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Conserved domains on  [gi|1958751991|ref|XP_008759007|]
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FYN-binding protein 1 isoform X2 [Rattus norvegicus]

Protein Classification

FYN-binding protein 1( domain architecture ID 10983874)

FYN-binding protein 1 acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells

CATH:  2.30.30.40
Gene Ontology:  GO:0005515|GO:0070064|GO:0050852|GO:0044877|GO:0007229|GO:0008289
PubMed:  28510178|1639195|11256992
SCOP:  4000369

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 738-826 3.22e-53

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


:

Pssm-ID: 464216  Cd Length: 89  Bit Score: 179.03  E-value: 3.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991 738 LRKKFKYDGEIRVLYSTKVASSLTSKKWGTRDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVDNDGEIYDDI 817
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMTVDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLLQNDGEIYDDI 80


                  ....*....
gi 1958751991 818 ADGCIYDND 826
Cdd:pfam14603  81 GDDCIYDND 89
hSH3 super family cl48258
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 495-598 8.89e-12

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


The actual alignment was detected with superfamily member pfam14603:

Pssm-ID: 464216  Cd Length: 89  Bit Score: 61.93  E-value: 8.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991 495 LRKKFKLTGPIQVIHHAK---ACCDVKGGKNELSFKQGEDIEIIRITDnpEGKWLGRTARGSYGYIKTTAVkidydslkr 571
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMTvdpNLTIKKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLRSNL--------- 69

                          90       100
                  ....*....|....*....|....*..
gi 1958751991 572 kkntinavpprpVEEDQDVYDDVAEQD 598
Cdd:pfam14603  70 ------------LQNDGEIYDDIGDDC 84
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 50-426 4.70e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 4.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991   50 DNQGNASPPAGPSnmskfgttkPPLAAKPTYEEKSEKEPKPPFLKPTGVSPRFGTQPNSVS----RDPEVKVGFLKPVSP 125
Cdd:PHA03247  2546 DDAGDPPPPLPPA---------APPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARprapVDDRGDPRGPAPPSP 2616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  126 KPTSLTKEDSKPVILRPPGNKLHnlnqesdlktlGPKPGSTPPVPENDLKPGFSKIAGAKSKFMPA-PQDADSKPRFPRH 204
Cdd:PHA03247  2617 LPPDTHAPDPPPPSPSPAANEPD-----------PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQASSPPQRPRR 2685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  205 -----TYGQKPSLSTEDAQEEESIPKNTPVQKGSPVQLGAKSRGSPFKPAKEDPedkdhGTPSSPFAGVVLKPAASRGSP 279
Cdd:PHA03247  2686 raarpTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP-----APPAVPAGPATPGGPARPARP 2760

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  280 GLSKNSEEKKE--------ERKTDIPKNIFLNKLNQEEPArfPKAPSKLTAGTPWGQSQEKEGDK--------DSATPKQ 343
Cdd:PHA03247  2761 PTTAGPPAPAPpaapaagpPRRLTRPAVASLSESRESLPS--PWDPADPPAAVLAPAAALPPAASpagplpppTSAQPTA 2838

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  344 KPLPPLSVLGPPPSKPSRPPNVDLTRFRKADSANSSNKSQTPYSTTSLPPPPPTQPASQPPLPASHPAHLPAPSLPPRNI 423
Cdd:PHA03247  2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918


                   ...
gi 1958751991  424 KPP 426
Cdd:PHA03247  2919 PQP 2921
 
Name Accession Description Interval E-value
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 738-826 3.22e-53

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


Pssm-ID: 464216  Cd Length: 89  Bit Score: 179.03  E-value: 3.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991 738 LRKKFKYDGEIRVLYSTKVASSLTSKKWGTRDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVDNDGEIYDDI 817
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMTVDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLLQNDGEIYDDI 80


                  ....*....
gi 1958751991 818 ADGCIYDND 826
Cdd:pfam14603  81 GDDCIYDND 89
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 737-808 2.80e-37

Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.


Pssm-ID: 212801  Cd Length: 77  Bit Score: 134.19  E-value: 2.80e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958751991 737 DLRKKFKYDGEIRVLYSTKVASSLTSKKWGTRDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVD 808
Cdd:cd11867     6 EFRKKFKYNGEIKVLYSTTVLQTLTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 495-598 8.89e-12

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


Pssm-ID: 464216  Cd Length: 89  Bit Score: 61.93  E-value: 8.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991 495 LRKKFKLTGPIQVIHHAK---ACCDVKGGKNELSFKQGEDIEIIRITDnpEGKWLGRTARGSYGYIKTTAVkidydslkr 571
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMTvdpNLTIKKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLRSNL--------- 69

                          90       100
                  ....*....|....*....|....*..
gi 1958751991 572 kkntinavpprpVEEDQDVYDDVAEQD 598
Cdd:pfam14603  70 ------------LQNDGEIYDDIGDDC 84
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 495-557 1.92e-06

Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.


Pssm-ID: 212801  Cd Length: 77  Bit Score: 46.36  E-value: 1.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958751991 495 LRKKFKLTGPIQVIHHAKACCDV---KGGKNELSFKQGEDIEIIRITDnpEGKWLGRTARGSYGYI 557
Cdd:cd11867     7 FRKKFKYNGEIKVLYSTTVLQTLtikKFGSKDLQVKPGESLEVIQHTD--DTKVLCRNEEGKYGYV 70
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 507-563 3.59e-06

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: 44.84  E-value: 3.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958751991  507 VIHHAKACCDVKG-GKNELSFKQGEDIEIIRITDnpEGKWLGRTARGSYGYIKTTAVK 563
Cdd:smart00326   1 EGPQVRALYDYTAqDPDELSFKKGDIITVLEKSD--DGWWKGRLGRGKEGLFPSNYVE 56
PHA03247 PHA03247
large tegument protein UL36; Provisional
 50-426 4.70e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 4.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991   50 DNQGNASPPAGPSnmskfgttkPPLAAKPTYEEKSEKEPKPPFLKPTGVSPRFGTQPNSVS----RDPEVKVGFLKPVSP 125
Cdd:PHA03247  2546 DDAGDPPPPLPPA---------APPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARprapVDDRGDPRGPAPPSP 2616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  126 KPTSLTKEDSKPVILRPPGNKLHnlnqesdlktlGPKPGSTPPVPENDLKPGFSKIAGAKSKFMPA-PQDADSKPRFPRH 204
Cdd:PHA03247  2617 LPPDTHAPDPPPPSPSPAANEPD-----------PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQASSPPQRPRR 2685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  205 -----TYGQKPSLSTEDAQEEESIPKNTPVQKGSPVQLGAKSRGSPFKPAKEDPedkdhGTPSSPFAGVVLKPAASRGSP 279
Cdd:PHA03247  2686 raarpTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP-----APPAVPAGPATPGGPARPARP 2760

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  280 GLSKNSEEKKE--------ERKTDIPKNIFLNKLNQEEPArfPKAPSKLTAGTPWGQSQEKEGDK--------DSATPKQ 343
Cdd:PHA03247  2761 PTTAGPPAPAPpaapaagpPRRLTRPAVASLSESRESLPS--PWDPADPPAAVLAPAAALPPAASpagplpppTSAQPTA 2838

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  344 KPLPPLSVLGPPPSKPSRPPNVDLTRFRKADSANSSNKSQTPYSTTSLPPPPPTQPASQPPLPASHPAHLPAPSLPPRNI 423
Cdd:PHA03247  2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918


                   ...
gi 1958751991  424 KPP 426
Cdd:PHA03247  2919 PQP 2921
 
Name Accession Description Interval E-value
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 738-826 3.22e-53

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


Pssm-ID: 464216  Cd Length: 89  Bit Score: 179.03  E-value: 3.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991 738 LRKKFKYDGEIRVLYSTKVASSLTSKKWGTRDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVDNDGEIYDDI 817
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMTVDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLLQNDGEIYDDI 80


                  ....*....
gi 1958751991 818 ADGCIYDND 826
Cdd:pfam14603  81 GDDCIYDND 89
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 737-808 2.80e-37

Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.


Pssm-ID: 212801  Cd Length: 77  Bit Score: 134.19  E-value: 2.80e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958751991 737 DLRKKFKYDGEIRVLYSTKVASSLTSKKWGTRDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVD 808
Cdd:cd11867     6 EFRKKFKYNGEIKVLYSTTVLQTLTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 495-598 8.89e-12

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


Pssm-ID: 464216  Cd Length: 89  Bit Score: 61.93  E-value: 8.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991 495 LRKKFKLTGPIQVIHHAK---ACCDVKGGKNELSFKQGEDIEIIRITDnpEGKWLGRTARGSYGYIKTTAVkidydslkr 571
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMTvdpNLTIKKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLRSNL--------- 69

                          90       100
                  ....*....|....*....|....*..
gi 1958751991 572 kkntinavpprpVEEDQDVYDDVAEQD 598
Cdd:pfam14603  70 ------------LQNDGEIYDDIGDDC 84
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 495-557 1.92e-06

Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.


Pssm-ID: 212801  Cd Length: 77  Bit Score: 46.36  E-value: 1.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958751991 495 LRKKFKLTGPIQVIHHAKACCDV---KGGKNELSFKQGEDIEIIRITDnpEGKWLGRTARGSYGYI 557
Cdd:cd11867     7 FRKKFKYNGEIKVLYSTTVLQTLtikKFGSKDLQVKPGESLEVIQHTD--DTKVLCRNEEGKYGYV 70
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 507-563 3.59e-06

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: 44.84  E-value: 3.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958751991  507 VIHHAKACCDVKG-GKNELSFKQGEDIEIIRITDnpEGKWLGRTARGSYGYIKTTAVK 563
Cdd:smart00326   1 EGPQVRALYDYTAqDPDELSFKKGDIITVLEKSD--DGWWKGRLGRGKEGLFPSNYVE 56
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 510-565 4.40e-06

Variant 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: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 44.51  E-value: 4.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958751991 510 HAKACCDVKG-GKNELSFKQGEdieIIRITD-NPEGKWLGRTaRGSYGYIKTTAVKID 565
Cdd:pfam07653   1 YGRVIFDYVGtDKNGLTLKKGD---VVKVLGkDNDGWWEGET-GGRVGLVPSTAVEEI 54
PHA03247 PHA03247
large tegument protein UL36; Provisional
 50-426 4.70e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 4.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991   50 DNQGNASPPAGPSnmskfgttkPPLAAKPTYEEKSEKEPKPPFLKPTGVSPRFGTQPNSVS----RDPEVKVGFLKPVSP 125
Cdd:PHA03247  2546 DDAGDPPPPLPPA---------APPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARprapVDDRGDPRGPAPPSP 2616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  126 KPTSLTKEDSKPVILRPPGNKLHnlnqesdlktlGPKPGSTPPVPENDLKPGFSKIAGAKSKFMPA-PQDADSKPRFPRH 204
Cdd:PHA03247  2617 LPPDTHAPDPPPPSPSPAANEPD-----------PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQASSPPQRPRR 2685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  205 -----TYGQKPSLSTEDAQEEESIPKNTPVQKGSPVQLGAKSRGSPFKPAKEDPedkdhGTPSSPFAGVVLKPAASRGSP 279
Cdd:PHA03247  2686 raarpTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP-----APPAVPAGPATPGGPARPARP 2760

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  280 GLSKNSEEKKE--------ERKTDIPKNIFLNKLNQEEPArfPKAPSKLTAGTPWGQSQEKEGDK--------DSATPKQ 343
Cdd:PHA03247  2761 PTTAGPPAPAPpaapaagpPRRLTRPAVASLSESRESLPS--PWDPADPPAAVLAPAAALPPAASpagplpppTSAQPTA 2838

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  344 KPLPPLSVLGPPPSKPSRPPNVDLTRFRKADSANSSNKSQTPYSTTSLPPPPPTQPASQPPLPASHPAHLPAPSLPPRNI 423
Cdd:PHA03247  2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918


                   ...
gi 1958751991  424 KPP 426
Cdd:PHA03247  2919 PQP 2921
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 510-557 8.05e-04

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: 37.83  E-value: 8.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958751991 510 HAKACCDVKGGK-NELSFKQGEDIEIIRITDnpEGKWLGRTARGSYGYI 557
Cdd:cd00174     1 YARALYDYEAQDdDELSFKKGDIITVLEKDD--DGWWEGELNGGREGLF 47
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 20-325 1.27e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.37  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  20 PTEEVSTSSRPFKVAGQNSpsgiQSKKNLFDNQGNASPPAG--PSNMSKFGTTKPPLAAKptyeeksekEPKPPFLKPTG 97
Cdd:PTZ00449  510 PPEGPEASGLPPKAPGDKE----GEEGEHEDSKESDEPKEGgkPGETKEGEVGKKPGPAK---------EHKPSKIPTLS 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  98 VSPRFGTQPNSvSRDPEVKVGFLKPVSPKPTSLTKEDSKPVILRPPGNKLHNLNQESDLKTLGPKPGSTPPVPENDLKPG 177
Cdd:PTZ00449  577 KKPEFPKDPKH-PKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIK 655

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991 178 FSKIAGA---------KSKFMPAPQDADSKPRFPRHTYGQKPSLSTEDAQEEESIPkNTPVQKGSPV-QLGAKSRGSPFK 247
Cdd:PTZ00449  656 SPKPPKSpkppfdpkfKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETP-GTPFTTPRPLpPKLPRDEEFPFE 734

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958751991 248 PAKEdpEDKDHGTPSSPFAGVVLKPAASRGSPGLSKNSEEKKEERKTDipkNIFLNKLNQEEPARFPKAPSKLTAGTP 325
Cdd:PTZ00449  735 PIGD--PDAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEE---DIHAETGEPDEAMKRPDSPSEHEDKPP 807
SH3_Nck_3 cd11767
Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain ...
 523-564 4.84e-03

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: 36.14  E-value: 4.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958751991 523 ELSFKQGEDIEIIRITDNPEGKWLGRTARGSYGYIKTTAVKI 564
Cdd:cd11767    15 ELSFEKGERLEIIEKPEDDPDWWKARNALGTTGLVPRNYVEV 56
PHA03378 PHA03378
EBNA-3B; Provisional
 20-275 7.20e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.05  E-value: 7.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  20 PTEEVSTSSRPFKVAGQNSPSGIQSKKNLFDNQGNASPPAGPSNMSKFG--TTKPPLAAKPTYeeksekepKPPFLKPTG 97
Cdd:PHA03378  632 PMRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGanTMLPIQWAPGTM--------QPPPRAPTP 703

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991  98 VSPRFGtqPNSVSRDPEVKVGFLKPVSPKPTSLTKEDSKPVILRPPGNKLHNLNQESDLKTLGPKPGSTPPVPENDLKPG 177
Cdd:PHA03378  704 MRPPAA--PPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQ 781

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751991 178 FSKIAGAKSKFMPAPQDADSKPRFPRHTYGQKPSLSTEDAQEEESIPKNTPVQKGSPvQLGAKSRGSPFKPAKEDPeDKD 257
Cdd:PHA03378  782 APPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRP-SLKKPAALERQAAAGPTP-SPG 859

                         250
                  ....*....|....*...
gi 1958751991 258 HGTPSSPFAGVVLKPAAS 275
Cdd:PHA03378  860 SGTSDKIVQAPVFYPPVL 877
 
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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