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Conserved domains on  [gi|157817165|ref|NP_001103127|]
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growth arrest-specific protein 7 isoform b [Mus musculus]

Protein Classification

BAR domain-containing protein; PX and BAR domain-containing protein( domain architecture ID 11244376)

BAR (Bin/Amphiphysin/Rvs) domain-containing protein may bind membranes and detect membrane curvature| PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domain-containing protein similar to Saccoglossus kowalevskii sorting nexin 2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 154-386 3.22e-156

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: 440.22  E-value: 3.22e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 154 NGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFS 233
Cdd:cd07649    1 NTTVTGFEILLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEEGTLGEAWAQVKKSLADEAEVHLKFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 234 AKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKAR 313
Cdd:cd07649   81 SKLQSEVEKPLLNFRENFKKDMKKLDHHIADLRKQLASRYAAVEKARKALLERQKDLEGKTQQLEIKLSNKTEEDIKKAR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817165 314 RKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQ 386
Cdd:cd07649  161 RKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTSLELERLEVERIEMIRQHLCQYTQLRHETDMFNQSTVEPVDQ 233
WW_FCH_linker pfam16623
Unstructured linker region between on GAS7 protein; WW_FCH_linker is a natively unstructured ...
 49-141 1.50e-59

Unstructured linker region between on GAS7 protein; WW_FCH_linker is a natively unstructured region on GAS7 or Growth arrest-specific protein 7 higher eukaryote proteins. It lies between the WW and the FCH domains. The function is not known but it carries a highly conserved TINCVTFP sequence motif which might be a binding domain.


:

Pssm-ID: 465206  Cd Length: 92  Bit Score: 188.54  E-value: 1.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165   49 SSSPGISASPGPHRSSLPTtVNGYHASGTPAHPPETAHMSLRKSTGDSQNLGSSSPGRKQSKENTITINCVTFPHPDTMP 128
Cdd:pfam16623   1 SSSPGTPKSPGRHKNSLPA-VNGYHSSGSPVHHGEHSHMSLRKSSTDPQSPGSPSPTRKQNKETTITINCVTFPHPDTMP 79

                          90
                  ....*....|...
gi 157817165  129 EQQLLKPTEWSYC 141
Cdd:pfam16623  80 EQQLLKPNEWSYC 92
 
Name Accession Description Interval E-value
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 154-386 3.22e-156

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: 440.22  E-value: 3.22e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 154 NGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFS 233
Cdd:cd07649    1 NTTVTGFEILLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEEGTLGEAWAQVKKSLADEAEVHLKFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 234 AKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKAR 313
Cdd:cd07649   81 SKLQSEVEKPLLNFRENFKKDMKKLDHHIADLRKQLASRYAAVEKARKALLERQKDLEGKTQQLEIKLSNKTEEDIKKAR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817165 314 RKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQ 386
Cdd:cd07649  161 RKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTSLELERLEVERIEMIRQHLCQYTQLRHETDMFNQSTVEPVDQ 233
WW_FCH_linker pfam16623
Unstructured linker region between on GAS7 protein; WW_FCH_linker is a natively unstructured ...
 49-141 1.50e-59

Unstructured linker region between on GAS7 protein; WW_FCH_linker is a natively unstructured region on GAS7 or Growth arrest-specific protein 7 higher eukaryote proteins. It lies between the WW and the FCH domains. The function is not known but it carries a highly conserved TINCVTFP sequence motif which might be a binding domain.


Pssm-ID: 465206  Cd Length: 92  Bit Score: 188.54  E-value: 1.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165   49 SSSPGISASPGPHRSSLPTtVNGYHASGTPAHPPETAHMSLRKSTGDSQNLGSSSPGRKQSKENTITINCVTFPHPDTMP 128
Cdd:pfam16623   1 SSSPGTPKSPGRHKNSLPA-VNGYHSSGSPVHHGEHSHMSLRKSSTDPQSPGSPSPTRKQNKETTITINCVTFPHPDTMP 79

                          90
                  ....*....|...
gi 157817165  129 EQQLLKPTEWSYC 141
Cdd:pfam16623  80 EQQLLKPNEWSYC 92
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 150-232 7.58e-18

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: 77.77  E-value: 7.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165   150 DPQGNGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQN----SLAAQEEGSLGEAWAQVKKSLADE 225
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKlravRDTEPEYGSLSKAWEVLLSETDAL 80


                   ....*..
gi 157817165   226 AEVHLKF 232
Cdd:smart00055  81 AKQHLEL 87
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 159-231 1.04e-15

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: 71.53  E-value: 1.04e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157817165  159 GFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSL-----AAQEEGSLGEAWAQVKKSLADEAEVHLK 231
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLkkkkkPEDDGGTLKKAWDELLTETEQLAKQHLK 78
PRK12704 PRK12704
phosphodiesterase; Provisional
 208-361 8.93e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 8.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 208 EGSLGEAWAQVKKSLAD---EAEVHLKfsaKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALT 284
Cdd:PRK12704  30 EAKIKEAEEEAKRILEEakkEAEAIKK---EALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817165 285 ERQKDLEMKTQQLEIKLSN--KTEEDIKKARRKSTQAGDDLMRcvdlYNQAQSKwfeEMVTTTLElERLEVERVEMIRQ 361
Cdd:PRK12704 107 KREEELEKKEKELEQKQQEleKKEEELEELIEEQLQELERISG----LTAEEAK---EILLEKVE-EEARHEAAVLIKE 177
 
Name Accession Description Interval E-value
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 154-386 3.22e-156

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: 440.22  E-value: 3.22e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 154 NGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFS 233
Cdd:cd07649    1 NTTVTGFEILLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEEGTLGEAWAQVKKSLADEAEVHLKFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 234 AKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKAR 313
Cdd:cd07649   81 SKLQSEVEKPLLNFRENFKKDMKKLDHHIADLRKQLASRYAAVEKARKALLERQKDLEGKTQQLEIKLSNKTEEDIKKAR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817165 314 RKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQ 386
Cdd:cd07649  161 RKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTSLELERLEVERIEMIRQHLCQYTQLRHETDMFNQSTVEPVDQ 233
WW_FCH_linker pfam16623
Unstructured linker region between on GAS7 protein; WW_FCH_linker is a natively unstructured ...
 49-141 1.50e-59

Unstructured linker region between on GAS7 protein; WW_FCH_linker is a natively unstructured region on GAS7 or Growth arrest-specific protein 7 higher eukaryote proteins. It lies between the WW and the FCH domains. The function is not known but it carries a highly conserved TINCVTFP sequence motif which might be a binding domain.


Pssm-ID: 465206  Cd Length: 92  Bit Score: 188.54  E-value: 1.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165   49 SSSPGISASPGPHRSSLPTtVNGYHASGTPAHPPETAHMSLRKSTGDSQNLGSSSPGRKQSKENTITINCVTFPHPDTMP 128
Cdd:pfam16623   1 SSSPGTPKSPGRHKNSLPA-VNGYHSSGSPVHHGEHSHMSLRKSSTDPQSPGSPSPTRKQNKETTITINCVTFPHPDTMP 79

                          90
                  ....*....|...
gi 157817165  129 EQQLLKPTEWSYC 141
Cdd:pfam16623  80 EQQLLKPNEWSYC 92
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 159-386 6.65e-44

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: 151.34  E-value: 6.65e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 159 GFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEG--SLGEAWAQVKKSLADEAEVHLKFSAKL 236
Cdd:cd07610    1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPESGktSLGTSWNSLREETESAATVHEELSEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 237 HSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKarkalterqkdlemktqqleiklsnkteedikkarrks 316
Cdd:cd07610   81 SQLIREPLEKVKEDKEQARKKELAEGEKLKKKLQELWAKLAK-------------------------------------- 122

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 317 tQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQ 386
Cdd:cd07610  123 -KADEEYREQVEKLNPAQSEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKEIPQKIQQELEQSIN 191
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 156-369 3.95e-31

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: 119.12  E-value: 3.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 156 TVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAK 235
Cdd:cd07647    3 STTGFDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGDEIGTLKSSWDSLRKETENVANAHIQLAQS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 236 LHSEVEKpLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKARRK 315
Cdd:cd07647   83 LREEAEK-LEEFREKQKEERKKTEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKAEQAYEKSSSGAQPKEAEKLKKK 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157817165 316 -------STQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQL 369
Cdd:cd07647  162 aaqcktsAEEADSAYKSSIGCLEDARVEWESEHATACQVFQNMEEERIKFLRNALWVHCNL 222
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 158-415 5.63e-20

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: 88.94  E-value: 5.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 158 AGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLH 237
Cdd:cd07648    5 NGFDVLYHNMKHGQIAVKELADFLRERATIEETYSKALNKLAKQASNSSQLGTFAPLWLVLRVSTEKLSELHLQLVQKLQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 238 sEVEKPLMNFRENFKKDMKKC---DHHIADLRKQLASRYASVEKARKALTERQKDLEMKtqqleiKLSNKTEEDIKKARR 314
Cdd:cd07648   85 -ELIKDVQKYGEEQHKKHKKVkeeESGTAEAVQAIQTTTAALQKAKEAYHARCLELERL------RRENASPKEIEKAEA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 315 KSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHET--------DMFNQSTVE-PVD 385
Cdd:cd07648  158 KLKKAQDEYKALVEKYNNIRADFETKMTDSCKRFQEIEESHLRQMKEFLASYAEVLSENhsavgqvhEEFKRQVDElTVD 237

                        250       260       270
                 ....*....|....*....|....*....|
gi 157817165 386 QLLRKvdpakdrelWVREHKTGNIRPVDME 415
Cdd:cd07648  238 KLLRQ---------FVESKGTGTEKPELIE 258
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 150-232 7.58e-18

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: 77.77  E-value: 7.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165   150 DPQGNGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQN----SLAAQEEGSLGEAWAQVKKSLADE 225
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKlravRDTEPEYGSLSKAWEVLLSETDAL 80


                   ....*..
gi 157817165   226 AEVHLKF 232
Cdd:smart00055  81 AKQHLEL 87
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 159-363 9.63e-18

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


Pssm-ID: 153355 [Multi-domain]  Cd Length: 242  Bit Score: 81.93  E-value: 9.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 159 GFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHS 238
Cdd:cd07671    6 GYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAGGQTEINTLKASFDQLKQQIENIGNSHIQLAGMLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 239 EVeKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKARRKSTQ 318
Cdd:cd07671   86 EL-KSLEEFRERQKEQRKKYEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAEQTFERSSSTGNPKQSEKSQNKAKQ 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157817165 319 AGDDLMRCVDLYNQ-------AQSKWFEEMVTTTLELERLEVERVEMIRQHL 363
Cdd:cd07671  165 CRDAATEAERVYKQnieqldkARTEWETEHILTCEVFQLQEDDRITILRNAL 216
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 140-415 1.36e-17

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: 82.03  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 140 YCDYFWADKKdpqgngtvAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVK 219
Cdd:cd07673    2 FLENFWGEKN--------SGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 220 KSLADEAEVHLKFSAKLHsEVEKPLMNFRENFKKDMKKCDHHIADLRKQLasryASVEKARKALTERQKDLEMKT-QQLE 298
Cdd:cd07673   74 TSTEKLANCHLELVRKLQ-ELIKEVQKYGEEQVKSHKKTKEEVAGTLEAV----QNIQSITQALQKSKENYNAKClEQER 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 299 IKLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHET----- 373
Cdd:cd07673  149 LKKEGATQREIEKAAVKSKKATESYKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIRIKEIIGSYSNSVKEIhiqig 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 157817165 374 ----DMFNQSTVEPVDQLLRKVDPAKDrelwvrehkTGNIRPVDME 415
Cdd:cd07673  229 qvheEFINNMANTTVESLIQKFAESKG---------TGKERPGPIE 265
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 158-360 1.81e-17

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: 81.19  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 158 AGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLH 237
Cdd:cd07651    5 AGFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSLGGSEEGGLKNSLDTLRLETESMAKSHLKFAKQIR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 238 SEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTE---RQKDLEMKTQQLEIKLSNKTEEDIKKARR 314
Cdd:cd07651   85 QDLEEKLAAFASSYTQKRKKIQSHMEKLLKKKQDQEKYLEKAREKYEAdcsKINSYTLQSQLTWGKELEKNNAKLNKAQS 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157817165 315 KSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIR 360
Cdd:cd07651  165 SINSSRRDYQNAVKALRELNEIWNREWKAALDDFQDLEEERIQFLK 210
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
 159-378 3.83e-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: 77.42  E-value: 3.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 159 GFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQ--NSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKL 236
Cdd:cd07658    6 GFEELRRYVKQGGDFCKELATVLQERAELELNYAKGLSKLSGklSKASKSVSGTLSSAWTCVAEEMESEADIHRNLGSAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 237 HSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKARRKS 316
Cdd:cd07658   86 TEEAIKPLRQVLDEQHKTRKPVENEVDKAAKLLTDWRSEQIKVKKKLHGLARENEKLQDQVEDNKQSCTKQKMLNKLKKS 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817165 317 TQAGD----DLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQlrHETDMFNQ 378
Cdd:cd07658  166 AEVQDkedeKLEAKRKKGEESRLKAENEYYTCCVRLERLRLEWESALRKGLNQYES--LEEERLQH 229
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 159-231 1.04e-15

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: 71.53  E-value: 1.04e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157817165  159 GFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSL-----AAQEEGSLGEAWAQVKKSLADEAEVHLK 231
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLkkkkkPEDDGGTLKKAWDELLTETEQLAKQHLK 78
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 158-373 1.54e-13

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: 70.36  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 158 AGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLH 237
Cdd:cd07674    5 AGFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNGSPLGTFAPMWEVFRVSSDKLALCHLELMRKLN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 238 SEVEKPLMNFRENFKKDMKKCDHHIADLR--KQLASRYASVEKARKALTERQKDLEmktqqlEIKLSNKTEEDIKKARRK 315
Cdd:cd07674   85 DLIKDINRYGDEQVKIHKKTKEEAIGTLEavQSLQVQSQHLQKSRENYHSKCVEQE------RLRREGVPQKELEKAELK 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157817165 316 STQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHET 373
Cdd:cd07674  159 TKKAAESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDT 216
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 156-368 3.01e-13

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: 68.82  E-value: 3.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 156 TVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEE-GSLGEAWAQVKKSLADEAEVHLKFSA 234
Cdd:cd07672    3 STGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEiNTLKRSLDVFKQQIDNVGQSHIQLAQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 235 KLHSEVEKpLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLE--IKLSNKTEED---I 309
Cdd:cd07672   83 TLRDEAKK-MEDFRERQKLARKKIELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEAEQAVNrnANLVNVKQQEklfA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157817165 310 KKARRKSTQAGDD--LMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQ----HLCQYTQ 368
Cdd:cd07672  162 KLAQSKQNAEDADrlYMQNISVLDKIREDWQKEHVKACEFFEKQECERINFFRNavwtHVNQLSQ 226
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 180-368 4.18e-13

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


Pssm-ID: 153337 [Multi-domain]  Cd Length: 251  Bit Score: 68.82  E-value: 4.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 180 FIRERIKIEEEYAKNLAKLSQNSLA-AQEEG----SLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENFKKD 254
Cdd:cd07653   27 FVKERAAIEQEYAKKLRKLVKKYLPkKKEEDeysfSSVKAFRSILNEVNDIAGQHELIAENLNSNVCKELKTLISELRQE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 255 MKKCDHHIADLRKQLASRYASVEKARKALTERQKDLE---MKTQQLEiKLSNKTEEDIKKARRKSTQAGDDLMRC----- 326
Cdd:cd07653  107 RKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEkakQKYEKAD-ADMNLTKADVEKAKANANLKTQAAEEAkneya 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157817165 327 --VDLYNQAQSK-WFEEMVTTTLELERLEVERVEMIRQHLCQYTQ 368
Cdd:cd07653  186 aqLQKFNKEQRQhYSTDLPQIFDKLQELDEKRINRTVELLLQAAE 230
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 175-341 3.85e-11

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: 63.10  E-value: 3.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 175 KEMSEFIRERIKIEEEYAKNLA-------KLSQNSLaaqEEGSLGEAWaqvkKSLADEAE----VHLKFSAKLHSEVEKP 243
Cdd:cd07655   22 DDLMKMVQERAEIEKAYAKKLKewakkwrDLIEKGP---EYGTLETAW----KGLLSEAErlseLHLSIRDKLLNDVVEE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 244 LMNFR-ENFKKDM-------KKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNK--TEEDIKKAR 313
Cdd:cd07655   95 VKTWQkENYHKSMmggfketKEAEDGFAKAQKPWAKLLKKVEKAKKAYHAACKAEKSAQKQENNAKSDTslSPDQVKKLQ 174

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 157817165 314 RKSTQAGDDLMRCVDLYNQA-------QSKWFEEM 341
Cdd:cd07655  175 DKVEKCKQEVSKTKDKYEKAledlnkyNPRYMEDM 209
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 175-370 5.69e-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: 56.20  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 175 KEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQE-----EGSLGEAWAQVKKSLADEAEVHLKFSAKLH----------SE 239
Cdd:cd07652   22 KEFATFLKKRAAIEEEHARGLKKLARTTLDTYKrpdhkQGSFSNAYHSSLEFHEKLADNGLRFAKALNemsdelsslaKT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 240 VEKPLMNFRENFKKDMKKCDHHIADLRKqLASRYASVEK--ARKALTERQKDLemKTQQLEIKLSNKTEEDikkARRKST 317
Cdd:cd07652  102 VEKSRKSIKETGKRAEKKVQDAEAAAEK-AKARYDSLADdlERVKTGDPGKKL--KFGLKGNKSAAQHEDE---LLRKVQ 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157817165 318 QAGDDLMRCVdlynQAQSKWFEEMVTTTL-----ELERLEVERVEMIRQHLCQYTQLR 370
Cdd:cd07652  176 AADQDYASKV----NAAQALRQELLSRHRpeavkDLFDLILEIDAALRLQYQKYALPN 229
F-BAR_Syp1p_like cd07650
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein; F-BAR ...
 171-412 2.43e-07

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


Pssm-ID: 153334 [Multi-domain]  Cd Length: 228  Bit Score: 51.17  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 171 KQMQKEMSEFIRERIKIEEEYAKNLAKLSQNS--LAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFR 248
Cdd:cd07650   18 KLVNTELADWLQERRRLERQYVQGLRKLARRNepLNKSLLGVFQNPWLTIESETEFIAASHGELAQRIETDVEEPLRDFA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 249 ENfKKDMKKCDHhiadlrkqlasryasvekaRKALTERQKDLEmktqqleiKLSNKTEEDIKKARRKSTQAGDDLMRCVD 328
Cdd:cd07650   98 TS-TEFMNTLDD-------------------DQNLSNLAKELD--------ESQKKWDKLKKKHSKASSKAVSAAVSDLE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 329 lynQAQSKW-------FEemvtttlELERLEVERVEMIRQHLCQYTQlrHETDMF--NQSTVEPVDQLLRKVDPAKDREL 399
Cdd:cd07650  150 ---EARQQWdsqapflFE-------LLQAIDEERLNHLKDVLLQFQT--HESDYAlrTTESAEECMNQLLEFDTEDEIQR 217

                        250
                 ....*....|...
gi 157817165 400 WVRehKTGNIRPV 412
Cdd:cd07650  218 FAR--KASAGRFA 228
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 175-380 2.67e-06

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: 47.82  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 175 KEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGsLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENFKKD 254
Cdd:cd07307   17 KKLLDSLKELPAAAEKLSEALQELGKELPDLSNTD-LGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDLKE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 255 MKKCdhhiadlrkqlasryasvekaRKALTERQKDLE-MKTQQLEIKLSNKTEEDIKKARRKstqagddlmrcvdlYNQA 333
Cdd:cd07307   96 IKKR---------------------RKKLDKARLDYDaAREKLKKLRKKKKDSSKLAEAEEE--------------LQEA 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157817165 334 QSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQlrHETDMFNQST 380
Cdd:cd07307  141 KEKYEELREELIEDLNKLEEKRKELFLSLLLSFIE--AQSEFFKEVL 185
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 170-340 3.03e-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: 45.42  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 170 GKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEG----SLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLM 245
Cdd:cd07680   17 GHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGpqygSLERAWGAIMTEADKVSELHQEVKNNLLNEDLEKVK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 246 NF-RENFKKDM-------KKCDHHIADLRKQLASRYASVEKARKA--LTERQKDLEMK-----------TQQLEIKLSNK 304
Cdd:cd07680   97 NWqKDAYHKQImggfketKEAEDGFRKAQKPWAKKMKELEAAKKAyhLACKEEKLAMTreanskaeqsvTPEQQKKLQDK 176

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157817165 305 TE---EDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEE 340
Cdd:cd07680  177 VDkckQDVQKTQEKYEKVLDDVGKTTPQYMENMEQVFEQ 215
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 170-368 1.23e-04

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: 43.52  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 170 GKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEE----GSLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLM 245
Cdd:cd07679   17 GHRLCNDLMNCLHERARIEKVYAQQLTEWAKRWRQLVEKgpqyGTVEKAWCALMSEAEKVSELHLEVKASLMNEDFEKIK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 246 NF-RENFKKDM-------KKCDHHIADLRKQLASRYASVEKARKAL--------------TERQKDLEMKTQQLEiKLSN 303
Cdd:cd07679   97 NWqKEAFHKQMmggfketKEAEDGFRKAQKPWAKKLKEVEAAKKAYhtackeeklatsreANSKADPALNPEQLK-KLQD 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157817165 304 KTE---EDIKKARRKSTQAGDDLmrcvdlyNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQ 368
Cdd:cd07679  176 KVEkckQDVLKTKEKYEKSLKEL-------DQTTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQK 236
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 176-340 2.28e-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: 42.32  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 176 EMSEFIRERIKIEEEYAKNLAKLS-------QNSLAAQEEGSLG---EAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLM 245
Cdd:cd07656   23 DLQDYFRRRAEIELEYSRSLEKLAdrfsskhKNEKSKREDWSLLspvNCWNTLLVQTKQESRDHSTLSDIYSNNLVQRLG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 246 NFRENFKKDMKKC-----------------------DHHIAdlrkQLASRYA-----SVEKARKALTERQKDLEMKTQQL 297
Cdd:cd07656  103 QMSEDLQRISKKCreigsqlhdellrvlnelqtamkTYHTY----HAESKSAerklkEAEKQEEKQEQSPEKKLERSRSS 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157817165 298 EI--KLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEE 340
Cdd:cd07656  179 KKieKEVEKRQAKYSEAKLKCTKARNEYLLNLAAANATIHKYFVQ 223
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 171-334 3.36e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165   171 KQMQKEMSEFIRERIKIEEEYAKNLAKL-----------SQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHS- 238
Cdd:pfam01576  415 QELQARLSESERQRAELAEKLSKLQSELesvssllneaeGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQl 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165   239 EVEKPLM--------NFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKteEDIK 310
Cdd:pfam01576  495 EDERNSLqeqleeeeEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAY--DKLE 572

                          170       180
                   ....*....|....*....|....
gi 157817165   311 KARRKSTQAGDDLMrcVDLYNQAQ 334
Cdd:pfam01576  573 KTKNRLQQELDDLL--VDLDHQRQ 594
F-BAR_FBP17 cd07676
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; ...
 170-369 5.34e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Formin Binding Protein 17 (FBP17), also called FormiN Binding Protein 1 (FNBP1), is involved in dynamin-mediated endocytosis. It is recruited to clathrin-coated pits late in the endocytosis process and may play a role in the invagination and scission steps. FBP17 binds in vivo to tankyrase, a protein involved in telomere maintenance and mitogen activated protein kinase (MAPK) signaling. 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: 153360 [Multi-domain]  Cd Length: 253  Bit Score: 41.57  E-value: 5.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 170 GKQMQKEMSEFIRERIKIEEEYAK---NLAKLSQNSLAAQEEG----SLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEK 242
Cdd:cd07676   17 GIEVLEKYIKFVKERTEIELSYAKqlrNLSKKYQPKKNSKEEEeykyTSCRAFLMTLNEMNDYAGQHEVISENLASQIIV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 243 PLMNFRENFKKDMK-------KCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLeiklsNKTEEDIKKARRK 315
Cdd:cd07676   97 ELTRYVQELKQERKshfhdgrKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADI-----NVTKADVEKARQQ 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157817165 316 -------STQAGDDLMRCVDLYNQAQSKWFEEMVTTTLE-LERLEVERVEMIRQHLCQYTQL 369
Cdd:cd07676  172 aqirhqmAEDSKAEYSSYLQKFNKEQHEHYYTHIPNIFQkIQEMEERRIGRVGESMKTYAEV 233
PRK12704 PRK12704
phosphodiesterase; Provisional
 208-361 8.93e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 8.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 208 EGSLGEAWAQVKKSLAD---EAEVHLKfsaKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALT 284
Cdd:PRK12704  30 EAKIKEAEEEAKRILEEakkEAEAIKK---EALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817165 285 ERQKDLEMKTQQLEIKLSN--KTEEDIKKARRKSTQAGDDLMRcvdlYNQAQSKwfeEMVTTTLElERLEVERVEMIRQ 361
Cdd:PRK12704 107 KREEELEKKEKELEQKQQEleKKEEELEELIEEQLQELERISG----LTAEEAK---EILLEKVE-EEARHEAAVLIKE 177
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
 171-327 1.05e-03

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 41.30  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165  171 KQMQKEMSEFIRERIKIEEEYAKNLAKLSQN----SLAAQEEGSLGEAWAQVKKSLADEAEVhLKFSAKLHSeVEKPLMN 246
Cdd:pfam18971 613 KKAQKDLEKSLRKREHLEKEVEKKLESKSGNknkmEAKAQANSQKDEIFALINKEANRDARA-IAYTQNLKG-IKRELSD 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165  247 FRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEM------KTQQLEIKLsNKTEEDIKKARRKSTQAG 320
Cdd:pfam18971 691 KLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGInpewisKVENLNAAL-NEFKNGKNKDFSKVTQAK 769


                  ....*..
gi 157817165  321 DDLMRCV 327
Cdd:pfam18971 770 SDLENSV 776
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
160-318 8.92e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 160 FELLLQKQLKGKQMQKEmsefIRERIKIEEEYAKNLAKLSQNSLAAQEEgslgeawaqvKKSLADEAEvhlKFSAKLHSE 239
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKS----LKKELEKLEELKKKLAELEKKLDELEEE----------LAELLKELE---ELGFESVEE 589

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 240 VEKPLMNFRENFKK--DMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKARRKST 317
Cdd:PRK03918 590 LEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL 669


                 .
gi 157817165 318 Q 318
Cdd:PRK03918 670 E 670
F-BAR_FNBP1L cd07675
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; ...
 178-315 9.52e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FormiN Binding Protein 1-Like (FNBP1L), also known as Toca-1 (Transducer of Cdc42-dependent actin assembly), forms a complex with neural Wiskott-Aldrich syndrome protein (N-WASP). The FNBP1L/N-WASP complex induces the formation of filopodia and endocytic vesicles. FNBP1L is required for Cdc42-induced actin assembly and is essential for autophagy of intracellular pathogens. It contains an N-terminal F-BAR domain, a central Cdc42-binding HR1 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: 153359 [Multi-domain]  Cd Length: 252  Bit Score: 37.72  E-value: 9.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 178 SEFIRERIKIEEEYAKNLAKLSQNSL----AAQEEGSLGE--AWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENF 251
Cdd:cd07675   25 AKFVKERLEIEQNYAKQLRNLVKKYCpkrsSKDEEPRFTSclSFYNILNELNDYAGQREVVAEEMGHRVYGELMRYSHDL 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817165 252 KKDMKkcdHHIADLRKQ---LASRYASVEKARKALTERQKDLEmKTQQLEIKL---SNKTEEDIKKARRK 315
Cdd:cd07675  105 KGERK---MHLQEGRKAqqyLDMCWKQMDNSKKKFERECREAE-KAQQSYERLdndTNATKSDVEKAKQQ 170
 
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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