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Conserved domains on  [gi|226371725|ref|NP_001139504|]
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F-BAR domain only protein 2 isoform b [Homo sapiens]

Protein Classification

BAR and FCHo2_MHD domain-containing protein( domain architecture ID 10311967)

BAR and FCHo2_MHD domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FCHo2_MHD cd09267
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 ...
 511-777 0e+00

mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 (FCH domain only 2 or FCHo2) and similar proteins; This family corresponds to the MHD found in the ubiquitously expressed mammalian membrane-sculpting FCHo2 and similar proteins. FCHo2 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engages the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo2 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin.


:

Pssm-ID: 211378  Cd Length: 267  Bit Score: 591.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 511 PVAVALTESVNAYFKGADPTKCIVKITGDMTMSFPSGIIKVFTSNPTPAVLCFRVKNISRLEQILPNAQLVFSDPSQCDS 590
Cdd:cd09267    1 PVAVALTESVNAYFKGADPTKCIVKITGDMTVSFPSGIIKVFTSNPSPAVLCFRLKNTSRLEQILPNAQLLYSDPSQSDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 591 NTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVL 670
Cdd:cd09267   81 NTKDFWMNMQAVTVYLKKSSEQNPAASYYNVDILKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMQPPSPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 671 SNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSSISEKSENGGSGSLRAKFDLSEGPSKPTTLAVQFLSEGSTLSGV 750
Cdd:cd09267  161 SNVQVLVPVDGGVTNMQSLPPAIWNAEQMKALWKLSSISEKSENGGSGSLRAKFELSEGPSKPATLAVQFFSEGSTLSGV 240

                        250       260
                 ....*....|....*....|....*..
gi 226371725 751 DFELVGTGYRLSLIKKRFATGRYLADC 777
Cdd:cd09267  241 DMELVGTGYRLSLNKKRFATGRYMADC 267
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 5-240 4.14e-170

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 cd07673:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 269  Bit Score: 490.34  E-value: 4.14e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725   5 YFVENFWGEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLA 84
Cdd:cd07673    1 YFLENFWGEKNSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  85 NCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEQERLKKEGATQREIE 164
Cdd:cd07673   81 NCHLELVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEQERLKKEGATQREIE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 165 KAAVKSKKATDTYKLYVEKYALAKADFEQKMTETAQ---------------------------------VHEEFINNMAN 211
Cdd:cd07673  161 KAAVKSKKATESYKLYVEKYALAKADFEQKMTETAQkfqdieethlirikeiigsysnsvkeihiqigqVHEEFINNMAN 240

                        250       260
                 ....*....|....*....|....*....
gi 226371725 212 TTVESLIQKFAESKGTGKERPGLIEFEEC 240
Cdd:cd07673  241 TTVESLIQKFAESKGTGKERPGPIEFEEC 269
 
Name Accession Description Interval E-value
FCHo2_MHD cd09267
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 ...
 511-777 0e+00

mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 (FCH domain only 2 or FCHo2) and similar proteins; This family corresponds to the MHD found in the ubiquitously expressed mammalian membrane-sculpting FCHo2 and similar proteins. FCHo2 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engages the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo2 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin.


Pssm-ID: 211378  Cd Length: 267  Bit Score: 591.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 511 PVAVALTESVNAYFKGADPTKCIVKITGDMTMSFPSGIIKVFTSNPTPAVLCFRVKNISRLEQILPNAQLVFSDPSQCDS 590
Cdd:cd09267    1 PVAVALTESVNAYFKGADPTKCIVKITGDMTVSFPSGIIKVFTSNPSPAVLCFRLKNTSRLEQILPNAQLLYSDPSQSDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 591 NTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVL 670
Cdd:cd09267   81 NTKDFWMNMQAVTVYLKKSSEQNPAASYYNVDILKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMQPPSPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 671 SNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSSISEKSENGGSGSLRAKFDLSEGPSKPTTLAVQFLSEGSTLSGV 750
Cdd:cd09267  161 SNVQVLVPVDGGVTNMQSLPPAIWNAEQMKALWKLSSISEKSENGGSGSLRAKFELSEGPSKPATLAVQFFSEGSTLSGV 240

                        250       260
                 ....*....|....*....|....*..
gi 226371725 751 DFELVGTGYRLSLIKKRFATGRYLADC 777
Cdd:cd09267  241 DMELVGTGYRLSLNKKRFATGRYMADC 267
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 5-240 4.14e-170

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. The specific function of FCH domain Only 2 (FCHO2) is still unknown. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO1 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153357 [Multi-domain]  Cd Length: 269  Bit Score: 490.34  E-value: 4.14e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725   5 YFVENFWGEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLA 84
Cdd:cd07673    1 YFLENFWGEKNSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  85 NCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEQERLKKEGATQREIE 164
Cdd:cd07673   81 NCHLELVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEQERLKKEGATQREIE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 165 KAAVKSKKATDTYKLYVEKYALAKADFEQKMTETAQ---------------------------------VHEEFINNMAN 211
Cdd:cd07673  161 KAAVKSKKATESYKLYVEKYALAKADFEQKMTETAQkfqdieethlirikeiigsysnsvkeihiqigqVHEEFINNMAN 240

                        250       260
                 ....*....|....*....|....*....
gi 226371725 212 TTVESLIQKFAESKGTGKERPGLIEFEEC 240
Cdd:cd07673  241 TTVESLIQKFAESKGTGKERPGPIEFEEC 269
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 510-774 5.04e-89

Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that is conserved from yeast to humans.This C-terminal domain is structurally similar to mu homology domains, and is the region of the muniscin proteins involved in the interactions with the endocytic adaptor-scaffold proteins Ede1-eps15. This interaction influences muniscin localization. The muniscins provide a combined adaptor-membrane-tubulation activity that is important for regulating endocytosis.


Pssm-ID: 463046  Cd Length: 255  Bit Score: 280.74  E-value: 5.04e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  510 LPVAVALTESVNAYFKGADPTKciVKITGDMTMSFPSGIIKVFTSnptPAVLCFRVKNISRLEQILPNAQLVFsDPSQCD 589
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK--SKVTGEVALSYPAGIAASFTP---PAVLNFRLNNFSRLEKVAPNPAFVT-DESQSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  590 SNtkdFWMNMQAVTVYLKKLSeqnpaasyynvdvLKYQVSSNG-IQSTPLNLATYWKCSASTTDLRVDYKYNPE-AMVAP 667
Cdd:pfam10291  75 GE---FKVNPQFLASRTPLGA-------------LKYQVHIDPlSASCPLILHPVWKCEPHQASLILTYSLNPSlAIASA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  668 SVLSNIQVVVPVDGG-VTNMQSLPPAIWNAEQMKAFWKLSSISEKSENGGsGSLRAKFDLSEGPSKPTTLAVQFLSE-GS 745
Cdd:pfam10291 139 VVLENLQVVVNLDGShATSAQSKPQGTFNKEKSRITWKLPELSLTSDGDG-GKLIARFMTEGGASKPGGVAVKFEIEtGD 217

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 226371725  746 TLSGVDFELV---------GTGYRLSLIKKRFATGRYL 774
Cdd:pfam10291 218 TLSGLGISLVdqvdeedpfGGGWKLVPTKRRLAAGKYL 255
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 17-88 1.31e-21

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 89.25  E-value: 1.31e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226371725   17 GFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQ-----LGTFAPVWDVFKTSTEKLANCHL 88
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKkpeddGGTLKKAWDELLTETEQLAKQHL 77
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 10-90 9.61e-17

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 75.84  E-value: 9.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725    10 FWGEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAK----SASNYSQLGTFAPVWDVFKTSTEKLAN 85
Cdd:smart00055   3 FWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKklraVRDTEPEYGSLSKAWEVLLSETDALAK 82


                   ....*
gi 226371725    86 CHLDL 90
Cdd:smart00055  83 QHLEL 87
 
Name Accession Description Interval E-value
FCHo2_MHD cd09267
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 ...
 511-777 0e+00

mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 (FCH domain only 2 or FCHo2) and similar proteins; This family corresponds to the MHD found in the ubiquitously expressed mammalian membrane-sculpting FCHo2 and similar proteins. FCHo2 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engages the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo2 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin.


Pssm-ID: 211378  Cd Length: 267  Bit Score: 591.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 511 PVAVALTESVNAYFKGADPTKCIVKITGDMTMSFPSGIIKVFTSNPTPAVLCFRVKNISRLEQILPNAQLVFSDPSQCDS 590
Cdd:cd09267    1 PVAVALTESVNAYFKGADPTKCIVKITGDMTVSFPSGIIKVFTSNPSPAVLCFRLKNTSRLEQILPNAQLLYSDPSQSDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 591 NTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVL 670
Cdd:cd09267   81 NTKDFWMNMQAVTVYLKKSSEQNPAASYYNVDILKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMQPPSPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 671 SNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSSISEKSENGGSGSLRAKFDLSEGPSKPTTLAVQFLSEGSTLSGV 750
Cdd:cd09267  161 SNVQVLVPVDGGVTNMQSLPPAIWNAEQMKALWKLSSISEKSENGGSGSLRAKFELSEGPSKPATLAVQFFSEGSTLSGV 240

                        250       260
                 ....*....|....*....|....*..
gi 226371725 751 DFELVGTGYRLSLIKKRFATGRYLADC 777
Cdd:cd09267  241 DMELVGTGYRLSLNKKRFATGRYMADC 267
AP_Syp1_like_MHD cd09265
Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to ...
 511-776 9.14e-178

Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to the MHD found in the metazoan counterparts of yeast Syp1, which includes two ubiquitously expressed membrane-sculpting F-BAR domain-containing Fer/Cip4 homology domain-only proteins 1 and 2 (FCH domain only 1 and 2, or FCHo1/FCHo2), neuronal-specific SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related uncharacterized proteins. FCHo1/FCHo2 represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They are required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Both FCHo1/FCHo2 contain an N-terminal EFC/F-BAR domain that induces membrane tabulation, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD responsible for the binding of eps15 and intersectin. Another mammalian neuronal-specific protein, neuronal-specific transcript Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 [SGIP1] does not contain EFC/F-BAR domain, but does have a PRD and a C-terminal MHD and has been classified into this family as well. SGIP1 is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271171  Cd Length: 266  Bit Score: 509.73  E-value: 9.14e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 511 PVAVALTESVNAYFKGADPTKCIVKITGDMTMSFPSGIIKVFTSNPTPAVLCFRVKNISRLEQILPNAQLVFSDPSQCDS 590
Cdd:cd09265    1 PVAAAFTETVHAYFKGADPSKCIVKITGDMMMSFPAGIIRLLTSNPTPAPLTFRLKNASRLEHVLPNKQLIFSDPSQSDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 591 NTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVL 670
Cdd:cd09265   81 ETKDFWFNMPALTTYLKRQAEQNPTASYYNVDVLKYQVSPTGPQSTPLQLASYWKCEPSSTDLRVDYKYNPEAMAIATPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 671 SNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSSISEKSENGGSGSLRAKFDLSEGPSKPTTLAVQFLSEGSTLSGV 750
Cdd:cd09265  161 LNVQFSVPVDGGVTNVQSEPPATWNAEQKRLLWKLPDISQNSEGGGVGSLRARFELSEGPSKPAPLAVQFNSEGTTLSGV 240

                        250       260
                 ....*....|....*....|....*.
gi 226371725 751 DFELVGTGYRLSLIKKRFATGRYLAD 776
Cdd:cd09265  241 DIELVGSGYRLSLIKKRFAAGKYLCD 266
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 5-240 4.14e-170

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. The specific function of FCH domain Only 2 (FCHO2) is still unknown. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO1 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153357 [Multi-domain]  Cd Length: 269  Bit Score: 490.34  E-value: 4.14e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725   5 YFVENFWGEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLA 84
Cdd:cd07673    1 YFLENFWGEKNSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  85 NCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEQERLKKEGATQREIE 164
Cdd:cd07673   81 NCHLELVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEQERLKKEGATQREIE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 165 KAAVKSKKATDTYKLYVEKYALAKADFEQKMTETAQ---------------------------------VHEEFINNMAN 211
Cdd:cd07673  161 KAAVKSKKATESYKLYVEKYALAKADFEQKMTETAQkfqdieethlirikeiigsysnsvkeihiqigqVHEEFINNMAN 240

                        250       260
                 ....*....|....*....|....*....
gi 226371725 212 TTVESLIQKFAESKGTGKERPGLIEFEEC 240
Cdd:cd07673  241 TTVESLIQKFAESKGTGKERPGPIEFEEC 269
SGIP1_MHD cd09266
mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2) ...
 511-776 2.31e-141

mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 (also known as endophilin-3-interacting protein, SGIP1) and similar proteins; This family corresponds to the MHD found in mammalian neuronal-specific transcript SGIP1 and similar proteins. Unlike other members in this family, SGIP1 does not contain EFC/F-BAR domain, but does have a proline-rich domain (PRD) and a C-terminal MHD. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis, and is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271172  Cd Length: 267  Bit Score: 416.76  E-value: 2.31e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 511 PVAVALTESVNAYFKGADPTKCIVKITGDMTMSFPSGIIKVFTSNPTPAVLCFRVKNISRLEQILPNAQLVFSDPSQCDS 590
Cdd:cd09266    1 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 591 NTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVL 670
Cdd:cd09266   81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 671 SNIQVVVPVDGGVTNMQS-LPPAIWNAEQMKAFWKLSSISEKSENGGSGSLRAKFDLSEGPSKPTTLAVQFLSEGSTLSG 749
Cdd:cd09266  161 NNVQFLVPIDGGVTKLQAvLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                        250       260
                 ....*....|....*....|....*..
gi 226371725 750 VDFELVGTGYRLSLIKKRFATGRYLAD 776
Cdd:cd09266  241 CDIELVGPGYRFSLIKKRFAAGKYLAD 267
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 12-239 2.78e-134

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proteins in this group have been named FCH domain Only (FCHO) proteins. Vertebrates have two members, FCHO1 and FCHO2. These proteins contain an F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153332 [Multi-domain]  Cd Length: 261  Bit Score: 398.25  E-value: 2.78e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  12 GEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLV 91
Cdd:cd07648    1 GEKNNGFDVLYHNMKHGQIAVKELADFLRERATIEETYSKALNKLAKQASNSSQLGTFAPLWLVLRVSTEKLSELHLQLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  92 RKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEQERLKKEGATQREIEKAAVKSK 171
Cdd:cd07648   81 QKLQELIKDVQKYGEEQHKKHKKVKEEESGTAEAVQAIQTTTAALQKAKEAYHARCLELERLRRENASPKEIEKAEAKLK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 172 KATDTYKLYVEKYALAKADFEQKMTETA---------------------------------QVHEEFINNMANTTVESLI 218
Cdd:cd07648  161 KAQDEYKALVEKYNNIRADFETKMTDSCkrfqeieeshlrqmkeflasyaevlsenhsavgQVHEEFKRQVDELTVDKLL 240

                        250       260
                 ....*....|....*....|.
gi 226371725 219 QKFAESKGTGKERPGLIEFEE 239
Cdd:cd07648  241 RQFVESKGTGTEKPELIEFEE 261
FCHo1_MHD cd09268
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 ...
 511-775 2.90e-121

mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 (FCH domain only 1 or FCHo1, also known as KIAA0290) and similar proteins; This family corresponds to the MHD found in ubiquitously expressed mammalian membrane-sculpting FCHo1 and similar proteins. FCHo1 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo1 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin. Unlike other F-BAR domain containing proteins, FCHo1 has neither the Src homology 3 (SH3) domain nor any other known domain for interaction with dynamin and actin cytoskeleton. However, it can periodically accumulate at the budding site of clathrin. FCHo1 may utilize a unique action mode for vesicle formation as compared with other F-BAR proteins.


Pssm-ID: 271173  Cd Length: 265  Bit Score: 365.06  E-value: 2.90e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 511 PVAVALTESVNAYFKGADPTKCIVKITGDMTMSFPSGIIKVFTSNPTPAVLCFRVKNISRLEQILPNAQLVFSDPSQCDS 590
Cdd:cd09268    1 PVAAAFTEYVHAYFRGGALEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 591 NTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVaPSVL 670
Cdd:cd09268   81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNPATAP-ATFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 671 SNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSSISEKSENGGSGSLRAKFDLSEGPSKPTTLAVQFLSEGSTLSGV 750
Cdd:cd09268  160 TDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGNEHDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSGV 239

                        250       260
                 ....*....|....*....|....*
gi 226371725 751 DFELVGTGYRLSLIKKRFATGRYLA 775
Cdd:cd09268  240 DIELVGSGYRMSLVKKRFATGKYLV 264
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 12-239 2.46e-115

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 349.63  E-value: 2.46e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  12 GEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLV 91
Cdd:cd07674    1 GEKNAGFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNGSPLGTFAPMWEVFRVSSDKLALCHLELM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  92 RKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEQERLKKEGATQREIEKAAVKSK 171
Cdd:cd07674   81 RKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQKELEKAELKTK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 172 KATDTYKLYVEKYALAKADFEQKMTETA---------------------------------QVHEEFINNMANTTVESLI 218
Cdd:cd07674  161 KAAESLRGSVEKYNRARGDFEQKMLESAqkfqdieethlrhmkllikgyshsvedthvqigQVHEEFKQNVENVGVENLI 240

                        250       260
                 ....*....|....*....|.
gi 226371725 219 QKFAESKGTGKERPGLIEFEE 239
Cdd:cd07674  241 RKFAESKGTGKERPGPVGFEE 261
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 510-774 5.04e-89

Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that is conserved from yeast to humans.This C-terminal domain is structurally similar to mu homology domains, and is the region of the muniscin proteins involved in the interactions with the endocytic adaptor-scaffold proteins Ede1-eps15. This interaction influences muniscin localization. The muniscins provide a combined adaptor-membrane-tubulation activity that is important for regulating endocytosis.


Pssm-ID: 463046  Cd Length: 255  Bit Score: 280.74  E-value: 5.04e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  510 LPVAVALTESVNAYFKGADPTKciVKITGDMTMSFPSGIIKVFTSnptPAVLCFRVKNISRLEQILPNAQLVFsDPSQCD 589
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK--SKVTGEVALSYPAGIAASFTP---PAVLNFRLNNFSRLEKVAPNPAFVT-DESQSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  590 SNtkdFWMNMQAVTVYLKKLSeqnpaasyynvdvLKYQVSSNG-IQSTPLNLATYWKCSASTTDLRVDYKYNPE-AMVAP 667
Cdd:pfam10291  75 GE---FKVNPQFLASRTPLGA-------------LKYQVHIDPlSASCPLILHPVWKCEPHQASLILTYSLNPSlAIASA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  668 SVLSNIQVVVPVDGG-VTNMQSLPPAIWNAEQMKAFWKLSSISEKSENGGsGSLRAKFDLSEGPSKPTTLAVQFLSE-GS 745
Cdd:pfam10291 139 VVLENLQVVVNLDGShATSAQSKPQGTFNKEKSRITWKLPELSLTSDGDG-GKLIARFMTEGGASKPGGVAVKFEIEtGD 217

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 226371725  746 TLSGVDFELV---------GTGYRLSLIKKRFATGRYL 774
Cdd:pfam10291 218 TLSGLGISLVdqvdeedpfGGGWKLVPTKRRLAAGKYL 255
AP_muniscins_like_MHD cd09257
Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family ...
 511-776 1.18e-71

Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family corresponds to the MHD found in muniscins, a novel family of endocytic adaptor proteins. The term, muniscins, has been assigned to name the MHD of proteins with both EFC/F-BAR domain and MHD. These two domains are responsible for the membrane-tubulation activity associated with transmembrane cargo proteins. Members in this family include an endocytic adaptor Syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related uncharacterized proteins. Syp1 is a poorly characterized yeast protein with multiple biological functions. Syp1 contains an N-terminal EFC/F-BAR domain that induces membrane tabulation, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD that can directly binds to the endocytic adaptor/scaffold protein Ede1 or a transmembrane stress sensor cargo protein Mid2. Thus, Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress response. Syp1 shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, the membrane-sculpting F-BAR domain-containing Fer/Cip4 homology domain-only proteins 1 and 2 (FCHo1/2). FCHo1/2 represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They are required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein, neuronal-specific transcript Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 [SGIP1] does not contain EFC/F-BAR domain, but does have a PRD and a C-terminal MHD and has been classified into this family as well. SGIP1 is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271165  Cd Length: 244  Bit Score: 234.57  E-value: 1.18e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 511 PVAVALTESVNAYFKGadPTKCIVKITGDMTMSFPSGIIKvftsnPTPAVLCFRVKNISRLEQILPNAQLVFSDPSqcDS 590
Cdd:cd09257    1 GVKAALTEELNAEFKG--SSLQSVGVEGEVQLAVPSSDAK-----PKPAPFNLRLNDASSLEKAAPNVAFLNSVPS--GS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 591 NTKDFWMNMQAVTvylkklseqnpaASYYNVDVLKYQVSSNGIqSTPLNLATYWKCSASTTDLRVDYKYNPEAmvaPSVL 670
Cdd:cd09257   72 SPGEFLVNTKAIR------------ASEVGSPILKYSCSSKLR-PVPLRVQTVWRCESHQTSVMLQYVSNPSL---PGPL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 671 SNIQVVVPVDGG-VTNMQSLPPAIWNAEQMKAFWKLSSIsekSENGGSGSLRAKFDLSEGPS---KPTTLAVQFLSEGST 746
Cdd:cd09257  136 QDVTVIVNVPPGaGENLKSSPGAVWNEEKRRLTWKLPEL---GVNGEGGELRARFQIDAGQTaekVPFPVLVRCLSEGST 212

                        250       260       270
                 ....*....|....*....|....*....|..
gi 226371725 747 LSGVDFELVGTGYRL--SLIKKRFATGRYLAD 776
Cdd:cd09257  213 LSGLGLEVVALEEEWafIEVKVTRRFGVYHAE 244
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 17-212 5.13e-30

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153331 [Multi-domain]  Cd Length: 239  Bit Score: 118.73  E-value: 5.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  17 GFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQE 96
Cdd:cd07647    6 GFDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGDEIGTLKSSWDSLRKETENVANAHIQLAQSLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  97 LIKEVQKYGEEQVKSHKKTKEEVagtlEAVQTIQSIT-QALQKSKENYNAKCVEQERL------KKEGATQREIEKAAVK 169
Cdd:cd07647   86 EAEKLEEFREKQKEERKKTEDIM----KRSQKNKKELyKKTMKAKKSYEQKCREKDKAeqayekSSSGAQPKEAEKLKKK 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226371725 170 SK-------KATDTYKLYVEKYALAKADFEQKMTETAQV----HEEFINNMANT 212
Cdd:cd07647  162 AAqcktsaeEADSAYKSSIGCLEDARVEWESEHATACQVfqnmEEERIKFLRNA 215
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 17-204 1.77e-27

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.


Pssm-ID: 153294 [Multi-domain]  Cd Length: 191  Bit Score: 110.12  E-value: 1.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  17 GFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLG--TFAPVWDVFKTSTEKLANCHLDLVRKL 94
Cdd:cd07610    1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPESGktSLGTSWNSLREETESAATVHEELSEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  95 QELIKEVQKYGEEQVKshKKTKEEVAGTLEAVQTIQSITQALqkskenynakcveqerlkkegatqreiekaavkSKKAT 174
Cdd:cd07610   81 SQLIREPLEKVKEDKE--QARKKELAEGEKLKKKLQELWAKL---------------------------------AKKAD 125

                        170       180       190
                 ....*....|....*....|....*....|
gi 226371725 175 DTYKLYVEKYALAKADFEQKMTETAQVHEE 204
Cdd:cd07610  126 EEYREQVEKLNPAQSEYEEEKLNKIQAEQE 155
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 17-88 1.31e-21

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 89.25  E-value: 1.31e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226371725   17 GFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQ-----LGTFAPVWDVFKTSTEKLANCHL 88
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKkpeddGGTLKKAWDELLTETEQLAKQHL 77
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 16-198 2.93e-20

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153333 [Multi-domain]  Cd Length: 233  Bit Score: 90.46  E-value: 2.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  16 SGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQ 95
Cdd:cd07649    5 TGFEILLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEEGTLGEAWAQVKKSLADEAEVHLKFSSKLQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  96 -ELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQT----IQSITQALQKSKENYNAKcVEQERLKKEGATQREIEKAAVKS 170
Cdd:cd07649   85 sEVEKPLLNFRENFKKDMKKLDHHIADLRKQLASryaaVEKARKALLERQKDLEGK-TQQLEIKLSNKTEEDIKKARRKS 163

                        170       180
                 ....*....|....*....|....*....
gi 226371725 171 KKATDTYKLYVEKYALAKAD-FEQKMTET 198
Cdd:cd07649  164 TQAGDDLMRCVDLYNQAQSKwFEEMVTTS 192
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-201 1.49e-18

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153355 [Multi-domain]  Cd Length: 242  Bit Score: 85.78  E-value: 1.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  15 NSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKL 94
Cdd:cd07671    4 NTGYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAGGQTEINTLKASFDQLKQQIENIGNSHIQLAGML 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  95 QELIKEVQKYGEEQVKSHKKTKeevaGTLEAVQTIQ-SITQALQKSKENYNAKCVEQ-------ERLKKEGaTQREIEKA 166
Cdd:cd07671   84 REELKSLEEFRERQKEQRKKYE----AVMERVQKSKvSLYKKTMESKKTYEQRCREAdeaeqtfERSSSTG-NPKQSEKS 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226371725 167 AVKSKK----ATDTYKLY---VEKYALAKADFEQKMTETAQV 201
Cdd:cd07671  159 QNKAKQcrdaATEAERVYkqnIEQLDKARTEWETEHILTCEV 200
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 10-90 9.61e-17

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 75.84  E-value: 9.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725    10 FWGEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAK----SASNYSQLGTFAPVWDVFKTSTEKLAN 85
Cdd:smart00055   3 FWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKklraVRDTEPEYGSLSKAWEVLLSETDALAK 82


                   ....*
gi 226371725    86 CHLDL 90
Cdd:smart00055  83 QHLEL 87
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 17-205 3.94e-16

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153356 [Multi-domain]  Cd Length: 240  Bit Score: 78.45  E-value: 3.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  17 GFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLA-KSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQ 95
Cdd:cd07672    6 GYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSkKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQLAQTLR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  96 ELIKEVQKYGEEQvKSHKKTKEEVAGTLEAVQTIQsiTQALQKSKENYNAKCVEQErlKKEGATQREIEKAAVKSKKATd 175
Cdd:cd07672   86 DEAKKMEDFRERQ-KLARKKIELIMDAIHKQRAMQ--FKKTMESKKNYEQKCRDKD--EAEQAVNRNANLVNVKQQEKL- 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 226371725 176 TYKLYVEKYALAKAD--FEQKMTETAQVHEEF 205
Cdd:cd07672  160 FAKLAQSKQNAEDADrlYMQNISVLDKIREDW 191
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 12-185 3.54e-15

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 75.80  E-value: 3.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  12 GEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLV 91
Cdd:cd07651    1 GKNDAGFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSLGGSEEGGLKNSLDTLRLETESMAKSHLKFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  92 RKL-QELIKEVQKYgEEQVKSHKKTKEevAGTLEAVQTIQSITQALQKSKENYNAKC--VEQERLKKEGATQREIEKAAV 168
Cdd:cd07651   81 KQIrQDLEEKLAAF-ASSYTQKRKKIQ--SHMEKLLKKKQDQEKYLEKAREKYEADCskINSYTLQSQLTWGKELEKNNA 157

                        170       180
                 ....*....|....*....|....
gi 226371725 169 KSKKATDT-------YKLYVEKYA 185
Cdd:cd07651  158 KLNKAQSSinssrrdYQNAVKALR 181
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 15-190 3.31e-14

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153336 [Multi-domain]  Cd Length: 234  Bit Score: 72.77  E-value: 3.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  15 NSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQL-----GTFAPVWDVFKTSTEKLANCHLD 89
Cdd:cd07652    4 DVGLSTLLDRLKQSIASAKEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRpdhkqGSFSNAYHSSLEFHEKLADNGLR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  90 LVRKLQELIKEVQKYGEEQVKSHKKTKEEvagTLEAVQTIQSITQALQKSKENYNAKCVEQERLKkegaTQREIEKAAVK 169
Cdd:cd07652   84 FAKALNEMSDELSSLAKTVEKSRKSIKET---GKRAEKKVQDAEAAAEKAKARYDSLADDLERVK----TGDPGKKLKFG 156

                        170       180
                 ....*....|....*....|.
gi 226371725 170 SKKATDTYKLyvEKYALAKAD 190
Cdd:cd07652  157 LKGNKSAAQH--EDELLRKVQ 175
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 18-223 9.05e-14

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: 70.55  E-value: 9.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  18 FDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQlgtfapvwDVFKTSTEKLANCHLDLVRKLQEL 97
Cdd:cd07307    2 LDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSN--------TDLGEALEKFGKIQKELEEFRDQL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  98 IKEVQKYGEEQVKSHKKtkeevagtlEAVQTIQSITQALQKSKENYNAKCVEQERLKKEGATQREIEKAAVKskkatdtY 177
Cdd:cd07307   74 EQKLENKVIEPLKEYLK---------KDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKLAEAEEE-------L 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226371725 178 KLYVEKYALAKADFEQKMTETAQVHEEFINNMANTTVESLIQKFAE 223
Cdd:cd07307  138 QEAKEKYEELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKE 183
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 34-225 7.76e-12

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 2 (PACSIN2); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSIN 2 contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153363 [Multi-domain]  Cd Length: 258  Bit Score: 66.24  E-value: 7.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  34 ELADFVRERATIEEAYSRSMTKLAK----SASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQ----ELIKEVQK-- 103
Cdd:cd07679   23 DLMNCLHERARIEKVYAQQLTEWAKrwrqLVEKGPQYGTVEKAWCALMSEAEKVSELHLEVKASLMnedfEKIKNWQKea 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 104 YGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEqERLkkegATQREIEKAAVKS------KKATDTY 177
Cdd:cd07679  103 FHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHTACKE-EKL----ATSREANSKADPAlnpeqlKKLQDKV 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226371725 178 KLYVEKYALAKADFEQKMTETAQVHEEFINNMANttVESLIQKFAESK 225
Cdd:cd07679  178 EKCKQDVLKTKEKYEKSLKELDQTTPQYMENMEQ--VFEQCQQFEEKR 223
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
 10-217 7.81e-10

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic INducer (NOSTRIN); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Nitric Oxide Synthase TRaffic INducer (NOSTRIN) is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). NOSTRIN facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of NOSTRIN may be correlated to preeclampsia. NOSTRIN contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of NOSTRIN is necessary and sufficient for its membrane association and is responsible for its subcellular localization.


Pssm-ID: 153342 [Multi-domain]  Cd Length: 239  Bit Score: 60.09  E-value: 7.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  10 FWGekNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQ--LGTFAPVWDVFKTSTEKLANCH 87
Cdd:cd07658    1 FMG--QKGFEELRRYVKQGGDFCKELATVLQERAELELNYAKGLSKLSGKLSKASKsvSGTLSSAWTCVAEEMESEADIH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  88 LDLVRKL-QELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQTIQSITQ--------------ALQKSKENYNAKCVEQER 152
Cdd:cd07658   79 RNLGSALtEEAIKPLRQVLDEQHKTRKPVENEVDKAAKLLTDWRSEQIkvkkklhglareneKLQDQVEDNKQSCTKQKM 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226371725 153 LKKEGA----TQREIEKAAVKSKKATDT--------YKLYVEKYALAKaDFEQKMTETAQVHEEFINNMANTTVESL 217
Cdd:cd07658  159 LNKLKKsaevQDKEDEKLEAKRKKGEESrlkaeneyYTCCVRLERLRL-EWESALRKGLNQYESLEEERLQHLKHSL 234
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 34-225 5.97e-09

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 57.75  E-value: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  34 ELADFVRERATIEEAYSRSMTKLAKSASNY----SQLGTFAPVWDVFKTSTEKLANCHLD----LVRKLQELIKEVQK-- 103
Cdd:cd07680   23 DLMNCVQERAKIEKAYGQQLTDWAKRWRQLiekgPQYGSLERAWGAIMTEADKVSELHQEvknnLLNEDLEKVKNWQKda 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 104 YGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEQE-RLKKEGATQREIEKAAVKSKKATDTYKLYVE 182
Cdd:cd07680  103 YHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKlAMTREANSKAEQSVTPEQQKKLQDKVDKCKQ 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226371725 183 KYALAKADFEQKMTETAQVHEEFINNManTTVESLIQKFAESK 225
Cdd:cd07680  183 DVQKTQEKYEKVLDDVGKTTPQYMENM--EQVFEQCQQFEEKR 223
F-BAR_PACSIN3 cd07681
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 34-204 3.96e-08

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 3 or Syndapin III is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. PACSIN 3 contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153365 [Multi-domain]  Cd Length: 258  Bit Score: 55.33  E-value: 3.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  34 ELADFVRERATIEEAYSRSMTKLAK----SASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQ----ELIKEVQK-- 103
Cdd:cd07681   23 DLVSCFQERAKIEKGYAQQLSDWARkwrgIVEKGPQYGTLEKAWHAFLTAAERLSEIHLELRENLVgedsEKVRAWQKea 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 104 YGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNA------------------KCVEQERLKK-----EGATQ 160
Cdd:cd07681  103 FHKQMIGGFRESKEAEEGFRKAQKPWVKKLKEVESSKKGYHAarkdertaqtrethakadSTVSQEQLRKlqdrvEKCTQ 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226371725 161 rEIEKAAVKSKKATDTYKLYVEKYAlakADFEQKMtETAQVHEE 204
Cdd:cd07681  183 -EAEKAKEQYEKALEELNRYNPRYM---EDMEQAF-EICQEAER 221
F-BAR_Syp1p_like cd07650
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein; F-BAR ...
 33-229 1.23e-07

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Syp1p is associated with septins, a family of GTP-binding proteins that serve as elements of septin filaments, which are required for cell morphogenesis and division. Syp1p regulates cell-cycle dependent septin cytoskeletal dynamics in yeast. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCH domain Only (FCHO) proteins and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153334 [Multi-domain]  Cd Length: 228  Bit Score: 53.10  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  33 KELADFVRERATIEEAYSRSMTKLAKSA--SNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQELIkevqkygeEQVK 110
Cdd:cd07650   22 TELADWLQERRRLERQYVQGLRKLARRNepLNKSLLGVFQNPWLTIESETEFIAASHGELAQRIETDV--------EEPL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 111 SHKKTKEEVAGTLEavqTIQSITqALQKSKENYNAKCVEQERLKKEGATQR-EIEKAAVKSK---------------KAT 174
Cdd:cd07650   94 RDFATSTEFMNTLD---DDQNLS-NLAKELDESQKKWDKLKKKHSKASSKAvSAAVSDLEEArqqwdsqapflfellQAI 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 175 DTYKLY-----VEKYALAKADFEQKMTETAqvhEEFINNMANTTVESLIQKFAESKGTGK 229
Cdd:cd07650  170 DEERLNhlkdvLLQFQTHESDYALRTTESA---EECMNQLLEFDTEDEIQRFARKASAGR 226
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 33-197 2.09e-07

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153339 [Multi-domain]  Cd Length: 258  Bit Score: 53.09  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  33 KELADFVRERATIEEAYSRSMTKLAK----SASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQ----ELIKEVQK- 103
Cdd:cd07655   22 DDLMKMVQERAEIEKAYAKKLKEWAKkwrdLIEKGPEYGTLETAWKGLLSEAERLSELHLSIRDKLLndvvEEVKTWQKe 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 104 -YGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKC------------------VEQERLKKegaTQREIE 164
Cdd:cd07655  102 nYHKSMMGGFKETKEAEDGFAKAQKPWAKLLKKVEKAKKAYHAACkaeksaqkqennaksdtsLSPDQVKK---LQDKVE 178

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371725 165 KAAVKSKKATDTYKLYVEKYALAKADFEQKMTE 197
Cdd:cd07655  179 KCKQEVSKTKDKYEKALEDLNKYNPRYMEDMEQ 211
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 34-188 9.28e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs, all of which are expressed during embryonic and early development in the nervous system but with different localization and timing. srGAPs contain an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153340 [Multi-domain]  Cd Length: 241  Bit Score: 44.63  E-value: 9.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  34 ELADFVRERATIEEAYSRSMTKLAKS-ASNYSQLGTFAPVWDVFKTSteklaNC-HLDLVRKLQE--------------L 97
Cdd:cd07656   23 DLQDYFRRRAEIELEYSRSLEKLADRfSSKHKNEKSKREDWSLLSPV-----NCwNTLLVQTKQEsrdhstlsdiysnnL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  98 IKEVQKYGEEQVKSHKKTKEEvagTLEAVQTIQSITQALQKSKENY---NAKCVEQERLKKEGATQREIEKAAV------ 168
Cdd:cd07656   98 VQRLGQMSEDLQRISKKCREI---GSQLHDELLRVLNELQTAMKTYhtyHAESKSAERKLKEAEKQEEKQEQSPekkler 174

                        170       180
                 ....*....|....*....|..
gi 226371725 169 --KSKKATDTYKLYVEKYALAK 188
Cdd:cd07656  175 srSSKKIEKEVEKRQAKYSEAK 196
F-BAR_FCHSD2 cd07677
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 ...
 29-194 9.77e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 (FCHSD2); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 2 (FCHSD2) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153361 [Multi-domain]  Cd Length: 260  Bit Score: 44.73  E-value: 9.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  29 QISTKELAD---FVRERATIEEAYSRSMTKLAK----------SASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQ 95
Cdd:cd07677   15 QAECKLLEDereFSQKIAAIESEYAQKEQKLASqylksdwrgmKADERADYRSMYTVWKSFLEGTMQVAQSRINICENYK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  96 ELIKE----VQKYGEEQVKshkktkeEVAGTLEAVQT-IQSITQALQKSKENYnakcVEQERLKKEGATQREIEkaaVKS 170
Cdd:cd07677   95 NLISEpartVRLYKEQQLK-------RCVDQLTKIQAeLQETVKDLAKGKKKY----FETEQMAHAVREKADIE---AKS 160

                        170       180
                 ....*....|....*....|....
gi 226371725 171 KkatdtYKLYVEKYALAKADFEQK 194
Cdd:cd07677  161 K-----LSLFQSRISLQKASVKLK 179
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 38-194 1.07e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153337 [Multi-domain]  Cd Length: 251  Bit Score: 44.55  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  38 FVRERATIEEAYSRSMTKLAKS---------ASNYSQLGTFApvwDVFKtSTEKLANCHLDLVRKLQ-ELIKEVQKYGEE 107
Cdd:cd07653   27 FVKERAAIEQEYAKKLRKLVKKylpkkkeedEYSFSSVKAFR---SILN-EVNDIAGQHELIAENLNsNVCKELKTLISE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 108 QVKSHKKTKEEVAgtlEAVQTIQSITQALQKSKENYnakcveqERlkkegaTQREIEKAAVKSKKA---TDTYKLYVEKy 184
Cdd:cd07653  103 LRQERKKHLSEGS---KLQQKLESSIKQLEKSKKAY-------EK------AFKEAEKAKQKYEKAdadMNLTKADVEK- 165

                        170
                 ....*....|
gi 226371725 185 alAKADFEQK 194
Cdd:cd07653  166 --AKANANLK 173
F-BAR_srGAP2 cd07682
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 33-175 3.99e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP2 is expressed in zones of neuronal differentiation. It plays a role in the regeneration of neurons and axons. srGAP2 contains an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153366 [Multi-domain]  Cd Length: 263  Bit Score: 43.14  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  33 KELADFVRERATIEEAYSRSMTKLAK---SASNYSQLGTF-------APV--WDVFKTSTEKLANCHLDLVR-KLQELIK 99
Cdd:cd07682   22 QDLQDFFRKKAEIEMDYSRNLEKLAErflAKTRSTKDQQFkkdqnvlSPVncWNLLLNQVKRESRDHATLSDiYLNNIIP 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226371725 100 EVQKYGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEQERLKKEGATQReiEKAAVKSKKATD 175
Cdd:cd07682  102 RFVQISEDSGRLFKKSKEVGLQLQEDLMKVLNELYTVMKTYHMYNADSISAQSKLKEAEKQE--EKQMSRSVRQED 175
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
 624-761 5.14e-04

C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3 subunit, which includes two closely related homologs, mu3A (P47A, encoded by ap3m1) and mu1B (P47B, encoded by ap3m2). Mu3A is ubiquitously expressed, but mu3B is specifically expressed in neurons and neuroendocrine cells. AP-3 is particularly important for targeting integral membrane proteins to lysosomes and lysome-related organelles at trans-Golgi network (TGN) and/or endosomes, such as the yeast vacuole, fly pigment granules and mammalian melanosomes, platelet dense bodies and the secretory lysosomes of cytotoxic T lymphocytes. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271160  Cd Length: 251  Bit Score: 42.57  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 624 LKYQVSSNGIQSTPLNLATYWKCSASTT--DLRVDYKYNPeamvaPSVLSNIQVVVPVDGGVTNMQSLPP---AIWNAEQ 698
Cdd:cd09252   96 MSYRVDLNSLVSLPVYVKPQISFSGSSGrfEITVGSRQNL-----GKSIENVVVEIPLPKGVKSLRLTAShgsFSFDSST 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226371725 699 MKAFWKLSSISekseNGGSGSLRAKFDLSEG---PSKPTTLAVQFLSEGSTLSG--VD-FELVGTGYRL 761
Cdd:cd09252  171 KTLVWNIGKLT----PGKTPTLRGSVSLSSGleaPSESPSISVQFKIPGYTPSGlkVDsLDIYNEKYKP 235
F-BAR_srGAP1 cd07683
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 33-162 1.47e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP1, also called Rho GTPase-Activating Protein 13 (ARHGAP13), is a Cdc42- and RhoA-specific GAP and is expressed later in the development of CNS (central nervous system) tissues. It is an important downstream signaling molecule of Robo1. srGAP1 contains an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153367 [Multi-domain]  Cd Length: 253  Bit Score: 41.21  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  33 KELADFVRERATIEEAYSRSMTKLA-------KSASNYSQL----GTFAPV--WDVFKTSTEKLANCHLDLVR-KLQELI 98
Cdd:cd07683   22 QDLQDFFRKKAEIESEYSRNLEKLAerfmaktRSTKDHQQYkkdqNLLSPVncWYLLLNQVRRESKDHATLSDiYLNNVI 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226371725  99 KEVQKYGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEQERLKKEGATQRE 162
Cdd:cd07683  102 MRFMQISEDSTRMFKKSKEIAFQLHEDLMKVLNELYTVMKTYHMYHTESISAESKLKEAEKQEE 165
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 3-224 1.73e-03

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 40.73  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725    3 MAY-FVEN--FWGEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAK---SASNYSQLGTFAPVWDVF 76
Cdd:pfam09325  15 SSYkFNEPdeWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASlelSTGLSRALSQLAEVEERI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725   77 KTSTEKLANCHldlVRKLQELIKEVQKYgeeqVKSHKKTKEEvagTLEAVQTIQSITQALQKSKENYnAKCVEQERLKKE 156
Cdd:pfam09325  95 KELLERQALQD---VLTLGETIDEYLRL----IGSVKAVFNQ---RVKAWQSWQNAEQELSKKKEQL-EKLLRANKSQND 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  157 GATQ--REIEKAavkSKKATDTYKLYVEKYALAKADFEQKMTETAqvhEEFINNMaNTTVESLIQKFAES 224
Cdd:pfam09325 164 KLQQakKEVEEL---ERRVQQAEKEFEDISELIKKELERFELERV---DDFKNSV-EIYLESAIESQKEL 226
F-BAR_Fes_Fer cd07657
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer ...
 47-204 4.40e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer (Fes related) tyrosine kinases; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Fes (feline sarcoma), also called Fps (Fujinami poultry sarcoma), and Fer (Fes related) are cytoplasmic (or nonreceptor) tyrosine kinases that play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Although Fes and Fer show redundancy in their biological functions, they show differences in their expression patterns. Fer is ubiquitously expressed while Fes is expressed predominantly in myeloid and endothelial cells. Fes and Fer contain an N-terminal F-BAR domain, an SH2 domain, and a C-terminal catalytic kinase domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of Fes is critical in its role in microtubule nucleation and bundling.


Pssm-ID: 153341 [Multi-domain]  Cd Length: 237  Bit Score: 39.67  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725  47 EAYSRSMTKLAKSASNY-SQLGTFA---------------PVWDVFKT---STEKLANC---HLD-----LVRKLQELIK 99
Cdd:cd07657   22 ETMKKYMAKRAKSDREYaSTLGSLAnqglkieagddlqgsPISKSWKEimdSTDQLSKLikqHAEalesgTLDKLTLLIK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371725 100 EVQK----YGEEQVKSH---KKTKEEVAG-TLEAVQTIQSITQALQKSKENYnakcveqerlKKEGATQREIEKAAVKSK 171
Cdd:cd07657  102 DKRKakkaYQEERQQIDeqyKKLTDEVEKlKSEYQKLLEDYKAAKSKFEEAV----------VKGGRGGRKLDKARDKYQ 171

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371725 172 KATDTYKLYVEKYALAKADfeqkmtetAQVHEE 204
Cdd:cd07657  172 KACRKLHLCHNDYVLALLE--------AQEHEE 196
 
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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