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Conserved domains on  [gi|19112281|ref|NP_595489|]
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BAR adaptor protein Hob3 [Schizosaccharomyces pombe]

Protein Classification

BAR domain-containing protein( domain architecture ID 10166122)

BAR (Bin/Amphiphysin/Rvs) domain-containing protein may bind membranes and detect membrane curvature; similar to Saccharomyces cerevisiae reduced viability upon starvation protein 161 (RVS161), a component of a cytoskeletal structure that is required for the formation of endocytic vesicles at the plasma membrane level

CATH:  1.20.1270.60
Gene Ontology:  GO:0097753|GO:0140090
PubMed:  15649145|30456600|14993925|16524918|19379681
SCOP:  4001895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_Rvs161p cd07591
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 20-241 2.65e-149

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 161 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 161 (Rvs161p) and Schizosaccharomyces pombe Hob3 (homolog of Bin3). S. cerevisiae Rvs161p plays a role in regulating cell polarity, actin cytoskeleton polarization, vesicle trafficking, endocytosis, bud formation, and the mating response. It forms a heterodimer with another BAR domain protein Rvs167p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. S. pombe Hob3 is important in regulating filamentous actin localization and may be required in activating Cdc42 and recruiting it to cell division sites. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153275  Cd Length: 224  Bit Score: 415.97  E-value: 2.65e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  20 KTGHVERTVDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQTRIANTIDAFYGDAGSKD--GVSAYYRQVVED 97
Cdd:cd07591   1 KTGQVERTVDREFEFEERRYRTMEKASTKLQKEAKGYLDSLRALTSSQARIAETISSFYGDAGDKDgaMLSQEYKQAVEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  98 LDADTVKELDGPFRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKLVDKPSNDTTKLPRTEKEAAMAKEVY 177
Cdd:cd07591  81 LDAETVKELDGPYRQTVLDPIGRFNSYFPEINEAIKKRNHKLLDYDAARAKVRKLIDKPSEDPTKLPRAEKELDEAKEVY 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112281 178 ETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCREGYEKMAQVQQYFDNSVREDYSNGLL 241
Cdd:cd07591 161 ETLNDQLKTELPQLVDLRIPYLDPSFEAFVKIQLRFFTEGYERLAQVQRYLDAQTREDYANGQL 224
 
Name Accession Description Interval E-value
BAR_Rvs161p cd07591
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 20-241 2.65e-149

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 161 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 161 (Rvs161p) and Schizosaccharomyces pombe Hob3 (homolog of Bin3). S. cerevisiae Rvs161p plays a role in regulating cell polarity, actin cytoskeleton polarization, vesicle trafficking, endocytosis, bud formation, and the mating response. It forms a heterodimer with another BAR domain protein Rvs167p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. S. pombe Hob3 is important in regulating filamentous actin localization and may be required in activating Cdc42 and recruiting it to cell division sites. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153275  Cd Length: 224  Bit Score: 415.97  E-value: 2.65e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  20 KTGHVERTVDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQTRIANTIDAFYGDAGSKD--GVSAYYRQVVED 97
Cdd:cd07591   1 KTGQVERTVDREFEFEERRYRTMEKASTKLQKEAKGYLDSLRALTSSQARIAETISSFYGDAGDKDgaMLSQEYKQAVEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  98 LDADTVKELDGPFRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKLVDKPSNDTTKLPRTEKEAAMAKEVY 177
Cdd:cd07591  81 LDAETVKELDGPYRQTVLDPIGRFNSYFPEINEAIKKRNHKLLDYDAARAKVRKLIDKPSEDPTKLPRAEKELDEAKEVY 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112281 178 ETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCREGYEKMAQVQQYFDNSVREDYSNGLL 241
Cdd:cd07591 161 ETLNDQLKTELPQLVDLRIPYLDPSFEAFVKIQLRFFTEGYERLAQVQRYLDAQTREDYANGQL 224
BAR smart00721
BAR domain;
5-229 9.71e-68

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 209.55  E-value: 9.71e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281      5 GFKKAVNRAGTSVMMKTGHVERT-VDREFETEERRYRTMESAAKKLQKEAKGYL---DALRAMTASQTRIANTIDAFY-- 78
Cdd:smart00721   1 GFKKQFNRAKQKVGEKVGKAEKTkLDEDFEELERRFDTTEAEIEKLQKDTKLYLqpnPAVRAKLASQKKLSKSLGEVYeg 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281     79 GDAGSKDGVSAYYRQVVEDLDADTVKELDGP------FRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKL 152
Cdd:smart00721  81 GDDGEGLGADSSYGKALDKLGEALKKLLQVEeslsqvKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281    153 ---VDKPSNDttKLPRTEKEAAMAKEVYETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCREGYEKMAQVQQYFD 229
Cdd:smart00721 161 kksKEKKKDE--KLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQLD 238
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 6-230 2.41e-59

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: 187.93  E-value: 2.41e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281     6 FKKAVNRAGTSVMMKTGHVERT-VDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQ-------TRIANTIDAF 77
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTkLDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQtvleqpeELLAESMIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281    78 YGDAGSKDGVSA---YYRQVVEDLdADTVKELDGPFRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKLVD 154
Cdd:pfam03114  81 GKDLGEDSSFGKaleDYGEALKRL-AQLLEQLDDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112281   155 KPSNDTTKLPRTEKEAAMAKEVYETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCREGYEKMAQVQQYFDN 230
Cdd:pfam03114 160 KKSSKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
 
Name Accession Description Interval E-value
BAR_Rvs161p cd07591
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 20-241 2.65e-149

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 161 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 161 (Rvs161p) and Schizosaccharomyces pombe Hob3 (homolog of Bin3). S. cerevisiae Rvs161p plays a role in regulating cell polarity, actin cytoskeleton polarization, vesicle trafficking, endocytosis, bud formation, and the mating response. It forms a heterodimer with another BAR domain protein Rvs167p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. S. pombe Hob3 is important in regulating filamentous actin localization and may be required in activating Cdc42 and recruiting it to cell division sites. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153275  Cd Length: 224  Bit Score: 415.97  E-value: 2.65e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  20 KTGHVERTVDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQTRIANTIDAFYGDAGSKD--GVSAYYRQVVED 97
Cdd:cd07591   1 KTGQVERTVDREFEFEERRYRTMEKASTKLQKEAKGYLDSLRALTSSQARIAETISSFYGDAGDKDgaMLSQEYKQAVEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  98 LDADTVKELDGPFRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKLVDKPSNDTTKLPRTEKEAAMAKEVY 177
Cdd:cd07591  81 LDAETVKELDGPYRQTVLDPIGRFNSYFPEINEAIKKRNHKLLDYDAARAKVRKLIDKPSEDPTKLPRAEKELDEAKEVY 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112281 178 ETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCREGYEKMAQVQQYFDNSVREDYSNGLL 241
Cdd:cd07591 161 ETLNDQLKTELPQLVDLRIPYLDPSFEAFVKIQLRFFTEGYERLAQVQRYLDAQTREDYANGQL 224
BAR smart00721
BAR domain;
5-229 9.71e-68

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 209.55  E-value: 9.71e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281      5 GFKKAVNRAGTSVMMKTGHVERT-VDREFETEERRYRTMESAAKKLQKEAKGYL---DALRAMTASQTRIANTIDAFY-- 78
Cdd:smart00721   1 GFKKQFNRAKQKVGEKVGKAEKTkLDEDFEELERRFDTTEAEIEKLQKDTKLYLqpnPAVRAKLASQKKLSKSLGEVYeg 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281     79 GDAGSKDGVSAYYRQVVEDLDADTVKELDGP------FRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKL 152
Cdd:smart00721  81 GDDGEGLGADSSYGKALDKLGEALKKLLQVEeslsqvKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281    153 ---VDKPSNDttKLPRTEKEAAMAKEVYETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCREGYEKMAQVQQYFD 229
Cdd:smart00721 161 kksKEKKKDE--KLAKAEEELRKAKQEFEESNAQLVEELPQLVASRVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQLD 238
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 6-230 2.41e-59

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: 187.93  E-value: 2.41e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281     6 FKKAVNRAGTSVMMKTGHVERT-VDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQ-------TRIANTIDAF 77
Cdd:pfam03114   1 LKKQFNRASQLLGEKVGGAEKTkLDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGARAKQtvleqpeELLAESMIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281    78 YGDAGSKDGVSA---YYRQVVEDLdADTVKELDGPFRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKLVD 154
Cdd:pfam03114  81 GKDLGEDSSFGKaleDYGEALKRL-AQLLEQLDDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112281   155 KPSNDTTKLPRTEKEAAMAKEVYETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCREGYEKMAQVQQYFDN 230
Cdd:pfam03114 160 KKSSKAKDESQAEEELRKAQAKFEESNEQLKALLPNLLSLEVEFVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
 27-235 1.90e-31

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: 115.93  E-value: 1.90e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  27 TVDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQTRI---------ANTIDAFygdagskdgvsayyRQVVED 97
Cdd:cd07590   8 TVDRELEREVQKLQQLESTTKKLYKDMKKYIEAVLALSKAEQRLsqdlasgplCEDNDEL--------------RNLVEA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  98 LDA------DTVKELDGPFRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKLVDK---PSNDTtKLPRTEK 168
Cdd:cd07590  74 LDSvttqldKTVQELVNLIQKTFIEPLKRLRSVFPSVNAAIKRREQSLQEYERLQAKVEKLAEKektGPNLA-KLEQAEK 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112281 169 EAAMAKEVYETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCREGYEKMAQVQQYFDNSVRED 235
Cdd:cd07590 153 ALAAARADFEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYYSQSTKIFTQLAPNLDNPIEQL 219
BAR_Rvs167p cd07599
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 29-221 7.26e-24

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 167 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 167 (Rvs167p) and Schizosaccharomyces pombe Hob1 (homolog of Bin1). S. cerevisiae Rvs167p plays a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. It forms a heterodimer with another BAR domain protein Rvs161p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. Rvs167p also interacts with the GTPase activating protein (GAP) Gyp5p, which is involved in ER to Golgi vesicle trafficking. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153283 [Multi-domain]  Cd Length: 216  Bit Score: 95.78  E-value: 7.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  29 DREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQTRIAntiDAFYGD----AGSKDGVSAY------------YR 92
Cdd:cd07599   1 DEQFEELEKDFKSLEKSLKKLIEQSKAFRDSWRSILTHQIAFA---KEFAELydpiVGPKESVGSHpapestlarlsrYV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  93 QVVEDLDADTVKELDgPFRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKV----QKLVDKPSNDTTKLPRTEK 168
Cdd:cd07599  78 KALEELKKELLEELE-FFEERVILPAKELKKYIKKIRKTIKKRDHKKLDYDKLQNKLnkllQKKKELSLKDEKQLAKLER 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 19112281 169 EAAMAKEVYETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCREGYEKM 221
Cdd:cd07599 157 KLEEAKEEYEALNELLKSELPKLLALADEFLPPLFKSFYYIQLNIYYTLHEYL 209
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 38-227 6.88e-22

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: 89.81  E-value: 6.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  38 RYRTMESAAKKLQKEAKGYLDALRAMTASQTRIANTIDAFYGDAGSKDGVSA-----YYRQVVEDLDaDTVKELDGPFRT 112
Cdd:cd07307   1 KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSNTDLgealeKFGKIQKELE-EFRDQLEQKLEN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281 113 TVLDPISRF-CSYFPDINAAITKRNHKLLDHDAMRAKVQKLVDKPSNDTtKLPRTEKEAAMAKEVYETLNNQLVSELPQL 191
Cdd:cd07307  80 KVIEPLKEYlKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSS-KLAEAEEELQEAKEKYEELREELIEDLNKL 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19112281 192 IALRVPYLDPSFEALVKIQLRFCREGYEKMAQVQQY 227
Cdd:cd07307 159 EEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
BAR_Amphiphysin cd07588
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysins; BAR domains are dimerization, lipid ...
 20-216 4.35e-20

The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. This subfamily is composed of different isoforms of amphiphysin and Bridging integrator 2 (Bin2). Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin and synaptojanin. They function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Bin2 is mainly expressed in hematopoietic cells and is upregulated during granulocyte differentiation. The N-BAR domains of amphiphysins form a curved dimer with a positively-charged concave face that can drive membrane bending and curvature.


Pssm-ID: 153272  Cd Length: 211  Bit Score: 85.48  E-value: 4.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  20 KTGHVERTVDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQTRIANTI-DAFYGDAGSKDGVSAyyrqVVEDL 98
Cdd:cd07588   2 KLGKADETRDEVFDEHVNNFNKQQASANRLQKDLKNYLNSVRAMKQASKTLSETLkELYEPDWPGREHLAS----IFEQL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  99 D---ADTVKELDgpfrTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKLVDKPSNDTTKLPRTEKEAAMAKE 175
Cdd:cd07588  78 DllwNDLEEKLS----DQVLGPLTAYQSQFPEVKKRIAKRGRKLVDYDSARHNLEALKAKKKVDDQKLTKAEEELQQAKK 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19112281 176 VYETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCRE 216
Cdd:cd07588 154 VYEELNTELHEELPALYDSRIAFYVDTLQSIFAAESVFHKE 194
BAR_Amphiphysin_I_II cd07611
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, ...
 20-216 1.24e-17

The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin and synaptojanin. They function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature. Human autoantibodies to amphiphysin-1 hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Mutations in amphiphysin-2 (BIN1) are associated with autosomal recessive centronuclear myopathy.


Pssm-ID: 153295  Cd Length: 211  Bit Score: 78.83  E-value: 1.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  20 KTGHVERTVDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQTRIANTIDAFYG-DAGSKDGVsayyRQVVEDL 98
Cdd:cd07611   2 KLGKADETKDEQFEEYVQNFKRQETEGTRLQRELRAYLAAIKGMQEASKKLTESLHEVYEpDWYGRDDV----KTIGEKC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  99 DA---DTVKEL-DGPFRTtvldpISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKLVDKPSNDTTKLPRTEKEAAMAK 174
Cdd:cd07611  78 DLlweDFHQKLvDGALLT-----LDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQTSKRKDEGRIAKAEEEFQKAQ 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19112281 175 EVYETLNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCRE 216
Cdd:cd07611 153 KVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKE 194
BAR_Bin2 cd07612
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, ...
 20-216 4.19e-15

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 2 (Bin2) is a BAR domain containing protein that is mainly expressed in hematopoietic cells. It is upregulated during granulocyte differentiation and is thought to function primarily in this lineage. The BAR domain of Bin2 is closely related to the BAR domains of amphiphysins, which function primarily in endocytosis and other membrane remodeling events. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Unlike amphiphysins, Bin2 does not appear to contain a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), function in intracellular vessicle trafficking. Bin2 can form a stable complex with Bin1 in cells but cannot replace the function of Bin1, and thus, appears to harbor a nonredundant function. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature.


Pssm-ID: 153296  Cd Length: 211  Bit Score: 71.81  E-value: 4.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  20 KTGHVERTVDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQTRIANTIDAFYGDagSKDGVSAYyRQVVEDLD 99
Cdd:cd07612   2 KLGKTVETKDEQFEQCAMNLNMQQSDGNRLYKDLKAYLNAVKVMHESSKRLSQTLQDIYEP--DWDGHEDL-GAIVEGED 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281 100 aDTVKELDGPFRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKVQKLVDKPSNDTTKLPRTEKEAAMAKEVYET 179
Cdd:cd07612  79 -LLWNDYEAKLHDQALRTMESYMAQFPDVKERVAKRGRKLVDYDSARHHLEALQNAKKKDDAKIAKAEEEFNRAQVVFED 157

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19112281 180 LNNQLVSELPQLIALRVPYLDPSFEALVKIQLRFCRE 216
Cdd:cd07612 158 INRELREELPILYDSRIGCYVTVFQNISNLRDTFYKE 194
BAR_DNMBP cd07589
The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, ...
 27-210 1.01e-14

The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. DyNamin Binding Protein (DNMBP), also called Tuba, is a Cdc42-specific Guanine nucleotide Exchange Factor (GEF) that binds dynamin and various actin regulatory proteins. It serves as a link between dynamin function, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. DNMBP contains BAR and SH3 domains as well as a Dbl Homology domain (DH domain), which harbors GEF activity. 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 DNMBP may be involved in binding to membranes. The gene encoding DNMBP is a candidate gene for late onset Alzheimer's disease.


Pssm-ID: 153273  Cd Length: 195  Bit Score: 70.42  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281  27 TVDREFETEERRYRTMESAAKKLQKEAKGYLDALRAMTASQTRIANTIDAFYGDAGSKDGVS-AYYRQVVEDLDADTVKE 105
Cdd:cd07589   2 TKDKEFDELEKKFGSLEKQVQLVVRNVELYLQHVQESVLVKVLALEVVLDLYPSNHPRLESKwERFRRVVRGISSKALPE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112281 106 LDGPFRTTVLDPISRFCSYFPDINAAITKRNHKLLDHDAMRAKvqklvdkpsndTTKLPRTEKEAAMAKEVYETLNNQLV 185
Cdd:cd07589  82 FKSRVRKLVIEPLSSLLKLFSGPQKLIQKRYDKLLDYERYKEK-----------KERGGKVDEELEEAANQYEALNAQLK 150

                       170       180
                ....*....|....*....|....*
gi 19112281 186 SELPQLIALRVPYLDPSFEALVKIQ 210
Cdd:cd07589 151 EELPKFNQLTAQLLETCLKSFVELQ 175
 
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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