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Conserved domains on  [gi|1734342175|ref|NP_001359496|]
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rho GTPase-activating protein 42 isoform 6 [Mus musculus]

Protein Classification

BAR and BAR-PH_GRAF_family domain-containing protein( domain architecture ID 10311838)

BAR and BAR-PH_GRAF_family domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 19-225 1.77e-137

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.


The actual alignment was detected with superfamily member cd07634:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 207  Bit Score: 390.16  E-value: 1.77e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVE 98
Cdd:cd07634     1 RERLQCHEIELERTNKFIKELIKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  99 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADSQIGREHQNFYEAS 178
Cdd:cd07634    81 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILEKHLNLSAKKKESHLQRADTQIDREHQNFYEAS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1734342175 179 LEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYK 225
Cdd:cd07634   161 LEYVFKIQEVQEKKKFEFVEPLLAFLQGLFTFYHEGYELAQEFAPYK 207
BAR-PH_GRAF_family cd01249
GTPase Regulator Associated with Focal adhesion and related proteins Pleckstrin homology (PH) ...
 267-375 3.04e-59

GTPase Regulator Associated with Focal adhesion and related proteins Pleckstrin homology (PH) domain; This hierarchy contains GRAF family members: OPHN1/oligophrenin1, GRAF1 (also called ARHGAP26/Rho GTPase activating protein 26), GRAF2 (also called ARHGAP10/ARHGAP42), AK057372, and LOC129897, all of which are members of the APPL family. OPHN1 is a RhoGAP involved in X-linked mental retardation, epilepsy, rostral ventricular enlargement, and cerebellar hypoplasia. Affected individuals have morphological abnormalities of their brain with enlargement of the cerebral ventricles and cerebellar hypoplasia. OPHN1 negatively regulates RhoA, Cdc42, and Rac1 in neuronal and non-neuronal cells. GRAF1 sculpts the endocytic membranes of the CLIC/GEEC (clathrin-independent carriers/GPI-enriched early endosomal compartments) endocytic pathway. It strongly interacts with dynamin and inhibition of dynamin abolishes CLIC/GEEC endocytosis. GRAF2, GRAF3 and oligophrenin are likely to play similar roles during clathrin-independent endocytic events. GRAF1 mutations are linked to leukaemia. All members are composed of a N-terminal BAR-PH domain, followed by a RhoGAP domain, a proline rich region, and a C-terminal SH3 domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269953  Cd Length: 105  Bit Score: 187.15  E-value: 3.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 267 TMEGYLYVQEKRPLGFTWTKHYCTYDKGSKMFTMSVSDVKASGKmnglvTGSPEMFKLKSCIRRKTDSIDKRFCFDIEVV 346
Cdd:cd01249     1 TKEGYLYLQEKKPLGSTWTKHYCTYRKESKMFTMIPYNQQSSGK-----LGTTEVVTLKSCVRRKTDSIDRRFCFDIEVV 75

                          90       100
                  ....*....|....*....|....*....
gi 1734342175 347 ERHGIITLQAFSEANRKLWLEAMDGKEPV 375
Cdd:cd01249    76 DRPTVLTLQALSEEDRKLWLEAMDGKEPI 104
 
Name Accession Description Interval E-value
BAR_GAP10-like cd07634
The Bin/Amphiphysin/Rvs (BAR) domain of Rho GTPase activating protein 10-like; BAR domains are ...
 19-225 1.77e-137

The Bin/Amphiphysin/Rvs (BAR) domain of Rho GTPase activating protein 10-like; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This group is composed of uncharacterized proteins called Rho GTPase activating protein (GAP) 10-like. GAP10-like may be a GAP with activity towards RhoA and Cdc42. Similar to GRAF and GRAF2, it contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domains of the related proteins GRAF and OPHN1, directly interact with their Rho GAP domains and inhibit theiractivity. The autoinhibited proteins are capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously.


Pssm-ID: 153318 [Multi-domain]  Cd Length: 207  Bit Score: 390.16  E-value: 1.77e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVE 98
Cdd:cd07634     1 RERLQCHEIELERTNKFIKELIKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  99 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADSQIGREHQNFYEAS 178
Cdd:cd07634    81 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILEKHLNLSAKKKESHLQRADTQIDREHQNFYEAS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1734342175 179 LEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYK 225
Cdd:cd07634   161 LEYVFKIQEVQEKKKFEFVEPLLAFLQGLFTFYHEGYELAQEFAPYK 207
BAR_3 pfam16746
BAR domain of APPL family; BAR_12 is the BAR coiled-coil domain at the N-terminus of APPL or ...
 6-249 1.52e-99

BAR domain of APPL family; BAR_12 is the BAR coiled-coil domain at the N-terminus of APPL or adaptor protein containing PH domain, PTB domain, and leucine zipper motif proteins in higher eukaryotes. This BAR domain contains four helices whereas the other classical BAR domains contain only three helices. The first three helices form an antiparallel coiled-coil, while the fourth helix, is unique to APPL1. BAR domains take part in many varied biological processes such as fission of synaptic vesicles, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, apoptosis, secretory vesicle fusion, and tissue differentiation.


Pssm-ID: 465256  Cd Length: 235  Bit Score: 294.85  E-value: 1.52e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175   6 LEFSDSYLDSPDFRERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDdeisiaQ 85
Cdd:pfam16746   1 LEFEECLKDSPQFRSLLEEHEAELDELEKKLKKLLKLCKRMIEAGKEYSAAQRLFANSLLDFKFEFIGDEETD------E 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  86 SLKEFARLLIAVEEERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADS 165
Cdd:pfam16746  75 SLKKFSQLLQEMENFHTILLDQAQRTIIKPLENFRKEDLKEVKELKKKFDKASEKLDAALEKNAQLSKKKKPSELEEADN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 166 QIGREHQNFYEASLEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYKQQLQFNLQNTRnnfESTRQE 245
Cdd:pfam16746 155 ELAATRKCFHHASLDYVLQINELQERKKFEILEPLLSFMHAQFTFFHQGYELFKDLEPFMKDLQAQLQQTR---EDTREE 231


                  ....
gi 1734342175 246 VERL 249
Cdd:pfam16746 232 KEEL 235
BAR-PH_GRAF_family cd01249
GTPase Regulator Associated with Focal adhesion and related proteins Pleckstrin homology (PH) ...
 267-375 3.04e-59

GTPase Regulator Associated with Focal adhesion and related proteins Pleckstrin homology (PH) domain; This hierarchy contains GRAF family members: OPHN1/oligophrenin1, GRAF1 (also called ARHGAP26/Rho GTPase activating protein 26), GRAF2 (also called ARHGAP10/ARHGAP42), AK057372, and LOC129897, all of which are members of the APPL family. OPHN1 is a RhoGAP involved in X-linked mental retardation, epilepsy, rostral ventricular enlargement, and cerebellar hypoplasia. Affected individuals have morphological abnormalities of their brain with enlargement of the cerebral ventricles and cerebellar hypoplasia. OPHN1 negatively regulates RhoA, Cdc42, and Rac1 in neuronal and non-neuronal cells. GRAF1 sculpts the endocytic membranes of the CLIC/GEEC (clathrin-independent carriers/GPI-enriched early endosomal compartments) endocytic pathway. It strongly interacts with dynamin and inhibition of dynamin abolishes CLIC/GEEC endocytosis. GRAF2, GRAF3 and oligophrenin are likely to play similar roles during clathrin-independent endocytic events. GRAF1 mutations are linked to leukaemia. All members are composed of a N-terminal BAR-PH domain, followed by a RhoGAP domain, a proline rich region, and a C-terminal SH3 domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269953  Cd Length: 105  Bit Score: 187.15  E-value: 3.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 267 TMEGYLYVQEKRPLGFTWTKHYCTYDKGSKMFTMSVSDVKASGKmnglvTGSPEMFKLKSCIRRKTDSIDKRFCFDIEVV 346
Cdd:cd01249     1 TKEGYLYLQEKKPLGSTWTKHYCTYRKESKMFTMIPYNQQSSGK-----LGTTEVVTLKSCVRRKTDSIDRRFCFDIEVV 75

                          90       100
                  ....*....|....*....|....*....
gi 1734342175 347 ERHGIITLQAFSEANRKLWLEAMDGKEPV 375
Cdd:cd01249    76 DRPTVLTLQALSEEDRKLWLEAMDGKEPI 104
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 267-369 3.29e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 42.54  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  267 TMEGYLYVQEKRPLGfTWTKHYCTYDKGSKMFTMSVSDVKASGKmnglvtgsPEMFKLKSCIRR---KTDSIDKRFCFDI 343
Cdd:smart00233   2 IKEGWLYKKSGGGKK-SWKKRYFVLFNSTLLYYKSKKDKKSYKP--------KGSIDLSGCTVReapDPDSSKKPHCFEI 72

                           90       100
                   ....*....|....*....|....*.
gi 1734342175  344 EVVERHgIITLQAFSEANRKLWLEAM 369
Cdd:smart00233  73 KTSDRK-TLLLQAESEEEREKWVEAL 97
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 267-369 5.33e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 39.08  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 267 TMEGYLYVQEKRpLGFTWTKHYCTYDKGSKMFTMSVSDVKASGKMNglvtgspeMFKLKSCIRR---KTDSIDKRFCFDI 343
Cdd:pfam00169   2 VKEGWLLKKGGG-KKKSWKKRYFVLFDGSLLYYKDDKSGKSKEPKG--------SISLSGCEVVevvASDSPKRKFCFEL 72

                          90       100
                  ....*....|....*....|....*...
gi 1734342175 344 EVVERHGI--ITLQAFSEANRKLWLEAM 369
Cdd:pfam00169  73 RTGERTGKrtYLLQAESEEERKDWIKAI 100
 
Name Accession Description Interval E-value
BAR_GAP10-like cd07634
The Bin/Amphiphysin/Rvs (BAR) domain of Rho GTPase activating protein 10-like; BAR domains are ...
 19-225 1.77e-137

The Bin/Amphiphysin/Rvs (BAR) domain of Rho GTPase activating protein 10-like; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This group is composed of uncharacterized proteins called Rho GTPase activating protein (GAP) 10-like. GAP10-like may be a GAP with activity towards RhoA and Cdc42. Similar to GRAF and GRAF2, it contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domains of the related proteins GRAF and OPHN1, directly interact with their Rho GAP domains and inhibit theiractivity. The autoinhibited proteins are capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously.


Pssm-ID: 153318 [Multi-domain]  Cd Length: 207  Bit Score: 390.16  E-value: 1.77e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVE 98
Cdd:cd07634     1 RERLQCHEIELERTNKFIKELIKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  99 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADSQIGREHQNFYEAS 178
Cdd:cd07634    81 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILEKHLNLSAKKKESHLQRADTQIDREHQNFYEAS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1734342175 179 LEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYK 225
Cdd:cd07634   161 LEYVFKIQEVQEKKKFEFVEPLLAFLQGLFTFYHEGYELAQEFAPYK 207
BAR_RhoGAP_OPHN1-like cd07602
The Bin/Amphiphysin/Rvs (BAR) domain of Oligophrenin1-like Rho GTPase Activating Proteins; BAR ...
 19-225 4.84e-119

The Bin/Amphiphysin/Rvs (BAR) domain of Oligophrenin1-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 oligophrenin1 (OPHN1). Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, and a Rho GAP domain. Some members contain a C-terminal SH3 domain. Vertebrates harbor at least three Rho GAPs in this subfamily including OPHN1, GTPase Regulator Associated with Focal adhesion kinase (GRAF), GRAF2, and an uncharacterized protein called GAP10-like. OPHN1, GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. In addition, OPHN1 is active towards Rac. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domains of OPHN1 and GRAF directly interact with their Rho GAP domains and inhibit their activity. The autoinhibited proteins are able to bind membranes and tubulate liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domains can occur simultaneously.


Pssm-ID: 153286  Cd Length: 207  Bit Score: 343.14  E-value: 4.84e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVE 98
Cdd:cd07602     1 RENLHEHEAELERTNKAIKELIKECKNLISATKNLSKAQRSFAQTLQNFKFECIGETQTDDEIEIAESLKEFGRLIETVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  99 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADSQIGREHQNFYEAS 178
Cdd:cd07602    81 DERDRMLENAEEQLIEPLEKFRKEQIGGAKEEKKKFDKETEKFCSSLEKHLNLSTKKKENQLQEADAQLDMERRNFHQAS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1734342175 179 LEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYK 225
Cdd:cd07602   161 LEYVFKLQEVQERKKFEFVETLLSFMYGWLTFYHQGHEVAKDFKPYL 207
BAR_GRAF cd07636
The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion kinase; ...
 19-225 2.10e-105

The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion kinase; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. GTPase Regulator Associated with Focal adhesion kinase (GRAF), also called Rho GTPase activating protein 26 (ARHGAP26), is a GAP with activity towards RhoA and Cdc42 and is only weakly active towards Rac1. It influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase (FAK), which is a critical component of integrin signaling. GRAF contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. 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 GRAF directly interacts with its Rho GAP domain and inhibits its activity. Autoinhibited GRAF is capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously.


Pssm-ID: 153320 [Multi-domain]  Cd Length: 207  Bit Score: 308.91  E-value: 2.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVE 98
Cdd:cd07636     1 RERLKSHEAELDKTNKFIKELIKDGKSLIAALKNLSSAKRKFADSLNEFKFQCIGDAETDDEICIARSLQEFAAVLRNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  99 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADSQIGREHQNFYEAS 178
Cdd:cd07636    81 DERTRMIENASEVLITPLEKFRKEQIGAAKEAKKKYDKETEKYCAVLEKHLNLSSKKKESQLHEADSQVDLVRQHFYEVS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1734342175 179 LEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYK 225
Cdd:cd07636   161 LEYVFKVQEVQERKMFEFVEPLLAFLQGLFTFYHHGYELAKDFSDFK 207
BAR_3 pfam16746
BAR domain of APPL family; BAR_12 is the BAR coiled-coil domain at the N-terminus of APPL or ...
 6-249 1.52e-99

BAR domain of APPL family; BAR_12 is the BAR coiled-coil domain at the N-terminus of APPL or adaptor protein containing PH domain, PTB domain, and leucine zipper motif proteins in higher eukaryotes. This BAR domain contains four helices whereas the other classical BAR domains contain only three helices. The first three helices form an antiparallel coiled-coil, while the fourth helix, is unique to APPL1. BAR domains take part in many varied biological processes such as fission of synaptic vesicles, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, apoptosis, secretory vesicle fusion, and tissue differentiation.


Pssm-ID: 465256  Cd Length: 235  Bit Score: 294.85  E-value: 1.52e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175   6 LEFSDSYLDSPDFRERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDdeisiaQ 85
Cdd:pfam16746   1 LEFEECLKDSPQFRSLLEEHEAELDELEKKLKKLLKLCKRMIEAGKEYSAAQRLFANSLLDFKFEFIGDEETD------E 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  86 SLKEFARLLIAVEEERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADS 165
Cdd:pfam16746  75 SLKKFSQLLQEMENFHTILLDQAQRTIIKPLENFRKEDLKEVKELKKKFDKASEKLDAALEKNAQLSKKKKPSELEEADN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 166 QIGREHQNFYEASLEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYKQQLQFNLQNTRnnfESTRQE 245
Cdd:pfam16746 155 ELAATRKCFHHASLDYVLQINELQERKKFEILEPLLSFMHAQFTFFHQGYELFKDLEPFMKDLQAQLQQTR---EDTREE 231


                  ....
gi 1734342175 246 VERL 249
Cdd:pfam16746 232 KEEL 235
BAR_GRAF2 cd07635
The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion 2; BAR ...
 19-225 3.12e-96

The Bin/Amphiphysin/Rvs (BAR) domain of GTPase Regulator Associated with Focal adhesion 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. GTPase Regulator Associated with Focal adhesion kinase 2 (GRAF2), also called Rho GTPase activating protein 10 (ARHGAP10) or PS-GAP, is a GAP with activity towards Cdc42 and RhoA which regulates caspase-activated p21-activated protein kinase-2 (PAK-2p34). GRAF2 interacts with PAK-2p34, leading to its stabilization and decrease of cell death. It is highly expressed in skeletal muscle and also interacts with PKNbeta, which is a target of Rho. GRAF2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. 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 the related protein GRAF directly interacts with its Rho GAP domain and inhibits its activity. Autoinhibited GRAF is capable of binding membranes and tubulating liposomes, showing that the membrane-tubulation and GAP-inhibitory functions of the BAR domain can occur simultaneously.


Pssm-ID: 153319  Cd Length: 207  Bit Score: 285.35  E-value: 3.12e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVE 98
Cdd:cd07635     1 RERIRAHEAELERTNRFIKELLKDGKNLIAATKSLSAAQRKFAHSLRDFKFEFIGDAETDDERCIDASLQEFSNFLKNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  99 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADSQIGREHQNFYEAS 178
Cdd:cd07635    81 EQREIMALNVTETLIKPLERFRKEQLGAVKEEKKKFDKETEKNYSLLEKHLNLSAKKKEPQLQEADVQVEQNRQHFYELS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1734342175 179 LEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYK 225
Cdd:cd07635   161 LEYVCKLQEIQERKKFECVEPMLSFFQGVFTFYHQGYELAKDFNHYK 207
BAR_OPHN1 cd07633
The Bin/Amphiphysin/Rvs (BAR) domain of Oligophrenin-1; BAR domains are dimerization, lipid ...
 19-225 3.06e-95

The Bin/Amphiphysin/Rvs (BAR) domain of Oligophrenin-1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Oligophrenin-1 (OPHN1) is a GTPase activating protein (GAP) with activity towards RhoA, Rac, and Cdc42, that is expressed in developing spinal cord and in adult brain areas with high plasticity. It plays a role in regulating the actin cystoskeleton as well as morphology changes in axons and dendrites, and may also function in modulating neuronal connectivity. Mutations in the OPHN1 gene causes X-linked mental retardation associated with cerebellar hypoplasia, lateral ventricle enlargement and epilepsy. OPHN1 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, and a Rho GAP 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: 153317 [Multi-domain]  Cd Length: 207  Bit Score: 283.05  E-value: 3.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVE 98
Cdd:cd07633     1 RERLKCYEQELERTNKFIKDVIKDGNALISAIKEYSSAVQKFSQTLQSFQFDFIGDTLTDDEINIAESFKEFAELLQEVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  99 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADSQIGREHQNFYEAS 178
Cdd:cd07633    81 EERMMMVQNASDLLIKPLENFRKEQIGFTKERKKKFEKDSEKFYSLLDRHVNLSSKKKESQLQEADLQVDKERQNFYESS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1734342175 179 LEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYK 225
Cdd:cd07633   161 LEYVYQIQEVQESKKFDVVEPVLAFLHSLFTSNNLTVELTQDFLPYK 207
BAR-PH_GRAF_family cd01249
GTPase Regulator Associated with Focal adhesion and related proteins Pleckstrin homology (PH) ...
 267-375 3.04e-59

GTPase Regulator Associated with Focal adhesion and related proteins Pleckstrin homology (PH) domain; This hierarchy contains GRAF family members: OPHN1/oligophrenin1, GRAF1 (also called ARHGAP26/Rho GTPase activating protein 26), GRAF2 (also called ARHGAP10/ARHGAP42), AK057372, and LOC129897, all of which are members of the APPL family. OPHN1 is a RhoGAP involved in X-linked mental retardation, epilepsy, rostral ventricular enlargement, and cerebellar hypoplasia. Affected individuals have morphological abnormalities of their brain with enlargement of the cerebral ventricles and cerebellar hypoplasia. OPHN1 negatively regulates RhoA, Cdc42, and Rac1 in neuronal and non-neuronal cells. GRAF1 sculpts the endocytic membranes of the CLIC/GEEC (clathrin-independent carriers/GPI-enriched early endosomal compartments) endocytic pathway. It strongly interacts with dynamin and inhibition of dynamin abolishes CLIC/GEEC endocytosis. GRAF2, GRAF3 and oligophrenin are likely to play similar roles during clathrin-independent endocytic events. GRAF1 mutations are linked to leukaemia. All members are composed of a N-terminal BAR-PH domain, followed by a RhoGAP domain, a proline rich region, and a C-terminal SH3 domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269953  Cd Length: 105  Bit Score: 187.15  E-value: 3.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 267 TMEGYLYVQEKRPLGFTWTKHYCTYDKGSKMFTMSVSDVKASGKmnglvTGSPEMFKLKSCIRRKTDSIDKRFCFDIEVV 346
Cdd:cd01249     1 TKEGYLYLQEKKPLGSTWTKHYCTYRKESKMFTMIPYNQQSSGK-----LGTTEVVTLKSCVRRKTDSIDRRFCFDIEVV 75

                          90       100
                  ....*....|....*....|....*....
gi 1734342175 347 ERHGIITLQAFSEANRKLWLEAMDGKEPV 375
Cdd:cd01249    76 DRPTVLTLQALSEEDRKLWLEAMDGKEPI 104
BAR_ACAPs cd07603
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain ...
 19-224 4.23e-21

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of ACAPs (ArfGAP with Coiled-coil, ANK repeat and PH domain containing proteins), which are Arf GTPase activating proteins (GAPs) containing an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. Vertebrates contain at least three members, ACAP1, ACAP2, and ACAP3. ACAP1 and ACAP2 are Arf6-specific GAPs, involved in the regulation of endocytosis, phagocytosis, cell adhesion and migration, by mediating Arf6 signaling. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153287  Cd Length: 200  Bit Score: 90.05  E-value: 4.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAEtddeisIAQSLKEFARLLIAVE 98
Cdd:cd07603     1 RASLEQVEADVSELETRLEKLLKLCNGMVDSGKTYVNANSLFVNSLNDLSDYFRDDSL------VQNCLNKFIQALQEMN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  99 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSaKKKESHLQEADSQIGREHQNFYEAS 178
Cdd:cd07603    75 NFHTILLDQAQRTVSTQLQNFVKEDIKKVKESKKHFEKISDDLDNALVKNAQAP-RSKPQEAEEATNILTATRSCFRHTA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1734342175 179 LEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPY 224
Cdd:cd07603   154 LDYVLQINVLQAKKRHEILSTLLSYMHAQFTFFHQGYDLLEDLEPY 199
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 28-224 2.00e-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: 87.89  E-value: 2.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  28 ELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDdeisIAQSLKEFARLLIAVEEERRRLIQN 107
Cdd:cd07307     1 KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSNTD----LGEALEKFGKIQKELEEFRDQLEQK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 108 ANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESH-LQEADSQIGREHQNFYEASLEYVFKIQ 186
Cdd:cd07307    77 LENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSkLAEAEEELQEAKEKYEELREELIEDLN 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1734342175 187 EVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPY 224
Cdd:cd07307   157 KLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
BAR_ACAP3 cd07637
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain ...
 36-224 8.00e-17

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ACAP3 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 3), also called centaurin beta-5, is presumed to be an Arf GTPase activating protein (GAP) based on its similarity to the Arf6-specific GAPs ACAP1 and ACAP2. The specific function of ACAP3 is still unknown. ACAP3 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: 153321  Cd Length: 200  Bit Score: 78.12  E-value: 8.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  36 IKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAetddeiSIAQSLKEFARLLIAVEEERRRLIQNANDVLIAP 115
Cdd:cd07637    18 LDKLVKLCSGMIEAGKAYATTNKLFVSGIRDLSQQCKKDE------MISECLDKFGDSLQEMVNYHMILFDQAQRSVRQQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 116 LEKFRKEQIGAAKDGKKKFDKESEKYYSILDKhlNLSAKKKESH-LQEADSQIGREHQNFYEASLEYVFKIQEVQEKKKF 194
Cdd:cd07637    92 LHSFVKEDVRKFKETKKQFDKVREDLEIALVK--NAQAPRHKPHeVEEATSTLTITRKCFRHLALDYVLQINVLQAKKKF 169

                         170       180       190
                  ....*....|....*....|....*....|
gi 1734342175 195 EFVEPLLSFLQGLFTFYHEGYELAQEFAPY 224
Cdd:cd07637   170 EILDSMLSFMHAQYTFFQQGYSLLHELDPY 199
BAR_ACAP2 cd07638
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain ...
 46-224 2.71e-15

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ACAP2 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 2), also called centaurin beta-2, is an Arf6-specific GTPase activating protein (GAP) which mediates Arf6 signaling. Arf6 is involved in the regulation of endocytosis, phagocytosis, cell adhesion and migration. ACAP2 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: 153322  Cd Length: 200  Bit Score: 73.88  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  46 LIGALRNLSMAVQKFSQSLQDfqfecIGDAETDDEIsIAQSLKEFARLLIAVEEERRRLIQNANDVLIAPLEKFRKEQIG 125
Cdd:cd07638    28 MIDAGKAFCQANKQFMNGIRD-----LAQYSSKDAV-IETSLTKFSDTLQEMINYHTILFDQAQRSIKAQLQTFVKEDLR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 126 AAKDGKKKFDKESEKYYSILDKHLNLSaKKKESHLQEADSQIGREHQNFYEASLEYVFKIQEVQEKKKFEFVEPLLSFLQ 205
Cdd:cd07638   102 KFKDAKKQFDKVSEEKENALVKNAQVQ-RNKQHEVEEATNILTATRKCFRHIALDYVLQINVLQSKRRSEILKSMLSFMY 180

                         170
                  ....*....|....*....
gi 1734342175 206 GLFTFYHEGYELAQEFAPY 224
Cdd:cd07638   181 AHLTFFHQGYDLFSELGPY 199
BAR_SFC_plant cd07606
The Bin/Amphiphysin/Rvs (BAR) domain of the plant protein SCARFACE (SFC); BAR domains are ...
 30-224 3.37e-11

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: 62.12  E-value: 3.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  30 ERTNKFIKELLKdgslLIGALRNLSMAVQKFSQSLQDFQfecigdAETDDEISIAQSLKEFARLLIAVEE---ERRRLIQ 106
Cdd:cd07606    15 DRSLKLYKGCRK----YRDALGEAYDGDSAFAESLEEFG------GGHDDPISVAVGGPVMTKFTSALREigsYKEVLRS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 107 NANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADSQIGREHQNFYEASLEYVFKIQ 186
Cdd:cd07606    85 QVEHMLNDRLAQFADTDLQEVKDARRRFDKASLDYEQARSKFLSLTKDAKPEILAAAEEDLGTTRSAFETARFDLMNRLH 164

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1734342175 187 EVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPY 224
Cdd:cd07606   165 AADARKRVEFLERLSGSMDAHLAFFKSGYELLRQLEPY 202
BAR_ACAP1 cd07639
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain ...
 19-225 1.36e-10

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ACAP1 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 1), also called centaurin beta-1, is an Arf6-specific GTPase activating protein (GAP) which mediates Arf6 signaling. Arf6 is involved in the regulation of endocytosis, phagocytosis, cell adhesion and migration. ACAP1 also participates in the cargo sorting and recycling of the transferrin receptor and integrin beta1. It may also play a role in innate immune responses. ACAP1 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: 153323  Cd Length: 200  Bit Score: 60.31  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAetddeiSIAQSLKEFARLLIAVE 98
Cdd:cd07639     1 RAAIEEVEAEVSELETRLEKLVKLGSGMLEGGRHYCAASRAFVDGLCDLAHHGPKDP------MMAECLEKFSDGLNHIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  99 EERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILdKHLNLSAKKKESHLQEADSQIGREHQNFYEAS 178
Cdd:cd07639    75 DSHAELLEATQFSFKQQLQLLVKEDLRGFRDARKEFERGAESLEAAL-QHNAETPRRKAQEVEEAAAALLGARATFRDRA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1734342175 179 LEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYK 225
Cdd:cd07639   154 LDYALQINVIEDKKKFDILEFMLQLMEAQASFFQQGHEALSALHQYR 200
BAR_ASAPs cd07604
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain ...
 20-228 4.08e-10

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of ASAPs (ArfGAP with SH3 domain, ANK repeat and PH domain containing proteins), which are Arf GTPase activating proteins (GAPs) with similarity to ACAPs (ArfGAP with Coiled-coil, ANK repeat and PH domain containing proteins) in that they contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, and ankyrin (ANK) repeats. However, ASAPs contain an additional C-terminal SH3 domain. ASAPs function in regulating cell growth, migration, and invasion. Vertebrates contain at least three members, ASAP1, ASAP2, and ASAP3. ASAP1 and ASAP2 shows GTPase activating protein (GAP) activity towards Arf1 and Arf5. They do not show GAP activity towards Arf6, but is able to mediate Arf6 signaling by binding stably to GTP-Arf6. ASAP3 is an Arf6-specific GAP. 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 ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains.


Pssm-ID: 153288  Cd Length: 215  Bit Score: 58.96  E-value: 4.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  20 ERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSqslqdfqfeciGDAETDDEISIAQSLKEFARLLIAVEE 99
Cdd:cd07604     9 ESLEGDRVGLQKLKKAVKAIHNSGLAHVENELQFAEALEKLG-----------SKALSREEEDLGAAFLKFSVFTKELAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 100 ERRRLIQNANDVLIAPLEKFRKEQI-GAAKDGKKKFDKeSEKYYSILDKHLNlSAKKKESHLQ----------EADSQIG 168
Cdd:cd07604    78 LFKNLMQNLNNIIMFPLDSLLKGDLkGSKGDLKKPFDK-AWKDYETKASKIE-KEKKQLAKEAgmirteitgaEIAEEME 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 169 REHQNFYEASLEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYKQQL 228
Cdd:cd07604   156 KERRMFQLQMCEYLIKVNEIKTKKGVDLLQHLVEYYHAQNSYFQDGLKVIEHFRPYIEKL 215
BAR_APPL2 cd07632
The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor protein, Phosphotyrosine interaction, PH ...
 35-217 1.74e-09

The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing (APPL) proteins are effectors of the small GTPase Rab5 that function in endosome-mediated signaling. They contain BAR, pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains. They form homo- and hetero-oligomers that are mediated by their BAR domains. Vertebrates contain two APPL proteins, APPL1 and APPL2. Both APPL proteins interact with the transcriptional repressor Reptin, acting as activators of beta-catenin/TCF-mediated trancription. APPL2 is essential for cell proliferation. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153316  Cd Length: 215  Bit Score: 57.35  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  35 FIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEIsiAQSLKEFARLLIAVEEERRRLIQNANDVLIA 114
Cdd:cd07632    17 YTNQLLQAMQRVYGAQNEMCLATQQLSKQLLAYEKQNFALGKGDEEV--ISTLQYFAKVVDELNVLHSELAKQLADTMVL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 115 PLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKK-ESHLQEADSQIGREHQNFYEASLEYVFKIQEVQEKKK 193
Cdd:cd07632    95 PIIQFREKDLTEVSTLKDLFGIASNEHDLSMAKYSRLPKKREnEKVKAEVAKEVAYSRRKQHLSSLQYYCALNALQYRKR 174

                         170       180
                  ....*....|....*....|....
gi 1734342175 194 FEFVEPLLSFLQGLFTFYHEGYEL 217
Cdd:cd07632   175 VAMLEPMLGYTHGQINFFKKGAEL 198
BAR_ASAP3 cd07640
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain ...
 102-228 1.88e-08

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP3 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 3) is also known as ACAP4 (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein 4), DDEFL1 (Development and Differentiation Enhancing Factor-Like 1), or centaurin beta-6. It is an Arf6-specific GTPase activating protein (GAP) and is co-localized with Arf6 in ruffling membranes upon EGF stimulation. ASAP3 is implicated in the pathogenesis of hepatocellular carcinoma and plays a role in regulating cell migration and invasion. ASAP3 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. 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 the related protein ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains.


Pssm-ID: 153324  Cd Length: 213  Bit Score: 54.23  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 102 RRLIQNANDVLIAPLEKFRKEQIgaaKDGKKKFDKESEKYYSILDKHL-----NLSAKKKESHLQEADSQ-----IGREH 171
Cdd:cd07640    80 KNLVQNLNNIVSFPLDSLLKGQL---RDGRLESKKQMEKAWKDYEAKIgklekERREKQKQHGLIRLDMTdtaedMQRER 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734342175 172 QNFYEASLEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYKQQL 228
Cdd:cd07640   157 RNFQLHMCEYLLKAQESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQNLGPFIEKL 213
PH_ACAP cd13250
ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP ...
 268-371 6.90e-08

ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270070  Cd Length: 98  Bit Score: 49.91  E-value: 6.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 268 MEGYLYVQEKRPLGfTWTKHYCTYDKG---------SKMFTMSVSDvkasgkmnglvtgspemfkLKSCIRRKTDSIDKR 338
Cdd:cd13250     1 KEGYLFKRSSNAFK-TWKRRWFSLQNGqlyyqkrdkKDEPTVMVED-------------------LRLCTVKPTEDSDRR 60

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1734342175 339 FCFdiEVVERHGIITLQAFSEANRKLWLEAMDG 371
Cdd:cd13250    61 FCF--EVISPTKSYMLQAESEEDRQAWIQAIQS 91
BAR_APPL1 cd07631
The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor protein, Phosphotyrosine interaction, PH ...
 19-216 2.20e-07

The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing (APPL) proteins are effectors of the small GTPase Rab5 that function in endosome-mediated signaling. They contain BAR, pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains. They form homo- and hetero-oligomers that are mediated by their BAR domains. Vertebrates contain two APPL proteins, APPL1 and APPL2. APPL1 interacts with diverse receptors (e.g. NGF receptor TrkA, FSHR, adiponectin receptors) and signaling proteins (e.g. Akt, PI3K), and may function as an adaptor linked to many distinct signaling pathways. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153315  Cd Length: 215  Bit Score: 51.24  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQ---FECIGDaetdDEIsIAQSLKEFARLLI 95
Cdd:cd07631     1 RSLLGVFEEDAAAISNYFNQLFQAMHRIYDAQNELSAATHLTSKLLKEYEkqrFPLGGD----DEV-MSSTLQQFSKVID 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  96 AVEEERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQ-EADSQIGREHQNF 174
Cdd:cd07631    76 ELSSCHAVLSTQLADAMMFPITQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKRRENEKVKyEVTEDVYTSRKKQ 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1734342175 175 YEASLEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYE 216
Cdd:cd07631   156 HQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSE 197
BAR_APPL cd07601
The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor protein, Phosphotyrosine interaction, PH ...
 19-217 2.35e-07

The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Adaptor protein, Phosphotyrosine interaction, PH domain and Leucine zipper containing (APPL) proteins are effectors of the small GTPase Rab5 that function in endosome-mediated signaling. They contain BAR, pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains. They form homo- and hetero-oligomers that are mediated by their BAR domains, and are localized to cytoplasmic membranes. Vertebrates contain two APPL proteins, APPL1 and APPL2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153285  Cd Length: 215  Bit Score: 51.06  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  19 RERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQ---FECIGDaetdDEISIAqSLKEFARLLI 95
Cdd:cd07601     1 RSLLNVFEEDALQLSSYMNQLLQACKRVYDAQNELKSATQALSKKLGEYEkqkFELGRD----DEILVS-TLKQFSKVVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  96 AVEEERRRLIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQ-EADSQIGREHQNF 174
Cdd:cd07601    76 ELSTMHSTLSSQLADTVLHPISQFMESDLAEIMTLKELFKAASNDHDGVLSKYSRLSKKRENTKVKiEVNDEVYACRKKQ 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1734342175 175 YEASLEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYEL 217
Cdd:cd07601   156 HQTAMNYYCALNLLQYKKTTALLEPMIGYLQAQIAFFKMGPEM 198
BAR_ASAP2 cd07642
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain ...
 58-228 8.90e-07

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP2 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 2) is also known as DDEF2 (Development and Differentiation Enhancing Factor 2), AMAP2, centaurin beta-3, or PAG3. ASAP2 mediates the functions of Arf GTPases vial dual mechanisms: it exhibits GTPase activating protein (GAP) activity towards class I (Arf1) and II (Arf5) Arfs; and binds class III Arfs (GTP-Arf6) stably without GAP activity. It binds paxillin and is implicated in Fcgamma receptor-mediated phagocytosis in macrophages and in cell migration. ASAP2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. 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 the related protein ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains.


Pssm-ID: 153326  Cd Length: 215  Bit Score: 49.26  E-value: 8.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  58 QKFSQSLQDFQFECIgdaeTDDEISIAQSLKEFARLLIAVEEERRRLIQNANDVLIAPLEKFRKEQI-GAAKDGKKKFDK 136
Cdd:cd07642    40 EQYTQALEKFGSNCV----CRDDPDLGSAFLKFSVFTKELTALFKNLVQNMNNIITFPLDSLLKGDLkGVKGDLKKPFDK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 137 ESEKYYSILDKhlnLSAKKKESHLQ-----------EADSQIGREHQNFYEASLEYVFKIQEVQEKKKFEFVEPLLSFLQ 205
Cdd:cd07642   116 AWKDYETKVTK---IEKEKKEHAKMhgmirteisgaEIAEEMEKERRFFQLQMCEYLLKVNEIKIKKGVDLLQNLIKYFH 192

                         170       180
                  ....*....|....*....|...
gi 1734342175 206 GLFTFYHEGYELAQEFAPYKQQL 228
Cdd:cd07642   193 AQCNFFQDGLKAVETLKPSIEKL 215
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 267-369 3.29e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 42.54  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  267 TMEGYLYVQEKRPLGfTWTKHYCTYDKGSKMFTMSVSDVKASGKmnglvtgsPEMFKLKSCIRR---KTDSIDKRFCFDI 343
Cdd:smart00233   2 IKEGWLYKKSGGGKK-SWKKRYFVLFNSTLLYYKSKKDKKSYKP--------KGSIDLSGCTVReapDPDSSKKPHCFEI 72

                           90       100
                   ....*....|....*....|....*.
gi 1734342175  344 EVVERHgIITLQAFSEANRKLWLEAM 369
Cdd:smart00233  73 KTSDRK-TLLLQAESEEEREKWVEAL 97
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 268-369 3.77e-04

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 39.06  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 268 MEGYLYVQEKRPLgFTWTKHYCTYDKGSKMFTMSVSDVKASGKMnglvtgspEMFKLKSCIRRKTDSIDKRFCFDIeVVE 347
Cdd:cd00821     1 KEGYLLKRGGGGL-KSWKKRWFVLFEGVLLYYKSKKDSSYKPKG--------SIPLSGILEVEEVSPKERPHCFEL-VTP 70

                          90       100
                  ....*....|....*....|..
gi 1734342175 348 RHGIITLQAFSEANRKLWLEAM 369
Cdd:cd00821    71 DGRTYYLQADSEEERQEWLKAL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 267-369 5.33e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 39.08  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 267 TMEGYLYVQEKRpLGFTWTKHYCTYDKGSKMFTMSVSDVKASGKMNglvtgspeMFKLKSCIRR---KTDSIDKRFCFDI 343
Cdd:pfam00169   2 VKEGWLLKKGGG-KKKSWKKRYFVLFDGSLLYYKDDKSGKSKEPKG--------SISLSGCEVVevvASDSPKRKFCFEL 72

                          90       100
                  ....*....|....*....|....*...
gi 1734342175 344 EVVERHGI--ITLQAFSEANRKLWLEAM 369
Cdd:pfam00169  73 RTGERTGKrtYLLQAESEEERKDWIKAI 100
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
 26-183 2.54e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153274  Cd Length: 225  Bit Score: 38.89  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  26 EIELERTNKF---IKELLKDGSLLIGALRNLSMAVQKFSQSLQDfqfecIGDAETDDEISiaQSLKEFARLLIAVEEERR 102
Cdd:cd07590    14 EREVQKLQQLestTKKLYKDMKKYIEAVLALSKAEQRLSQDLAS-----GPLCEDNDELR--NLVEALDSVTTQLDKTVQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 103 RLIQNANDVLIAPLEKFRKE--QIGAAKDGKKKFDKESEKYYSILDK----------HLNLSAKKKESHLQEAD-----S 165
Cdd:cd07590    87 ELVNLIQKTFIEPLKRLRSVfpSVNAAIKRREQSLQEYERLQAKVEKlaekektgpnLAKLEQAEKALAAARADfekqnI 166

                         170
                  ....*....|....*...
gi 1734342175 166 QIGREHQNFYEASLEYVF 183
Cdd:cd07590   167 KLLEELPKFYNGRTDYFQ 184
BAR_ASAP1 cd07641
The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain ...
 18-228 3.08e-03

The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. ASAP1 (ArfGAP with SH3 domain, ANK repeat and PH domain containing protein 1) is also known as DDEF1 (Development and Differentiation Enhancing Factor 1), AMAP1, centaurin beta-4, or PAG2. ASAP1 is an Arf GTPase activating protein (GAP) with activity towards Arf1 and Arf5 but not Arf6 However, it has been shown to bind GTP-Arf6 stably without GAP activity. It has been implicated in cell growth, migration, and survival, as well as in tumor invasion and malignancy. It binds paxillin and cortactin, two components of invadopodia which are essential for tumor invasiveness. It also binds focal adhesion kinase (FAK) and the SH2/SH3 adaptor CrkL. ASAP1 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. 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 ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains.


Pssm-ID: 153325  Cd Length: 215  Bit Score: 38.50  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  18 FRERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAEtddeISIAQSLKEFARLLiav 97
Cdd:cd07641     7 LEEALDQDRTALQKVKKSVKAIYNSGQDHVQNEENYAQALDKFGSNFLSRDNPDLGTAF----VKFSTLTKELSTLL--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  98 eeerRRLIQNANDVLIAPLEKFRKEQI-GAAKDGKKKFDKESEKY---YSILDKHLNLSAK-----KKESHLQEADSQIG 168
Cdd:cd07641    80 ----KNLLQGLSHNVIFTLDSLLKGDLkGVKGDLKKPFDKAWKDYetkFTKIEKEKREHAKqhgmiRTEITGAEIAEEME 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 169 REHQNFYEASLEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYKQQL 228
Cdd:cd07641   156 KERRLFQLQMCEYLIKVNEIKTKKGVDLLQNLIKYYHAQCNFFQDGLKTADKLKQYIEKL 215
BAR_SIP3_fungi cd07609
The Bin/Amphiphysin/Rvs (BAR) domain of fungal Snf1p-interacting protein 3; BAR domains are ...
 104-189 3.34e-03

The Bin/Amphiphysin/Rvs (BAR) domain of fungal Snf1p-interacting protein 3; 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 group is composed of mostly uncharacterized fungal proteins with similarity to Saccharomyces cerevisiae Snf1p-interacting protein 3 (SIP3). These proteins contain an N-terminal BAR domain followed by a Pleckstrin Homology (PH) domain. SIP3 interacts with SNF1 protein kinase and activates transcription when anchored to DNA. It may function in the SNF1 pathway. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153293  Cd Length: 214  Bit Score: 38.42  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175 104 LIQNANDVLIAPLEKFRKEQIGAAKDGKKKFDKESEKYYSILDKHLNLSAKKKESHLQEADSQIGREHQNFYEASLEYVF 183
Cdd:cd07609    82 ALKGNDSLILDPLRSFVKSDIRPYKELRKNFEYYQRKYDSMLARYVAQSKTKEPSSLREDAFQLFEARKAYLKASLDLVI 161


                  ....*.
gi 1734342175 184 KIQEVQ 189
Cdd:cd07609   162 AIPQLR 167
BAR_ArfGAP_fungi cd07608
The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized fungal Arf GAP proteins; BAR domains ...
 28-161 8.87e-03

The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized fungal Arf GAP 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 group is composed of uncharacterized fungal proteins containing an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, and an Arf GTPase Activating Protein (GAP) domain. These proteins may play roles in Arf-mediated functions involving membrane dynamics. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153292  Cd Length: 192  Bit Score: 36.95  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734342175  28 ELERTNK----FIKELLKDGSLLIGALRNLsmAVQKFSQSLQDFQFEcigdaeTDDEISIAQSLKEFARLLIAVEEERRR 103
Cdd:cd07608     5 NLERKTRllrsYLKRLIKRIVKLIEAQDQL--VDLEFNELLSEAKFK------NDFNVALDSYFDPFLLNLAFFLRDVCQ 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1734342175 104 LIQNandVLIAPLEKF-RKEQIGAAKDGKKKFDKESEKYYSILDKHL--NLSAKKKESHLQ 161
Cdd:cd07608    77 DLQL---KKIEPLLKIySINDIKELSDKKKDFEEESKDYYSWLSKYLsnESDKKRPDSKLL 134
 
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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