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Conserved domains on  [gi|572880983|ref|NP_001275892|]
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cdc42-interacting protein 4 isoform 3 [Homo sapiens]

Protein Classification

F-BAR and HR1 domain-containing protein( domain architecture ID 10166554)

F-BAR (FES-CIP4 homology and Bin/Amphiphysin/Rvs) and HR1 (homology region 1) domain-containing protein, similar to human thyroid hormone receptor interactor 10

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 5-257 2.33e-127

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: 373.90  E-value: 2.33e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   5 TELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRpaKDDPESKFSQQQSFVQILQEVNDFA 84
Cdd:cd07653    1 TELWDQFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPKK--KEEDEYSFSSVKAFRSILNEVNDIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  85 GQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINA 164
Cdd:cd07653   79 GQHELIAENLNSNVCKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 165 TKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPI 244
Cdd:cd07653  159 TKADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDKLQELDEKRINRTVELLLQAAEIERKVIPI 238

                        250
                 ....*....|...
gi 572880983 245 IAKCLEGMKVAAN 257
Cdd:cd07653  239 IAKCLDGIKKAGD 251
HR1_CIP4_FNBP1L cd11628
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of vertebrate ...
 339-419 8.33e-34

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of vertebrate Cdc42-Interacting Protein 4 and FormiN Binding Protein 1-Like; CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. FNBP1L, also called Toca-1 (Transducer of Cdc42-dependent actin assembly 1), forms a complex with neural WASP; the 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. CIP4 may also play a role in phagocytosis. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. CIP4 and FNBP1L contain an N-terminal F-BAR domain, a central HR1 domain, and a C-terminal SH3 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; the HR1 domain of CIP4 binds Cdc42 and TC10. Translocation of CIP4 is facilitated by its binding to TC10 at the plasma membrane.


:

Pssm-ID: 212018  Cd Length: 81  Bit Score: 123.48  E-value: 8.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 339 PPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESR 418
Cdd:cd11628    1 PPEQRRKRLQQKIDELSRELQKEMDQSEALMKMKDVYEKNPQMGDPASLQPQIAETASNIDRLRGELHKYEAWLAEAEGR 80


                 .
gi 572880983 419 V 419
Cdd:cd11628   81 V 81
 
Name Accession Description Interval E-value
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 5-257 2.33e-127

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: 373.90  E-value: 2.33e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   5 TELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRpaKDDPESKFSQQQSFVQILQEVNDFA 84
Cdd:cd07653    1 TELWDQFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPKK--KEEDEYSFSSVKAFRSILNEVNDIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  85 GQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINA 164
Cdd:cd07653   79 GQHELIAENLNSNVCKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 165 TKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPI 244
Cdd:cd07653  159 TKADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDKLQELDEKRINRTVELLLQAAEIERKVIPI 238

                        250
                 ....*....|...
gi 572880983 245 IAKCLEGMKVAAN 257
Cdd:cd07653  239 IAKCLDGIKKAGD 251
HR1_CIP4_FNBP1L cd11628
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of vertebrate ...
 339-419 8.33e-34

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of vertebrate Cdc42-Interacting Protein 4 and FormiN Binding Protein 1-Like; CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. FNBP1L, also called Toca-1 (Transducer of Cdc42-dependent actin assembly 1), forms a complex with neural WASP; the 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. CIP4 may also play a role in phagocytosis. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. CIP4 and FNBP1L contain an N-terminal F-BAR domain, a central HR1 domain, and a C-terminal SH3 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; the HR1 domain of CIP4 binds Cdc42 and TC10. Translocation of CIP4 is facilitated by its binding to TC10 at the plasma membrane.


Pssm-ID: 212018  Cd Length: 81  Bit Score: 123.48  E-value: 8.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 339 PPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESR 418
Cdd:cd11628    1 PPEQRRKRLQQKIDELSRELQKEMDQSEALMKMKDVYEKNPQMGDPASLQPQIAETASNIDRLRGELHKYEAWLAEAEGR 80


                 .
gi 572880983 419 V 419
Cdd:cd11628   81 V 81
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 1-88 6.62e-17

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


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 75.84  E-value: 6.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983     1 MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKkylpKRPAKDDPESKF-SQQQSFVQILQE 79
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSK----KLRAVRDTEPEYgSLSKAWEVLLSE 76


                   ....*....
gi 572880983    80 VNDFAGQRE 88
Cdd:smart00055  77 TDALAKQHL 85
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 10-88 6.84e-16

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: 72.69  E-value: 6.84e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572880983   10 QFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSqqQSFVQILQEVNDFAGQRE 88
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDGGTLK--KAWDELLTETEQLAKQHL 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-202 7.32e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 7.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983    27 RYVKFVKERTEVE-QAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQ----EVNDFAGQRELVAENLSVRVcLE 101
Cdd:TIGR02168  214 RYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEELQKEL-YA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   102 LTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAhlrsH 181
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL----E 368

                          170       180
                   ....*....|....*....|.
gi 572880983   182 MAEESKNEYAAQLQRFNRDQA 202
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVA 389
 
Name Accession Description Interval E-value
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 5-257 2.33e-127

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: 373.90  E-value: 2.33e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   5 TELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRpaKDDPESKFSQQQSFVQILQEVNDFA 84
Cdd:cd07653    1 TELWDQFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVKKYLPKK--KEEDEYSFSSVKAFRSILNEVNDIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  85 GQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINA 164
Cdd:cd07653   79 GQHELIAENLNSNVCKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 165 TKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPI 244
Cdd:cd07653  159 TKADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDKLQELDEKRINRTVELLLQAAEIERKVIPI 238

                        250
                 ....*....|...
gi 572880983 245 IAKCLEGMKVAAN 257
Cdd:cd07653  239 IAKCLDGIKKAGD 251
F-BAR_FNBP1L cd07675
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; ...
 5-256 2.82e-121

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: 358.59  E-value: 2.82e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   5 TELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDpESKFSQQQSFVQILQEVNDFA 84
Cdd:cd07675    1 TELWDQFDNLDKHTQWGIDFLERYAKFVKERLEIEQNYAKQLRNLVKKYCPKRSSKDE-EPRFTSCLSFYNILNELNDYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  85 GQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINA 164
Cdd:cd07675   80 GQREVVAEEMGHRVYGELMRYSHDLKGERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 165 TKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPI 244
Cdd:cd07675  160 TKSDVEKAKQQLNLRTHMADESKNEYAAQLQNFNGEQHKHFYIVIPQIYKQLQEMDERRTVKLSECYRGFADSERKVIPI 239

                        250
                 ....*....|..
gi 572880983 245 IAKCLEGMKVAA 256
Cdd:cd07675  240 ISKCLEGMVLAA 251
F-BAR_FBP17 cd07676
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; ...
 5-256 5.76e-113

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: 337.40  E-value: 5.76e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   5 TELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEVNDFA 84
Cdd:cd07676    1 TELWDQFDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCRAFLMTLNEMNDYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  85 GQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINA 164
Cdd:cd07676   81 GQHEVISENLASQIIVELTRYVQELKQERKSHFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 165 TKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPI 244
Cdd:cd07676  161 TKADVEKARQQAQIRHQMAEDSKAEYSSYLQKFNKEQHEHYYTHIPNIFQKIQEMEERRIGRVGESMKTYAEVDRQVIPI 240

                        250
                 ....*....|..
gi 572880983 245 IAKCLEGMKVAA 256
Cdd:cd07676  241 IGKCLDGITKAA 252
HR1_CIP4_FNBP1L cd11628
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of vertebrate ...
 339-419 8.33e-34

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of vertebrate Cdc42-Interacting Protein 4 and FormiN Binding Protein 1-Like; CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. FNBP1L, also called Toca-1 (Transducer of Cdc42-dependent actin assembly 1), forms a complex with neural WASP; the 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. CIP4 may also play a role in phagocytosis. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. CIP4 and FNBP1L contain an N-terminal F-BAR domain, a central HR1 domain, and a C-terminal SH3 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; the HR1 domain of CIP4 binds Cdc42 and TC10. Translocation of CIP4 is facilitated by its binding to TC10 at the plasma membrane.


Pssm-ID: 212018  Cd Length: 81  Bit Score: 123.48  E-value: 8.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 339 PPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESR 418
Cdd:cd11628    1 PPEQRRKRLQQKIDELSRELQKEMDQSEALMKMKDVYEKNPQMGDPASLQPQIAETASNIDRLRGELHKYEAWLAEAEGR 80


                 .
gi 572880983 419 V 419
Cdd:cd11628   81 V 81
HR1_FBP17 cd11629
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Formin Binding ...
 340-416 6.04e-25

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of 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. It also binds to the Fas ligand and may be implicated in the inflammatory response. FBP17 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, central HR1 domain, and a C-terminal SH3 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; the HR1 domain of the related protein, CIP4, binds Cdc42 and TC10. Translocation of CIP4 is facilitated by its binding to TC10 at the plasma membrane.


Pssm-ID: 212019  Cd Length: 77  Bit Score: 98.50  E-value: 6.04e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572880983 340 PEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAE 416
Cdd:cd11629    1 PEQRRKKLQQKVDELNKDIQKEMDQRDALTKMKDVYIKNPQMGDPASVDHRLEEITQNIEKLRVEVQKFEGWLAEVE 77
HR1_CIP4-like cd11619
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of ...
 352-416 1.23e-22

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Cdc42-Interacting Protein 4 and similar proteins; 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. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. Members of this subfamily typically contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, central HR1 domain, and a C-terminal SH3 domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family; the HR1 domain of CIP4 binds Cdc42 and TC10. Translocation of CIP4 is facilitated by its binding to TC10 at the plasma membrane.


Pssm-ID: 212009  Cd Length: 77  Bit Score: 91.90  E-value: 1.23e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572880983 352 EERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAE 416
Cdd:cd11619   13 DELEKEIEKETKSRDGLMKMKGVYEQNPQLGDPASVEGQLAEYAKKLDKLREELQKYQGYLAEAE 77
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 1-88 6.62e-17

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


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 75.84  E-value: 6.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983     1 MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKkylpKRPAKDDPESKF-SQQQSFVQILQE 79
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSK----KLRAVRDTEPEYgSLSKAWEVLLSE 76


                   ....*....
gi 572880983    80 VNDFAGQRE 88
Cdd:smart00055  77 TDALAKQHL 85
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 10-88 6.84e-16

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: 72.69  E-value: 6.84e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572880983   10 QFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSqqQSFVQILQEVNDFAGQRE 88
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDGGTLK--KAWDELLTETEQLAKQHL 77
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 10-194 1.99e-15

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: 74.68  E-value: 1.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  10 QFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKrpakdDPESKFSQQQSFVQILQEVNDFAGQREL 89
Cdd:cd07610    1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKK-----PESGKTSLGTSWNSLREETESAATVHEE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  90 VAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREaEKAAQTAERLDQDINATKADv 169
Cdd:cd07610   76 LSEKLSQLIREPLEKVKEDKEQARKKELAEGEKLKKKLQELWAKLAKKADEEYREQVE-KLNPAQSEYEEEKLNKIQAE- 153

                        170       180
                 ....*....|....*....|....*.
gi 572880983 170 ekakQQAHL-RSHMAEESKNEYAAQL 194
Cdd:cd07610  154 ----QEREEeRLEILKDNLKNYINAI 175
HR1 cd00089
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
 352-412 6.60e-12

Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region.


Pssm-ID: 212008 [Multi-domain]  Cd Length: 68  Bit Score: 61.19  E-value: 6.60e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572880983 352 EERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWL 412
Cdd:cd00089    8 EELRRKLEKELKIREGAENLLKLYSNPKVKKDLAEVQLNLKESKEKIDLLKRQLERYNALV 68
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 21-223 2.03e-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: 64.64  E-value: 2.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  21 GLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKrpAKDDPESKfSQQQSFVQILQEVNDFAgqrELvaeNLSVRVCL 100
Cdd:cd07655   17 GHKLCDDLMKMVQERAEIEKAYAKKLKEWAKKWRDL--IEKGPEYG-TLETAWKGLLSEAERLS---EL---HLSIRDKL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 101 eLTKYSQEMKQERK--------MHFQEGR-------RAQQQLENGFKQLENSKRKFERDCReAEKAAQTAER-------- 157
Cdd:cd07655   88 -LNDVVEEVKTWQKenyhksmmGGFKETKeaedgfaKAQKPWAKLLKKVEKAKKAYHAACK-AEKSAQKQENnaksdtsl 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572880983 158 LDQDINATKADVEKAKQQAHlrshmaeESKNEYAAQLQRFNRDQAHfYFSQMPQIFDKLQDMDERR 223
Cdd:cd07655  166 SPDQVKKLQDKVEKCKQEVS-------KTKDKYEKALEDLNKYNPR-YMEDMEQVFDKCQEFEEKR 223
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 11-190 8.78e-10

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: 59.41  E-value: 8.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  11 FEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKrpakddpESKFSQQQSFVQILQEVNDFAGqrelV 90
Cdd:cd07647    7 FDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPG-------DEIGTLKSSWDSLRKETENVAN----A 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  91 AENLSVRVCLELTKYSQ---EMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLdqDINATKA 167
Cdd:cd07647   76 HIQLAQSLREEAEKLEEfreKQKEERKKTEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKAEQAYEKS--SSGAQPK 153

                        170       180
                 ....*....|....*....|...
gi 572880983 168 DVEKAKQQAHLRSHMAEESKNEY 190
Cdd:cd07647  154 EAEKLKKKAAQCKTSAEEADSAY 176
F-BAR_FCHSD1 cd07678
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ...
 9-256 2.07e-09

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 (FCHSD1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 1 (FCHSD1) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153362 [Multi-domain]  Cd Length: 263  Bit Score: 58.48  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   9 DQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPK-----RPAKDDPESKFSQQQSFVqilqEVNDF 83
Cdd:cd07678    5 EQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALQRLASQFLKRdwhrgGNETEMDRSVRTVWGAWR----EGTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  84 AGQRELVAENLSVRVCLELTKYSQEMKQER-KMHFQEGRRAQQQLENGFKQLENSKRKF---ERDCREA-EKAAQTAERL 158
Cdd:cd07678   81 TGQGRVTRLEAYRRLRDEAGKTGRSAKEQVlKKSTEQLQKAQAELLETVKELSKSKKLYgqlERVSEVAkEKAADVEARL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 159 ---DQDINATKADVEKAkqQAHLRSHMAEESK------NEYAAQLQRFNRDQAHFYFSQMPQIfdkLQDMDERRATRLGA 229
Cdd:cd07678  161 nksDHGIFHSKASLQKL--SAKFSAQSAEYSQqlqaarNEYLLNLVAANAHLDHYYQEELPAI---MKALDGDLYERLRD 235

                        250       260
                 ....*....|....*....|....*..
gi 572880983 230 GYGLLSEAELEVVPIIAKCLEGMKVAA 256
Cdd:cd07678  236 PLTSLSHTELEACEVTQEHFHRIEQAT 262
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 32-223 2.48e-07

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: 52.36  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  32 VKERTEVEQAYAKQLRSLVKKYlpKRPAKDDPESKfSQQQSFVQILQEVNDFAGQRELVAENLsVRVCLELTKYSQEMKQ 111
Cdd:cd07680   28 VQERAKIEKAYGQQLTDWAKRW--RQLIEKGPQYG-SLERAWGAIMTEADKVSELHQEVKNNL-LNEDLEKVKNWQKDAY 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 112 ERKMH--FQEG-------RRAQQQLENGFKQLENSKRKFERDCREaEKAAQTAE---RLDQDINATKA-----DVEKAKQ 174
Cdd:cd07680  104 HKQIMggFKETkeaedgfRKAQKPWAKKMKELEAAKKAYHLACKE-EKLAMTREansKAEQSVTPEQQkklqdKVDKCKQ 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 572880983 175 QahlrshmAEESKNEYAAQLQRFNRDQAHfYFSQMPQIFDKLQDMDERR 223
Cdd:cd07680  183 D-------VQKTQEKYEKVLDDVGKTTPQ-YMENMEQVFEQCQQFEEKR 223
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 31-223 6.31e-07

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: 50.76  E-value: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  31 FVKERTEVEQAYAKQLRSLVKKYLpkrpakDDPESKfSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMK 110
Cdd:cd07651   27 FYKERASIEEEYAKRLEKLSRKSL------GGSEEG-GLKNSLDTLRLETESMAKSHLKFAKQIRQDLEEKLAAFASSYT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 111 QERKM---HFQEGRRAQQQLengFKQLENSKRKFERDC---------------REAEKAAQTAERLDQDINATKADVEKA 172
Cdd:cd07651  100 QKRKKiqsHMEKLLKKKQDQ---EKYLEKAREKYEADCskinsytlqsqltwgKELEKNNAKLNKAQSSINSSRRDYQNA 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 572880983 173 kqqahlrshmaeesKNEYAAQLQRFNRDQAHFyfsqmpqiFDKLQDMDERR 223
Cdd:cd07651  177 --------------VKALRELNEIWNREWKAA--------LDDFQDLEEER 205
F-BAR_Fer cd07686
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fer (Fes related) tyrosine ...
 5-221 9.38e-07

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fer (Fes related) tyrosine kinase; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Fer (Fes related) is a cytoplasmic (or nonreceptor) tyrosine kinase expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells. It contains an N-terminal F-BAR domain, an SH2 domain, and a C-terminal catalytic kinase domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153370 [Multi-domain]  Cd Length: 234  Bit Score: 50.44  E-value: 9.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   5 TELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQqqSFVQILQEVNDFA 84
Cdd:cd07686    1 SDLRNSHEALLKLQDWELRLLETVKKFMALRVKSDKEYASTLQNLCNQVDKESTSQLDYVSNVSK--SWLHMVQQTEQLS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  85 GQRELVAENLSVRVCLELTKYSQEMKQERKMHfqegRRAQQQLENGFKQLENSK-RKFERDCREAEKAAQTAERLDQDIN 163
Cdd:cd07686   79 KIMKTHAEELNSGPLHRLTMMIKDKQQVKKSY----IGVHQQIEAEMYKVTKTElEKLKCSYRQLTKEVNSAKEKYKDAV 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572880983 164 ATKADVEKAKQ---QAHLRSHMAEeskNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDE 221
Cdd:cd07686  155 AKGKETEKARErydKATMKLHMLH---NQYVLAVKGAQLHQHQYYDFTLPLLLDSLQKMQE 212
F-BAR_FCHSD cd07654
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains ...
 9-247 1.27e-06

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains proteins (FCHSD); 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 FCH and double SH3 domain (FCHSD) proteins, so named as they contain an N-terminal F-BAR domain and two SH3 domains at the C-terminus. Vertebrates harbor two subfamily members, FCHSD1 and FCHSD2, which have been characterized only in silico. Their biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153338 [Multi-domain]  Cd Length: 264  Bit Score: 50.27  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   9 DQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPK---RPAKDDPESKFSQQQSFVQILQEVNDFAG 85
Cdd:cd07654    5 EQLSKLQAKHQTECDLLEDIRTYSQKKAAIEREYGQALQKLASQFLKRewpGSGELKPEDDRSGYTVWGAWLEGLDAVAQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  86 QRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRK-FER-----DCREAEKAAQTAE-RL 158
Cdd:cd07654   85 SRQNRCEAYRRYISEPAKTGRSAKEQQLKKCTEQLQRAQAEVQQTVRELSKSRKTyFEReqvahLAREKAADVQAREaRS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 159 DQDINATKADVEKA----KQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIfdkLQDMDERRATRLGAGYGLL 234
Cdd:cd07654  165 DLSIFQSRTSLQKAsvklSARKAECSSKATAARNDYLLNLAATNAHQDRYYQTDLPAI---IKALDGELYDHLKDFLISL 241

                        250
                 ....*....|...
gi 572880983 235 SEAELEVVPIIAK 247
Cdd:cd07654  242 SHTELETAQVIQE 254
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 3-286 6.90e-06

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: 48.13  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   3 WGtELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKylpkrpakddpESKFSQQQSFVQIL----Q 78
Cdd:cd07673    7 WG-EKNSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAKS-----------ASNYSQLGTFAPVWdvfkT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  79 EVNDFAGQRELVAENLSvRVCLELTKYSQEMKQERKMHFQE---GRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTA 155
Cdd:cd07673   75 STEKLANCHLELVRKLQ-ELIKEVQKYGEEQVKSHKKTKEEvagTLEAVQNIQSITQALQKSKENYNAKCLEQERLKKEG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 156 erldqdinATKADVEKAKqqahLRSHMAEESkneYAAQLQRFNRDQAHFYfSQMPQIFDKLQDMDERRATRLGAGYGLLS 235
Cdd:cd07673  154 --------ATQREIEKAA----VKSKKATES---YKLYVEKYALAKADFE-QKMTETAQKFQDIEETHLIRIKEIIGSYS 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 572880983 236 EAELEVVPIIAKCLEgmKVAANAVDPKNDSHV--LIELHKSGFARPGDVEFED 286
Cdd:cd07673  218 NSVKEIHIQIGQVHE--EFINNMANTTVESLIqkFAESKGTGKERPGPIEFEE 268
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 32-199 1.03e-04

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: 44.18  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  32 VKERTEVEQAYAKQLRSLVKKylpkrpAKDDPESKfSQQQSFVQILQEVNDFAGQRELVAENLSVRVcLELTKYSQEMKQ 111
Cdd:cd07671   28 LKQRAQAEERYGKELVQIARK------AGGQTEIN-TLKASFDQLKQQIENIGNSHIQLAGMLREEL-KSLEEFRERQKE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 112 ERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQdiNATKADVEKAKQQAHLRSHMAEESKNEYA 191
Cdd:cd07671  100 QRKKYEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAEQTFERSSS--TGNPKQSEKSQNKAKQCRDAATEAERVYK 177


                 ....*...
gi 572880983 192 AQLQRFNR 199
Cdd:cd07671  178 QNIEQLDK 185
F-BAR_Fes_Fer cd07657
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer ...
 12-227 1.16e-04

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


Pssm-ID: 153341 [Multi-domain]  Cd Length: 237  Bit Score: 43.91  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  12 EVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQqqSFVQILQEVNDFAGQRELVA 91
Cdd:cd07657    8 EALLKRQDAELRLLETMKKYMAKRAKSDREYASTLGSLANQGLKIEAGDDLQGSPISK--SWKEIMDSTDQLSKLIKQHA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  92 ENLSVRVCLELTKYSQEMKQERKMhFQEGRraqQQLENGFKQLENSKRKFERDCREAEKA-AQTAERLDQDINATK---A 167
Cdd:cd07657   86 EALESGTLDKLTLLIKDKRKAKKA-YQEER---QQIDEQYKKLTDEVEKLKSEYQKLLEDyKAAKSKFEEAVVKGGrggR 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572880983 168 DVEKAK---QQAHLRSHMAEeskNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRL 227
Cdd:cd07657  162 KLDKARdkyQKACRKLHLCH---NDYVLALLEAQEHEEDYRTLLLPGLLNSLQSLQEEFITQW 221
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 30-150 1.68e-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: 43.49  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  30 KFVKERTEVEQAYAKQLRSLVKKYLpkrpakDDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCL---ELTKYS 106
Cdd:cd07652   26 TFLKKRAAIEEEHARGLKKLARTTL------DTYKRPDHKQGSFSNAYHSSLEFHEKLADNGLRFAKALNEmsdELSSLA 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 572880983 107 QEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEK 150
Cdd:cd07652  100 KTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLER 143
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 11-188 2.33e-04

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: 43.01  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  11 FEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESK---FSQQ-----QSFVQILQEVND 82
Cdd:cd07672    7 YDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSldvFKQQidnvgQSHIQLAQTLRD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  83 FAGQRElvaenlsvrvcleltKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERldqdi 162
Cdd:cd07672   87 EAKKME---------------DFRERQKLARKKIELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEAEQAVNR----- 146

                        170       180
                 ....*....|....*....|....*.
gi 572880983 163 natKADVEKAKQQAHLRSHMAEESKN 188
Cdd:cd07672  147 ---NANLVNVKQQEKLFAKLAQSKQN 169
F-BAR_FCHSD2 cd07677
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 2 ...
 9-216 2.52e-04

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


Pssm-ID: 153361 [Multi-domain]  Cd Length: 260  Bit Score: 43.19  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   9 DQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYL------PKRPAKDDPESKFSQQQSFV----QILQ 78
Cdd:cd07677    5 EQMTKLQAKHQAECKLLEDEREFSQKIAAIESEYAQKEQKLASQYLksdwrgMKADERADYRSMYTVWKSFLegtmQVAQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  79 -EVNDFAGQRELVAENLSVRVCLEltkysqemKQERKMHFQEGRRAQQQLENGFKQLENSKRKFerdcREAEKAAQtAER 157
Cdd:cd07677   85 sRINICENYKNLISEPARTVRLYK--------EQQLKRCVDQLTKIQAELQETVKDLAKGKKKY----FETEQMAH-AVR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572880983 158 LDQDINA--------TKADVEKAKQQAHLR----SHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKL 216
Cdd:cd07677  152 EKADIEAksklslfqSRISLQKASVKLKARrsecNSKATHARNDYLLTLAAANAHQDRYYQTDLVNIMKAL 222
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 32-223 5.80e-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: 41.97  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  32 VKERTEVEQAYAKQLRSLVKKY---LPKRPAKDDPESKFSQQQSFVQILQEVNdFAGQRELVAENLSVRVCLELTKYSQE 108
Cdd:cd07679   28 LHERARIEKVYAQQLTEWAKRWrqlVEKGPQYGTVEKAWCALMSEAEKVSELH-LEVKASLMNEDFEKIKNWQKEAFHKQ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 109 MK---QERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAEE 185
Cdd:cd07679  107 MMggfKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHTACKEEKLATSREANSKADPALNPEQLKKLQDKVEKCKQDVLK 186

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 572880983 186 SKNEYAAQLQRFNRDQAHfYFSQMPQIFDKLQDMDERR 223
Cdd:cd07679  187 TKEKYEKSLKELDQTTPQ-YMENMEQVFEQCQQFEEKR 223
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-202 7.32e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 7.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983    27 RYVKFVKERTEVE-QAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQ----EVNDFAGQRELVAENLSVRVcLE 101
Cdd:TIGR02168  214 RYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEELQKEL-YA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   102 LTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAhlrsH 181
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL----E 368

                          170       180
                   ....*....|....*....|.
gi 572880983   182 MAEESKNEYAAQLQRFNRDQA 202
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVA 389
F-BAR_srGAP3 cd07684
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 5-214 1.55e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Protein 3; 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. srGAP3, also called MEGAP (MEntal disorder associated GTPase-Activating Protein), is a Rho GAP with activity towards Rac1 and Cdc42. It impacts cell migration by regulating actin and microtubule cytoskeletal dynamics. The association between srGAP3 haploinsufficiency and mental retardation is under debate. srGAP3 contains an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153368 [Multi-domain]  Cd Length: 253  Bit Score: 40.46  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   5 TELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPK-RPAKDDPESKFSQQQSFV--------Q 75
Cdd:cd07684    1 TQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKiRTSREHQFKKDQQLLSPVncwylvleQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  76 ILQEVNDFAGQRELVAENLSVRVCL---------------------ELTKYSQEMKQERK---MHFQEGRRAQQQLENGF 131
Cdd:cd07684   81 TRRESRDHATLNDIFNNNVIVRLSQisedvirlfkkskeiglqmheELLKVTNELYTVMKtyhMYHAESISAESKLKEAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 132 KQLEnskRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAE--ESKNEYAAQLQRFNRDQAHFYFSQM 209
Cdd:cd07684  161 KQEE---KQFNKSGDISSNLLRHEERPQRRSSVKKIEKMKEKRQAKYSENKLKctKARNDYLLNLAATNAAVSKYYIHDV 237


                 ....*
gi 572880983 210 PQIFD 214
Cdd:cd07684  238 SDLID 242
F-BAR_srGAP1 cd07683
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 5-214 1.78e-03

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


Pssm-ID: 153367 [Multi-domain]  Cd Length: 253  Bit Score: 40.44  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983   5 TELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPK-RPAKDdpESKFSQQQSFV--------- 74
Cdd:cd07683    1 AQLVEQQKCLEQQTEMRVQLLQDLQDFFRKKAEIESEYSRNLEKLAERFMAKtRSTKD--HQQYKKDQNLLspvncwyll 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  75 --QILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQL--------------------ENGFK 132
Cdd:cd07683   79 lnQVRRESKDHATLSDIYLNNVIMRFMQISEDSTRMFKKSKEIAFQLHEDLMKVLnelytvmktyhmyhtesisaESKLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 133 QLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAE--ESKNEYAAQLQRFNRDQAHFYFSQMP 210
Cdd:cd07683  159 EAEKQEEKQIGRSGDPVFHIRLEDRHQRRSSVKKIEKMKEKRQAKYSENKLKsiKARNEYLLTLEATNASVFKYYIHDLS 238


                 ....
gi 572880983 211 QIFD 214
Cdd:cd07683  239 DLID 242
mS26_Tt cd23695
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ...
 101-222 4.79e-03

Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.


Pssm-ID: 467909 [Multi-domain]  Cd Length: 496  Bit Score: 39.81  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983 101 ELTKYSQEMKQERKMHFQEGRRAQQQLENGF-----KQLENSKRKfeRDCREAEKAAQTAERLDQDINATKadVEKAKQQ 175
Cdd:cd23695    6 ERRAYKQLFKEYRKKHKKDYWESQTIVENEFidkynKEELKKQRK--DLDKWRTSIITISKATQNHIKLLE--KKSVKKE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 572880983 176 AHLRSHMAEESKNEYAAQ--LQRFNRDQAHFYfsqmpqifdKLQDMDER 222
Cdd:cd23695   82 ENERKYLLEQDVKAMNKKiiLDVMNEESKNWI---------NLQNMNEK 121
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 101-201 9.38e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 38.83  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572880983  101 ELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREA----EKAAQTAERLDQDI-NATKADVEKAKQQ 175
Cdd:pfam05262 210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAknlpKPADTSSPKEDKQVaENQKREIEKAQIE 289

                          90       100
                  ....*....|....*....|....*.
gi 572880983  176 AHLRSHMAEESKNEYAAQLQRFNRDQ 201
Cdd:pfam05262 290 IKKNDEEALKAKDHKAFDLKQESKAS 315
 
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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