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Conserved domains on  [gi|112490398]
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Chain A, SH3-containing GRB2-like protein 2

Protein Classification

BAR domain-containing protein( domain architecture ID 10166294)

BAR (Bin/Amphiphysin/Rvs) domain-containing protein may bind membranes and detect membrane curvature

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 30-256 8.31e-149

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


:

Pssm-ID: 153297  Cd Length: 223  Bit Score: 414.40  E-value: 8.31e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  30 EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGREL 109
Cdd:cd07613    1 EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 110 GDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIqsalQHHLKKLEGRRLDFDYKKKRQGKIPD 189
Cdd:cd07613   81 GDECNFGPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREI----QHHLKKLEGRRLDFDYKKKRQGKIPD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112490398 190 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQA 256
Cdd:cd07613  157 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQILQQVTVKLEDRIREA 223
 
Name Accession Description Interval E-value
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 30-256 8.31e-149

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


Pssm-ID: 153297  Cd Length: 223  Bit Score: 414.40  E-value: 8.31e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  30 EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGREL 109
Cdd:cd07613    1 EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 110 GDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIqsalQHHLKKLEGRRLDFDYKKKRQGKIPD 189
Cdd:cd07613   81 GDECNFGPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREI----QHHLKKLEGRRLDFDYKKKRQGKIPD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112490398 190 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQA 256
Cdd:cd07613  157 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQILQQVTVKLEDRIREA 223
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 11-250 3.50e-70

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 215.28  E-value: 3.50e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398   11 LKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINtmskirgqekgpg 90
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTKLDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLE------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398   91 ypQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHdKDLREIqsalQHHLKKL 170
Cdd:pfam03114  68 --QPEELLAESMIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEI----QKHRKKL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  171 EGRRLDFDYKKKRQGKIP-------------DEELRQALEKFDESKEIAESSMFNLLEMDIEQV-SQLSALVQAQLEYHK 236
Cdd:pfam03114 141 ERKRLDYDAAKTRVKKAKkkksskakdesqaEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVvNQLVAFVEAQLDFHR 220

                         250
                  ....*....|....
gi 112490398  237 QAVQILQQVTVRLE 250
Cdd:pfam03114 221 QCYQLLEQLQQQLG 234
BAR smart00721
BAR domain;
10-249 3.84e-61

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 192.60  E-value: 3.84e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398    10 GLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGP 89
Cdd:smart00721   1 GFKKQFNRAKQKVGEKVGKAEKTKLDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398    90 GypqaeallaeamlKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLdIEVKQNFIDPLQNLHDKDLREIqsalQHHLKK 169
Cdd:smart00721  81 G-------------DDGEGLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEI----KKARKK 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398   170 LEGRRLDFDYKK------KRQGKIPD--------EELRQALEKFDESKEIAESSMFNLLEMDIE-QVSQLSALVQAQLEY 234
Cdd:smart00721 143 LERKLLDYDSARhklkkaKKSKEKKKdeklakaeEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNF 222

                          250
                   ....*....|....*
gi 112490398   235 HKQAVQILQQVTVRL 249
Cdd:smart00721 223 HRESYKLLQQLQQQL 237
 
Name Accession Description Interval E-value
BAR_Endophilin_A1 cd07613
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid ...
 30-256 8.31e-149

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A1 (or endophilin-1) is also referred to as SH3P4 (SH3 domain containing protein 4) or SH3GL2 (SH3 domain containing Grb2-like protein 2). It is localized in presynaptic nerve terminals. It plays many roles in clathrin-dependent endocytosis of synaptic vesicles including early vesicle formation, ubiquitin-dependent sorting of plasma membrane proteins, and regulation of calcium influx into neurons. The BAR domain of endophilin-A1 forms crescent-shaped dimers that can detect membrane curvature and drive membrane bending, while its SH3 domain binds the endocytic proteins, dynamin 1, synaptojanin 1, and amphiphysins.


Pssm-ID: 153297  Cd Length: 223  Bit Score: 414.40  E-value: 8.31e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  30 EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGREL 109
Cdd:cd07613    1 EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 110 GDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIqsalQHHLKKLEGRRLDFDYKKKRQGKIPD 189
Cdd:cd07613   81 GDECNFGPALGDVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREI----QHHLKKLEGRRLDFDYKKKRQGKIPD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112490398 190 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQA 256
Cdd:cd07613  157 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQATQILQQVTVKLEDRIREA 223
BAR_Endophilin_A cd07592
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid ...
 30-256 2.86e-133

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins, localized at synapses, which interact with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. The BAR domains of endophilin-A1 and A3 form crescent-shaped dimers that can detect membrane curvature and drive membrane bending.


Pssm-ID: 153276  Cd Length: 223  Bit Score: 375.11  E-value: 2.86e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  30 EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGREL 109
Cdd:cd07592    1 EGTKLDDEFLEMERKTDATSKLVEDLIPKTKEYLQPNPAARAKLAMQNTYSKIRGQAKSTKYPQPEGLLGEVMLKYGREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 110 GDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIqsalQHHLKKLEGRRLDFDYKKKRQGKIPD 189
Cdd:cd07592   81 GEDSNFGQALVEVGEALKQLAEVKDSLDDNVKQNFLDPLQQLQDKDLKEI----NHHRKKLEGRRLDYDYKKRKQGKGPD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112490398 190 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQA 256
Cdd:cd07592  157 EELKQAEEKFEESKELAENSMFNLLENDVEQVSQLSALVEAQLDYHRQSAEILEELQSKLQERISEA 223
BAR_Endophilin_A2 cd07614
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid ...
 30-256 2.94e-112

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins, localized at synapses, which interact with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A2 (or endophilin-2) is also referred to as SH3P8 (SH3 domain containing protein 8) or SH3GL1 (SH3 domain containing Grb2-like protein 1). It localizes to presynaptic nerve terminals and forms heterodimers with endophilin-A1 through their BAR domains. Endophilin-A2 binds dynamin 1, synaptojanin 1, and the beta1-adrenergic receptor cytoplasmic tail through its SH3 domain.


Pssm-ID: 153298  Cd Length: 223  Bit Score: 322.05  E-value: 2.94e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  30 EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGREL 109
Cdd:cd07614    1 EGTKLDDDFKEMEKKVDLTSKAVTEVLARTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGETMIRYGKEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 110 GDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIqsalQHHLKKLEGRRLDFDYKKKRQGKIPD 189
Cdd:cd07614   81 GDESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCDKDLKEI----QHHLKKLEGRRLDFDYKKKRQGKIPD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112490398 190 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQA 256
Cdd:cd07614  157 EELRQAMEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILDELAEKLKRRMREA 223
BAR_Endophilin_A3 cd07615
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid ...
 30-256 1.44e-111

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-A3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins are accessory proteins localized at synapses that interacts with the endocytic proteins, dynamin and synaptojanin. They are essential for synaptic vesicle formation from the plasma membrane. They interact with voltage-gated calcium channels, thus linking vesicle endocytosis to calcium regulation. They also play roles in virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. Endophilin-A3 (or endophilin-3) is also referred to as SH3P13 (SH3 domain containing protein 13) or SH3GL3 (SH3 domain containing Grb2-like protein 3). It regulates Arp2/3-dependent actin filament assembly during endocytosis. It binds N-WASP through its SH3 domain and enhances the ability of N-WASP to activate the Arp2/3 complex. Endophilin-A3 co-localizes with the vesicular glutamate transporter 1 (VGLUT1), and may play an important role in the synaptic release of glutamate.


Pssm-ID: 153299  Cd Length: 223  Bit Score: 320.04  E-value: 1.44e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  30 EGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGREL 109
Cdd:cd07615    1 EGTKLDDDFQEMERKIDVTNKVVAELLSKTTEYLQPNPAYRAKLGMLNTVSKIRGQVKTTGYPQTEGLLGDCMLRYGREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 110 GDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIqsalQHHLKKLEGRRLDFDYKKKRQGKIPD 189
Cdd:cd07615   81 GEESTFGNALLDVGESMKQMAEVKDSLDINVKQNFIDPLQLLQDKDLKEI----GHHLKKLEGRRLDFDYKKKRQGKIPD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112490398 190 EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQA 256
Cdd:cd07615  157 EEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLSVLIEAALDYHRQSTEILEDLQSKLQNRISTA 223
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 11-250 3.50e-70

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 215.28  E-value: 3.50e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398   11 LKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINtmskirgqekgpg 90
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTKLDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQTVLE------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398   91 ypQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHdKDLREIqsalQHHLKKL 170
Cdd:pfam03114  68 --QPEELLAESMIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDPLRNLL-KEFKEI----QKHRKKL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  171 EGRRLDFDYKKKRQGKIP-------------DEELRQALEKFDESKEIAESSMFNLLEMDIEQV-SQLSALVQAQLEYHK 236
Cdd:pfam03114 141 ERKRLDYDAAKTRVKKAKkkksskakdesqaEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVvNQLVAFVEAQLDFHR 220

                         250
                  ....*....|....
gi 112490398  237 QAVQILQQVTVRLE 250
Cdd:pfam03114 221 QCYQLLEQLQQQLG 234
BAR smart00721
BAR domain;
10-249 3.84e-61

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 192.60  E-value: 3.84e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398    10 GLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGP 89
Cdd:smart00721   1 GFKKQFNRAKQKVGEKVGKAEKTKLDEDFEELERRFDTTEAEIEKLQKDTKLYLQPNPAVRAKLASQKKLSKSLGEVYEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398    90 GypqaeallaeamlKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLdIEVKQNFIDPLQNLHDKDLREIqsalQHHLKK 169
Cdd:smart00721  81 G-------------DDGEGLGADSSYGKALDKLGEALKKLLQVEESL-SQVKRTFILPLLNFLLGEFKEI----KKARKK 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398   170 LEGRRLDFDYKK------KRQGKIPD--------EELRQALEKFDESKEIAESSMFNLLEMDIE-QVSQLSALVQAQLEY 234
Cdd:smart00721 143 LERKLLDYDSARhklkkaKKSKEKKKdeklakaeEELRKAKQEFEESNAQLVEELPQLVASRVDfFVNCLQALIEAQLNF 222

                          250
                   ....*....|....*
gi 112490398   235 HKQAVQILQQVTVRL 249
Cdd:smart00721 223 HRESYKLLQQLQQQL 237
BAR_Endophilin_B cd07594
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid ...
 20-244 6.82e-22

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle.


Pssm-ID: 153278  Cd Length: 229  Bit Score: 90.53  E-value: 6.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  20 QKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKirgqeKGPGYPQAEALLA 99
Cdd:cd07594    1 QFTEEKLGTAEKTEYDAHFENLLQRADKTKVWTEKILKQTEAVLQPNPNVRVEDFIYEKLDR-----KKPDRLSNLEQLG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 100 EAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQSalqhHLKKLEGRRLDFDY 179
Cdd:cd07594   76 QAMIEAGNDFGPGTAYGSALIKVGQAQKKLGQAEREFIQTSSSNFLQPLRNFLEGDMKTISK----ERKLLENKRLDLDA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112490398 180 KKKRQGKI--------PDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQ 244
Cdd:cd07594  152 CKTRVKKAksaeaieqAEQDLRVAQSEFDRQAEITKLLLEGISSTHANHLRCLRDFVEAQMTYYAQCYQYMDD 224
BAR_Endophilin_B2 cd07617
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid ...
 20-249 7.69e-20

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B2, also called SH3GLB2 (SH3-domain GRB2-like endophilin B2), is a cytoplasmic protein that interacts with the apoptosis inducer Bax. It is overexpressed in prostate cancer metastasis and has been identified as a cancer antigen with potential utility in immunotherapy. Endophilin-B2 forms homo- and heterodimers (with endophilin-B1) through its BAR domain, which can bind and bend membranes.


Pssm-ID: 153301  Cd Length: 220  Bit Score: 85.08  E-value: 7.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  20 QKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKirgqeKGPGYPQAEALLA 99
Cdd:cd07617    1 QFTEEKLGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDR-----KVPSRVTNAELLG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 100 EAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQSalqhHLKKLEGRRLDFDY 179
Cdd:cd07617   76 QYMTEAANDFGPGTPYGKTLIKVGETQKRLGAAERDFIHTSSINFLTPLRNFLEGDWKTISK----ERRLLQNRRLDLDA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 180 KKKRQGKiPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRL 249
Cdd:cd07617  152 CKARLKK-AEHELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEFVEAQATYYAQCYRHMLDLQKQL 220
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 86-245 7.92e-20

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 84.03  E-value: 7.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  86 EKGPGYPQAEALLAEAMLKFGRELGDDCN--FGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIqsal 163
Cdd:cd07307   21 DSLKELPAAAEKLSEALQELGKELPDLSNtdLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDLKEI---- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 164 QHHLKKLEGRRLDFDY----------KKKRQGKIP--DEELRQALEKFDESKEIAESSMFNLLE-MDIEQVSQLSALVQA 230
Cdd:cd07307   97 KKRRKKLDKARLDYDAareklkklrkKKKDSSKLAeaEEELQEAKEKYEELREELIEDLNKLEEkRKELFLSLLLSFIEA 176

                        170
                 ....*....|....*
gi 112490398 231 QLEYHKQAVQILQQV 245
Cdd:cd07307  177 QSEFFKEVLKILEQL 191
BAR_MUG137_fungi cd07593
The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated ...
 30-245 9.49e-20

The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This subfamily is composed predominantly of uncharacterized fungal proteins with similarity to Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein (MUG137), which may play a role in meiosis and sporulation in fission yeast. MUG137 contains an N-terminal BAR domain and a C-terminal SH3 domain, similar to endophilins. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153277  Cd Length: 215  Bit Score: 84.32  E-value: 9.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  30 EGTKLDDDFKEMERKvdvtsravMEIMTKTIEYLQpnpasRAKLSMINTMSKIR--GQEKGPGYPQAEalLAEAMLKFGR 107
Cdd:cd07593    1 QKTTLSEEFLELEKE--------IELRKEGMERLH-----RSTEAYVEYLSKKKplLDDKDKCLPVEA--LGLVMINHGE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 108 ELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNlHDKDLREIQSALqhhlKKLEGRRLDFD------YKK 181
Cdd:cd07593   66 EFPQDSEYGSCLSKLGRAHCKIGTLQEEFADRLSDTFLANIER-SLAEMKEYHSAR----KKLESRRLAYDaaltksQKA 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112490398 182 KRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQV 245
Cdd:cd07593  141 KKEDSRLEEELRRAKAKYEESSEDVEARMVAIKESEADQYRDLTDLLDAELDYHQQSLDVLREV 204
BAR_Endophilin_B1 cd07616
The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; BAR domains are dimerization, lipid ...
 20-242 4.27e-18

The Bin/Amphiphysin/Rvs (BAR) domain of Endophilin-B1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. They are classified into two types, A and B. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilin-B1, also called Bax-interacting factor 1 (Bif-1) or SH3GLB1 (SH3-domain GRB2-like endophilin B1), is localized mainly to the Golgi apparatus. It is involved in the regulation of many biological events including autophagy, tumorigenesis, nerve growth factor (NGF) trafficking, neurite outgrowth, mitochondrial outer membrane dynamics, and cell death. Endophilin-B1 forms homo- and heterodimers (with endophilin-B2) through its BAR domain, which can bind and bend membranes. It interacts with amphiphysin 1 and dynamin 1 through its SH3 domain.


Pssm-ID: 153300  Cd Length: 229  Bit Score: 80.50  E-value: 4.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  20 QKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKirgqeKGPGYPQAEALLA 99
Cdd:cd07616    1 QFTEEKFGQAEKTELDAHLENLLSKAECTKHWTEKIMKQTEVLLQPNPNARIEEFVYEKLDR-----KAPSRMNNPELLG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 100 EAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQSalqhHLKKLEGRRLDFDY 179
Cdd:cd07616   76 QYMIDAGNEFGPGTAYGNALIKCGETQKQIGTADRELIQTSAINFLTPLRNFIEGDYKTITK----ERKLLQNKRLDLDA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112490398 180 KKKRQGK--------IPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQIL 242
Cdd:cd07616  152 AKTRLKKakvaearaAAEQELRITQSEFDRQAEITRLLLEGISSTHAHHLRCLNDFVEAQMTYYAQCYQYM 222
BAR_RhoGAP_Rich-like cd07595
The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains ...
 24-256 9.28e-14

The Bin/Amphiphysin/Rvs (BAR) domain of Rich-like Rho GTPase Activating Proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of Rho and Rac GTPase activating proteins (GAPs) with similarity to GAP interacting with CIP4 homologs proteins (Rich). Members contain an N-terminal BAR domain, followed by a Rho GAP domain, and a C-terminal prolin-rich region. Vertebrates harbor at least three Rho GAPs in this subfamily including Rich1, Rich2, and SH3-domain binding protein 1 (SH3BP1). Rich1 and Rich2 play complementary roles in the establishment and maintenance of cell polarity. Rich1 is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. Rich2 is a Rac GAP that interacts with CD317 and plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. SH3BP1 is a Rac GAP that inhibits Rac-mediated platelet-derived growth factor (PDGF)-induced membrane ruffling. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of Rich1 has been shown to form oligomers, bind membranes and induce membrane tubulation.


Pssm-ID: 153279 [Multi-domain]  Cd Length: 244  Bit Score: 68.52  E-value: 9.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  24 EKVGGAE-GTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMIntmskirgqeKGPGYpqaeaLLAEAM 102
Cdd:cd07595    2 QTVGRAEkTEVLSDELLQIEKRVEAVKDACQNIHKKLISCLQGQSGEDKDKRLK----------KLPEY-----GLAQSM 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 103 LKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQSAlQHHLKKLegrRLDFDYKKK 182
Cdd:cd07595   67 LESSKELPDDSLLGKVLKLCGEAQNTLARELVDHEMNVEEDVLSPLQNILEVEIPNIQKQ-KKRLSKL---VLDMDSARS 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 183 R-------------QGKIP--DEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTV 247
Cdd:cd07595  143 RynaahkssggqgaAAKVDalKDEYEEAELKLEQCRDALATDMYEFLAKEAEIASYLIDLIEAQREYHRTALSVLEAVLP 222


                 ....*....
gi 112490398 248 RLEERIRQA 256
Cdd:cd07595  223 ELQEQIEQS 231
BAR_Rich1 cd07618
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR ...
 23-245 1.86e-08

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 1 (Rich1) is also called Neuron-associated developmentally-regulated protein (Nadrin) or Rho GTPase activating protein 17 (ARHGAP17). It is a Cdc42- and Rac-specific GAP that binds to polarity proteins through the scaffold protein angiomotin and plays a role in maintaining the integrity of tight junctions. It may be a component of a sorting mechanism in the recycling of tight junction transmembrane proteins. Rich1 contains an N-terminal BAR domain followed by a Rho GAP domain and a C-terminal proline-rich domain. It interacts with the BAR domain proteins endophilin and amphiphysin through its proline-rich region. The BAR domain of Rich1 forms oligomers and can bind membranes and induce membrane tubulation.


Pssm-ID: 153302  Cd Length: 246  Bit Score: 53.50  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  23 SEKVGGAEGTK-LDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKlsmintmskiRGQEKGPgypqaEALLAEA 101
Cdd:cd07618    1 NQTVGRAEKTEvLSEDLLQIERRLDTVRSVSHNVHKRLIACFQGQVGTDAE----------KRHKKLP-----LTALAQN 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 102 MLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQSAlQHHLKKLEgrrLDFDYKK 181
Cdd:cd07618   66 MQEGSAQLGEESLIGKMLDTCGDAENKLAFELSQHEVLLEKDILDPLNQLAEVEIPNIQKQ-RKQLAKLV---LDWDSAR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 182 KR------------QG---KIP--DEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQ 244
Cdd:cd07618  142 GRynqahkssgtnfQAmpsKIDmlKEEMDEAGNKVEQCKDQLAADMYNFASKEGEYAKFFVLLLEAQADYHRKALAVIEK 221


                 .
gi 112490398 245 V 245
Cdd:cd07618  222 V 222
BAR_Rich2 cd07619
The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR ...
 98-245 6.45e-08

The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP interacting with CIP4 homologs protein 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. RhoGAP interacting with CIP4 homologs protein 2 (Rich2) is a Rho GTPase activating protein that interacts with CD317, a lipid raft-associated integral membrane protein. It plays a role in actin cytoskeleton organization and the maintenance of microvilli in polarized epithelial cells. Rich2 contains an N-terminal BAR domain followed by a GAP domain for Rho and Rac GTPases and a C-terminal proline-rich domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153303  Cd Length: 248  Bit Score: 51.97  E-value: 6.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  98 LAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQSALQHHLK---KLEGRR 174
Cdd:cd07619   62 LAQCMVEGAAVLGDDSLLGKMLKLCGETEDKLAQELILFELQIERDVVEPLYVLAEVEIPNIQKQRKHLAKlvlDMDSSR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 175 LDFDYKKKRQGKIPD------------EELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQIL 242
Cdd:cd07619  142 TRWQQSSKSSGLSSNlqptgakadalrEEMEEAANRMEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLELL 221


                 ...
gi 112490398 243 QQV 245
Cdd:cd07619  222 QSV 224
BAR_Gvp36 cd07600
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ...
 111-245 3.38e-07

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 kDa and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Proteomic analysis shows that Golgi vesicle protein of 36 kDa (Gvp36) may be involved in vesicular trafficking and nutritional adaptation. A Saccharomyces cerevisiae strain deficient in Gvp36 shows defects in growth, in actin cytoskeleton polarization, in endocytosis, in vacuolar biogenesis, and in the cell cycle. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153284 [Multi-domain]  Cd Length: 242  Bit Score: 49.66  E-value: 3.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 111 DDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQSALqhhlKKLEGRRLDFD-----YKKKRQG 185
Cdd:cd07600  101 DEDPLSKALGKYSDAEEKIAEARLEQDQLIQKEFNAKLRETLNTSFQKAHKAR----KKVEDKRLQLDtaraeLKSAEPA 176

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112490398 186 KIPD---EELRQALEKFDESKEIAESSMFNLLEmDIEQVSQLSALVQAQLEYHKQAVQILQQV 245
Cdd:cd07600  177 EKQEaarVEVETAEDEFVSATEEAVELMKEVLD-NPEPLQLLKELVKAQLAYHKTAAELLEEL 238
BAR_SFC_plant cd07606
The Bin/Amphiphysin/Rvs (BAR) domain of the plant protein SCARFACE (SFC); BAR domains are ...
 94-246 1.78e-03

The Bin/Amphiphysin/Rvs (BAR) domain of the plant protein SCARFACE (SFC); BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. The plant protein SCARFACE (SFC), also called VAscular Network 3 (VAN3), is a plant ACAP (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein), an Arf GTPase Activating Protein (GAP) that plays a role in the trafficking of auxin efflux regulators from the plasma membrane to the endosome. It is required for the normal vein patterning in leaves. SCF contains an N-terminal BAR domain, followed by a Pleckstrin Homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153290  Cd Length: 202  Bit Score: 38.63  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398  94 AEALLAEAMLKFGRELGDD--CNF-GPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQSAlqhhLKKL 170
Cdd:cd07606   37 GDSAFAESLEEFGGGHDDPisVAVgGPVMTKFTSALREIGSYKEVLRSQVEHMLNDRLAQFADTDLQEVKDA----RRRF 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112490398 171 EGRRLDFDYKKKR----QGKIPDEELRQALEKFDESKEIAESSMFNLLE--MDIEQVSQ------LSALVQAQLEYHKQA 238
Cdd:cd07606  113 DKASLDYEQARSKflslTKDAKPEILAAAEEDLGTTRSAFETARFDLMNrlHAADARKRveflerLSGSMDAHLAFFKSG 192


                 ....*...
gi 112490398 239 VQILQQVT 246
Cdd:cd07606  193 YELLRQLE 200
 
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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