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Conserved domains on  [gi|568998469|ref|XP_006523463|]
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cdc42-interacting protein 4 isoform X1 [Mus musculus]

Protein Classification

cdc42-interacting protein 4( domain architecture ID 10166556)

cdc42-interacting protein 4 (CIP4) participates in insulin responsive facilitative sugar transporter mediated glucose transport pathway and thought to be involved in actin cytoskeleton organization, endocytosis, and signal transduction and is a biomarker of Huntington's disease

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 ...
 5-238 8.27e-111

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: 331.53  E-value: 8.27e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469   5 TELWDQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR-----------------FSQQQSFVQLLQEVNDFAGQ 67
Cdd:cd07653    1 TELWDQFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRklvkkylpkkkeedeysFSSVKAFRSILNEVNDIAGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  68 RELVAESLGIRVCLELAKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQDINATK 147
Cdd:cd07653   81 HELIAENLNSNVCKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNLTK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 148 ADVEKAKQQAHLRNHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELQVVPIIG 227
Cdd:cd07653  161 ADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDKLQELDEKRINRTVELLLQAAEIERKVIPIIA 240

                        250
                 ....*....|.
gi 568998469 228 KCLEGMKVAAE 238
Cdd:cd07653  241 KCLDGIKKAGD 251
HR1_CIP4_FNBP1L cd11628
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of vertebrate ...
 376-456 7.93e-32

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: 117.70  E-value: 7.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 376 PPEQQRKRLQQQLEERNRELQKEEDQREALKKMKDVYEKTPQMGDPASLEPRIAETLGNIERLKLEVQKYEAWLAEAESR 455
Cdd:cd11628    1 PPEQRRKRLQQKIDELSRELQKEMDQSEALMKMKDVYEKNPQMGDPASLQPQIAETASNIDRLRGELHKYEAWLAEAEGR 80


                 .
gi 568998469 456 V 456
Cdd:cd11628   81 V 81
SH3_CIP4-like cd11911
Src Homology 3 domain of Cdc42-Interacting Protein 4; This subfamily is composed of ...
 527-581 1.63e-28

Src Homology 3 domain of Cdc42-Interacting Protein 4; 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, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of CIP4 associates with Gapex-5, a Rab31 GEF. 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.


:

Pssm-ID: 212844 [Multi-domain]  Cd Length: 55  Bit Score: 107.73  E-value: 1.63e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568998469 527 QCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11911    1 TCTALYDFDGTSEGTLSMEEGEILLVLEEDGGDGWTRVRKNNGDEGYVPTSYIEV 55
 
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 ...
 5-238 8.27e-111

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: 331.53  E-value: 8.27e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469   5 TELWDQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR-----------------FSQQQSFVQLLQEVNDFAGQ 67
Cdd:cd07653    1 TELWDQFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRklvkkylpkkkeedeysFSSVKAFRSILNEVNDIAGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  68 RELVAESLGIRVCLELAKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQDINATK 147
Cdd:cd07653   81 HELIAENLNSNVCKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNLTK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 148 ADVEKAKQQAHLRNHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELQVVPIIG 227
Cdd:cd07653  161 ADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDKLQELDEKRINRTVELLLQAAEIERKVIPIIA 240

                        250
                 ....*....|.
gi 568998469 228 KCLEGMKVAAE 238
Cdd:cd07653  241 KCLDGIKKAGD 251
HR1_CIP4_FNBP1L cd11628
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of vertebrate ...
 376-456 7.93e-32

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: 117.70  E-value: 7.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 376 PPEQQRKRLQQQLEERNRELQKEEDQREALKKMKDVYEKTPQMGDPASLEPRIAETLGNIERLKLEVQKYEAWLAEAESR 455
Cdd:cd11628    1 PPEQRRKRLQQKIDELSRELQKEMDQSEALMKMKDVYEKNPQMGDPASLQPQIAETASNIDRLRGELHKYEAWLAEAEGR 80


                 .
gi 568998469 456 V 456
Cdd:cd11628   81 V 81
SH3_CIP4-like cd11911
Src Homology 3 domain of Cdc42-Interacting Protein 4; This subfamily is composed of ...
 527-581 1.63e-28

Src Homology 3 domain of Cdc42-Interacting Protein 4; 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, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of CIP4 associates with Gapex-5, a Rab31 GEF. 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.


Pssm-ID: 212844 [Multi-domain]  Cd Length: 55  Bit Score: 107.73  E-value: 1.63e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568998469 527 QCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11911    1 TCTALYDFDGTSEGTLSMEEGEILLVLEEDGGDGWTRVRKNNGDEGYVPTSYIEV 55
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 1-69 8.29e-13

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: 64.28  E-value: 8.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469     1 MDWGTELWDQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR----------------FSQQQSFVQLLQEVNDF 64
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQklskklravrdtepeyGSLSKAWEVLLSETDAL 80


                   ....*
gi 568998469    65 AGQRE 69
Cdd:smart00055  81 AKQHL 85
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 524-580 5.67e-11

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 57.93  E-value: 5.67e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568998469   524 PIGQCVAIYHFEGSSEGTVSMSEGEDLSLMEEDkGDGWTRVRRKQGAEGYVPTSYLR 580
Cdd:smart00326   1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKS-DDGWWKGRLGRGKEGLFPSNYVE 56
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 10-69 8.69e-10

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: 55.35  E-value: 8.69e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568998469   10 QFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR-----------------FSQQQSFVQLLQEVNDFAGQRE 69
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQklakkflkkkkkpeddgGTLKKAWDELLTETEQLAKQHL 77
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 529-576 2.18e-06

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.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 44.50  E-value: 2.18e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568998469  529 VAIYHFEGSSEGTVSMSEGEDLSLMEeDKGDGWTRVRRKQGAEGYVPT 576
Cdd:pfam00018   1 VALYDYTAQEPDELSFKKGDIIIVLE-KSEDGWWKGRNKGGKEGLIPS 47
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 543-582 1.36e-03

Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];


Pssm-ID: 442337 [Multi-domain]  Cd Length: 119  Bit Score: 38.95  E-value: 1.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568998469 543 SMSEGEDLSLMEEDkgDGWTRVRRKQGAEGYVPTSYLRVT 582
Cdd:COG3103   29 TLPKGEKVTVLGRS--GGWYKVRYSNGKTGWVSSRYLTVT 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-183 6.06e-03

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: 39.65  E-value: 6.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469    15 ERHTQWGLdLLDKYVKFVKERAEVEQAYAK-QLRFSQQQSFVQLLQ----EVNDFAGQRELVAESLGIRVcLELAKYSQE 89
Cdd:TIGR02168  222 LRELELAL-LVLRLEELREELEELQEELKEaEEELEELTAELQELEekleELRLEVSELEEEIEELQKEL-YALANEISR 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469    90 MKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQDINATKADVEKAKQQAhlrnHMAEESKN 169
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL----EELESRLE 375

                          170
                   ....*....|....
gi 568998469   170 EYAAQLQRFNRDQA 183
Cdd:TIGR02168  376 ELEEQLETLRSKVA 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 ...
 5-238 8.27e-111

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: 331.53  E-value: 8.27e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469   5 TELWDQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR-----------------FSQQQSFVQLLQEVNDFAGQ 67
Cdd:cd07653    1 TELWDQFDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRklvkkylpkkkeedeysFSSVKAFRSILNEVNDIAGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  68 RELVAESLGIRVCLELAKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQDINATK 147
Cdd:cd07653   81 HELIAENLNSNVCKELKTLISELRQERKKHLSEGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNLTK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 148 ADVEKAKQQAHLRNHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELQVVPIIG 227
Cdd:cd07653  161 ADVEKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHYSTDLPQIFDKLQELDEKRINRTVELLLQAAEIERKVIPIIA 240

                        250
                 ....*....|.
gi 568998469 228 KCLEGMKVAAE 238
Cdd:cd07653  241 KCLDGIKKAGD 251
F-BAR_FNBP1L cd07675
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; ...
 5-238 1.52e-106

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: 320.46  E-value: 1.52e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469   5 TELWDQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR------------------FSQQQSFVQLLQEVNDFAG 66
Cdd:cd07675    1 TELWDQFDNLDKHTQWGIDFLERYAKFVKERLEIEQNYAKQLRnlvkkycpkrsskdeeprFTSCLSFYNILNELNDYAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  67 QRELVAESLGIRVCLELAKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQDINAT 146
Cdd:cd07675   81 QREVVAEEMGHRVYGELMRYSHDLKGERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 147 KADVEKAKQQAHLRNHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELQVVPII 226
Cdd:cd07675  161 KSDVEKAKQQLNLRTHMADESKNEYAAQLQNFNGEQHKHFYIVIPQIYKQLQEMDERRTVKLSECYRGFADSERKVIPII 240

                        250
                 ....*....|..
gi 568998469 227 GKCLEGMKVAAE 238
Cdd:cd07675  241 SKCLEGMVLAAK 252
F-BAR_FBP17 cd07676
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; ...
 5-238 1.92e-100

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: 305.05  E-value: 1.92e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469   5 TELWDQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR-------------------FSQQQSFVQLLQEVNDFA 65
Cdd:cd07676    1 TELWDQFDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRnlskkyqpkknskeeeeykYTSCRAFLMTLNEMNDYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  66 GQRELVAESLGIRVCLELAKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQDINA 145
Cdd:cd07676   81 GQHEVISENLASQIIVELTRYVQELKQERKSHFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 146 TKADVEKAKQQAHLRNHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELQVVPI 225
Cdd:cd07676  161 TKADVEKARQQAQIRHQMAEDSKAEYSSYLQKFNKEQHEHYYTHIPNIFQKIQEMEERRIGRVGESMKTYAEVDRQVIPI 240

                        250
                 ....*....|...
gi 568998469 226 IGKCLEGMKVAAE 238
Cdd:cd07676  241 IGKCLDGITKAAE 253
HR1_CIP4_FNBP1L cd11628
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of vertebrate ...
 376-456 7.93e-32

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: 117.70  E-value: 7.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 376 PPEQQRKRLQQQLEERNRELQKEEDQREALKKMKDVYEKTPQMGDPASLEPRIAETLGNIERLKLEVQKYEAWLAEAESR 455
Cdd:cd11628    1 PPEQRRKRLQQKIDELSRELQKEMDQSEALMKMKDVYEKNPQMGDPASLQPQIAETASNIDRLRGELHKYEAWLAEAEGR 80


                 .
gi 568998469 456 V 456
Cdd:cd11628   81 V 81
SH3_CIP4-like cd11911
Src Homology 3 domain of Cdc42-Interacting Protein 4; This subfamily is composed of ...
 527-581 1.63e-28

Src Homology 3 domain of Cdc42-Interacting Protein 4; 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, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of CIP4 associates with Gapex-5, a Rab31 GEF. 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.


Pssm-ID: 212844 [Multi-domain]  Cd Length: 55  Bit Score: 107.73  E-value: 1.63e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568998469 527 QCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11911    1 TCTALYDFDGTSEGTLSMEEGEILLVLEEDGGDGWTRVRKNNGDEGYVPTSYIEV 55
SH3_CIP4_Bzz1_like cd11777
Src Homology 3 domain of Cdc42-Interacting Protein 4, Bzz1 and similar domains; This subfamily ...
 527-581 1.41e-27

Src Homology 3 domain of Cdc42-Interacting Protein 4, Bzz1 and similar domains; This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4) and similar proteins such as Formin Binding Protein 17 (FBP17) and FormiN Binding Protein 1-Like (FNBP1L), as well as yeast Bzz1 (or Bzz1p). 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. Bzz1 is also a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Members of this subfamily contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain as well as at least one C-terminal SH3 domain. Bzz1 contains a second SH3 domain at the C-terminus. 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.


Pssm-ID: 212711 [Multi-domain]  Cd Length: 55  Bit Score: 105.00  E-value: 1.41e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568998469 527 QCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11777    1 ECKALYAFVGSSEGTISMTEGEKLSLVEEDKGDGWTRVRRDTGEEGYVPTSYIRI 55
HR1_FBP17 cd11629
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Formin Binding ...
 377-453 1.80e-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: 100.04  E-value: 1.80e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568998469 377 PEQQRKRLQQQLEERNRELQKEEDQREALKKMKDVYEKTPQMGDPASLEPRIAETLGNIERLKLEVQKYEAWLAEAE 453
Cdd:cd11629    1 PEQRRKKLQQKVDELNKDIQKEMDQRDALTKMKDVYIKNPQMGDPASVDHRLEEITQNIEKLRVEVQKFEGWLAEVE 77
SH3_FNBP1L cd12072
Src Homology 3 domain of Formin Binding Protein 1-Like; FormiN Binding Protein 1-Like (FNBP1L), ...
 526-582 2.32e-24

Src Homology 3 domain of Formin Binding Protein 1-Like; 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. The SH3 domain of the related protein, CIP4, associates with Gapex-5, a Rab31 GEF. 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.


Pssm-ID: 213005 [Multi-domain]  Cd Length: 57  Bit Score: 96.22  E-value: 2.32e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568998469 526 GQCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRVT 582
Cdd:cd12072    1 GHCKALYPFDGSNEGTLAMKEGEVLYIIEEDKGDGWTRARKQNGEEGYVPTSYIEIT 57
SH3_FBP17 cd12071
Src Homology 3 domain of Formin Binding Protein 17; Formin Binding Protein 17 (FBP17), also ...
 526-581 2.38e-23

Src Homology 3 domain of Formin Binding Protein 17; 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 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, a Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of the related protein, CIP4, associates with Gapex-5, a Rab31 GEF. 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.


Pssm-ID: 213004 [Multi-domain]  Cd Length: 57  Bit Score: 93.12  E-value: 2.38e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568998469 526 GQCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd12071    1 GTCKALYPFEGQNEGTISVAEGEMLYVIEEDKGDGWTRIRRNEDEEGYVPTSYIEV 56
HR1_CIP4-like cd11619
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of ...
 389-453 2.22e-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: 91.13  E-value: 2.22e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568998469 389 EERNRELQKEEDQREALKKMKDVYEKTPQMGDPASLEPRIAETLGNIERLKLEVQKYEAWLAEAE 453
Cdd:cd11619   13 DELEKEIEKETKSRDGLMKMKGVYEQNPQLGDPASVEGQLAEYAKKLDKLREELQKYQGYLAEAE 77
SH3_Bzz1_1 cd11912
First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
 530-581 5.92e-15

First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the first 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.


Pssm-ID: 212845 [Multi-domain]  Cd Length: 55  Bit Score: 69.17  E-value: 5.92e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 530 AIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11912    4 VLYDYTASGDDEVSISEGEEVTVLEPDDGSGWTKVRNGSGEEGLVPTSYIEI 55
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 1-69 8.29e-13

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: 64.28  E-value: 8.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469     1 MDWGTELWDQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR----------------FSQQQSFVQLLQEVNDF 64
Cdd:smart00055   1 MGFWSELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQklskklravrdtepeyGSLSKAWEVLLSETDAL 80


                   ....*
gi 568998469    65 AGQRE 69
Cdd:smart00055  81 AKQHL 85
SH3_FCHSD_1 cd11761
First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
 528-579 2.66e-11

First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. 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.


Pssm-ID: 212695 [Multi-domain]  Cd Length: 57  Bit Score: 58.91  E-value: 2.66e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 528 CVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYL 579
Cdd:cd11761    4 CKVLYSYEAQRPDELTITEGEELEVIEDGDGDGWVKARNKSGEVGYVPENYL 55
HR1 cd00089
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ...
 389-449 3.59e-11

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: 58.88  E-value: 3.59e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568998469 389 EERNRELQKEEDQREALKKMKDVYEKTPQMGDPASLEPRIAETLGNIERLKLEVQKYEAWL 449
Cdd:cd00089    8 EELRRKLEKELKIREGAENLLKLYSNPKVKKDLAEVQLNLKESKEKIDLLKRQLERYNALV 68
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 524-580 5.67e-11

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 57.93  E-value: 5.67e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568998469   524 PIGQCVAIYHFEGSSEGTVSMSEGEDLSLMEEDkGDGWTRVRRKQGAEGYVPTSYLR 580
Cdd:smart00326   1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKS-DDGWWKGRLGRGKEGLFPSNYVE 56
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 10-231 8.60e-11

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: 61.20  E-value: 8.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  10 QFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR--------------FSQQQSFVQLLQEVNDFAGQRELVAESL 75
Cdd:cd07610    1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQklakkfskkpesgkTSLGTSWNSLREETESAATVHEELSEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  76 GIRVCLELAKYSQEMKQERKMHFQEGRRAQQQLENGFKQLEnskrkferdcreaekaahtaerldqdinatkadvekakq 155
Cdd:cd07610   81 SQLIREPLEKVKEDKEQARKKELAEGEKLKKKLQELWAKLA--------------------------------------- 121

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568998469 156 qahlrnhmaEESKNEYAAQLQRFNRDQaHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELQVVPIIGKCLE 231
Cdd:cd07610  122 ---------KKADEEYREQVEKLNPAQ-SEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKEIPQKIQQELE 187
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 21-204 2.69e-10

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: 61.18  E-value: 2.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  21 GLDLLDKYVKFVKERAEVEQAYAKQLRF----------------SQQQSFVQLLQEVNDFAgqrELVAEslgIRVCLeLA 84
Cdd:cd07655   17 GHKLCDDLMKMVQERAEIEKAYAKKLKEwakkwrdliekgpeygTLETAWKGLLSEAERLS---ELHLS---IRDKL-LN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  85 KYSQEMKQERK--------MHFQEGR-------RAQQQLENGFKQLENSKRKFERDCReAEKAAHTAER--------LDQ 141
Cdd:cd07655   90 DVVEEVKTWQKenyhksmmGGFKETKeaedgfaKAQKPWAKLLKKVEKAKKAYHAACK-AEKSAQKQENnaksdtslSPD 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568998469 142 DINATKADVEKAKQQAHlrnhmaeESKNEYAAQLQRFNRDQAHfYFSQMPQIFDKLQDMDERR 204
Cdd:cd07655  169 QVKKLQDKVEKCKQEVS-------KTKDKYEKALEDLNKYNPR-YMEDMEQVFDKCQEFEEKR 223
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 10-69 8.69e-10

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: 55.35  E-value: 8.69e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568998469   10 QFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR-----------------FSQQQSFVQLLQEVNDFAGQRE 69
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQklakkflkkkkkpeddgGTLKKAWDELLTETEQLAKQHL 77
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
 527-581 5.69e-09

Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. 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.


Pssm-ID: 212697 [Multi-domain]  Cd Length: 55  Bit Score: 52.33  E-value: 5.69e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568998469 527 QCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11763    1 KVRALYDFDSQPSGELSLRAGEVLTITRQDVGDGWLEGRNSRGEVGLFPSSYVEI 55
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 11-171 3.36e-08

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: 54.79  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  11 FEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQL-RFSQ----QQSFVQLLQEVNDFAGQRELVAE---SLGIRVCLE 82
Cdd:cd07647    7 FDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALlKLSKsagpGDEIGTLKSSWDSLRKETENVANahiQLAQSLREE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  83 LAKYSQ---EMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLdqDINATKADVEKAKQQAHL 159
Cdd:cd07647   87 AEKLEEfreKQKEERKKTEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKAEQAYEKS--SSGAQPKEAEKLKKKAAQ 164

                        170
                 ....*....|..
gi 568998469 160 RNHMAEESKNEY 171
Cdd:cd07647  165 CKTSAEEADSAY 176
SH3_CSK cd11769
Src Homology 3 domain of C-terminal Src kinase; CSK is a cytoplasmic (or nonreceptor) tyr ...
 527-578 1.63e-07

Src Homology 3 domain of C-terminal Src kinase; CSK is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, CSK is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. CSK catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. It is expressed in a wide variety of tissues and plays a role, as a regulator of Src, in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. In addition, CSK also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. 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.


Pssm-ID: 212703 [Multi-domain]  Cd Length: 57  Bit Score: 48.07  E-value: 1.63e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 527 QCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSY 578
Cdd:cd11769    3 ECIAKYNFNGASEEDLPFKKGDILTIVAVTKDPNWYKAKNKDGREGMIPANY 54
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 527-578 3.58e-07

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.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 47.07  E-value: 3.58e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 527 QCVAIYHFEGSSEGTVSMSEGEDLSLMEEDkGDGWTRVRRKQGAEGYVPTSY 578
Cdd:cd00174    1 YARALYDYEAQDDDELSFKKGDIITVLEKD-DDGWWEGELNGGREGLFPANY 51
SH3_Tec_like cd11768
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ...
 529-580 1.75e-06

Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. 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.


Pssm-ID: 212702 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.75e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEeDKGDGWTRVRRKQGAEGYVPTSYLR 580
Cdd:cd11768    3 VALYDFQPIEPGDLPLEKGEEYVVLD-DSNEHWWRARDKNGNEGYIPSNYVT 53
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
 527-580 1.78e-06

Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This family is composed of the tandem SH3 domains of p47phox subunit of NADPH oxidase and Nox Organizing protein 1 (NoxO1), the four SH3 domains of Tks4 (Tyr kinase substrate with four SH3 domains), the five SH3 domains of Tks5, the SH3 domain of obscurin, Myosin-I, and similar domains. Most members of this group also contain Phox homology (PX) domains, except for obscurin and Myosin-I. p47phox and NoxO1 are regulators of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) and nonphagocytic NADPH oxidase Nox1, respectively. They play roles in the activation of their respective NADPH oxidase, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Obscurin is a giant muscle protein that plays important roles in the organization and assembly of the myofibril and the sarcoplasmic reticulum. Type I myosins (Myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. 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.


Pssm-ID: 212790 [Multi-domain]  Cd Length: 53  Bit Score: 44.93  E-value: 1.78e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568998469 527 QCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGdGWTRVrRKQGAEGYVPTSYLR 580
Cdd:cd11856    1 SYVAIADYEAQGDDEISLQEGEVVEVLEKNDS-GWWYV-RKGDKEGWVPASYLE 52
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 529-576 2.18e-06

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.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 44.50  E-value: 2.18e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568998469  529 VAIYHFEGSSEGTVSMSEGEDLSLMEeDKGDGWTRVRRKQGAEGYVPT 576
Cdd:pfam00018   1 VALYDYTAQEPDELSFKKGDIIIVLE-KSEDGWWKGRNKGGKEGLIPS 47
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 32-204 3.32e-06

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: 48.89  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  32 VKERAEVEQAYAKQL-----RFSQ-----------QQSFVQLLQEVNDFAGQRELVAESLgIRVCLELAKYSQEMKQERK 95
Cdd:cd07680   28 VQERAKIEKAYGQQLtdwakRWRQliekgpqygslERAWGAIMTEADKVSELHQEVKNNL-LNEDLEKVKNWQKDAYHKQ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  96 MH--FQEG-------RRAQQQLENGFKQLENSKRKFERDCREaEKAAHTAE---RLDQDINATKA-----DVEKAKQQah 158
Cdd:cd07680  107 IMggFKETkeaedgfRKAQKPWAKKMKELEAAKKAYHLACKE-EKLAMTREansKAEQSVTPEQQkklqdKVDKCKQD-- 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568998469 159 lrnhmAEESKNEYAAQLQRFNRDQAHfYFSQMPQIFDKLQDMDERR 204
Cdd:cd07680  184 -----VQKTQEKYEKVLDDVGKTTPQ-YMENMEQVFEQCQQFEEKR 223
SH3_Fyn_Yrk cd12006
Src homology 3 domain of Fyn and Yrk Protein Tyrosine Kinases; Fyn and Yrk (Yes-related kinase) ...
 529-579 1.24e-05

Src homology 3 domain of Fyn and Yrk Protein Tyrosine Kinases; Fyn and Yrk (Yes-related kinase) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. 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.


Pssm-ID: 212939 [Multi-domain]  Cd Length: 56  Bit Score: 42.73  E-value: 1.24e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYL 579
Cdd:cd12006    4 VALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYV 54
SH3_SNX18 cd11897
Src Homology 3 domain of Sorting nexin 18; SNX18 is localized to peripheral endosomal ...
 530-581 1.89e-05

Src Homology 3 domain of Sorting nexin 18; SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. It binds FIP5 and is required for apical lumen formation. It may also play a role in axonal elongation. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX18 also contains BAR and SH3 domains. 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.


Pssm-ID: 212830 [Multi-domain]  Cd Length: 55  Bit Score: 42.29  E-value: 1.89e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 530 AIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11897    4 ALYDFRSENPGEISLREHEVLSLCSEQDIEGWLEGVNSRGDRGLFPASYVEV 55
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 3-267 1.91e-05

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: 46.59  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469   3 WGtELWDQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQL--------RFSQQQSFVQLL----QEVNDFAG-QRE 69
Cdd:cd07673    7 WG-EKNSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMtklaksasNYSQLGTFAPVWdvfkTSTEKLANcHLE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  70 LVAESLgiRVCLELAKYSQEMKQERKMHFQE---GRRAQQQLENGFKQLENSKRKFERDCREAEkaahtaeRLDQDiNAT 146
Cdd:cd07673   86 LVRKLQ--ELIKEVQKYGEEQVKSHKKTKEEvagTLEAVQNIQSITQALQKSKENYNAKCLEQE-------RLKKE-GAT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 147 KADVEKAKqqahLRNHMAEESkneYAAQLQRFNRDQAHFYfSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELQVVPII 226
Cdd:cd07673  156 QREIEKAA----VKSKKATES---YKLYVEKYALAKADFE-QKMTETAQKFQDIEETHLIRIKEIIGSYSNSVKEIHIQI 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568998469 227 GKCLEGMKVAAESVDAKNDSQVLIELHKSGFARPGDLEFED 267
Cdd:cd07673  228 GQVHEEFINNMANTTVESLIQKFAESKGTGKERPGPIEFEE 268
SH3_SPIN90 cd11849
Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also ...
 530-580 1.91e-05

Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also called NCK interacting protein with SH3 domain (NCKIPSD), Dia-interacting protein (DIP), 54 kDa vimentin-interacting protein (VIP54), or WASP-interacting SH3-domain protein (WISH). It is an F-actin binding protein that regulates actin polymerization and endocytosis. It associates with the Arp2/3 complex near actin filaments and determines filament localization at the leading edge of lamellipodia. SPIN90 is expressed in the early stages of neuronal differentiation and plays a role in regulating growth cone dynamics and neurite outgrowth. It also interacts with IRSp53 and regulates cell motility by playing a role in the formation of membrane protrusions. SPIN90 contains an N-terminal SH3 domain, a proline-rich domain, and a C-terminal VCA (verprolin-homology and cofilin-like acidic) 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.


Pssm-ID: 212783 [Multi-domain]  Cd Length: 53  Bit Score: 42.30  E-value: 1.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 530 AIYHFEGSSEGTVSMSEGEDLSLMEEDKGDgWTRVRRKQGAEGYVPTSYLR 580
Cdd:cd11849    4 ALYDFKSAEPNTLSFSEGETFLLLERSNAH-WWLVTNHSGETGYVPANYVK 53
SH3_Nck_3 cd11767
Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain ...
 529-581 4.18e-05

Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain of Nck, the first SH3 domain of Caenorhabditis elegans Ced-2 (Cell death abnormality protein 2), and similar domains. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. Ced-2 is a cell corpse engulfment protein that interacts with Ced-5 in a pathway that regulates the activation of Ced-10, a Rac small GTPase.


Pssm-ID: 212701 [Multi-domain]  Cd Length: 56  Bit Score: 41.53  E-value: 4.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKGD-GWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11767    3 VALYPFTGENDEELSFEKGERLEIIEKPEDDpDWWKARNALGTTGLVPRNYVEV 56
SH3_Src cd12008
Src homology 3 domain of Src Protein Tyrosine Kinase; Src (or c-Src) is a cytoplasmic (or ...
 529-579 4.58e-05

Src homology 3 domain of Src Protein Tyrosine Kinase; Src (or c-Src) is a cytoplasmic (or non-receptor) PTK and is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. 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.


Pssm-ID: 212941 [Multi-domain]  Cd Length: 56  Bit Score: 41.25  E-value: 4.58e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYL 579
Cdd:cd12008    3 VALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYV 53
SH3_DNMBP_C2_like cd11800
Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and ...
 529-580 6.40e-05

Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and similar domains; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. The C-terminal SH3 domains of DNMBP bind to N-WASP and Ena/VASP proteins, which are key regulatory proteins of the actin cytoskeleton. Also included in this subfamily is the second C-terminal SH3 domain of Rho guanine nucleotide exchange factor 37 (ARHGEF37), whose function is still unknown. 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.


Pssm-ID: 212734 [Multi-domain]  Cd Length: 57  Bit Score: 40.82  E-value: 6.40e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLME--EDKG-DGWTRVrRKQGAEGYVPTSYLR 580
Cdd:cd11800    3 YALYTFEARSPGELSVTEGQVVTVLEkhDLKGnPEWWLV-EDRGKQGYVPSNYLA 56
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 31-204 7.13e-05

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: 44.60  E-value: 7.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  31 FVKERAEVEQAYAKQL----RFS--------QQQSFVQLLQEVNDFAGQRELVAESLGIRVCLELAKYSQEMKQERKM-- 96
Cdd:cd07651   27 FYKERASIEEEYAKRLeklsRKSlggseeggLKNSLDTLRLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKiq 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  97 -HFQEGRRAQQQLengFKQLENSKRKFERDC---------------REAEKAAHTAERLDQDINATKADVekakqQAHLR 160
Cdd:cd07651  107 sHMEKLLKKKQDQ---EKYLEKAREKYEADCskinsytlqsqltwgKELEKNNAKLNKAQSSINSSRRDY-----QNAVK 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568998469 161 NhmaeeskneYAAQLQRFNRDQAHFyfsqmpqiFDKLQDMDERR 204
Cdd:cd07651  179 A---------LRELNEIWNREWKAA--------LDDFQDLEEER 205
SH3_Myosin-I_fungi cd11858
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ...
 530-579 9.57e-05

Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Saccharomyces cerevisiae has two myosins-I, Myo3 and Myo5, which are involved in endocytosis and the polarization of the actin cytoskeleton. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. 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.


Pssm-ID: 212792 [Multi-domain]  Cd Length: 55  Bit Score: 40.45  E-value: 9.57e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 530 AIYHFEGSSEGTVSMSEGeDLSLMEEDKGDGWTRVRR-KQGAEGYVPTSYL 579
Cdd:cd11858    4 ALYDFAGSVANELSLKKD-DIVYIVQKEDNGWWLAKKlDESKEGWVPAAYL 53
SH3_ITK cd11908
Src Homology 3 domain of Interleukin-2-inducible T-cell Kinase; ITK (also known as Tsk or Emt) ...
 529-579 1.14e-04

Src Homology 3 domain of Interleukin-2-inducible T-cell Kinase; ITK (also known as Tsk or Emt) is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. ITK is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, ITK plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, ITK is crucial for the development of T-helper(Th)2 effector responses. 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.


Pssm-ID: 212841 [Multi-domain]  Cd Length: 56  Bit Score: 40.00  E-value: 1.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKgDGWTRVRRKQGAEGYVPTSYL 579
Cdd:cd11908    4 IALYDYQTNDPQELALRYNEEYHLLDSSE-IHWWRVQDKNGHEGYVPSSYL 53
F-BAR_FCHSD1 cd07678
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ...
 9-226 1.20e-04

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: 44.23  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469   9 DQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQL-RFSQQ-------------------QSFVQLLQEVNDFAGQR 68
Cdd:cd07678    5 EQLSILQTKQQRDAELLEDIRSYSKQRAAIEREYGQALqRLASQflkrdwhrggnetemdrsvRTVWGAWREGTAATGQG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  69 ELVAESLGIRVCLELAKYSQEMKQER-KMHFQEGRRAQQQLENGFKQLENSKRKF---ERDCREA-EKAAHTAERL---D 140
Cdd:cd07678   85 RVTRLEAYRRLRDEAGKTGRSAKEQVlKKSTEQLQKAQAELLETVKELSKSKKLYgqlERVSEVAkEKAADVEARLnksD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 141 QDINATKADVEKAkqQAHLRNHMAEESK------NEYAAQLQRFNRDQAHFYFSQMPQIfdkLQDMDERRATRLGAGYGL 214
Cdd:cd07678  165 HGIFHSKASLQKL--SAKFSAQSAEYSQqlqaarNEYLLNLVAANAHLDHYYQEELPAI---MKALDGDLYERLRDPLTS 239

                        250
                 ....*....|..
gi 568998469 215 LSEAELQVVPII 226
Cdd:cd07678  240 LSHTELEACEVT 251
SH3_Nephrocystin cd11770
Src Homology 3 domain of Nephrocystin (or Nephrocystin-1); Nephrocystin contains an SH3 domain ...
 528-581 1.22e-04

Src Homology 3 domain of Nephrocystin (or Nephrocystin-1); Nephrocystin contains an SH3 domain involved in signaling pathways that regulate cell adhesion and cytoskeletal organization. It is a protein that in humans is associated with juvenile nephronophthisis, an inherited kidney disease characterized by renal fibrosis that lead to chronic renal failure in children. It is localized in cell-cell junctions in renal duct cells, and is known to interact with Ack1, an activated Cdc42-associated kinase. 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.


Pssm-ID: 212704 [Multi-domain]  Cd Length: 54  Bit Score: 39.99  E-value: 1.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568998469 528 CVAIYHFEGSSEGTVSMSEGEDLSLMEEdKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11770    2 YEALSDFQAEQEGDLSFKKGEVLRIISK-RADGWWLAENSKGNRGLVPKTYLKV 54
SH3_Blk cd12009
Src homology 3 domain of Blk Protein Tyrosine Kinase; Blk is a member of the Src subfamily of ...
 529-579 1.36e-04

Src homology 3 domain of Blk Protein Tyrosine Kinase; Blk is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. It is expressed specifically in B-cells and is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. 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.


Pssm-ID: 212942 [Multi-domain]  Cd Length: 54  Bit Score: 39.80  E-value: 1.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDkGDGWTRVRRKQGAEGYVPTSYL 579
Cdd:cd12009    3 IAQYDFVPSNERDLQLKKGEKLQVLKSD-GEWWLAKSLTTGKEGYIPSNYV 52
SH3_SNX33 cd11896
Src Homology 3 domain of Sorting Nexin 33; SNX33 interacts with Wiskott-Aldrich syndrome ...
 530-581 1.73e-04

Src Homology 3 domain of Sorting Nexin 33; SNX33 interacts with Wiskott-Aldrich syndrome protein (WASP) and plays a role in the maintenance of cell shape and cell cycle progression. It modulates the shedding and endocytosis of cellular prion protein (PrP(c)) and amyloid precursor protein (APP). SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX33 also contains BAR and SH3 domains. 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.


Pssm-ID: 212829 [Multi-domain]  Cd Length: 55  Bit Score: 39.56  E-value: 1.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 530 AIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11896    4 ALYSFQSENKEEINIQENEELVIFSENSLDGWLQGQNSRGETGLFPASYVEI 55
SH3_BTK cd11906
Src Homology 3 domain of Bruton's tyrosine kinase; BTK is a cytoplasmic (or nonreceptor) tyr ...
 529-579 1.94e-04

Src Homology 3 domain of Bruton's tyrosine kinase; BTK is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor (BCR), leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. 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.


Pssm-ID: 212839 [Multi-domain]  Cd Length: 55  Bit Score: 39.42  E-value: 1.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDgWTRVRRKQGAEGYVPTSYL 579
Cdd:cd11906    4 VALYDYTPMNAQDLQLRKGEEYVILEESNLP-WWRARDKNGREGYIPSNYV 53
F-BAR_Fer cd07686
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fer (Fes related) tyrosine ...
 5-202 2.55e-04

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: 42.74  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469   5 TELWDQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLR-FSQQ----------------QSFVQLLQEVNDFAGQ 67
Cdd:cd07686    1 SDLRNSHEALLKLQDWELRLLETVKKFMALRVKSDKEYASTLQnLCNQvdkestsqldyvsnvsKSWLHMVQQTEQLSKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  68 RELVAESLGIRVCLELAKYSQEMKQERKMHfqegRRAQQQLENGFKQLENSK-RKFERDCREAEKAAHTAERLDQDINAT 146
Cdd:cd07686   81 MKTHAEELNSGPLHRLTMMIKDKQQVKKSY----IGVHQQIEAEMYKVTKTElEKLKCSYRQLTKEVNSAKEKYKDAVAK 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568998469 147 KADVEKAKQ---QAHLRNHMAEeskNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDE 202
Cdd:cd07686  157 GKETEKARErydKATMKLHMLH---NQYVLAVKGAQLHQHQYYDFTLPLLLDSLQKMQE 212
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 11-180 3.72e-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: 42.25  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  11 FEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQL----RFSQQQSFVQLLQEVNDFAGQRELVAESLGIRVCLEL--- 83
Cdd:cd07671    7 YEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELvqiaRKAGGQTEINTLKASFDQLKQQIENIGNSHIQLAGMLree 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  84 ----AKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQdiNATKADVEKAKQQAHL 159
Cdd:cd07671   87 lkslEEFRERQKEQRKKYEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAEQTFERSSS--TGNPKQSEKSQNKAKQ 164

                        170       180
                 ....*....|....*....|.
gi 568998469 160 RNHMAEESKNEYAAQLQRFNR 180
Cdd:cd07671  165 CRDAATEAERVYKQNIEQLDK 185
SH3_Yes cd12007
Src homology 3 domain of Yes Protein Tyrosine Kinase; Yes (or c-Yes) is a member of the Src ...
 529-579 3.81e-04

Src homology 3 domain of Yes Protein Tyrosine Kinase; Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. 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.


Pssm-ID: 212940 [Multi-domain]  Cd Length: 58  Bit Score: 38.86  E-value: 3.81e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYL 579
Cdd:cd12007    4 VALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYV 54
SH3_Tec cd11905
Src Homology 3 domain of Tec (Tyrosine kinase expressed in hepatocellular carcinoma); Tec is a ...
 529-579 4.02e-04

Src Homology 3 domain of Tec (Tyrosine kinase expressed in hepatocellular carcinoma); Tec is a cytoplasmic (or nonreceptor) tyr kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. It is more widely-expressed than other Tec subfamily kinases. Tec is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Tec is a key component of T-cell receptor (TCR) signaling, and is important in TCR-stimulated proliferation, IL-2 production and phospholipase C-gamma1 activation. 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.


Pssm-ID: 212838 [Multi-domain]  Cd Length: 56  Bit Score: 38.64  E-value: 4.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDgWTRVRRKQGAEGYVPTSYL 579
Cdd:cd11905    4 VAMYDFQPTEPHDLRLETGEEYVILEKNDVH-WWKARDKYGKEGYIPSNYV 53
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 529-578 4.84e-04

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. 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.


Pssm-ID: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 38.33  E-value: 4.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSY 578
Cdd:cd11845    3 VALYDYEARTDDDLSFKKGDRLQILDDSDGDWWLARHLSTGKEGYIPSNY 52
SH3_PACSIN1-2 cd11998
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) ...
 530-579 5.27e-04

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN 2; PACSIN 1 or Syndapin I (Synaptic dynamin-associated protein 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. 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. PACSINs act as regulators of cytoskeletal and membrane dynamics. 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. 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.


Pssm-ID: 212931 [Multi-domain]  Cd Length: 56  Bit Score: 38.39  E-value: 5.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568998469 530 AIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYL 579
Cdd:cd11998    5 ALYDYDGQEQDELSFKAGDELTKLEDEDEQGWCKGRLDSGQVGLYPANYV 54
SH3_Abl cd11850
Src homology 3 domain of the Protein Tyrosine Kinase, Abelson kinase; Abl (or c-Abl) is a ...
 529-578 5.66e-04

Src homology 3 domain of the Protein Tyrosine Kinase, Abelson kinase; Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). 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.


Pssm-ID: 212784  Cd Length: 56  Bit Score: 38.16  E-value: 5.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVR-RKQGAEGYVPTSY 578
Cdd:cd11850    3 VALYDFVASGENQLSIKKGEQLRVLGYNKNGEWCEAEsKSTGGQGWVPSNY 53
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 32-204 5.90e-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: 5.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  32 VKERAEVEQAYAKQL-----RFSQ-----------QQSFVQLLQEVNDFAgqrELVAESLGIRVCLELAKYSQEMKQERK 95
Cdd:cd07679   28 LHERARIEKVYAQQLtewakRWRQlvekgpqygtvEKAWCALMSEAEKVS---ELHLEVKASLMNEDFEKIKNWQKEAFH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  96 MHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTA---ERL--DQDINATKADVEKAKQQAHLRNHM------A 164
Cdd:cd07679  105 KQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHTAckeEKLatSREANSKADPALNPEQLKKLQDKVekckqdV 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568998469 165 EESKNEYAAQLQRFNRDQAHfYFSQMPQIFDKLQDMDERR 204
Cdd:cd07679  185 LKTKEKYEKSLKELDQTTPQ-YMENMEQVFEQCQQFEEKR 223
SH3_9 pfam14604
Variant SH3 domain;
530-580 6.33e-04

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 37.98  E-value: 6.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568998469  530 AIYHFEGSSEGTVSMSEGEDLSLMEEDkGDGWTRVRRKqGAEGYVPTSYLR 580
Cdd:pfam14604   1 ALYPYEPKDDDELSLQRGDVITVIEES-EDGWWEGINT-GRTGLVPANYVE 49
SH3_SNX9 cd11898
Src Homology 3 domain of Sorting nexin 9; Sorting nexin 9 (SNX9), also known as SH3PX1, is a ...
 536-581 6.74e-04

Src Homology 3 domain of Sorting nexin 9; Sorting nexin 9 (SNX9), also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX9 also contains BAR and SH3 domains. 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.


Pssm-ID: 212831  Cd Length: 57  Bit Score: 37.92  E-value: 6.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568998469 536 GSSEGTVSmsEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRV 581
Cdd:cd11898   13 GNNELTVK--EGEIITVTNPNVGGGWIEAKNSQGERGLVPTDYVEI 56
SH3_SLAP2 cd12011
Src homology 3 domain of Src-Like Adaptor Protein 2; SLAP2 plays a role in c-Cbl-dependent ...
 527-578 8.38e-04

Src homology 3 domain of Src-Like Adaptor Protein 2; SLAP2 plays a role in c-Cbl-dependent regulation of CSF1R, a tyrosine kinase important for myeloid cell growth and differentiation. It has been shown to interact with CSF1R, c-Cbl, LAT, CD247, and Zap70. SLAPs are adaptor proteins with limited similarity to Src family tyrosine kinases. They contain an N-terminal SH3 domain followed by an SH2 domain, and a unique C-terminal sequence. They function in regulating the signaling, ubiquitination, and trafficking of T-cell receptor (TCR) and B-cell receptor (BCR) components. The SH3 domain of SLAP forms a complex with v-Abl. 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.


Pssm-ID: 212944  Cd Length: 55  Bit Score: 37.80  E-value: 8.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 527 QCVAIYHFEGSSEGTVSMSEGEDLSLMEEDkGDGWTRVRRKQGAEGYVPTSY 578
Cdd:cd12011    1 VAVALCNFPSGGPTELSIRMGEQLTILSED-GDWWKVSSAVTGRECYIPSNY 51
SH3_Bzz1_2 cd11778
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
 530-578 9.12e-04

Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the second 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.


Pssm-ID: 212712 [Multi-domain]  Cd Length: 51  Bit Score: 37.48  E-value: 9.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568998469 530 AIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRvRRKQGAEGYVPTSY 578
Cdd:cd11778    4 ALYDYEAQGDDEISIRVGDRIAVIRGDDGSGWTY-GEINGVKGLFPTSY 51
SH3_Nck_1 cd11765
First Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
 529-579 9.18e-04

First Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The first SH3 domain of Nck proteins preferentially binds the PxxDY sequence, which is present in the CD3e cytoplasmic tail. This binding inhibits phosphorylation by Src kinases, resulting in the downregulation of TCR surface expression. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. 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.


Pssm-ID: 212699 [Multi-domain]  Cd Length: 51  Bit Score: 37.40  E-value: 9.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKGdgWTRVRRKQGAEGYVPTSYL 579
Cdd:cd11765    3 VAKYDYTAQGDQELSIKKNEKLTLLDDSKH--WWKVQNSSNQTGYVPSNYV 51
SH3_PACSIN_like cd11999
Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C ...
 530-579 9.69e-04

Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, 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. 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.


Pssm-ID: 212932 [Multi-domain]  Cd Length: 56  Bit Score: 37.61  E-value: 9.69e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568998469 530 AIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYL 579
Cdd:cd11999    6 AVYDYTGQEPDELSFKAGEELLKVEDEDEQGWCKGVTDGGAVGLYPANYV 55
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 11-266 1.06e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 41.08  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  11 FEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLrfSQQQSFVQLLQEVNDFAGQRELV-AESLGIRVC-LELAKYSQ 88
Cdd:cd07674    7 FDVLYHNMKHGQISTKELADFVRERAAIEETYSKSM--SKLSKMASNGSPLGTFAPMWEVFrVSSDKLALChLELMRKLN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  89 EM--------KQERKMHFQEGRR------AQQQLENGFKQLENSKRKFERDCREaekaahtAERLDQDinatkADVEKAK 154
Cdd:cd07674   85 DLikdinrygDEQVKIHKKTKEEaigtleAVQSLQVQSQHLQKSRENYHSKCVE-------QERLRRE-----GVPQKEL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 155 QQAHLRNHMAEESkneYAAQLQRFNRDQAHFYfSQMPQIFDKLQDMDE---RRATRLGAGYG-LLSEAELQvvpiIGKCL 230
Cdd:cd07674  153 EKAELKTKKAAES---LRGSVEKYNRARGDFE-QKMLESAQKFQDIEEthlRHMKLLIKGYShSVEDTHVQ----IGQVH 224

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568998469 231 EGMKVAAESVDAKNDSQVLIELHKSGFARPGDLEFE 266
Cdd:cd07674  225 EEFKQNVENVGVENLIRKFAESKGTGKERPGPVGFE 260
SH3_Sla1p_3 cd11775
Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
 529-579 1.09e-03

Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. The third SH3 domain of Sla1p can bind ubiquitin while retaining the ability to bind proline-rich ligands; monoubiquitination of target proteins signals internalization and sorting through the endocytic pathway. 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.


Pssm-ID: 212709 [Multi-domain]  Cd Length: 57  Bit Score: 37.30  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRR-KQGAEGYVPTSYL 579
Cdd:cd11775    4 KVLYDFDAQSDDELTVKEGDVVYILDDKKSKDWWMVENvSTGKEGVVPASYI 55
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 543-582 1.36e-03

Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];


Pssm-ID: 442337 [Multi-domain]  Cd Length: 119  Bit Score: 38.95  E-value: 1.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568998469 543 SMSEGEDLSLMEEDkgDGWTRVRRKQGAEGYVPTSYLRVT 582
Cdd:COG3103   29 TLPKGEKVTVLGRS--GGWYKVRYSNGKTGWVSSRYLTVT 66
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 11-171 1.54e-03

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: 40.70  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  11 FEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQL------RFSQQQSFVQLLQEVNDFAGQRELVAESlGIRVCLELA 84
Cdd:cd07672    7 YDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELlnlskkKPCGQTEINTLKRSLDVFKQQIDNVGQS-HIQLAQTLR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  85 KYSQEMKQERKMHFQEGRRAQQQLEN-------GFKQLENSKRKFERDCREAEKAAHTAERLDQDINATKADVEKAKQQA 157
Cdd:cd07672   86 DEAKKMEDFRERQKLARKKIELIMDAihkqramQFKKTMESKKNYEQKCRDKDEAEQAVNRNANLVNVKQQEKLFAKLAQ 165

                        170
                 ....*....|....
gi 568998469 158 HLRNhmAEESKNEY 171
Cdd:cd07672  166 SKQN--AEDADRLY 177
SH3_PSTPIP1 cd11824
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ...
 529-579 2.02e-03

Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, also called 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. 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.


Pssm-ID: 212758 [Multi-domain]  Cd Length: 53  Bit Score: 36.58  E-value: 2.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDkGDGWTRVRRkQGAEGYVPTSYL 579
Cdd:cd11824    3 SVLYDYTAQEDDELSISKGDVVAVIEKG-EDGWWTVER-NGQKGLVPGTYL 51
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 26-131 2.25e-03

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: 40.02  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  26 DKYVKFVKERAEVEQAYAKQLR-------------FSQQQSFVQLLQEVNDFAGQRELVAESLGIRVCL---ELAKYSQE 89
Cdd:cd07652   22 KEFATFLKKRAAIEEEHARGLKklarttldtykrpDHKQGSFSNAYHSSLEFHEKLADNGLRFAKALNEmsdELSSLAKT 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568998469  90 MKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEK 131
Cdd:cd07652  102 VEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLER 143
SH3_Lyn cd12004
Src homology 3 domain of Lyn Protein Tyrosine Kinase; Lyn is a member of the Src subfamily of ...
 529-579 2.98e-03

Src homology 3 domain of Lyn Protein Tyrosine Kinase; Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. 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.


Pssm-ID: 212937 [Multi-domain]  Cd Length: 56  Bit Score: 36.12  E-value: 2.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEdKGDGWTRVRRKQGAEGYVPTSYL 579
Cdd:cd12004    3 VALYPYDGIHEDDLSFKKGEKLKVIEE-HGEWWKARSLTTKKEGFIPSNYV 52
SH3_GRAP_N cd11948
N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 527-581 3.51e-03

N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. 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.


Pssm-ID: 212881 [Multi-domain]  Cd Length: 54  Bit Score: 35.95  E-value: 3.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568998469 527 QCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRkQGAEGYVPTSYLRV 581
Cdd:cd11948    1 EAVALYSFQATESDELPFQKGDILKILNMEDDQNWYKAEL-QGREGYIPKNYIKV 54
SH3_Intersectin2_5 cd11996
Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
 526-581 4.09e-03

Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fifth SH3 domain (or SH3E) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. 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.


Pssm-ID: 212929 [Multi-domain]  Cd Length: 54  Bit Score: 35.73  E-value: 4.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568998469 526 GQCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTrvRRKQGAEGYVPTSYLRV 581
Cdd:cd11996    1 CQVIAMYDYTANNEDELSFSKGQLINVLNKDDPDWWQ--GEINGVTGLFPSNYVKM 54
SH3_PRMT2 cd11806
Src homology 3 domain of Protein arginine N-methyltransferase 2; PRMT2, also called HRMT1L1, ...
 528-579 4.48e-03

Src homology 3 domain of Protein arginine N-methyltransferase 2; PRMT2, also called HRMT1L1, belongs to the arginine methyltransferase protein family. It functions as a coactivator to both estrogen receptor alpha (ER-alpha) and androgen receptor (AR), presumably through arginine methylation. The ER-alpha transcription factor is involved in cell proliferation, differentiation, morphogenesis, and apoptosis, and is also implicated in the development and progression of breast cancer. PRMT2 and its variants are upregulated in breast cancer cells and may be involved in modulating the ER-alpha signaling pathway during formation of breast cancer. PRMT2 also plays a role in regulating the function of E2F transcription factors, which are critical cell cycle regulators, by binding to the retinoblastoma gene product (RB). It contains an N-terminal SH3 domain and an AdoMet binding 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.


Pssm-ID: 212740 [Multi-domain]  Cd Length: 53  Bit Score: 35.44  E-value: 4.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 528 CVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRvrRKQGAEGYVPTSYL 579
Cdd:cd11806    2 YVAIADFVATDDSQLSFESGDKLLVLRKPSVDWWWA--EHNGCCGYIPASHL 51
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 11-267 5.52e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proteins in this group have been named FCH domain Only (FCHO) proteins. Vertebrates have two members, FCHO1 and FCHO2. These proteins contain an F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153332 [Multi-domain]  Cd Length: 261  Bit Score: 38.86  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  11 FEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQL--------RFSQQQSFVQLLQEVNDFAgqrELVAE---SLGIRV 79
Cdd:cd07648    7 FDVLYHNMKHGQIAVKELADFLRERATIEETYSKALnklakqasNSSQLGTFAPLWLVLRVST---EKLSElhlQLVQKL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  80 C---LELAKYSQEMKQERKMHFQEGRRAQ---QQLENGFKQLenSKRKFERDCREAEKaahtaERLDQDINATKaDVEKA 153
Cdd:cd07648   84 QeliKDVQKYGEEQHKKHKKVKEEESGTAeavQAIQTTTAAL--QKAKEAYHARCLEL-----ERLRRENASPK-EIEKA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469 154 KQQahlrnhmAEESKNEYAAQLQRFNRDQAHFYfSQMPQIFDKLQDMDE---RRATRLGAGY-GLLSEAELQVvpiigkc 229
Cdd:cd07648  156 EAK-------LKKAQDEYKALVEKYNNIRADFE-TKMTDSCKRFQEIEEshlRQMKEFLASYaEVLSENHSAV------- 220

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568998469 230 legMKVAAE---SVDAKNDSQVLIELHKS---GFARPGDLEFED 267
Cdd:cd07648  221 ---GQVHEEfkrQVDELTVDKLLRQFVESkgtGTEKPELIEFEE 261
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-183 6.06e-03

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: 39.65  E-value: 6.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469    15 ERHTQWGLdLLDKYVKFVKERAEVEQAYAK-QLRFSQQQSFVQLLQ----EVNDFAGQRELVAESLGIRVcLELAKYSQE 89
Cdd:TIGR02168  222 LRELELAL-LVLRLEELREELEELQEELKEaEEELEELTAELQELEekleELRLEVSELEEEIEELQKEL-YALANEISR 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469    90 MKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQDINATKADVEKAKQQAhlrnHMAEESKN 169
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL----EELESRLE 375

                          170
                   ....*....|....
gi 568998469   170 EYAAQLQRFNRDQA 183
Cdd:TIGR02168  376 ELEEQLETLRSKVA 389
SH3_DOCK_AB cd11872
Src Homology 3 domain of Class A and B Dedicator of Cytokinesis proteins; DOCK proteins are ...
 529-578 6.46e-03

Src Homology 3 domain of Class A and B Dedicator of Cytokinesis proteins; DOCK proteins are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. They are divided into four classes (A-D) based on sequence similarity and domain architecture: class A includes Dock1, 2 and 5; class B includes Dock3 and 4; class C includes Dock6, 7, and 8; and class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate while DHR-2 contains the catalytic activity for Rac and/or Cdc42. This subfamily includes only Class A and B DOCKs, which also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus. Class A/B DOCKs are mostly specific GEFs for Rac, except Dock4 which activates the Ras family GTPase Rap1, probably indirectly through interaction with Rap regulatory proteins. The SH3 domain of class A/B DOCKs have been shown to bind Elmo, a scaffold protein that promotes GEF activity of DOCKs by releasing DHR-2 autoinhibition by the intramolecular 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.


Pssm-ID: 212805 [Multi-domain]  Cd Length: 56  Bit Score: 35.25  E-value: 6.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568998469 529 VAIYHFEGSSEGTVSMSEGEDLSLMEEDkgDGWTR--VRRKQGAEGYVPTSY 578
Cdd:cd11872    3 VAIYNFQGDGEHQLSLQVGDTVQILEEC--EGWYRgfSLRNKSLKGIFPKSY 52
F-BAR_Fes_Fer cd07657
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer ...
 12-208 6.59e-03

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: 38.52  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  12 EVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQL-RFSQQ----------------QSFVQLLQEVNDFAGQRELVAES 74
Cdd:cd07657    8 EALLKRQDAELRLLETMKKYMAKRAKSDREYASTLgSLANQglkieagddlqgspisKSWKEIMDSTDQLSKLIKQHAEA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568998469  75 LGIRVCLELAKYSQEMKQERKMhFQEGRraqQQLENGFKQLENSKRKFERDCR---EAEKAAHTaeRLDQDINATK---A 148
Cdd:cd07657   88 LESGTLDKLTLLIKDKRKAKKA-YQEER---QQIDEQYKKLTDEVEKLKSEYQkllEDYKAAKS--KFEEAVVKGGrggR 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568998469 149 DVEKAK---QQAHLRNHMAEeskNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRL 208
Cdd:cd07657  162 KLDKARdkyQKACRKLHLCH---NDYVLALLEAQEHEEDYRTLLLPGLLNSLQSLQEEFITQW 221
 
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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