The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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 proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159 157 VERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRH----AETELQRATIDATRTSRHLEE 232
Cdd:cd07598   81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQiisqAESELQKASVDANRSTKELEE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 894216159 233 TIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDL 283
Cdd:cd07598  161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211

The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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 proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159 157 VERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRH----AETELQRATIDATRTSRHLEE 232
Cdd:cd07598   81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQiisqAESELQKASVDANRSTKELEE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 894216159 233 TIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDL 283
Cdd:cd07598  161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211

MAEBL; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159   72 RRNLDERDAQ-TKQLQDA-VTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEinlyaSTETPNLKQGLKDFADEFAKL 149
Cdd:PTZ00121 1575 DKNMALRKAEeAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159  150 QDYRQAEVERL-----EAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRHAETELQRA----T 220
Cdd:PTZ00121 1650 EELKKAEEENKikaaeEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenK 1729

                         170       180       190
                  ....*....|....*....|....*....|....
gi 894216159  221 IDATRTSRHLEE--------TIDNFEKQKIKDIK 246
Cdd:PTZ00121 1730 IKAEEAKKEAEEdkkkaeeaKKDEEEKKKIAHLK 1763

The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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 proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159  77 ERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINLYASTETPNLKQGLKDFADEFAKLQDYRQAE 156
Cdd:cd07598    1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159 157 VERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTRQRNPSDRH----AETELQRATIDATRTSRHLEE 232
Cdd:cd07598   81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQiisqAESELQKASVDANRSTKELEE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 894216159 233 TIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQNIQNIDEDEDL 283
Cdd:cd07598  161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159  74 NLDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRDKADLLVNeinlyastetPNLKQGLKDFADEFAKLQDYR 153
Cdd:cd07307    1 KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSN----------TDLGEALEKFGKIQKELEEFR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159 154 QAEVERLEAKVVEPLKAYgtivkmKRDDLKATLTARNREAKQLSQLERTRQRNPSDR----------HAETELQRATIDA 223
Cdd:cd07307   71 DQLEQKLENKVIEPLKEY------LKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRkkkkdssklaEAEEELQEAKEKY 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 894216159 224 TRTSRHLEETIDNFEKQKIKDIKNILSEFITIEMLFHGKALEVFTAAYQN 273
Cdd:cd07307  145 EELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159  78 RDAQTKQLQDAVTNVEKHFGELCQIFAayvRKTARLRDKADLLVNEINLYAsTETPNLKQGLKDFADEFAKL-----QDY 152
Cdd:cd22656  101 DDLADATDDEELEEAKKTIKALLDDLL---KEAKKYQDKAAKVVDKLTDFE-NQTEKDQTALETLEKALKDLltdegGAI 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159 153 RQAEVERLEAKVVEPLKAYGTIVKMKRDDLKATLTARNREAKQLSQLERTrqrnpsdrhaeteLQRATIDATRTSRHLEE 232
Cdd:cd22656  177 ARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIAD-------------LTAADTDLDNLLALIGP 243

                        170       180       190
                 ....*....|....*....|....*....|.
gi 894216159 233 TIDNFEK-----QKIKD----IKNILSEFIT 254
Cdd:cd22656  244 AIPALEKlqgawQAIATdldsLKDLLEDDIS 274

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX1, SNX2, and similar proteins. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159  75 LDERDAQTKQLQDAVTNVEKHFGELCQIFAAYVRKTARLRdkadllvneinlyASTETPNLKQGLKDFADEFAKLQDYRQ 154
Cdd:cd07623   21 IENLDQQLRKLHASVESLVNHRKELALNTGSFAKSAAMLS-------------NCEEHTSLSRALSQLAEVEEKIEQLHG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216159 155 AEVERLEAKVVEPLKAY----GTI-------VKMKRDDLKATLT-ARNREAK---QLSQ-LERTRQRNPSDRHAETELQR 218
Cdd:cd07623   88 EQADTDFYILAELLKDYigliGAIkdvfherVKVWQNWQNAQQTlTKKREAKaklELSGrTDKLDQAQQEIKEWEAKVDR 167

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 894216159 219 ATIDATRTSRHLEETIDNFEKQKIKDIKNILSEFI 253
Cdd:cd07623  168 GQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYL 202