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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193     8 CFWDPNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARA 87
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEPEYGSLSKAWEVLLSETDALA 81

                   ....*
gi 392297193    88 QSHSK 92
Cdd:smart00055  82 KQHLE 86

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193   110 ANLQARYTTLSGKIERLRMDKFNKKKGCEVLQKKLQDAQIRFRDlqLNENNMIGAKRVEHNKRELLKWESNSQEYKVQLD 189
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR--LEQQKQILRERLANLERQLEELEAQLEELESKLD 333

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 392297193   190 VLKQEYKASQKfwihEWAQLSCELQEMEnARISFLQSKLQQFAT 233
Cdd:TIGR02168  334 ELAEELAELEE----KLEELKEELESLE-AELEELEAELEELES 372

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193     8 CFWDPNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARA 87
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEPEYGSLSKAWEVLLSETDALA 81

                   ....*
gi 392297193    88 QSHSK 92
Cdd:smart00055  82 KQHLE 86

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193  12 PNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLgaitGKLDKDIGTNMDYGKLNETFNVVLSVEKARAQSHS 91
Cdd:cd07651    2 KNDAGFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRL----EKLSRKSLGGSEEGGLKNSLDTLRLETESMAKSHL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193  92 KqseiLFRQIYTDTKAFAANLQARYTTLSGKIErLRMDKFNKKKGceVLQKKLQDAQIRFRD--LQLN----ENNMIGAK 165
Cdd:cd07651   78 K----FAKQIRQDLEEKLAAFASSYTQKRKKIQ-SHMEKLLKKKQ--DQEKYLEKAREKYEAdcSKINsytlQSQLTWGK 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392297193 166 RVEHNKRELLKWESNSQEYKVQLDVLKQEYKASQKFWIHEWAQLSCELQEMENARISFLQSKLQQFA 232
Cdd:cd07651  151 ELEKNNAKLNKAQSSINSSRRDYQNAVKALRELNEIWNREWKAALDDFQDLEEERIQFLKSNCWTFA 217

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392297193 603 YAKAMYPLIGNEAPGLaNFHKGDYLLITEIVNKDWYKGEVydndridRNHRIGLIPYNF 661
Cdd:cd00174    1 YARALYDYEAQDDDEL-SFKKGDIITVLEKDDDGWWEGEL-------NGGREGLFPANY 51

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193   110 ANLQARYTTLSGKIERLRMDKFNKKKGCEVLQKKLQDAQIRFRDlqLNENNMIGAKRVEHNKRELLKWESNSQEYKVQLD 189
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR--LEQQKQILRERLANLERQLEELEAQLEELESKLD 333

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 392297193   190 VLKQEYKASQKfwihEWAQLSCELQEMEnARISFLQSKLQQFAT 233
Cdd:TIGR02168  334 ELAEELAELEE----KLEELKEELESLE-AELEELEAELEELES 372

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193     8 CFWDPNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARA 87
Cdd:smart00055   2 GFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEPEYGSLSKAWEVLLSETDALA 81

                   ....*
gi 392297193    88 QSHSK 92
Cdd:smart00055  82 KQHLE 86

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193  12 PNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLgaitGKLDKDIGTNMDYGKLNETFNVVLSVEKARAQSHS 91
Cdd:cd07651    2 KNDAGFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRL----EKLSRKSLGGSEEGGLKNSLDTLRLETESMAKSHL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193  92 KqseiLFRQIYTDTKAFAANLQARYTTLSGKIErLRMDKFNKKKGceVLQKKLQDAQIRFRD--LQLN----ENNMIGAK 165
Cdd:cd07651   78 K----FAKQIRQDLEEKLAAFASSYTQKRKKIQ-SHMEKLLKKKQ--DQEKYLEKAREKYEAdcSKINsytlQSQLTWGK 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392297193 166 RVEHNKRELLKWESNSQEYKVQLDVLKQEYKASQKFWIHEWAQLSCELQEMENARISFLQSKLQQFA 232
Cdd:cd07651  151 ELEKNNAKLNKAQSSINSSRRDYQNAVKALRELNEIWNREWKAALDDFQDLEEERIQFLKSNCWTFA 217

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392297193 603 YAKAMYPLIGNEAPGLaNFHKGDYLLITEIVNKDWYKGEVydndridRNHRIGLIPYNF 661
Cdd:cd00174    1 YARALYDYEAQDDDEL-SFKKGDIITVLEKDDDGWWEGEL-------NGGREGLFPANY 51

First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model represents the first SH3 domain of SH3RF1 (or POSH), SH3RF2 (or POSHER), SH3RF3 (POSH2), and similar domains. Members of this family are scaffold proteins that function as E3 ubiquitin-protein ligases. They all contain an N-terminal RING finger domain and multiple SH3 domains; SH3RF1 and SH3RF3 have four SH3 domains while SH3RF2 has three. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3RF2 acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392297193 603 YAKAMYPLIGNEaPGLANFHKGDYLLITEIVNKDWYKGEVydndridrNHRIGLIPYNFIQ 663
Cdd:cd11786    1 CAKALYNYEGKE-PGDLSFKKGDIILLRKRIDENWYHGEC--------NGKQGFFPASYVQ 52

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193   9 FWDPNDNGVNIllGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARAQ 88
Cdd:cd07655    1 FWEVGNYKRTV--KRIEDGHKLCDDLMKMVQERAEIEKAYAKKLKEWAKKWRDLIEKGPEYGTLETAWKGLLSEAERLSE 78

                         90
                 ....*....|....*....
gi 392297193  89 SHSKQSEILFRQIYTDTKA 107
Cdd:cd07655   79 LHLSIRDKLLNDVVEEVKT 97

First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ligase; SH3RF3 is also called POSH2 (Plenty of SH3s 2) or SH3MD4 (SH3 multiple domains protein 4). It is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating JNK mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1; it also contains an N-terminal RING finger domain and four SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392297193 603 YAKAMYPLIGNEaPGLANFHKGDYLLITEIVNKDWYKGEVYDNDridrnhriGLIPYNFIQL 664
Cdd:cd11928    2 CGKALYSYEGKE-PGDLKFNKGDIIILRRKVDENWYHGELNGCH--------GFLPASYIQC 54

First Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the first SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392297193 604 AKAMYPLIGNEAPGLAnFHKGDYLLITEIVNKDWYKGEvydndridRNHRIGLIPYNFIQL 664
Cdd:cd11781    2 ARALYPFKAQSAKELS-LKKGDIIYIRRQIDKNWYEGE--------HNGRVGIFPASYVEI 53

C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 2 (Stac2); Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac2 contains a single SH3 domain at the C-terminus unlike Stac1 and Stac3, which contain two C-terminal SH3 domains. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392297193 606 AMYPLIGNEAPGLAnFHKGDYLLITEIVNKDWYKGEVYDndridrnhRIGLIPYNFIQ 663
Cdd:cd11985    4 ALYKFLPQENNDLP-LQPGDRVMVVDDSNEDWWKGKSGD--------RVGFFPANFVQ 52

First Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392297193 604 AKAMYPLIGNEaPGLANFHKGDYLLITEIVNKDWYKGEVydndridrNHRIGLIPYNFIQL 664
Cdd:cd11929    3 AKALCNYRGHN-PGDLKFNKGDVILLRRQLDENWYLGEI--------NGVSGIFPASSVEV 54

Src homology 3 domain of Slit-Robo GTPase Activating Proteins; 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 (srGAP1-3), all of which are expressed during embryonic and early development in the nervous system but with different localization and timing. A fourth member has also been reported (srGAP4, also called ARHGAP4). srGAPs contain an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392297193 604 AKAMYPLIGNEAPGLAnFHKGDYLLITEIVNKDWYKGEVYDNDridrnhriGLIPYNFIQL 664
Cdd:cd11809    2 ATAQFDYTGRSERELS-FKKGDSLTLYRQVSDDWWRGQLNGQD--------GLVPHKYITL 53

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392297193  605 KAMYPLIGNEAPGLAnFHKGDYLLITEIVNKDWYKGEvydndriDRNHRIGLIP 658
Cdd:pfam00018   1 VALYDYTAQEPDELS-FKKGDIIIVLEKSEDGWWKGR-------NKGGKEGLIP 46

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193  10 WDPNDNgvniLLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAIT----GKLDKDIGTNMDYGKlneTFNVVLSVEKA 85
Cdd:cd07653    4 WDQFDN----LEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVkkylPKKKEEDEYSFSSVK---AFRSILNEVND 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193  86 RAQSHSKQSEILFRQIYTDTKAFAANL-QARYT------TLSGKIERLR--MDKFNKK-----KGCEVLQKKLQDAQirf 151
Cdd:cd07653   77 IAGQHELIAENLNSNVCKELKTLISELrQERKKhlsegsKLQQKLESSIkqLEKSKKAyekafKEAEKAKQKYEKAD--- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193 152 rdlqlNENNMIGAK----RVEHNKRELLKwESNSQEYKVQLdvlkQEY-KASQKFWIHEWAQLSCELQEMENARISFLQS 226
Cdd:cd07653  154 -----ADMNLTKADvekaKANANLKTQAA-EEAKNEYAAQL----QKFnKEQRQHYSTDLPQIFDKLQELDEKRINRTVE 223

                        250
                 ....*....|..
gi 392297193 227 KLQQFATSSMET 238
Cdd:cd07653  224 LLLQAAEIERKV 235

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193  23 HISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKdiGTNMDYGKLNETFNVVLSVEKARAQSHSKQSEILFRQIY 102
Cdd:cd07658   13 YVKQGGDFCKELATVLQERAELELNYAKGLSKLSGKLSK--ASKSVSGTLSSAWTCVAEEMESEADIHRNLGSALTEEAI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392297193 103 TDTKAFAANLQARYTTLSGKIER-------LRMDKFNKKKGCEVLQKKLQDAQIRFRDLQLNENNMIGAKRVEHNKrell 175
Cdd:cd07658   91 KPLRQVLDEQHKTRKPVENEVDKaaklltdWRSEQIKVKKKLHGLARENEKLQDQVEDNKQSCTKQKMLNKLKKSA---- 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392297193 176 kweSNSQEYKVQLDVLKQEYKASQKFWIHEWAQLSCELQEMENARISFLQSKLQQFatSSMET 238
Cdd:cd07658  167 ---EVQDKEDEKLEAKRKKGEESRLKAENEYYTCCVRLERLRLEWESALRKGLNQY--ESLEE 224