NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568955653|ref|XP_006509828|]
View 

F-BAR domain only protein 1 isoform X1 [Mus musculus]

Protein Classification

BAR domain-containing protein( domain architecture ID 10166622)

BAR (Bin/Amphiphysin/Rvs) domain-containing protein may bind membranes and detect membrane curvature

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 5.18e-178

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: 513.34  E-value: 5.18e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  10 GDKNHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07674    1 GEKNAGFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNGSPLGTFAPMWEVFRVSSDKLALCHLELM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  90 RKLHDLLKDVLRYGEEQLKTHKKCKEEVLGTVDAVQMLSGVGQLLPKSRENYLSRCMDLERLRRENTSQKEMDKAETKSK 169
Cdd:cd07674   81 RKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQKELEKAELKTK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 170 KAADSLRRSVDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQNVENVTVDMLL 249
Cdd:cd07674  161 KAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDTHVQIGQVHEEFKQNVENVGVENLI 240

                        250       260
                 ....*....|....*....|.
gi 568955653 250 RKFAESKGTGREKPGPLDFDA 270
Cdd:cd07674  241 RKFAESKGTGKERPGPVGFEE 261
AP_MHD_Cterm super family cl10970
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
 611-872 2.22e-145

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.


The actual alignment was detected with superfamily member cd09268:

Pssm-ID: 472082  Cd Length: 265  Bit Score: 429.77  E-value: 2.22e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 611 PVATAFTEYVHAYFRGH-SPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVNTAPVEHFQPNADLIFSDPSQSDP 689
Cdd:cd09268    1 PVAAAFTEYVHAYFRGGaLEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 690 ETKDFWLNMAALTEALQHQAEQNPTASYYNLVLLRYQFSRPGPESVPLQMSAHWQCGPTLTRVSVEYSYRAgATAVSTPL 769
Cdd:cd09268   81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 770 TNVQILLPVGEPVTSVRLQPAATWNTEEKRFTWKLPDVCEA---GGSGHLSASWQPQSGPSTPSPVAAQFTSEGATLSGL 846
Cdd:cd09268  160 TDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGnehDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSGV 239

                        250       260
                 ....*....|....*....|....*.
gi 568955653 847 DLELLGGGYRMSLVKRRFATGMYLVS 872
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 5.18e-178

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: 513.34  E-value: 5.18e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  10 GDKNHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07674    1 GEKNAGFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNGSPLGTFAPMWEVFRVSSDKLALCHLELM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  90 RKLHDLLKDVLRYGEEQLKTHKKCKEEVLGTVDAVQMLSGVGQLLPKSRENYLSRCMDLERLRRENTSQKEMDKAETKSK 169
Cdd:cd07674   81 RKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQKELEKAELKTK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 170 KAADSLRRSVDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQNVENVTVDMLL 249
Cdd:cd07674  161 KAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDTHVQIGQVHEEFKQNVENVGVENLI 240

                        250       260
                 ....*....|....*....|.
gi 568955653 250 RKFAESKGTGREKPGPLDFDA 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 ...
 611-872 2.22e-145

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: 429.77  E-value: 2.22e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 611 PVATAFTEYVHAYFRGH-SPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVNTAPVEHFQPNADLIFSDPSQSDP 689
Cdd:cd09268    1 PVAAAFTEYVHAYFRGGaLEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 690 ETKDFWLNMAALTEALQHQAEQNPTASYYNLVLLRYQFSRPGPESVPLQMSAHWQCGPTLTRVSVEYSYRAgATAVSTPL 769
Cdd:cd09268   81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 770 TNVQILLPVGEPVTSVRLQPAATWNTEEKRFTWKLPDVCEA---GGSGHLSASWQPQSGPSTPSPVAAQFTSEGATLSGL 846
Cdd:cd09268  160 TDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGnehDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSGV 239

                        250       260
                 ....*....|....*....|....*.
gi 568955653 847 DLELLGGGYRMSLVKRRFATGMYLVS 872
Cdd:cd09268  240 DIELVGSGYRMSLVKKRFATGKYLVC 265
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 610-870 2.15e-73

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: 241.07  E-value: 2.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  610 LPVATAFTEYVHAYFRGHSPSClARVTGELTMTFPAGIVRVFsgtPPPPVLSFRLVNTAPVEHFQPNADLIFsDPSQSDP 689
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK-SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  690 EtkdFWLNMAALTEALQHQAeqnptasyynlvlLRYQFSR-PGPESVPLQMSAHWQCGPTLTRVSVEYSYRAG-ATAVST 767
Cdd:pfam10291  76 E---FKVNPQFLASRTPLGA-------------LKYQVHIdPLSASCPLILHPVWKCEPHQASLILTYSLNPSlAIASAV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  768 PLTNVQILLPVGEP-VTSVRLQPAATWNTEEKRFTWKLPDVCEA--GGSGHLSASWQPQSGPSTPSPVAAQFTSEGAT-- 842
Cdd:pfam10291 140 VLENLQVVVNLDGShATSAQSKPQGTFNKEKSRITWKLPELSLTsdGDGGKLIARFMTEGGASKPGGVAVKFEIETGDtl 219

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568955653  843 --------LSGLDLELLGGGYRMSLVKRRFATGMYL 870
Cdd:pfam10291 220 sglgislvDQVDEEDPFGGGWKLVPTKRRLAAGKYL 255
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 7-88 1.88e-19

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: 83.54  E-value: 1.88e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653     7 HFWGDKNHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSK----LASNGTPMGTFAPLWEVFRVSSDKLA 82
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKklraVRDTEPEYGSLSKAWEVLLSETDALA 81


                   ....*.
gi 568955653    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 1.20e-17

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: 78.08  E-value: 1.20e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955653   15 GFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSK-----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 5.18e-178

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: 513.34  E-value: 5.18e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  10 GDKNHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07674    1 GEKNAGFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNGSPLGTFAPMWEVFRVSSDKLALCHLELM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  90 RKLHDLLKDVLRYGEEQLKTHKKCKEEVLGTVDAVQMLSGVGQLLPKSRENYLSRCMDLERLRRENTSQKEMDKAETKSK 169
Cdd:cd07674   81 RKLNDLIKDINRYGDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQKELEKAELKTK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 170 KAADSLRRSVDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQNVENVTVDMLL 249
Cdd:cd07674  161 KAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDTHVQIGQVHEEFKQNVENVGVENLI 240

                        250       260
                 ....*....|....*....|.
gi 568955653 250 RKFAESKGTGREKPGPLDFDA 270
Cdd:cd07674  241 RKFAESKGTGKERPGPVGFEE 261
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 10-268 4.28e-147

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: 434.08  E-value: 4.28e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  10 GDKNHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07648    1 GEKNNGFDVLYHNMKHGQIAVKELADFLRERATIEETYSKALNKLAKQASNSSQLGTFAPLWLVLRVSTEKLSELHLQLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  90 RKLHDLLKDVLRYGEEQLKTHKKCKEEVLGTVDAVQMLSGVGQLLPKSRENYLSRCMDLERLRRENTSQKEMDKAETKSK 169
Cdd:cd07648   81 QKLQELIKDVQKYGEEQHKKHKKVKEEESGTAEAVQAIQTTTAALQKAKEAYHARCLELERLRRENASPKEIEKAEAKLK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 170 KAADSLRRSVDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQNVENVTVDMLL 249
Cdd:cd07648  161 KAQDEYKALVEKYNNIRADFETKMTDSCKRFQEIEESHLRQMKEFLASYAEVLSENHSAVGQVHEEFKRQVDELTVDKLL 240

                        250
                 ....*....|....*....
gi 568955653 250 RKFAESKGTGREKPGPLDF 268
Cdd:cd07648  241 RQFVESKGTGTEKPELIEF 259
FCHo1_MHD cd09268
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 ...
 611-872 2.22e-145

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: 429.77  E-value: 2.22e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 611 PVATAFTEYVHAYFRGH-SPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVNTAPVEHFQPNADLIFSDPSQSDP 689
Cdd:cd09268    1 PVAAAFTEYVHAYFRGGaLEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 690 ETKDFWLNMAALTEALQHQAEQNPTASYYNLVLLRYQFSRPGPESVPLQMSAHWQCGPTLTRVSVEYSYRAgATAVSTPL 769
Cdd:cd09268   81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 770 TNVQILLPVGEPVTSVRLQPAATWNTEEKRFTWKLPDVCEA---GGSGHLSASWQPQSGPSTPSPVAAQFTSEGATLSGL 846
Cdd:cd09268  160 TDVQILLPLDEPFTNLQSQPPAAWNAEERRLHWQLPHESAGnehDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSGV 239

                        250       260
                 ....*....|....*....|....*.
gi 568955653 847 DLELLGGGYRMSLVKRRFATGMYLVS 872
Cdd:cd09268  240 DIELVGSGYRMSLVKKRFATGKYLVC 265
AP_Syp1_like_MHD cd09265
Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to ...
 611-872 6.59e-137

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: 408.03  E-value: 6.59e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 611 PVATAFTEYVHAYFRGHSPS-CLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVNTAPVEHFQPNADLIFSDPSQSDP 689
Cdd:cd09265    1 PVAAAFTETVHAYFKGADPSkCIVKITGDMMMSFPAGIIRLLTSNPTPAPLTFRLKNASRLEHVLPNKQLIFSDPSQSDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 690 ETKDFWLNMAALTEALQHQAEQNPTASYYNLVLLRYQFSRPGPESVPLQMSAHWQCGPTLTRVSVEYSYRAGATAVSTPL 769
Cdd:cd09265   81 ETKDFWFNMPALTTYLKRQAEQNPTASYYNVDVLKYQVSPTGPQSTPLQLASYWKCEPSSTDLRVDYKYNPEAMAIATPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 770 TNVQILLPVGEPVTSVRLQPAATWNTEEKRFTWKLPDVCEA---GGSGHLSASWQPQSGPSTPSPVAAQFTSEGATLSGL 846
Cdd:cd09265  161 LNVQFSVPVDGGVTNVQSEPPATWNAEQKRLLWKLPDISQNsegGGVGSLRARFELSEGPSKPAPLAVQFNSEGTTLSGV 240

                        250       260
                 ....*....|....*....|....*.
gi 568955653 847 DLELLGGGYRMSLVKRRFATGMYLVS 872
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; ...
 3-269 2.85e-129

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: 388.65  E-value: 2.85e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653   3 YFGEHFWGDKNHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLA 82
Cdd:cd07673    1 YFLENFWGEKNSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  83 LCHLELTRKLHDLLKDVLRYGEEQLKTHKKCKEEVLGTVDAVQMLSGVGQLLPKSRENYLSRCMDLERLRRENTSQKEMD 162
Cdd:cd07673   81 NCHLELVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQNIQSITQALQKSKENYNAKCLEQERLKKEGATQREIE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 163 KAETKSKKAADSLRRSVDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQNVEN 242
Cdd:cd07673  161 KAAVKSKKATESYKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIRIKEIIGSYSNSVKEIHIQIGQVHEEFINNMAN 240

                        250       260
                 ....*....|....*....|....*..
gi 568955653 243 VTVDMLLRKFAESKGTGREKPGPLDFD 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 ...
 611-873 4.61e-96

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: 301.94  E-value: 4.61e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 611 PVATAFTEYVHAYFRGHSPS-CLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVNTAPVEHFQPNADLIFSDPSQSDP 689
Cdd:cd09267    1 PVAVALTESVNAYFKGADPTkCIVKITGDMTVSFPSGIIKVFTSNPSPAVLCFRLKNTSRLEQILPNAQLLYSDPSQSDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 690 ETKDFWLNMAALTEALQHQAEQNPTASYYNLVLLRYQFSRPGPESVPLQMSAHWQCGPTLTRVSVEYSYRAGATAVSTPL 769
Cdd:cd09267   81 NTKDFWMNMQAVTVYLKKSSEQNPAASYYNVDILKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMQPPSPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 770 TNVQILLPVGEPVTSVRLQPAATWNTEEKRFTWKLPDVCEA---GGSGHLSASWQPQSGPSTPSPVAAQFTSEGATLSGL 846
Cdd:cd09267  161 SNVQVLVPVDGGVTNMQSLPPAIWNAEQMKALWKLSSISEKsenGGSGSLRAKFELSEGPSKPATLAVQFFSEGSTLSGV 240

                        250       260
                 ....*....|....*....|....*..
gi 568955653 847 DLELLGGGYRMSLVKRRFATGMYLVSC 873
Cdd:cd09267  241 DMELVGTGYRLSLNKKRFATGRYMADC 267
SGIP1_MHD cd09266
mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2) ...
 611-870 1.99e-85

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: 273.86  E-value: 1.99e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 611 PVATAFTEYVHAYFRGHSPS-CLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVNTAPVEHFQPNADLIFSDPSQSDP 689
Cdd:cd09266    1 PVAAAFTETVNAYFKGADPSkCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 690 ETKDFWLNMAALTEALQHQAEQNPTASYYNLVLLRYQFSRPGPESVPLQMSAHWQCGPTLTRVSVEYSYRAGATAVSTPL 769
Cdd:cd09266   81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 770 TNVQILLPVGEPVTSVR-LQPAATWNTEEKRFTWKLPDV---CEAGGSGHLSASWQPQSGPSTPSPVAAQFTSEGATLSG 845
Cdd:cd09266  161 NNVQFLVPIDGGVTKLQaVLPPAVWNAEQQRILWKIPDIsqkSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                        250       260
                 ....*....|....*....|....*
gi 568955653 846 LDLELLGGGYRMSLVKRRFATGMYL 870
Cdd:cd09266  241 CDIELVGPGYRFSLIKKRFAAGKYL 265
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 610-870 2.15e-73

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: 241.07  E-value: 2.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  610 LPVATAFTEYVHAYFRGHSPSClARVTGELTMTFPAGIVRVFsgtPPPPVLSFRLVNTAPVEHFQPNADLIFsDPSQSDP 689
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK-SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  690 EtkdFWLNMAALTEALQHQAeqnptasyynlvlLRYQFSR-PGPESVPLQMSAHWQCGPTLTRVSVEYSYRAG-ATAVST 767
Cdd:pfam10291  76 E---FKVNPQFLASRTPLGA-------------LKYQVHIdPLSASCPLILHPVWKCEPHQASLILTYSLNPSlAIASAV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  768 PLTNVQILLPVGEP-VTSVRLQPAATWNTEEKRFTWKLPDVCEA--GGSGHLSASWQPQSGPSTPSPVAAQFTSEGAT-- 842
Cdd:pfam10291 140 VLENLQVVVNLDGShATSAQSKPQGTFNKEKSRITWKLPELSLTsdGDGGKLIARFMTEGGASKPGGVAVKFEIETGDtl 219

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568955653  843 --------LSGLDLELLGGGYRMSLVKRRFATGMYL 870
Cdd:pfam10291 220 sglgislvDQVDEEDPFGGGWKLVPTKRRLAAGKYL 255
AP_muniscins_like_MHD cd09257
Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family ...
 611-872 1.70e-35

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: 135.19  E-value: 1.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 611 PVATAFTEYVHAYFRGHSPSCLArVTGELTMTFPAGIVrvfsgTPPPPVLSFRLVNTAPVEHFQPNADLIFSDPSQSDPe 690
Cdd:cd09257    1 GVKAALTEELNAEFKGSSLQSVG-VEGEVQLAVPSSDA-----KPKPAPFNLRLNDASSLEKAAPNVAFLNSVPSGSSP- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 691 tKDFWLNMAALTealqhqaeqnptASYYNLVLLRYQFSrPGPESVPLQMSAHWQCGPTLTRVSVEYSYRAgatAVSTPLT 770
Cdd:cd09257   74 -GEFLVNTKAIR------------ASEVGSPILKYSCS-SKLRPVPLRVQTVWRCESHQTSVMLQYVSNP---SLPGPLQ 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 771 NVQILLPV-GEPVTSVRLQPAATWNTEEKRFTWKLPDVCEAGGSGHLSASWQPQSGPST---PSPVAAQFTSEGATLSGL 846
Cdd:cd09257  137 DVTVIVNVpPGAGENLKSSPGAVWNEEKRRLTWKLPELGVNGEGGELRARFQIDAGQTAekvPFPVLVRCLSEGSTLSGL 216

                        250       260
                 ....*....|....*....|....*...
gi 568955653 847 DLELLGGGYRM--SLVKRRFATGMYLVS 872
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 1.67e-29

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: 115.90  E-value: 1.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  15 GFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMG--TFAPLWEVFRVSSDKLALCHLELTRKL 92
Cdd:cd07610    1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPESGktSLGTSWNSLREETESAATVHEELSEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  93 HDLLKDVLRYGEEQLKTH-KKCKEEVLgtvdavqmlsgvgqllpksrenylsrcmDLERLRRENTSQKEmdkaetksKKA 171
Cdd:cd07610   81 SQLIREPLEKVKEDKEQArKKELAEGE----------------------------KLKKKLQELWAKLA--------KKA 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955653 172 ADSLRRSVDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQ 238
Cdd:cd07610  125 DEEYREQVEKLNPAQSEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKEIPQKIQQELEQSIN 191
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-238 1.27e-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: 115.27  E-value: 1.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  15 GFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLHD 94
Cdd:cd07647    6 GFDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGDEIGTLKSSWDSLRKETENVANAHIQLAQSLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  95 LLKDVLRYGEEQLKTHKKCKEevlgTVDAVQMLSGVG-QLLPKSRENYLSRCMD-------LERLrRENTSQKEMDKAET 166
Cdd:cd07647   86 EAEKLEEFREKQKEERKKTED----IMKRSQKNKKELyKKTMKAKKSYEQKCREkdkaeqaYEKS-SSGAQPKEAEKLKK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955653 167 KSKKA------ADSL-RRSVDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQ 238
Cdd:cd07647  161 KAAQCktsaeeADSAyKSSIGCLEDARVEWESEHATACQVFQNMEEERIKFLRNALWVHCNLGSMQCVKLDEMYEDVRK 239
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 15-225 3.70e-26

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: 107.79  E-value: 3.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  15 GFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLH- 93
Cdd:cd07649    6 GFEILLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEEGTLGEAWAQVKKSLADEAEVHLKFSSKLQs 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  94 DLLKDVLRYGEEQLKTHKKCKEEVlgtVDAVQMLSGVGQLLPKSRENYLSRCMDLE------RLRRENTSQKEMDKAETK 167
Cdd:cd07649   86 EVEKPLLNFRENFKKDMKKLDHHI---ADLRKQLASRYAAVEKARKALLERQKDLEgktqqlEIKLSNKTEEDIKKARRK 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568955653 168 SKKAADSLRRSVDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDT 225
Cdd:cd07649  163 STQAGDDLMRCVDLYNQAQSKWFEEMVTTSLELERLEVERIEMIRQHLCQYTQLRHET 220
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 7-88 1.88e-19

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: 83.54  E-value: 1.88e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653     7 HFWGDKNHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSK----LASNGTPMGTFAPLWEVFRVSSDKLA 82
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKklraVRDTEPEYGSLSKAWEVLLSETDALA 81


                   ....*.
gi 568955653    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 1.20e-17

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: 78.08  E-value: 1.20e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955653   15 GFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSK-----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-15

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: 76.14  E-value: 2.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  15 GFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNG-TPMGTFAPLWEVFRVSSDKLALCHLELTRKLH 93
Cdd:cd07672    6 GYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGqTEINTLKRSLDVFKQQIDNVGQSHIQLAQTLR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  94 DLLKDVLRYGEEQlKTHKKCKEEVLGTVDAVQMLSGVGQLlpKSRENYLSRCMDLERL-----RRENTS-QKEMDKAETK 167
Cdd:cd07672   86 DEAKKMEDFRERQ-KLARKKIELIMDAIHKQRAMQFKKTM--ESKKNYEQKCRDKDEAeqavnRNANLVnVKQQEKLFAK 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955653 168 ---SKKAADSLRRS----VDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQ 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 3.45e-15

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: 75.88  E-value: 3.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653   8 FWGdkNHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLS-KL--ASNGTPmGTFAPLWEVFRVSSDKLALC 84
Cdd:cd07658    1 FMG--QKGFEELRRYVKQGGDFCKELATVLQERAELELNYAKGLSKLSgKLskASKSVS-GTLSSAWTCVAEEMESEADI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  85 HLELTRKLH-DLLKDVLRYGEEQLKTHKKCKEEVLGTVDAV-----QMLSGVGQLLPKSREN-YLSRCMDLERLRR---- 153
Cdd:cd07658   78 HRNLGSALTeEAIKPLRQVLDEQHKTRKPVENEVDKAAKLLtdwrsEQIKVKKKLHGLARENeKLQDQVEDNKQSCtkqk 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 154 --------ENTSQKEMDKAETKSKKAADSLRRS-VDKYNS------ARADFEIKMLDSALRFQAMEEAHLQHMKALLGSY 218
Cdd:cd07658  158 mlnklkksAEVQDKEDEKLEAKRKKGEESRLKAeNEYYTCcvrlerLRLEWESALRKGLNQYESLEEERLQHLKHSLSQY 237


                 ..
gi 568955653 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 1.70e-12

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: 68.10  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  10 GDKNHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07651    1 GKNDAGFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSLGGSEEGGLKNSLDTLRLETESMAKSHLKFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  90 RKLHDLLKDVLRYGEEQLKTHKKCKEEVLGTVDAVQmlSGVGQLLPKSRENYLSRCMDLERLRRE-NTSQ-KEMDKAETK 167
Cdd:cd07651   81 KQIRQDLEEKLAAFASSYTQKRKKIQSHMEKLLKKK--QDQEKYLEKAREKYEADCSKINSYTLQsQLTWgKELEKNNAK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955653 168 SKKAADS--------------LRRSVDKYNSARADFeikmLDSalrFQAMEEAHLQHMKALLGSYAHSV 222
Cdd:cd07651  159 LNKAQSSinssrrdyqnavkaLRELNEIWNREWKAA----LDD---FQDLEEERIQFLKSNCWTFANNI 220
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 13-241 7.27e-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: 66.14  E-value: 7.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  13 NHGFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKL 92
Cdd:cd07671    4 NTGYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAGGQTEINTLKASFDQLKQQIENIGNSHIQLAGML 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  93 HDLLKDVLRYGEEQLKTHKKCKeevlGTVDAVQ--MLSGVGQLLpKSRENYLSRCMD-------LERLrRENTSQKEMDK 163
Cdd:cd07671   84 REELKSLEEFRERQKEQRKKYE----AVMERVQksKVSLYKKTM-ESKKTYEQRCREadeaeqtFERS-SSTGNPKQSEK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 164 AETKSKKAADS-------LRRSVDKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEF 236
Cdd:cd07671  158 SQNKAKQCRDAateaervYKQNIEQLDKARTEWETEHILTCEVFQLQEDDRITILRNALWVHCNHFSMQCVKDDELYEEV 237


                 ....*
gi 568955653 237 KQNVE 241
Cdd:cd07671  238 RTTLE 242
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 15-181 1.09e-11

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: 65.45  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  15 GFEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSK-----LASNGTPMGTFAPLWEVFRVSSDKLALCHLELT 89
Cdd:cd07652    6 GLSTLLDRLKQSIASAKEFATFLKKRAAIEEEHARGLKKLARttldtYKRPDHKQGSFSNAYHSSLEFHEKLADNGLRFA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  90 RKL---HDLLKDVLRYGEEQLKTHK---KCKEEVLGtvDAVqmlsgvgQLLPKSRENYLSRCMDLERLRRENTSQKEMDK 163
Cdd:cd07652   86 KALnemSDELSSLAKTVEKSRKSIKetgKRAEKKVQ--DAE-------AAAEKAKARYDSLADDLERVKTGDPGKKLKFG 156

                        170       180
                 ....*....|....*....|..
gi 568955653 164 aeTKSKKAA----DSLRRSVDK 181
Cdd:cd07652  157 --LKGNKSAaqheDELLRKVQA 176
F-BAR_Syp1p_like cd07650
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein; F-BAR ...
 31-262 2.30e-06

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: 49.63  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  31 KELADFIRERANIEETYSKAMAKLSKLASNGTPM--GTFAPLWEvfRVSSDklalchLELTRKLHDLLKDVLRYGEEQLK 108
Cdd:cd07650   22 TELADWLQERRRLERQYVQGLRKLARRNEPLNKSllGVFQNPWL--TIESE------TEFIAASHGELAQRIETDVEEPL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 109 THKKCKEEVLGTVDAVQMLSGVgqllpksrenylsrcmdlerLRRENTSQKEMDKAETKSKKAADSlrrSVDKYNSARAD 188
Cdd:cd07650   94 RDFATSTEFMNTLDDDQNLSNL--------------------AKELDESQKKWDKLKKKHSKASSK---AVSAAVSDLEE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 189 ------------FEIkmldsalrFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQNVENVTVDMLLRKFAESK 256
Cdd:cd07650  151 arqqwdsqapflFEL--------LQAIDEERLNHLKDVLLQFQTHESDYALRTTESAEECMNQLLEFDTEDEIQRFARKA 222


                 ....*.
gi 568955653 257 GTGREK 262
Cdd:cd07650  223 SAGRFA 228
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 16-239 2.13e-05

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: 46.28  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  16 FEVLYHCVKQGPVATKELADFIRERANIEETYSKAMAKLSKLASNGTPmgtfaplwEVFRVSSDKLALCHLELTRKLHDL 95
Cdd:cd07307    2 LDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSN--------TDLGEALEKFGKIQKELEEFRDQL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  96 LKDVLRYGEEQLKTHKKckeevlgtvdavqmlsgvgqllpksrenylSRCMDLERLRRE-NTSQKEMDKAETK----SKK 170
Cdd:cd07307   74 EQKLENKVIEPLKEYLK------------------------------KDLKEIKKRRKKlDKARLDYDAAREKlkklRKK 123

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955653 171 AADSLRRSV--DKYNSARADFEIKMLDSALRFQAMEEAHLQHMKALLGSYAHSVEDTHVQIGQVHEEFKQN 239
Cdd:cd07307  124 KKDSSKLAEaeEELQEAKEKYEELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
AP_Syp1_MHD cd09264
mu-homology domain (MHD) of adaptor protein (AP), Syp1, and related proteins; This family ...
 635-837 6.66e-05

mu-homology domain (MHD) of adaptor protein (AP), Syp1, and related proteins; This family corresponds to the MHD found in a novel endocytic adaptor Syp1 and related proteins. Syp1 is a poorly characterized yeast protein with multiple biological functions. It was originally identified as a suppressor of a yeast profiling deletion and later as a suppressor of arf3delta (Arf3 is the yeast homologue of Arf6, a mammalian regulator of endocytosis). Syp1 can bind to septins and physically link with cell polarity factors. It also directly binds to the endocytic adaptor/scaffold protein Ede1, and plays a role in endocytosis. Further studies show that Syp1 is itself an endocytic adaptor protein contributing to stress responses. Its mu-homology domain at the C-terminus binds to the cargo protein Mid2, a transmembrane stress sensor protein, and mediates Mid2 internalization. In addition, Syp1 contains an EFC/F-BAR domain which can induce membrane tabulation.


Pssm-ID: 271170  Cd Length: 257  Bit Score: 45.46  E-value: 6.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 635 VTGELTMTFpagivRVFSGTPPPPVLSFRLVNTAPVEHFQPNADLIfsdpsQSDPETKDFWLNMAALTEAlqhqaeqnpt 714
Cdd:cd09264   24 VIGEVALNY-----NSDPNVTPTSNINVRLNNFQVLEKVLLNPTFV-----EPVVSPNEFTVNPSLITSK---------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 715 asyyNLVLLRYQFSRPGPES-VPLQMSAHWQCGPTLTRVSVEYSYRAGATAVST-PLTNVQILLPVGE--PVTSVRLQPA 790
Cdd:cd09264   84 ----TLGAFKYQLHLDPSASqCPIIVTPVWKFEEHQASLIIFVKLNPSFRNSESlTLENLVLSVALDGavKATSAQSKPQ 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568955653 791 ATWNTEEKRFTWKLPDVCEAGGSGH-LSASWQ-PQSGPSTPSPVAAQFT 837
Cdd:cd09264  160 GSFSREKSRITWRLPDPTVLDDSEEkLIARFMtEGLGSEAPGGVEARFE 208
F-BAR_PACSIN3 cd07681
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 32-206 2.69e-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: 43.77  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  32 ELADFIRERANIEETYSKAMAKLSK----LASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLHDLLKDVLR------ 101
Cdd:cd07681   23 DLVSCFQERAKIEKGYAQQLSDWARkwrgIVEKGPQYGTLEKAWHAFLTAAERLSEIHLELRENLVGEDSEKVRawqkea 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 102 YGEEQLKTHKKCKEEVLGTVDA----VQMLSGVgqllPKSRENY-LSRCMDLERLRRENTSQKEMDKAETKSKKAADSLR 176
Cdd:cd07681  103 FHKQMIGGFRESKEAEEGFRKAqkpwVKKLKEV----ESSKKGYhAARKDERTAQTRETHAKADSTVSQEQLRKLQDRVE 178

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568955653 177 RSVDKYNSARADFEiKMLDSALRF-----QAMEEA 206
Cdd:cd07681  179 KCTQEAEKAKEQYE-KALEELNRYnprymEDMEQA 212
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 32-186 3.46e-04

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: 43.09  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653  32 ELADFIRERANIEETYSKAMAKLSK-LASNGTPMGTFAPLWEVFRVSSDKLALchLELTRKL---HDLLKDVLRY----- 102
Cdd:cd07656   23 DLQDYFRRRAEIELEYSRSLEKLADrFSSKHKNEKSKREDWSLLSPVNCWNTL--LVQTKQEsrdHSTLSDIYSNnlvqr 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 103 ----GEEQLKTHKKCKEevLGTVDAVQMLSGVGQLLPKSRENYL--SRCMDLERLRREntsqkemdkAETKSKKAADSLR 176
Cdd:cd07656  101 lgqmSEDLQRISKKCRE--IGSQLHDELLRVLNELQTAMKTYHTyhAESKSAERKLKE---------AEKQEEKQEQSPE 169

                        170
                 ....*....|
gi 568955653 177 RSVDKYNSAR 186
Cdd:cd07656  170 KKLERSRSSK 179
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
 719-842 1.77e-03

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: 41.03  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955653 719 NLVLLRYQFSRPGPESVPLQMSAHWQCGPTLTRVSVeysyRAG-ATAVSTPLTNVQILLPVGEPVTSVRLQPA---ATWN 794
Cdd:cd09252   92 KFTLMSYRVDLNSLVSLPVYVKPQISFSGSSGRFEI----TVGsRQNLGKSIENVVVEIPLPKGVKSLRLTAShgsFSFD 167

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568955653 795 TEEKRFTWKLPDVcEAGGSGHLSASWQPQSG---PSTPSPVAAQFTSEGAT 842
Cdd:cd09252  168 SSTKTLVWNIGKL-TPGKTPTLRGSVSLSSGleaPSESPSISVQFKIPGYT 217
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH