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Conserved domains on  [gi|1858900827|ref|NP_001371331|]
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F-BAR domain only protein 1 isoform j [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 10-270 0e+00

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: 531.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  10 GEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07674     1 GEKNAGFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNGSPLGTFAPMWEVFRVSSDKLALCHLELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  90 RKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTK 169
Cdd:cd07674    81 RKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQKELEKAELKTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 170 KAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLL 249
Cdd:cd07674   161 KAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDTHVQIGQVHEEFKQNVENVGVENLI 240

                         250       260
                  ....*....|....*....|.
gi 1858900827 250 RKFAESKGTGREKPGPLDFEA 270
Cdd:cd07674   241 RKFAESKGTGKERPGPVGFEE 261
FCHo1_MHD cd09268
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 ...
 535-796 4.71e-171

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: 493.33  E-value: 4.71e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 535 PIATAFTEYVHAYFRGH-SPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 613
Cdd:cd09268     1 PVAAAFTEYVHAYFRGGaLEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 614 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPgATAVPTPL 693
Cdd:cd09268    81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 694 TNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEA---GGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGV 770
Cdd:cd09268   160 TDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGnehDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSGV 239

                         250       260
                  ....*....|....*....|....*.
gi 1858900827 771 DLELVGSGYRMSLVKRRFATGMYLVS 796
Cdd:cd09268   240 DIELVGSGYRMSLVKKRFATGKYLVC 265
 
Name Accession Description Interval E-value
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 10-270 0e+00

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: 531.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  10 GEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07674     1 GEKNAGFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNGSPLGTFAPMWEVFRVSSDKLALCHLELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  90 RKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTK 169
Cdd:cd07674    81 RKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQKELEKAELKTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 170 KAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLL 249
Cdd:cd07674   161 KAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDTHVQIGQVHEEFKQNVENVGVENLI 240

                         250       260
                  ....*....|....*....|.
gi 1858900827 250 RKFAESKGTGREKPGPLDFEA 270
Cdd:cd07674   241 RKFAESKGTGKERPGPVGFEE 261
FCHo1_MHD cd09268
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 ...
 535-796 4.71e-171

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: 493.33  E-value: 4.71e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 535 PIATAFTEYVHAYFRGH-SPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 613
Cdd:cd09268     1 PVAAAFTEYVHAYFRGGaLEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 614 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPgATAVPTPL 693
Cdd:cd09268    81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 694 TNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEA---GGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGV 770
Cdd:cd09268   160 TDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGnehDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSGV 239

                         250       260
                  ....*....|....*....|....*.
gi 1858900827 771 DLELVGSGYRMSLVKRRFATGMYLVS 796
Cdd:cd09268   240 DIELVGSGYRMSLVKKRFATGKYLVC 265
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 534-794 4.83e-77

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: 249.54  E-value: 4.83e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 534 LPIATAFTEYVHAYFRGHSPSClARVTGELTMTFPAGIVRVFsgtPPPPVLSFRLVHTTAIEHFQPNADLLFsDPSQSDP 613
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK-SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 614 EtkdFWLNMAALTEALQRQAeqnptasyynvvlLRYQFSR-PGPQSVPLQLSAHWQCGATLTQVSVEYGYRPG-ATAVPT 691
Cdd:pfam10291  76 E---FKVNPQFLASRTPLGA-------------LKYQVHIdPLSASCPLILHPVWKCEPHQASLILTYSLNPSlAIASAV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 692 PLTNVQILLPVGEP-VTNVRLQPAATWNLEEKRLTWRLPDVSEA--GGSGRLSASWEPLSGPSTPSPVAAQFTSE-GTTL 767
Cdd:pfam10291 140 VLENLQVVVNLDGShATSAQSKPQGTFNKEKSRITWKLPELSLTsdGDGGKLIARFMTEGGASKPGGVAVKFEIEtGDTL 219

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1858900827 768 SGVDLELV---------GSGYRMSLVKRRFATGMYL 794
Cdd:pfam10291 220 SGLGISLVdqvdeedpfGGGWKLVPTKRRLAAGKYL 255
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 7-88 1.69e-20

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: 86.63  E-value: 1.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827    7 HFWGEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSK----LASNGTPMGTFAPLWEVFRVSSDKLA 82
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKklraVRDTEPEYGSLSKAWEVLLSETDALA 81


                   ....*.
gi 1858900827   83 LCHLEL 88
Cdd:smart00055  82 KQHLEL 87
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 15-87 6.10e-18

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: 78.85  E-value: 6.10e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1858900827  15 GFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSK-----LASNGTPMGTFAPLWEVFRVSSDKLALCHLE 87
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKkflkkKKKPEDDGGTLKKAWDELLTETEQLAKQHLK 78
 
Name Accession Description Interval E-value
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 10-270 0e+00

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: 531.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  10 GEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07674     1 GEKNAGFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNGSPLGTFAPMWEVFRVSSDKLALCHLELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  90 RKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTK 169
Cdd:cd07674    81 RKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQKELEKAELKTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 170 KAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLL 249
Cdd:cd07674   161 KAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDTHVQIGQVHEEFKQNVENVGVENLI 240

                         250       260
                  ....*....|....*....|.
gi 1858900827 250 RKFAESKGTGREKPGPLDFEA 270
Cdd:cd07674   241 RKFAESKGTGKERPGPVGFEE 261
FCHo1_MHD cd09268
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 ...
 535-796 4.71e-171

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: 493.33  E-value: 4.71e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 535 PIATAFTEYVHAYFRGH-SPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 613
Cdd:cd09268     1 PVAAAFTEYVHAYFRGGaLEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 614 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPgATAVPTPL 693
Cdd:cd09268    81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 694 TNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEA---GGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGV 770
Cdd:cd09268   160 TDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGnehDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSGV 239

                         250       260
                  ....*....|....*....|....*.
gi 1858900827 771 DLELVGSGYRMSLVKRRFATGMYLVS 796
Cdd:cd09268   240 DIELVGSGYRMSLVKKRFATGKYLVC 265
AP_Syp1_like_MHD cd09265
Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to ...
 535-796 1.96e-161

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: 468.89  E-value: 1.96e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 535 PIATAFTEYVHAYFRGHSPS-CLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 613
Cdd:cd09265     1 PVAAAFTETVHAYFKGADPSkCIVKITGDMMMSFPAGIIRLLTSNPTPAPLTFRLKNASRLEHVLPNKQLIFSDPSQSDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 614 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPGATAVPTPL 693
Cdd:cd09265    81 ETKDFWFNMPALTTYLKRQAEQNPTASYYNVDVLKYQVSPTGPQSTPLQLASYWKCEPSSTDLRVDYKYNPEAMAIATPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 694 TNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEA---GGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGV 770
Cdd:cd09265   161 LNVQFSVPVDGGVTNVQSEPPATWNAEQKRLLWKLPDISQNsegGGVGSLRARFELSEGPSKPAPLAVQFNSEGTTLSGV 240

                         250       260
                  ....*....|....*....|....*.
gi 1858900827 771 DLELVGSGYRMSLVKRRFATGMYLVS 796
Cdd:cd09265   241 DIELVGSGYRLSLIKKRFAAGKYLCD 266
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 10-269 1.08e-155

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: 453.72  E-value: 1.08e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  10 GEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07648     1 GEKNNGFDVLYHNMKHGQIAVKELADFLRERATIEETYSKALNKLAKQASNSSQLGTFAPLWLVLRVSTEKLSELHLQLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  90 RKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTK 169
Cdd:cd07648    81 QKLQELIKDVQKYGEEQHKKHKKVKEEESGTAEAVQAIQTTTAALQKAKEAYHARCLELERLRRENASPKEIEKAEAKLK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 170 KAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLL 249
Cdd:cd07648   161 KAQDEYKALVEKYNNIRADFETKMTDSCKRFQEIEESHLRQMKEFLASYAEVLSENHSAVGQVHEEFKRQVDELTVDKLL 240

                         250       260
                  ....*....|....*....|
gi 1858900827 250 RKFAESKGTGREKPGPLDFE 269
Cdd:cd07648   241 RQFVESKGTGTEKPELIEFE 260
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 3-269 1.18e-140

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: 415.61  E-value: 1.18e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827   3 YFGEHFWGEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLA 82
Cdd:cd07673     1 YFLENFWGEKNSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  83 LCHLELTRKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMD 162
Cdd:cd07673    81 NCHLELVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEQERLKKEGATQREIE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 163 KAETKTKKAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIEN 242
Cdd:cd07673   161 KAAVKSKKATESYKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIRIKEIIGSYSNSVKEIHIQIGQVHEEFINNMAN 240

                         250       260
                  ....*....|....*....|....*..
gi 1858900827 243 VSVEMLLRKFAESKGTGREKPGPLDFE 269
Cdd:cd07673   241 TTVESLIQKFAESKGTGKERPGPIEFE 267
FCHo2_MHD cd09267
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 ...
 535-797 1.54e-114

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: 348.17  E-value: 1.54e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 535 PIATAFTEYVHAYFRGHSPS-CLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 613
Cdd:cd09267     1 PVAVALTESVNAYFKGADPTkCIVKITGDMTVSFPSGIIKVFTSNPSPAVLCFRLKNTSRLEQILPNAQLLYSDPSQSDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 614 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPGATAVPTPL 693
Cdd:cd09267    81 NTKDFWMNMQAVTVYLKKSSEQNPAASYYNVDILKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMQPPSPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 694 TNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEA---GGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGV 770
Cdd:cd09267   161 SNVQVLVPVDGGVTNMQSLPPAIWNAEQMKALWKLSSISEKsenGGSGSLRAKFELSEGPSKPATLAVQFFSEGSTLSGV 240

                         250       260
                  ....*....|....*....|....*..
gi 1858900827 771 DLELVGSGYRMSLVKRRFATGMYLVSC 797
Cdd:cd09267   241 DMELVGTGYRLSLNKKRFATGRYMADC 267
SGIP1_MHD cd09266
mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2) ...
 535-794 2.56e-98

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: 306.21  E-value: 2.56e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 535 PIATAFTEYVHAYFRGHSPS-CLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDP 613
Cdd:cd09266     1 PVAAAFTETVNAYFKGADPSkCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 614 ETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPGATAVPTPL 693
Cdd:cd09266    81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 694 TNVQILLPVGEPVTNVR-LQPAATWNLEEKRLTWRLPDV---SEAGGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSG 769
Cdd:cd09266   161 NNVQFLVPIDGGVTKLQaVLPPAVWNAEQQRILWKIPDIsqkSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                         250       260
                  ....*....|....*....|....*
gi 1858900827 770 VDLELVGSGYRMSLVKRRFATGMYL 794
Cdd:cd09266   241 CDIELVGPGYRFSLIKKRFAAGKYL 265
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 534-794 4.83e-77

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: 249.54  E-value: 4.83e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 534 LPIATAFTEYVHAYFRGHSPSClARVTGELTMTFPAGIVRVFsgtPPPPVLSFRLVHTTAIEHFQPNADLLFsDPSQSDP 613
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK-SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 614 EtkdFWLNMAALTEALQRQAeqnptasyynvvlLRYQFSR-PGPQSVPLQLSAHWQCGATLTQVSVEYGYRPG-ATAVPT 691
Cdd:pfam10291  76 E---FKVNPQFLASRTPLGA-------------LKYQVHIdPLSASCPLILHPVWKCEPHQASLILTYSLNPSlAIASAV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 692 PLTNVQILLPVGEP-VTNVRLQPAATWNLEEKRLTWRLPDVSEA--GGSGRLSASWEPLSGPSTPSPVAAQFTSE-GTTL 767
Cdd:pfam10291 140 VLENLQVVVNLDGShATSAQSKPQGTFNKEKSRITWKLPELSLTsdGDGGKLIARFMTEGGASKPGGVAVKFEIEtGDTL 219

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1858900827 768 SGVDLELV---------GSGYRMSLVKRRFATGMYL 794
Cdd:pfam10291 220 SGLGISLVdqvdeedpfGGGWKLVPTKRRLAAGKYL 255
AP_muniscins_like_MHD cd09257
Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family ...
 535-796 2.88e-44

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: 159.84  E-value: 2.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 535 PIATAFTEYVHAYFRGHSPSCLArVTGELTMTFPAGIVRvfsgtPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDPe 614
Cdd:cd09257     1 GVKAALTEELNAEFKGSSLQSVG-VEGEVQLAVPSSDAK-----PKPAPFNLRLNDASSLEKAAPNVAFLNSVPSGSSP- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 615 tKDFWLNMAALTealqrqaeqnptASYYNVVLLRYQFSrPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPgatAVPTPLT 694
Cdd:cd09257    74 -GEFLVNTKAIR------------ASEVGSPILKYSCS-SKLRPVPLRVQTVWRCESHQTSVMLQYVSNP---SLPGPLQ 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 695 NVQILLPV-GEPVTNVRLQPAATWNLEEKRLTWRLPDVSEAGGSGRLSASWEPLSGPST---PSPVAAQFTSEGTTLSGV 770
Cdd:cd09257   137 DVTVIVNVpPGAGENLKSSPGAVWNEEKRRLTWKLPELGVNGEGGELRARFQIDAGQTAekvPFPVLVRCLSEGSTLSGL 216

                         250       260
                  ....*....|....*....|....*...
gi 1858900827 771 DLELVGSGYRM--SLVKRRFATGMYLVS 796
Cdd:cd09257   217 GLEVVALEEEWafIEVKVTRRFGVYHAE 244
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 15-238 8.24e-33

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: 125.53  E-value: 8.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  15 GFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMG--TFAPLWEVFRVSSDKLALCHLELTRKL 92
Cdd:cd07610     1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPESGktSLGTSWNSLREETESAATVHEELSEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  93 QDLIKDVLRYGEEQLKTHKkcKEEVVSTLDAVQvlsgvsqllpksrenylnrcmdqerLRRESTSQKEmdkaetktKKAA 172
Cdd:cd07610    81 SQLIREPLEKVKEDKEQAR--KKELAEGEKLKK-------------------------KLQELWAKLA--------KKAD 125

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1858900827 173 ESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQ 238
Cdd:cd07610   126 EEYREQVEKLNPAQSEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKEIPQKIQQELEQSIN 191
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-238 2.58e-28

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: 114.11  E-value: 2.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  15 GFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLQD 94
Cdd:cd07647     6 GFDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGDEIGTLKSSWDSLRKETENVANAHIQLAQSLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  95 LIKDVLRYGEEQLKTHKKCKEEVvstlDAVQVLSGVS-QLLPKSRENYLNRCMD----QERLRRES--TSQKEMDKAETK 167
Cdd:cd07647    86 EAEKLEEFREKQKEERKKTEDIM----KRSQKNKKELyKKTMKAKKSYEQKCREkdkaEQAYEKSSsgAQPKEAEKLKKK 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1858900827 168 TKKAAES-------LRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQ 238
Cdd:cd07647   162 AAQCKTSaeeadsaYKSSIGCLEDARVEWESEHATACQVFQNMEEERIKFLRNALWVHCNLGSMQCVKLDEMYEDVRK 239
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 15-225 7.63e-24

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: 100.86  E-value: 7.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  15 GFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLQD 94
Cdd:cd07649     6 GFEILLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEEGTLGEAWAQVKKSLADEAEVHLKFSSKLQS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  95 LI-KDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKS---RENYLNRCMDQERLRRESTSQKEMDKAETKTKK 170
Cdd:cd07649    86 EVeKPLLNFRENFKKDMKKLDHHIADLRKQLASRYAAVEKARKAlleRQKDLEGKTQQLEIKLSNKTEEDIKKARRKSTQ 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1858900827 171 AAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDT 225
Cdd:cd07649   166 AGDDLMRCVDLYNQAQSKWFEEMVTTSLELERLEVERIEMIRQHLCQYTQLRHET 220
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 7-88 1.69e-20

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: 86.63  E-value: 1.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827    7 HFWGEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSK----LASNGTPMGTFAPLWEVFRVSSDKLA 82
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKklraVRDTEPEYGSLSKAWEVLLSETDALA 81


                   ....*.
gi 1858900827   83 LCHLEL 88
Cdd:smart00055  82 KQHLEL 87
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 15-87 6.10e-18

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: 78.85  E-value: 6.10e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1858900827  15 GFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSK-----LASNGTPMGTFAPLWEVFRVSSDKLALCHLE 87
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKkflkkKKKPEDDGGTLKKAWDELLTETEQLAKQHLK 78
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-238 2.79e-17

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: 81.92  E-value: 2.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  15 GFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNG-TPMGTFAPLWEVFRVSSDKLALCHLELTRKLQ 93
Cdd:cd07672     6 GYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGqTEINTLKRSLDVFKQQIDNVGQSHIQLAQTLR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  94 DLIKDVLRYGEEQlKTHKKCKEEVVSTLDAVQVLSGVSQLlpKSRENYLNRCMDQERL-----RRESTS-QKEMDKAETK 167
Cdd:cd07672    86 DEAKKMEDFRERQ-KLARKKIELIMDAIHKQRAMQFKKTM--ESKKNYEQKCRDKDEAeqavnRNANLVnVKQQEKLFAK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1858900827 168 ---TKKAAESLRRS----VEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQ 238
Cdd:cd07672   163 laqSKQNAEDADRLymqnISVLDKIREDWQKEHVKACEFFEKQECERINFFRNAVWTHVNQLSQQCVTSDEMYEEVRK 240
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
 8-220 1.95e-16

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: 79.35  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827   8 FWGEKnhGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLS-KL--ASNGTPmGTFAPLWEVFRVSSDKLALC 84
Cdd:cd07658     1 FMGQK--GFEELRRYVKQGGDFCKELATVLQERAELELNYAKGLSKLSgKLskASKSVS-GTLSSAWTCVAEEMESEADI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  85 HLELTRKL-QDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAV-----QVLSGVSQLLPKSREN---------YLNRCMDQE 149
Cdd:cd07658    78 HRNLGSALtEEAIKPLRQVLDEQHKTRKPVENEVDKAAKLLtdwrsEQIKVKKKLHGLARENeklqdqvedNKQSCTKQK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 150 RLRRES----TSQKEMDKAETKTKKAAESLRRS-VEKYNS------ARADFEQKMLDSALRFQAMEETHLRHMKALLGSY 218
Cdd:cd07658   158 MLNKLKksaeVQDKEDEKLEAKRKKGEESRLKAeNEYYTCcvrlerLRLEWESALRKGLNQYESLEEERLQHLKHSLSQY 237


                  ..
gi 1858900827 219 AH 220
Cdd:cd07658   238 LR 239
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 10-222 8.72e-13

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: 68.87  E-value: 8.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  10 GEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07651     1 GKNDAGFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSLGGSEEGGLKNSLDTLRLETESMAKSHLKFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  90 RKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLsgVSQLLPKSRENYLNRCMDQERLRRES--TSQKEMDKAETK 167
Cdd:cd07651    81 KQIRQDLEEKLAAFASSYTQKRKKIQSHMEKLLKKKQD--QEKYLEKAREKYEADCSKINSYTLQSqlTWGKELEKNNAK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1858900827 168 TKKAAESL---RRSVEKYNSARADFEQKMLD---SAL-RFQAMEETHLRHMKALLGSYAHSV 222
Cdd:cd07651   159 LNKAQSSInssRRDYQNAVKALRELNEIWNRewkAALdDFQDLEEERIQFLKSNCWTFANNI 220
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 13-241 8.93e-12

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: 65.75  E-value: 8.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  13 NHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKL 92
Cdd:cd07671     4 NTGYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAGGQTEINTLKASFDQLKQQIENIGNSHIQLAGML 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  93 QDLIKDVLRYGEEQlKTHKKCKEEVVSTLDAVQVlsGVSQLLPKSRENYLNRCMD----QERLRRESTS--QKEMDKAET 166
Cdd:cd07671    84 REELKSLEEFRERQ-KEQRKKYEAVMERVQKSKV--SLYKKTMESKKTYEQRCREadeaEQTFERSSSTgnPKQSEKSQN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 167 KTKKAAES-------LRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQN 239
Cdd:cd07671   161 KAKQCRDAateaervYKQNIEQLDKARTEWETEHILTCEVFQLQEDDRITILRNALWVHCNHFSMQCVKDDELYEEVRTT 240


                  ..
gi 1858900827 240 IE 241
Cdd:cd07671   241 LE 242
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 31-241 5.98e-10

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: 60.79  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  31 KELADFIRERATIEETYSKAMA----KLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLQDLIKD-VLRYGEE 105
Cdd:cd07655    22 DDLMKMVQERAEIEKAYAKKLKewakKWRDLIEKGPEYGTLETAWKGLLSEAERLSELHLSIRDKLLNDVVEeVKTWQKE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 106 --------QLKTHKKCKEEV-------VSTLDAVQvlsgvsqllpKSRENYLNRCmDQER--LRRESTSQKEMDKAETKT 168
Cdd:cd07655   102 nyhksmmgGFKETKEAEDGFakaqkpwAKLLKKVE----------KAKKAYHAAC-KAEKsaQKQENNAKSDTSLSPDQV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 169 KKAAESLRRSVEKYNSARADFEQK-----------MLDSALRF---QAMEETHLRHMKALLGSYaHSVED--THVQIGQV 232
Cdd:cd07655   171 KKLQDKVEKCKQEVSKTKDKYEKAledlnkynpryMEDMEQVFdkcQEFEEKRLDFFKEILLSY-HRHLDlsTNPSFKAI 249


                  ....*....
gi 1858900827 233 HEEFKQNIE 241
Cdd:cd07655   250 YRDLQQTII 258
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 15-192 1.05e-09

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: 59.67  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  15 GFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSK-----LASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07652     6 GLSTLLDRLKQSIASAKEFATFLKKRAAIEEEHARGLKKLARttldtYKRPDHKQGSFSNAYHSSLEFHEKLADNGLRFA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  90 RKLQ---DLIKDVLRYGEEQLKTHK---KCKEEVVStlDAVQVLSgvsqllpKSRENYLNRCMDQERLR--RESTSQKEM 161
Cdd:cd07652    86 KALNemsDELSSLAKTVEKSRKSIKetgKRAEKKVQ--DAEAAAE-------KAKARYDSLADDLERVKtgDPGKKLKFG 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1858900827 162 DKAETKTKKAAESLRRSVEKynsARADFEQK 192
Cdd:cd07652   157 LKGNKSAAQHEDELLRKVQA---ADQDYASK 184
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 16-239 8.80e-08

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: 53.22  E-value: 8.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  16 FEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPmgtfaplwEVFRVSSDKLALCHLELTRKLQDL 95
Cdd:cd07307     2 LDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSN--------TDLGEALEKFGKIQKELEEFRDQL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  96 IKDVLRYGEEQLKTHKKckeevvstldavqvlsgvSQLlpksrenylnRCMDQERLRRESTSQkEMDKAETKTKKAAESL 175
Cdd:cd07307    74 EQKLENKVIEPLKEYLK------------------KDL----------KEIKKRRKKLDKARL-DYDAAREKLKKLRKKK 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 176 RRSV------EKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQN 239
Cdd:cd07307   125 KDSSklaeaeEELQEAKEKYEELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
 643-780 4.22e-06

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: 49.12  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 643 NVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPgatAVPTPLTNVQILLPVGEPVTNVRLQPA---ATWNL 719
Cdd:cd09252    92 KFTLMSYRVDLNSLVSLPVYVKPQISFSGSSGRFEITVGSRQ---NLGKSIENVVVEIPLPKGVKSLRLTAShgsFSFDS 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1858900827 720 EEKRLTWRLPDVSeAGGSGRLSASWEPLSG---PSTPSPVAAQFTSEGTTLSG--VD-LELVGSGYR 780
Cdd:cd09252   169 STKTLVWNIGKLT-PGKTPTLRGSVSLSSGleaPSESPSISVQFKIPGYTPSGlkVDsLDIYNEKYK 234
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 32-240 2.21e-05

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: 46.96  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  32 ELADFIRERATIEETYSKAMAKLSK----LASNGTPMGTFAPLWEVFRVSSDKLALCHLELT--------RKLQDLIKDV 99
Cdd:cd07680    23 DLMNCVQERAKIEKAYGQQLTDWAKrwrqLIEKGPQYGSLERAWGAIMTEADKVSELHQEVKnnllnedlEKVKNWQKDA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 100 lrYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQE-RLRRESTS--------------QKEMDKA 164
Cdd:cd07680   103 --YHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKlAMTREANSkaeqsvtpeqqkklQDKVDKC 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1858900827 165 ETKTKKAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQ-IGQVHEEFKQNI 240
Cdd:cd07680   181 KQDVQKTQEKYEKVLDDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAESSsYAHVYRELEQTI 257
F-BAR_Syp1p_like cd07650
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein; F-BAR ...
 31-262 2.23e-05

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: 46.55  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  31 KELADFIRERATIEETYSKAMAKLSKLASNGTPM--GTFAPLWEVFRVSSDKLALCHLELTRKLQdliKDVlrygeEQLK 108
Cdd:cd07650    22 TELADWLQERRRLERQYVQGLRKLARRNEPLNKSllGVFQNPWLTIESETEFIAASHGELAQRIE---TDV-----EEPL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 109 THKKCKEEVVSTLDAVQVLSGVsqllpksrenylnrcmdQERLRRESTSQKEMDKAETKTKKAAESLRRSveKYNSARAD 188
Cdd:cd07650    94 RDFATSTEFMNTLDDDQNLSNL-----------------AKELDESQKKWDKLKKKHSKASSKAVSAAVS--DLEEARQQ 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1858900827 189 FEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLLRKFAESKGTGREK 262
Cdd:cd07650   155 WDSQAPFLFELLQAIDEERLNHLKDVLLQFQTHESDYALRTTESAEECMNQLLEFDTEDEIQRFARKASAGRFA 228
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 8-241 4.42e-05

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: 45.83  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827   8 FWGEKNHGFEVlyHSVKQGPISTKELADFIRERATIEETYSKAMAKLSK----LASNGTPMGTFAPLWEVFRVSSDKLAL 83
Cdd:cd07679     1 FWEVGNYKRTV--KRIDDGHRLCNDLMNCLHERARIEKVYAQQLTEWAKrwrqLVEKGPQYGTVEKAWCALMSEAEKVSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  84 CHLELT--------RKLQDLIKDVlrYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQE-RLRRE 154
Cdd:cd07679    79 LHLEVKaslmnedfEKIKNWQKEA--FHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHTACKEEKlATSRE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 155 STSQK-------EMDKAETKTKKAAESLRRSVEKYNSARADFE----QKMLDSALRF---QAMEETHLRHMKALLGSYAH 220
Cdd:cd07679   157 ANSKAdpalnpeQLKKLQDKVEKCKQDVLKTKEKYEKSLKELDqttpQYMENMEQVFeqcQQFEEKRLRFFREVLLEVQK 236

                         250       260
                  ....*....|....*....|..
gi 1858900827 221 SVEDTHV-QIGQVHEEFKQNIE 241
Cdd:cd07679   237 HLDLSNVaSYKNIYRELEQSIK 258
F-BAR_PACSIN3 cd07681
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 8-200 3.25e-04

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: 43.39  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827   8 FWGEKNHGFEVlyHSVKQGPISTKELADFIRERATIEETYSKAMAKLSK----LASNGTPMGTFAPLWEVFRVSSDKLAL 83
Cdd:cd07681     1 FWEAGNYRRTV--KRIEDGYRLCNDLVSCFQERAKIEKGYAQQLSDWARkwrgIVEKGPQYGTLEKAWHAFLTAAERLSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  84 CHLELTRKLQDLIKDVLR------YGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENY-LNRCMDQERLRREST 156
Cdd:cd07681    79 IHLELRENLVGEDSEKVRawqkeaFHKQMIGGFRESKEAEEGFRKAQKPWVKKLKEVESSKKGYhAARKDERTAQTRETH 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1858900827 157 SQKEMDKAETKTKKAAESLRRSVEKYNSARADFEqKMLDSALRF 200
Cdd:cd07681   159 AKADSTVSQEQLRKLQDRVEKCTQEAEKAKEQYE-KALEELNRY 201
AP_MHD_Cterm cd07954
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
 646-769 3.26e-04

C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins, delta-subunit of the heteroheptameric coat protein I (delta-COPI), a protein encoded by a pro-death gene referred as MuD (also known as MUDENG, mu-2 related death-inducing gene), an endocytic adaptor syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related proteins. 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. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, FCHo1/2, which represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. 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 SGIP1 does have a C-terminal MHD and has been classified into this family as well. It 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: 271157  Cd Length: 245  Bit Score: 43.16  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 646 LLRYQFSRPgPQSVPLQLSAHWQCGATLTQVSVEYGYRPGataVPTPLTNVQILLPVGEPVTNVRLQPA---ATWNLEEK 722
Cdd:cd07954    85 LMSYRTVEP-WSILPITIFPVVSEEGSQLEVVITLKLSES---LQLTAENVEVHIPLPSGVTSLKSKPSdgqAKFDPEKN 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1858900827 723 RLTWRLPDVSEAGGSGRLSASWEPLSGPSTPS----PVAAQFTSEGTTLSG 769
Cdd:cd07954   161 ALVWRIKRIPVGGKEQSLSAHVELGSLAHECPeeapPVSVSFEIPETTGSG 211
AP_delta-COPI_MHD cd09254
Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI ...
 643-775 4.37e-04

Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI complex-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. COPI complex-coated vesicles consist of a small GTPase, ADP-ribosylation factor 1 (ARF1) and a heteroheptameric coatomer composed of two subcomplexes, F-COPI and B-COPI. ARF1 regulates COPI vesicle formation by recruiting the coatomer onto Golgi membranes to initiate its coat function. Coatomer complexes then bind cargo molecules and self-assemble to form spherical cages that yield COPI-coated vesicles. The heterotetrameric F-COPI subcomplex contains beta-, gamma-, delta-, and zeta-COP subunits, where beta- and gamma-COP subunits are related to the large AP subunits, and delta- and zeta-COP subunits are related to the medium and small AP subunits, respectively. Due to the sequence similarity to the AP complexes, the F-COPI subcomplex might play a role in the cargo-binding. The heterotrimeric B-COPI contains alpha-, beta-, and epsilon-COP subunits, which are not related to the adaptins. This subcomplex is thought to participate in the cage-forming and might serve a function similar to that of clathrin. This family corresponds to the mu homology domain of delta-subunit of COPI complex (delta-COP), which is distantly related to the C-terminal domain of mu chains among AP complexes. The delta-COP subunit appears tightly associated with the beta-COP subunit to confer its interaction with ARF1. In addition, both delta- and beta-COP subunits contribute to a common binding site for arginine (R)-based signals, which are sorting motifs conferring transient endoplasmic reticulum (ER) localization to unassembled subunits of multimeric membrane proteins.


Pssm-ID: 271162  Cd Length: 237  Bit Score: 42.60  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827 643 NVVLLRYQFSRPGPQSVPLQLSAhWQC-GATLTQVSVEYGyrpgATAVPTPLTNVQILLPV---GEPVTNvrlQPAATWN 718
Cdd:cd09254    87 PVGVLKWRLQGSDESLLPLTINC-WPSeSGGGCDVTIEYE----LNRDDLELNDVVISIPLpsgDAPVVN---SIDGNYE 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1858900827 719 LEEKR--LTWRLPDVSEAGGSGRLSASWEPlSGPSTPSPVAAQFTSEgTTLSGVDLELV 775
Cdd:cd09254   159 YDSRKnvLEWKIPVIDASNSSGSLEFSIPA-DDEDAFFPISVSFTSS-KTFCGVKVVEV 215
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 32-182 4.61e-03

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: 39.62  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  32 ELADFIRERATIEETYSKAMAKL-----SKLASNGTPMGTFAPL-----WEVF-----RVSSDKLALCHL---ELTRKLQ 93
Cdd:cd07656    23 DLQDYFRRRAEIELEYSRSLEKLadrfsSKHKNEKSKREDWSLLspvncWNTLlvqtkQESRDHSTLSDIysnNLVQRLG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900827  94 DLIKDVLRygeeqlkTHKKCKEevVSTLDAVQVLSGVSQLLPKSRENYL--NRCMDQERLRRESTSQKEMDKAETKTKKA 171
Cdd:cd07656   103 QMSEDLQR-------ISKKCRE--IGSQLHDELLRVLNELQTAMKTYHTyhAESKSAERKLKEAEKQEEKQEQSPEKKLE 173

                         170
                  ....*....|.
gi 1858900827 172 AESLRRSVEKY 182
Cdd:cd07656   174 RSRSSKKIEKE 184
 
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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