NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2123155003|gb|KAH6210772|]
View 

hypothetical protein HBI15_148970 [Parastagonospora nodorum]

Protein Classification

BAR domain-containing protein( domain architecture ID 10166464)

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
AP_Syp1_MHD cd09264
mu-homology domain (MHD) of adaptor protein (AP), Syp1, and related proteins; This family ...
 598-875 1.65e-100

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: 313.17  E-value: 1.65e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 598 GLNASLVETVSAWFEQGKVTKAMVIGQVALAYNPIDlSSGPFGTESVRLENFPVLEKVAPNPAFIEQAHdSPGNYTVDLS 677
Cdd:cd09264     1 GLNASIVETVNASFKDGQLTKSSVIGEVALNYNSDP-NVTPTSNINVRLNNFQVLEKVLLNPTFVEPVV-SPNEFTVNPS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 678 KIM-KTSVAFHYQLHIENEnvAALAPLILAPLWKTEASQASAILHYSLNPKFNLGgaTSVTIRNLVLVVRLEPGSKATSC 756
Cdd:cd09264    79 LITsKTLGAFKYQLHLDPS--ASQCPIIVTPVWKFEEHQASLIIFVKLNPSFRNS--ESLTLENLVLSVALDGAVKATSA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 757 QSKPSGTFSREKGLIYWRLGDVTFSKDePTQTIRVRFITEGEAK--PGNVEARWEISGDQTltlGSGLGVSMSAPLNETK 834
Cdd:cd09264   155 QSKPQGSFSREKSRITWRLPDPTVLDD-SEEKLIARFMTEGLGSeaPGGVEARFEITDPDA---GSGLTISVFETTENSE 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2123155003 835 QDGeadpfadidenappASPATGWKPVATVKRITSGTYLGV 875
Cdd:cd09264   231 RSS--------------AESAGEWKEVPTSRKLVSGNYSSH 257
F-BAR_Syp1p_like cd07650
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein; F-BAR ...
 15-240 1.24e-93

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: 293.85  E-value: 1.24e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  15 LTPAQAVTVLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRHPPDESSDLGIFTTPWQKIVGATEAVAQSHEY 94
Cdd:cd07650     1 LSPYEATEILRIRLSQIKLVNTELADWLQERRRLERQYVQGLRKLARRNEPLNKSLLGVFQNPWLTIESETEFIAASHGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  95 LARKIEADVERPLRDYSRGSREIQAMGNISgNLAATAKEIDTAQKKTAKLRDKGAKAKASAVGDAVQEVEKAELSWDSSA 174
Cdd:cd07650    81 LAQRIETDVEEPLRDFATSTEFMNTLDDDQ-NLSNLAKELDESQKKWDKLKKKHSKASSKAVSAAVSDLEEARQQWDSQA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123155003 175 PYVFEQLQAIDESRLNHLRDVLTQFQTHEVDQVERNRITAEETLNALLNIETADEIQTWALRMRSG 240
Cdd:cd07650   160 PFLFELLQAIDEERLNHLKDVLLQFQTHESDYALRTTESAEECMNQLLEFDTEDEIQRFARKASAG 225
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 304-573 2.88e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  304 STHPYGRASSPERKSSTNIGSAFGGFGKGKSKDRDAPGSSDRPISPLRSLP--ETPGSPEPPESS---NHSRLPSADIPN 378
Cdd:PHA03247  2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPpaASPAGPLPPPTSaqpTAPPPPPGPPPP 2848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  379 GTATEVSHETSAPIATNGTVHESIPELIEPLQPPQIEEPKPEPEKDAEGFSVPPSVIDAITEAEreagfSQSESSTTPQF 458
Cdd:PHA03247  2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ-----APPPPQPQPQP 2923

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  459 KLDIRNAPIQEEDGDADAAMAnmvntlrAQAAPPKRSSTLRGRRDVRNSIFVPNP-AAPELQSIGEAPPLPsAGSGSGST 537
Cdd:PHA03247  2924 PPPPQPQPPPPPPPRPQPPLA-------PTTDPAGAGEPSGAVPQPWLGALVPGRvAVPRFRVPQPAPSRE-APASSTPP 2995

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2123155003  538 STTFPTPALPAQPASPAF----KPPHRSLLTDDHAASDTQ 573
Cdd:PHA03247  2996 LTGHSLSRVSSWASSLALheetDPPPVSLKQTLWPPDDTE 3035
 
Name Accession Description Interval E-value
AP_Syp1_MHD cd09264
mu-homology domain (MHD) of adaptor protein (AP), Syp1, and related proteins; This family ...
 598-875 1.65e-100

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: 313.17  E-value: 1.65e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 598 GLNASLVETVSAWFEQGKVTKAMVIGQVALAYNPIDlSSGPFGTESVRLENFPVLEKVAPNPAFIEQAHdSPGNYTVDLS 677
Cdd:cd09264     1 GLNASIVETVNASFKDGQLTKSSVIGEVALNYNSDP-NVTPTSNINVRLNNFQVLEKVLLNPTFVEPVV-SPNEFTVNPS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 678 KIM-KTSVAFHYQLHIENEnvAALAPLILAPLWKTEASQASAILHYSLNPKFNLGgaTSVTIRNLVLVVRLEPGSKATSC 756
Cdd:cd09264    79 LITsKTLGAFKYQLHLDPS--ASQCPIIVTPVWKFEEHQASLIIFVKLNPSFRNS--ESLTLENLVLSVALDGAVKATSA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 757 QSKPSGTFSREKGLIYWRLGDVTFSKDePTQTIRVRFITEGEAK--PGNVEARWEISGDQTltlGSGLGVSMSAPLNETK 834
Cdd:cd09264   155 QSKPQGSFSREKSRITWRLPDPTVLDD-SEEKLIARFMTEGLGSeaPGGVEARFEITDPDA---GSGLTISVFETTENSE 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2123155003 835 QDGeadpfadidenappASPATGWKPVATVKRITSGTYLGV 875
Cdd:cd09264   231 RSS--------------AESAGEWKEVPTSRKLVSGNYSSH 257
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 597-873 4.30e-96

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: 301.54  E-value: 4.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 597 PGLNASLVETVSAWFEQGKVTKAMVIGQVALAYNP-IDLSSGPFGTESVRLENFPVLEKVAPNPAFIEQAHDSPGNYTVD 675
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTKSKVTGEVALSYPAgIAASFTPPAVLNFRLNNFSRLEKVAPNPAFVTDESQSDGEFKVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 676 LSKIMKTS--VAFHYQLHIENenVAALAPLILAPLWKTEASQASAILHYSLNPKFNLggATSVTIRNLVLVVRLEpGSKA 753
Cdd:pfam10291  81 PQFLASRTplGALKYQVHIDP--LSASCPLILHPVWKCEPHQASLILTYSLNPSLAI--ASAVVLENLQVVVNLD-GSHA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 754 TSCQSKPSGTFSREKGLIYWRLGDVTFSKDEPTQTIRVRFITEGEA-KPGNVEARWEISGDQTLtlgSGLGVSMSAplne 832
Cdd:pfam10291 156 TSAQSKPQGTFNKEKSRITWKLPELSLTSDGDGGKLIARFMTEGGAsKPGGVAVKFEIETGDTL---SGLGISLVD---- 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2123155003 833 tkQDGEADPFADidenappaspatGWKPVATVKRITSGTYL 873
Cdd:pfam10291 229 --QVDEEDPFGG------------GWKLVPTKRRLAAGKYL 255
F-BAR_Syp1p_like cd07650
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein; F-BAR ...
 15-240 1.24e-93

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: 293.85  E-value: 1.24e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  15 LTPAQAVTVLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRHPPDESSDLGIFTTPWQKIVGATEAVAQSHEY 94
Cdd:cd07650     1 LSPYEATEILRIRLSQIKLVNTELADWLQERRRLERQYVQGLRKLARRNEPLNKSLLGVFQNPWLTIESETEFIAASHGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  95 LARKIEADVERPLRDYSRGSREIQAMGNISgNLAATAKEIDTAQKKTAKLRDKGAKAKASAVGDAVQEVEKAELSWDSSA 174
Cdd:cd07650    81 LAQRIETDVEEPLRDFATSTEFMNTLDDDQ-NLSNLAKELDESQKKWDKLKKKHSKASSKAVSAAVSDLEEARQQWDSQA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123155003 175 PYVFEQLQAIDESRLNHLRDVLTQFQTHEVDQVERNRITAEETLNALLNIETADEIQTWALRMRSG 240
Cdd:cd07650   160 PFLFELLQAIDEERLNHLKDVLLQFQTHESDYALRTTESAEECMNQLLEFDTEDEIQRFARKASAG 225
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 21-93 2.36e-09

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: 54.58  E-value: 2.36e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123155003  21 VTVLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRHPPD---ESSDLGIFTTPWQKIVGATEAVAQSHE 93
Cdd:pfam00611   2 FKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKkkkPEDDGGTLKKAWDELLTETEQLAKQHL 77
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 19-93 5.23e-05

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: 42.71  E-value: 5.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2123155003   19 QAVTVLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRHPP--DESSDLGIFTTPWQKIVGATEAVAQSHE 93
Cdd:smart00055   9 DGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAvrDTEPEYGSLSKAWEVLLSETDALAKQHL 85
PHA03247 PHA03247
large tegument protein UL36; Provisional
 304-573 2.88e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  304 STHPYGRASSPERKSSTNIGSAFGGFGKGKSKDRDAPGSSDRPISPLRSLP--ETPGSPEPPESS---NHSRLPSADIPN 378
Cdd:PHA03247  2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPpaASPAGPLPPPTSaqpTAPPPPPGPPPP 2848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  379 GTATEVSHETSAPIATNGTVHESIPELIEPLQPPQIEEPKPEPEKDAEGFSVPPSVIDAITEAEreagfSQSESSTTPQF 458
Cdd:PHA03247  2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ-----APPPPQPQPQP 2923

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  459 KLDIRNAPIQEEDGDADAAMAnmvntlrAQAAPPKRSSTLRGRRDVRNSIFVPNP-AAPELQSIGEAPPLPsAGSGSGST 537
Cdd:PHA03247  2924 PPPPQPQPPPPPPPRPQPPLA-------PTTDPAGAGEPSGAVPQPWLGALVPGRvAVPRFRVPQPAPSRE-APASSTPP 2995

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2123155003  538 STTFPTPALPAQPASPAF----KPPHRSLLTDDHAASDTQ 573
Cdd:PHA03247  2996 LTGHSLSRVSSWASSLALheetDPPPVSLKQTLWPPDDTE 3035
 
Name Accession Description Interval E-value
AP_Syp1_MHD cd09264
mu-homology domain (MHD) of adaptor protein (AP), Syp1, and related proteins; This family ...
 598-875 1.65e-100

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: 313.17  E-value: 1.65e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 598 GLNASLVETVSAWFEQGKVTKAMVIGQVALAYNPIDlSSGPFGTESVRLENFPVLEKVAPNPAFIEQAHdSPGNYTVDLS 677
Cdd:cd09264     1 GLNASIVETVNASFKDGQLTKSSVIGEVALNYNSDP-NVTPTSNINVRLNNFQVLEKVLLNPTFVEPVV-SPNEFTVNPS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 678 KIM-KTSVAFHYQLHIENEnvAALAPLILAPLWKTEASQASAILHYSLNPKFNLGgaTSVTIRNLVLVVRLEPGSKATSC 756
Cdd:cd09264    79 LITsKTLGAFKYQLHLDPS--ASQCPIIVTPVWKFEEHQASLIIFVKLNPSFRNS--ESLTLENLVLSVALDGAVKATSA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 757 QSKPSGTFSREKGLIYWRLGDVTFSKDePTQTIRVRFITEGEAK--PGNVEARWEISGDQTltlGSGLGVSMSAPLNETK 834
Cdd:cd09264   155 QSKPQGSFSREKSRITWRLPDPTVLDD-SEEKLIARFMTEGLGSeaPGGVEARFEITDPDA---GSGLTISVFETTENSE 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2123155003 835 QDGeadpfadidenappASPATGWKPVATVKRITSGTYLGV 875
Cdd:cd09264   231 RSS--------------AESAGEWKEVPTSRKLVSGNYSSH 257
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 597-873 4.30e-96

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: 301.54  E-value: 4.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 597 PGLNASLVETVSAWFEQGKVTKAMVIGQVALAYNP-IDLSSGPFGTESVRLENFPVLEKVAPNPAFIEQAHDSPGNYTVD 675
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTKSKVTGEVALSYPAgIAASFTPPAVLNFRLNNFSRLEKVAPNPAFVTDESQSDGEFKVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 676 LSKIMKTS--VAFHYQLHIENenVAALAPLILAPLWKTEASQASAILHYSLNPKFNLggATSVTIRNLVLVVRLEpGSKA 753
Cdd:pfam10291  81 PQFLASRTplGALKYQVHIDP--LSASCPLILHPVWKCEPHQASLILTYSLNPSLAI--ASAVVLENLQVVVNLD-GSHA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 754 TSCQSKPSGTFSREKGLIYWRLGDVTFSKDEPTQTIRVRFITEGEA-KPGNVEARWEISGDQTLtlgSGLGVSMSAplne 832
Cdd:pfam10291 156 TSAQSKPQGTFNKEKSRITWKLPELSLTSDGDGGKLIARFMTEGGAsKPGGVAVKFEIETGDTL---SGLGISLVD---- 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2123155003 833 tkQDGEADPFADidenappaspatGWKPVATVKRITSGTYL 873
Cdd:pfam10291 229 --QVDEEDPFGG------------GWKLVPTKRRLAAGKYL 255
F-BAR_Syp1p_like cd07650
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein; F-BAR ...
 15-240 1.24e-93

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: 293.85  E-value: 1.24e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  15 LTPAQAVTVLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRHPPDESSDLGIFTTPWQKIVGATEAVAQSHEY 94
Cdd:cd07650     1 LSPYEATEILRIRLSQIKLVNTELADWLQERRRLERQYVQGLRKLARRNEPLNKSLLGVFQNPWLTIESETEFIAASHGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  95 LARKIEADVERPLRDYSRGSREIQAMGNISgNLAATAKEIDTAQKKTAKLRDKGAKAKASAVGDAVQEVEKAELSWDSSA 174
Cdd:cd07650    81 LAQRIETDVEEPLRDFATSTEFMNTLDDDQ-NLSNLAKELDESQKKWDKLKKKHSKASSKAVSAAVSDLEEARQQWDSQA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123155003 175 PYVFEQLQAIDESRLNHLRDVLTQFQTHEVDQVERNRITAEETLNALLNIETADEIQTWALRMRSG 240
Cdd:cd07650   160 PFLFELLQAIDEERLNHLKDVLLQFQTHESDYALRTTESAEECMNQLLEFDTEDEIQRFARKASAG 225
AP_muniscins_like_MHD cd09257
Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family ...
 598-837 1.45e-30

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: 120.94  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 598 GLNASLVETVSAWFEQGKVTKAMVIGQVALAYNP--IDLSSGPFgteSVRLENFPVLEKVAPNPAFIEQ--AHDSPGNYT 673
Cdd:cd09257     1 GVKAALTEELNAEFKGSSLQSVGVEGEVQLAVPSsdAKPKPAPF---NLRLNDASSLEKAAPNVAFLNSvpSGSSPGEFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 674 VDLSKIMKTSV---AFHYQLHIENENVaalaPLILAPLWKTEASQASAILHYSLNPkfNLGGAtsvtIRNLVLVVRLePG 750
Cdd:cd09257    78 VNTKAIRASEVgspILKYSCSSKLRPV----PLRVQTVWRCESHQTSVMLQYVSNP--SLPGP----LQDVTVIVNV-PP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 751 SKATSCQSKPSGTFSREKGLIYWRLGDVtfSKDEPTQTIRVRFITEG----EAKPGNVEARWEISGDQtltlGSGLGVSM 826
Cdd:cd09257   147 GAGENLKSSPGAVWNEEKRRLTWKLPEL--GVNGEGGELRARFQIDAgqtaEKVPFPVLVRCLSEGST----LSGLGLEV 220

                         250
                  ....*....|.
gi 2123155003 827 SAPLNETKQDG 837
Cdd:cd09257   221 VALEEEWAFIE 231
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 21-219 1.04e-12

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: 67.75  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  21 VTVLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRHPPDESSDLGIFTTPWQKIVGATEAVAQSHEYLARKIE 100
Cdd:cd07610     2 FELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPESGKTSLGTSWNSLREETESAATVHEELSEKLS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 101 ADVERPLRDYSRGSReiQAMGNISGNLAATAKEIDTAQKKTAKlrdkgaKAKASAVgDAVQEVEKAELSWDSSAPYVFEQ 180
Cdd:cd07610    82 QLIREPLEKVKEDKE--QARKKELAEGEKLKKKLQELWAKLAK------KADEEYR-EQVEKLNPAQSEYEEEKLNKIQA 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2123155003 181 LQAIDESRLNHLRDVLTQFQTHEVDQVERNRITAEETLN 219
Cdd:cd07610   153 EQEREEERLEILKDNLKNYINAIKEIPQKIQQELEQSIN 191
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 23-234 1.15e-10

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: 63.15  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  23 VLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANrhPPDESSDLGIFTTPWQKIVGATEAVAQSHEYLARK---- 98
Cdd:cd07673    16 VLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAK--SASNYSQLGTFAPVWDVFKTSTEKLANCHLELVRKlqel 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  99 ---IEADVERPLRDYSRGSREI----QAMGNISGNLAATAKEIDTAQKKT---AKLRDKGAKAKasAVGDAVQEVEKAEL 168
Cdd:cd07673    94 ikeVQKYGEEQVKSHKKTKEEVagtlEAVQNIQSITQALQKSKENYNAKCleqERLKKEGATQR--EIEKAAVKSKKATE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 169 SWDS------SAPYVFEQ--------LQAIDESRLNHLRDVLTQF-----QTH-EVDQVErnritaEETLNALLNIETAD 228
Cdd:cd07673   172 SYKLyvekyaLAKADFEQkmtetaqkFQDIEETHLIRIKEIIGSYsnsvkEIHiQIGQVH------EEFINNMANTTVES 245


                  ....*.
gi 2123155003 229 EIQTWA 234
Cdd:cd07673   246 LIQKFA 251
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 27-202 8.23e-10

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: 60.44  E-value: 8.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  27 RMNHVDRLNNHIADWLQERRRVEEQYIQGL-------RKLANRHPpdessDLGIFTTPWQKIVGATEAVAQSHEYLARKI 99
Cdd:cd07680    13 RIDDGHRLCNDLMNCVQERAKIEKAYGQQLtdwakrwRQLIEKGP-----QYGSLERAWGAIMTEADKVSELHQEVKNNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 100 EADVERPLRDYSRGSREIQAMGNISGN-------------LAATAKEIDTAQK---------KTAKLRDKGAKAKASAVG 157
Cdd:cd07680    88 LNEDLEKVKNWQKDAYHKQIMGGFKETkeaedgfrkaqkpWAKKMKELEAAKKayhlackeeKLAMTREANSKAEQSVTP 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 158 DAV-----------QEVEKAELSWD--------------SSAPYVFEQLQAIDESRLNHLRDVLTQFQTH 202
Cdd:cd07680   168 EQQkklqdkvdkckQDVQKTQEKYEkvlddvgkttpqymENMEQVFEQCQQFEEKRLVFLKEVLLDIKRH 237
FCHo2_MHD cd09267
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 ...
 602-826 2.26e-09

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: 59.27  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 602 SLVETVSAWFEQGKVTKAMV--IGQVALAYNP----IDLSSGPFGTESVRLENFPVLEKVAPNPAFIEQAHDSPGNYTVD 675
Cdd:cd09267     5 ALTESVNAYFKGADPTKCIVkiTGDMTVSFPSgiikVFTSNPSPAVLCFRLKNTSRLEQILPNAQLLYSDPSQSDSNTKD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 676 LSKIMKTSVAFHYQLHIENE-----NVAAL-----------APLILAPLWKTEASQASAILHYSLNPKfnlGGATSVTIR 739
Cdd:cd09267    85 FWMNMQAVTVYLKKSSEQNPaasyyNVDILkyqvssngiqsTPLNLATYWKCSASTTDLRVDYKYNPE---AMQPPSPLS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 740 NLVLVVRLEPGskATSCQSKPSGTFSREKGLIYWRLGDVT-FSKDEPTQTIRVRF-ITEGEAKPGNVEARW-----EISG 812
Cdd:cd09267   162 NVQVLVPVDGG--VTNMQSLPPAIWNAEQMKALWKLSSISeKSENGGSGSLRAKFeLSEGPSKPATLAVQFfsegsTLSG 239

                         250
                  ....*....|....
gi 2123155003 813 DQTLTLGSGLGVSM 826
Cdd:cd09267   240 VDMELVGTGYRLSL 253
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 21-93 2.36e-09

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: 54.58  E-value: 2.36e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123155003  21 VTVLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRHPPD---ESSDLGIFTTPWQKIVGATEAVAQSHE 93
Cdd:pfam00611   2 FKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKkkkPEDDGGTLKKAWDELLTETEQLAKQHL 77
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 27-202 5.68e-08

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: 55.07  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  27 RMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANR--HPPDESSDLGIFTTPWQKIVGATEAVAQSH-EYLARKIEADV 103
Cdd:cd07679    13 RIDDGHRLCNDLMNCLHERARIEKVYAQQLTEWAKRwrQLVEKGPQYGTVEKAWCALMSEAEKVSELHlEVKASLMNEDF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 104 ERpLRDYSRGSREIQAMGNISGN-------------LAATAKEIDTAQK---------KTAKLRDKGAKAKASA------ 155
Cdd:cd07679    93 EK-IKNWQKEAFHKQMMGGFKETkeaedgfrkaqkpWAKKLKEVEAAKKayhtackeeKLATSREANSKADPALnpeqlk 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123155003 156 -----VGDAVQEV-------EKAELSWDSSAP-------YVFEQLQAIDESRLNHLRDVLTQFQTH 202
Cdd:cd07679   172 klqdkVEKCKQDVlktkekyEKSLKELDQTTPqymenmeQVFEQCQQFEEKRLRFFREVLLEVQKH 237
AP_Syp1_like_MHD cd09265
Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to ...
 599-826 1.00e-07

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: 54.03  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 599 LNASLVETVSAWFEQGKVTKAMV--IGQVALAYnPID----LSSGPFGTE-SVRLENFPVLEKVAPNPAFI--------- 662
Cdd:cd09265     2 VAAAFTETVHAYFKGADPSKCIVkiTGDMMMSF-PAGiirlLTSNPTPAPlTFRLKNASRLEHVLPNKQLIfsdpsqsds 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 663 -----------------EQAHDSPGN--YTVDLSKimktsvafhYQLHIENENVaalAPLILAPLWKTEASQASAILHYS 723
Cdd:cd09265    81 etkdfwfnmpalttylkRQAEQNPTAsyYNVDVLK---------YQVSPTGPQS---TPLQLASYWKCEPSSTDLRVDYK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 724 LNPKfnlGGATSVTIRNLVLVVRLEPGskATSCQSKPSGTFSREKGLIYWRLGDVT-FSKDEPTQTIRVRF-ITEGEAKP 801
Cdd:cd09265   149 YNPE---AMAIATPLLNVQFSVPVDGG--VTNVQSEPPATWNAEQKRLLWKLPDISqNSEGGGVGSLRARFeLSEGPSKP 223

                         250       260       270
                  ....*....|....*....|....*....|
gi 2123155003 802 GNVEARWE-----ISGDQTLTLGSGLGVSM 826
Cdd:cd09265   224 APLAVQFNsegttLSGVDIELVGSGYRLSL 253
SGIP1_MHD cd09266
mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2) ...
 601-829 1.28e-07

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: 53.91  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 601 ASLVETVSAWFEQGKVTKAMV--IGQVALAYnPIDL----SSGPF-GTESVRLENFPVLEKVAPNPAFI----EQAHDSP 669
Cdd:cd09266     4 AAFTETVNAYFKGADPSKCIVkiTGEMVLSF-PAGItrhfANNPSpAALTFRITNYSRLEHVLPNPQLLccdnTQAKGNA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 670 GNYTVDLSKIM--------KTSVAFHYQLHIENENVAALA----PLILAPLWKTEASQASAILHYSLNPKfnlGGATSVT 737
Cdd:cd09266    83 KEFWVNMPNLMthlkkvseQKPQATYYNVDMLKYQVSAQGpqstPLNLAVSWRCEPSSTDLRIDYKYNGD---AMTTPVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 738 IRNLVLVVRLEPGskATSCQSK-PSGTFSREKGLIYWRLGDVT-FSKDEPTQTIRVRF-ITEGEAKPGNVEARWEISGdQ 814
Cdd:cd09266   160 LNNVQFLVPIDGG--VTKLQAVlPPAVWNAEQQRILWKIPDISqKSENGGVGSLLARFqLSEGPSKPAPLAVQFTSEG-S 236

                         250
                  ....*....|....*
gi 2123155003 815 TLtlgSGLGVSMSAP 829
Cdd:cd09266   237 TL---SGCDIELVGP 248
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 33-205 1.30e-07

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: 53.48  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  33 RLNNHIADWLQERRRVEEQYIQGLRKLANRhpPDESSDLGIFTTPWQKIVGATEAVAQSHEYLARKIEADVERPLRDYSR 112
Cdd:cd07649    19 QMQKEMAEFIRERIKIEEEYAKNLSKLSQS--SLAAQEEGTLGEAWAQVKKSLADEAEVHLKFSSKLQSEVEKPLLNFRE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 113 GSReiQAMGNISGNLAATAKEI-------DTAQK-----------KTAKLR----------DKGAKAKASAVGD----AV 160
Cdd:cd07649    97 NFK--KDMKKLDHHIADLRKQLasryaavEKARKallerqkdlegKTQQLEiklsnkteedIKKARRKSTQAGDdlmrCV 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2123155003 161 QEVEKAELSWDSSAPYVFEQLQAIDESRLNHLRDVLTQFQT--HEVD 205
Cdd:cd07649   175 DLYNQAQSKWFEEMVTTSLELERLEVERIEMIRQHLCQYTQlrHETD 221
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 23-199 2.29e-07

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: 53.11  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  23 VLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRhpPDESSDLGIFTTPWQKIVGATEAVAQSHEYLARKIE-- 100
Cdd:cd07648     9 VLYHNMKHGQIAVKELADFLRERATIEETYSKALNKLAKQ--ASNSSQLGTFAPLWLVLRVSTEKLSELHLQLVQKLQel 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 101 -ADVERPLRDYSRGSREI-----------QAMGNISGNLaATAKEIDTAQ-KKTAKLRDKGAKAKasavgdavqEVEKAE 167
Cdd:cd07648    87 iKDVQKYGEEQHKKHKKVkeeesgtaeavQAIQTTTAAL-QKAKEAYHARcLELERLRRENASPK---------EIEKAE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2123155003 168 L----SWDSSAPYV---------FEQ--------LQAIDESRLNHLRDVLTQF 199
Cdd:cd07648   157 AklkkAQDEYKALVekynniradFETkmtdsckrFQEIEESHLRQMKEFLASY 209
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 23-196 6.97e-07

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: 51.32  E-value: 6.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  23 VLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRHPPDESSdlGIFTTPWQKIVGATEAVAQSHEYLA------ 96
Cdd:cd07647     9 TLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGDEI--GTLKSSWDSLRKETENVANAHIQLAqslree 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  97 ---------------RKIEADVERPLRD--------------YSRGSREIQAMGNISGNLAATA--KEIDTAQKKTAKLR 145
Cdd:cd07647    87 aekleefrekqkeerKKTEDIMKRSQKNkkelykktmkakksYEQKCREKDKAEQAYEKSSSGAqpKEAEKLKKKAAQCK 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2123155003 146 DKGAKAKaSAVGDAVQEVEKAELSWDSSAPYVFEQLQAIDESRLNHLRDVL 196
Cdd:cd07647   167 TSAEEAD-SAYKSSIGCLEDARVEWESEHATACQVFQNMEEERIKFLRNAL 216
F-BAR_PACSIN3 cd07681
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 27-202 1.19e-06

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: 50.71  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  27 RMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLAN--RHPPDESSDLGIFTTPWQKIVGATEAVAQSHEYLARKIEADVE 104
Cdd:cd07681    13 RIEDGYRLCNDLVSCFQERAKIEKGYAQQLSDWARkwRGIVEKGPQYGTLEKAWHAFLTAAERLSEIHLELRENLVGEDS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 105 RPLRDYSRGSREIQAMGNISGNLAA-------------TAKEIDTAQK---------KTAKLRDKGAKAKASAVGDAV-- 160
Cdd:cd07681    93 EKVRAWQKEAFHKQMIGGFRESKEAeegfrkaqkpwvkKLKEVESSKKgyhaarkdeRTAQTRETHAKADSTVSQEQLrk 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123155003 161 ---------QEVEKAELSWDSS--------------APYVFEQLQAIDESRLNHLRDVLTQFQTH 202
Cdd:cd07681   173 lqdrvekctQEAEKAKEQYEKAleelnrynprymedMEQAFEICQEAERKRLCFFKEMLLDLHQH 237
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 42-202 2.52e-06

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: 50.01  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  42 LQERRRVEEQYIQGLRKLANRHPP--DESSDLGIFTTPWQKIVGATEAVAQSHEYLARKIEADVERPLRDYSRGSREIQA 119
Cdd:cd07655    28 VQERAEIEKAYAKKLKEWAKKWRDliEKGPEYGTLETAWKGLLSEAERLSELHLSIRDKLLNDVVEEVKTWQKENYHKSM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 120 MGNISgnlaaTAKEIDT----AQK-----------------------KTAKLRDKGAKAKASAVGDAV-----------Q 161
Cdd:cd07655   108 MGGFK-----ETKEAEDgfakAQKpwakllkkvekakkayhaackaeKSAQKQENNAKSDTSLSPDQVkklqdkvekckQ 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2123155003 162 EVEK---------AELSWDSSA-----PYVFEQLQAIDESRLNHLRDVLTQFQTH 202
Cdd:cd07655   183 EVSKtkdkyekalEDLNKYNPRymedmEQVFDKCQEFEEKRLDFFKEILLSYHRH 237
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
 36-203 6.19e-06

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: 48.53  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  36 NHIADWLQERRRVEEQYIQGLRKLANRHPPDESSDLGIFTTPWQKIVGATEAVAQSHEYLARKIEADVERPLRDY-SRGS 114
Cdd:cd07658    22 KELATVLQERAELELNYAKGLSKLSGKLSKASKSVSGTLSSAWTCVAEEMESEADIHRNLGSALTEEAIKPLRQVlDEQH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 115 REIQAMGN--------ISGNLAATAK---EIDTAQKKTAKLRD--------------KGAKAKASAVGDAVQE-----VE 164
Cdd:cd07658   102 KTRKPVENevdkaaklLTDWRSEQIKvkkKLHGLARENEKLQDqvednkqsctkqkmLNKLKKSAEVQDKEDEkleakRK 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2123155003 165 KAE---LSWDSSAPYVFEQLQAIDESRLNHLRDVLTQFQTHE 203
Cdd:cd07658   182 KGEesrLKAENEYYTCCVRLERLRLEWESALRKGLNQYESLE 223
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 42-199 1.28e-05

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: 47.63  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  42 LQERRRVEEQYIQGLRKLANRHPPDESSDLGI---FTTPWQKIVGATEAVAQSHEYLARKIEADVERPLRDY-------- 110
Cdd:cd07653    28 VKERAAIEQEYAKKLRKLVKKYLPKKKEEDEYsfsSVKAFRSILNEVNDIAGQHELIAENLNSNVCKELKTLiselrqer 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 111 ----SRGSREIQAMGNISGNLAATAKEIDTAQKKTAKLRDKGAKAKASAVgDAVQEVEKAELSWDSSA------------ 174
Cdd:cd07653   108 kkhlSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMN-LTKADVEKAKANANLKTqaaeeakneyaa 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2123155003 175 -----------------PYVFEQLQAIDESRLNHLRDVLTQF 199
Cdd:cd07653   187 qlqkfnkeqrqhystdlPQIFDKLQELDEKRINRTVELLLQA 228
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 23-205 1.37e-05

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: 47.63  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  23 VLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRhpPDESSDLGIFTTPWQKIVGATEAVAQSHEYLARKIEaD 102
Cdd:cd07674     9 VLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKM--ASNGSPLGTFAPMWEVFRVSSDKLALCHLELMRKLN-D 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003 103 VERPLRDYS-------RGSRE--------IQAMGNISGNLAATAKEIDTAQKKTAKLRDKGAKAKasavgdavqEVEKAE 167
Cdd:cd07674    86 LIKDINRYGdeqvkihKKTKEeaigtleaVQSLQVQSQHLQKSRENYHSKCVEQERLRREGVPQK---------ELEKAE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2123155003 168 LSWDSSAPYV-------------FEQ--------LQAIDESRLNHLRDVLTQFqTHEVD 205
Cdd:cd07674   157 LKTKKAAESLrgsvekynrargdFEQkmlesaqkFQDIEETHLRHMKLLIKGY-SHSVE 214
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 19-93 5.23e-05

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: 42.71  E-value: 5.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2123155003   19 QAVTVLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLANRHPP--DESSDLGIFTTPWQKIVGATEAVAQSHE 93
Cdd:smart00055   9 DGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAvrDTEPEYGSLSKAWEVLLSETDALAKQHL 85
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 19-116 1.82e-04

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: 43.83  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  19 QAVTVLNDRMNHVDRLNNHIADWLQERRRVEEQYIQGLRKLAnrhppdESSDLGIFTTP----WQKIVGATEAVAQSHEY 94
Cdd:cd07651     5 AGFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLS------RKSLGGSEEGGlknsLDTLRLETESMAKSHLK 78

                          90       100
                  ....*....|....*....|..
gi 2123155003  95 LARKIEADVERPLRDYSRGSRE 116
Cdd:cd07651    79 FAKQIRQDLEEKLAAFASSYTQ 100
PHA03247 PHA03247
large tegument protein UL36; Provisional
 304-573 2.88e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  304 STHPYGRASSPERKSSTNIGSAFGGFGKGKSKDRDAPGSSDRPISPLRSLP--ETPGSPEPPESS---NHSRLPSADIPN 378
Cdd:PHA03247  2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPpaASPAGPLPPPTSaqpTAPPPPPGPPPP 2848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  379 GTATEVSHETSAPIATNGTVHESIPELIEPLQPPQIEEPKPEPEKDAEGFSVPPSVIDAITEAEreagfSQSESSTTPQF 458
Cdd:PHA03247  2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ-----APPPPQPQPQP 2923

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  459 KLDIRNAPIQEEDGDADAAMAnmvntlrAQAAPPKRSSTLRGRRDVRNSIFVPNP-AAPELQSIGEAPPLPsAGSGSGST 537
Cdd:PHA03247  2924 PPPPQPQPPPPPPPRPQPPLA-------PTTDPAGAGEPSGAVPQPWLGALVPGRvAVPRFRVPQPAPSRE-APASSTPP 2995

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2123155003  538 STTFPTPALPAQPASPAF----KPPHRSLLTDDHAASDTQ 573
Cdd:PHA03247  2996 LTGHSLSRVSSWASSLALheetDPPPVSLKQTLWPPDDTE 3035
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 20-174 2.95e-04

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: 43.10  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  20 AVTVLNDRMNhvDRLNN--HIADWLQERRRVEEQYIQGLRKLAnRHPPD--ESSDL--GIFTTPWQKIVGATEAVAQSHe 93
Cdd:cd07652     6 GLSTLLDRLK--QSIASakEFATFLKKRAAIEEEHARGLKKLA-RTTLDtyKRPDHkqGSFSNAYHSSLEFHEKLADNG- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  94 ylarkieadverplrdySRGSREIQAMgniSGNLAATAKEIDTAqKKTAKlrdKGAKAKASAVGDAVQEVEKAELSWDSS 173
Cdd:cd07652    82 -----------------LRFAKALNEM---SDELSSLAKTVEKS-RKSIK---ETGKRAEKKVQDAEAAAEKAKARYDSL 137


                  .
gi 2123155003 174 A 174
Cdd:cd07652   138 A 138
PHA03247 PHA03247
large tegument protein UL36; Provisional
 253-558 3.33e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  253 GTPSRSLAPPQTTPTQGQSDDNRSQKSGSVKEKPSSNPlkrfgtvlGRRRQSTHPYGRASSPERKSSTNIGSAfggfGKG 332
Cdd:PHA03247  2610 GPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVP--------PPERPRDDPAPGRVSRPRRARRLGRAA----QAS 2677

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  333 KSKDRDAPGSSDRPISPLRSLPETPGSPEPPESSNHSRLPSADIPNGTATEVSHETSAPIA------TNGTVhesIPELI 406
Cdd:PHA03247  2678 SPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAApappavPAGPA---TPGGP 2754

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  407 EPLQPPQIEEPKPEPEKDAEGFSVPPSVIDAITEAEREAGFSQSESSTTPQFKLDIRNAPIQEEDGDADAAMANMVNTLR 486
Cdd:PHA03247  2755 ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSA 2834

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  487 AQAAPPKRSS----------------TLRGRRDVRNSIFVP-NPAAPELQSIGEAPPLPSAGSGSG--STSTTFPTPALP 547
Cdd:PHA03247  2835 QPTAPPPPPGppppslplggsvapggDVRRRPPSRSPAAKPaAPARPPVRRLARPAVSRSTESFALppDQPERPPQPQAP 2914

                          330
                   ....*....|.
gi 2123155003  548 AQPASPAFKPP 558
Cdd:PHA03247  2915 PPPQPQPQPPP 2925
PHA03247 PHA03247
large tegument protein UL36; Provisional
 345-554 1.33e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  345 RPISPLRSLPETPGSPEPPESSNHSRLPSADIPNGTATevsheTSAPIATNGTVHESIPELIEPLQPPQIEEPKPEPekd 424
Cdd:PHA03247  2560 PPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSAR-----PRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSP--- 2631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  425 aegfsvppsvidaiteaeREAGFSQSESSTTPqfkldirnAPIQEEDGDADA-AMANMVNTLRAQAAPPKRSSTLRG--R 501
Cdd:PHA03247  2632 ------------------SPAANEPDPHPPPT--------VPPPERPRDDPApGRVSRPRRARRLGRAAQASSPPQRprR 2685

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2123155003  502 RDVRNSIFV--------PNPAAPELQSIGEAPPLPSAGSGSGSTSTTFPTPALPAQPASPA 554
Cdd:PHA03247  2686 RAARPTVGSltsladppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPA 2746
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 307-561 4.90e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 4.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  307 PYGRASSPERKSSTNIGSAFGGFGKGKSKDRDAPGSSDRPISPLRSLPETPGSPEPPESSNHS---RLPSADIPNGTATE 383
Cdd:PHA03307    73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSemlRPVGSPGPPPAASP 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  384 VSHETSAPIATNGTVH--------ESIPELIEPLQPPQIEEPKPEPEKDAEGFSVPPSVIDAITEAE------REAGFSQ 449
Cdd:PHA03307   153 PAAGASPAAVASDAASsrqaalplSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSpapapgRSAADDA 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123155003  450 SESSTTPQFKLDIRNAPIQEEDGDADAAMANMVNTLRAQAAPPKRSSTLRGRRDVRNSIFVPNPAA-PELQSIGEAPPLP 528
Cdd:PHA03307   233 GASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPsPSSPGSGPAPSSP 312

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2123155003  529 SAGSGSGSTST-----TFPTPALPAQPASPAFKPPHRS 561
Cdd:PHA03307   313 RASSSSSSSREsssssTSSSSESSRGAAVSPGPSPSRS 350
 
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