFH 81
Cdd:smart00160  18 DEEVIFSARAKLYRFANDKKEWKERGVG-----DLKIlKSKDNGGKVRIVMRRDGV-LKVCANHPIFKSMTLKPLAGSNR 91

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2318155607   82 QWRDARQVWG----------LNFGSKEDAALFANGMMHA 110
Cdd:smart00160  92 ALKWTPEDFAddipklvlyaVRFKTKEEADSFKNIFEEA 130
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 3-80 1.58e-03

Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, acts as a CRM1 cofactor, enhancing nuclear export signal (NES) export by stabilizing the export complex in the nucleus. CRM1/Exportin1 is responsible for exporting many proteins and ribonucleoproteins from the nucleus to the cytosol. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. RanBP3 contains a N-terminal nuclear localization signal (NLS), 2 FxFG motifs, and a single RanBD. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270001  Cd Length: 113  Bit Score: 37.98  E-value: 1.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2318155607   3 SESSICQARATVMIYDDGNKKWVPAGTGAQafsRVQIYHNPSNNAFRVVGRKMQTdQQVVMNCPIVKGIKYNQATPNF 80
Cdd:cd13180     5 GETNVFQVNCKLYAFDKSKQSWKERGRGTL---RLNDSKSDGSGQSRIVMRTQGS-LRVILNTKIWPGMTVEKVSEKS 78
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH