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Conserved domains on  [gi|340545556|ref|NP_001230022|]
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FYN-binding protein 1 isoform 3 [Homo sapiens]

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

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 ...
 751-839 3.67e-52

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: 176.33  E-value: 3.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  751 FRKKFKYDGEIRVLYSTKVTTSITSKKWGTRDLQVKPGESLEVIQTTDDTKVLCRNEEGKYGYVLRSYLADNDGEIYDDI 830
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMTVDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLLQNDGEIYDDI 80


                  ....*....
gi 340545556  831 ADGCIYDND 839
Cdd:pfam14603  81 GDDCIYDND 89
hSH3 super family cl48258
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 518-614 7.73e-08

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: 50.76  E-value: 7.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  518 GPIQVIH---LAKACCDVKGGKNELSFKQGEQIEIIRITDnpEGKWLGRTARGSYGYIKTTAVeidydslklkkdslgap 594
Cdd:pfam14603   9 GEIKVLYsmtVDPNLTIKKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLRSNL----------------- 69

                          90       100
                  ....*....|....*....|
gi 340545556  595 srpIEDDQEVYDDVAEqDDI 614
Cdd:pfam14603  70 ---LQNDGEIYDDIGD-DCI 85
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 50-437 3.05e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556   50 NNQGNASPPAGPSNVPkfgsPKPPVAVKPsseekPDKEPKPPFLKPTGAGQRFGTPA-SLTTRDPEAKVGflKPVGPKPI 128
Cdd:PHA03247 2546 DDAGDPPPPLPPAAPP----AAPDRSVPP-----PRPAPRPSEPAVTSRARRPDAPPqSARPRAPVDDRG--DPRGPAPP 2614

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  129 NLPKEDSKPTFPWPPGNKPSLHSVNQDHDL---KPLGPKSGPTPPtseneqKQAFPKLTGVKGKFMSASQDLE-PKPLFP 204
Cdd:PHA03247 2615 SPLPPDTHAPDPPPPSPSPAANEPDPHPPPtvpPPERPRDDPAPG------RVSRPRRARRLGRAAQASSPPQrPRRRAA 2688

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  205 KPAFGQKPPLSTENSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSENKDHAGEISSLPFPGVVLKPAASRGGPG 284
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  285 LSKNGEEKKEDRKIDAAKNTFQSKINQEELASGTPPARFPKAPSKLTVGGPWGQSQEKEKGDKNSATPKQKPLPPLFTLG 364
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 340545556  365 PPPPKPNRPPNVDLTKFHKTSSGNSTSKGQTSYSTTSLPPPPPSHPASQPPLPASHPSQPPVPSLPPRNIKPP 437
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP 2921
 
Name Accession Description Interval E-value
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 751-839 3.67e-52

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: 176.33  E-value: 3.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  751 FRKKFKYDGEIRVLYSTKVTTSITSKKWGTRDLQVKPGESLEVIQTTDDTKVLCRNEEGKYGYVLRSYLADNDGEIYDDI 830
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMTVDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLLQNDGEIYDDI 80


                  ....*....
gi 340545556  831 ADGCIYDND 839
Cdd:pfam14603  81 GDDCIYDND 89
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 751-821 2.76e-38

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: 136.88  E-value: 2.76e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340545556 751 FRKKFKYDGEIRVLYSTKVTTSITSKKWGTRDLQVKPGESLEVIQTTDDTKVLCRNEEGKYGYVLRSYLAD 821
Cdd:cd11867    7 FRKKFKYNGEIKVLYSTTVLQTLTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 518-614 7.73e-08

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: 50.76  E-value: 7.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  518 GPIQVIH---LAKACCDVKGGKNELSFKQGEQIEIIRITDnpEGKWLGRTARGSYGYIKTTAVeidydslklkkdslgap 594
Cdd:pfam14603   9 GEIKVLYsmtVDPNLTIKKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLRSNL----------------- 69

                          90       100
                  ....*....|....*....|
gi 340545556  595 srpIEDDQEVYDDVAEqDDI 614
Cdd:pfam14603  70 ---LQNDGEIYDDIGD-DCI 85
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 522-578 9.89e-07

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: 46.38  E-value: 9.89e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 340545556   522 VIHLAKACCDVKG-GKNELSFKQGEQIEIIRITDnpEGKWLGRTARGSYGYIKTTAVE 578
Cdd:smart00326   1 EGPQVRALYDYTAqDPDELSFKKGDIITVLEKSD--DGWWKGRLGRGKEGLFPSNYVE 56
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
 537-579 2.51e-04

Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. 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: 212753 [Multi-domain]  Cd Length: 54  Bit Score: 39.60  E-value: 2.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 340545556 537 NELSFKQGEQIEIIRITDnpEGKWLGRTARGSYGYIKTTAVEI 579
Cdd:cd11819   14 NEISFVEGDIITQIEQID--EGWWLGVNAKGQKGLFPANYVEL 54
PHA03247 PHA03247
large tegument protein UL36; Provisional
 50-437 3.05e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556   50 NNQGNASPPAGPSNVPkfgsPKPPVAVKPsseekPDKEPKPPFLKPTGAGQRFGTPA-SLTTRDPEAKVGflKPVGPKPI 128
Cdd:PHA03247 2546 DDAGDPPPPLPPAAPP----AAPDRSVPP-----PRPAPRPSEPAVTSRARRPDAPPqSARPRAPVDDRG--DPRGPAPP 2614

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  129 NLPKEDSKPTFPWPPGNKPSLHSVNQDHDL---KPLGPKSGPTPPtseneqKQAFPKLTGVKGKFMSASQDLE-PKPLFP 204
Cdd:PHA03247 2615 SPLPPDTHAPDPPPPSPSPAANEPDPHPPPtvpPPERPRDDPAPG------RVSRPRRARRLGRAAQASSPPQrPRRRAA 2688

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  205 KPAFGQKPPLSTENSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSENKDHAGEISSLPFPGVVLKPAASRGGPG 284
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  285 LSKNGEEKKEDRKIDAAKNTFQSKINQEELASGTPPARFPKAPSKLTVGGPWGQSQEKEKGDKNSATPKQKPLPPLFTLG 364
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 340545556  365 PPPPKPNRPPNVDLTKFHKTSSGNSTSKGQTSYSTTSLPPPPPSHPASQPPLPASHPSQPPVPSLPPRNIKPP 437
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP 2921
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 68-259 9.34e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 39.37  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  68 GSPKPPVAVKPSSEEKPDKEPKPPFLKPTGAGQRFGTPASLTTRDPEAKVgflKPVGPKPINLPK-EDSKPTFPWPPGN- 145
Cdd:NF033839 307 KKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKP---QPEKPKPEVKPQpEKPKPEVKPQPETp 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556 146 ----KPSLHSVNQDHDLKPLGPKS--GPTPPTSENEQKQAFPKLT-GVKGKFMSASQDLEPKPLFPKPAFGQKPPL-STE 217
Cdd:NF033839 384 kpevKPQPEKPKPEVKPQPEKPKPevKPQPEKPKPEVKPQPEKPKpEVKPQPEKPKPEVKPQPEKPKPEVKPQPETpKPE 463

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 340545556 218 NSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSENKD 259
Cdd:NF033839 464 VKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSKD 505
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 25-270 9.97e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.75  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556   25 SVNSRPFRVTGPNSSSGIQARKNLFNNQGNASPPAGPSNVPKFGSPKPPVAVKPSSEEKPDKEPKP------PFLKPTGA 98
Cdd:pfam03154 281 SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPpaplsmPHIKPPPT 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556   99 GQRFGTPASLTTRDPEakvgflKPVGPKPINLPKedskpTFPWPPGNKPsLHSVNQDHDLKP------LGPKSGPTPPTS 172
Cdd:pfam03154 361 TPIPQLPNPQSHKHPP------HLSGPSPFQMNS-----NLPPPPALKP-LSSLSTHHPPSAhppplqLMPQSQQLPPPP 428

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  173 EN----EQKQAFPKlTGVKGKFMSASQDLEPKPLFPKPAFGQK----------PPLSTENSHEDESPMKNVSSSKGSPAP 238
Cdd:pfam03154 429 AQppvlTQSQSLPP-PAASHPPTSGLHQVPSQSPFPQHPFVPGgpppitppsgPPTSTSSAMPGIQPPSSASVSSSGPVP 507

                         250       260       270
                  ....*....|....*....|....*....|..
gi 340545556  239 LGVrskSGPLKPAREDSENKDHAGEISSLPFP 270
Cdd:pfam03154 508 AAV---SCPLPPVQIKEEALDEAEEPESPPPP 536
 
Name Accession Description Interval E-value
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 751-839 3.67e-52

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: 176.33  E-value: 3.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  751 FRKKFKYDGEIRVLYSTKVTTSITSKKWGTRDLQVKPGESLEVIQTTDDTKVLCRNEEGKYGYVLRSYLADNDGEIYDDI 830
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMTVDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLLQNDGEIYDDI 80


                  ....*....
gi 340545556  831 ADGCIYDND 839
Cdd:pfam14603  81 GDDCIYDND 89
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 751-821 2.76e-38

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: 136.88  E-value: 2.76e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340545556 751 FRKKFKYDGEIRVLYSTKVTTSITSKKWGTRDLQVKPGESLEVIQTTDDTKVLCRNEEGKYGYVLRSYLAD 821
Cdd:cd11867    7 FRKKFKYNGEIKVLYSTTVLQTLTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
 518-614 7.73e-08

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: 50.76  E-value: 7.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  518 GPIQVIH---LAKACCDVKGGKNELSFKQGEQIEIIRITDnpEGKWLGRTARGSYGYIKTTAVeidydslklkkdslgap 594
Cdd:pfam14603   9 GEIKVLYsmtVDPNLTIKKWGGKDLPVKPGEVLDVIQKTD--DTKVLCRNEEGKYGYVLRSNL----------------- 69

                          90       100
                  ....*....|....*....|
gi 340545556  595 srpIEDDQEVYDDVAEqDDI 614
Cdd:pfam14603  70 ---LQNDGEIYDDIGD-DCI 85
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 522-578 9.89e-07

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: 46.38  E-value: 9.89e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 340545556   522 VIHLAKACCDVKG-GKNELSFKQGEQIEIIRITDnpEGKWLGRTARGSYGYIKTTAVE 578
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 ...
 526-580 3.86e-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: 3.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 340545556  526 AKACCDVKG-GKNELSFKQGEQIEIIRiTDNPEGkWLGRTaRGSYGYIKTTAVEID 580
Cdd:pfam07653   2 GRVIFDYVGtDKNGLTLKKGDVVKVLG-KDNDGW-WEGET-GGRVGLVPSTAVEEI 54
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
 537-579 2.51e-04

Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. 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: 212753 [Multi-domain]  Cd Length: 54  Bit Score: 39.60  E-value: 2.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 340545556 537 NELSFKQGEQIEIIRITDnpEGKWLGRTARGSYGYIKTTAVEI 579
Cdd:cd11819   14 NEISFVEGDIITQIEQID--EGWWLGVNAKGQKGLFPANYVEL 54
PHA03247 PHA03247
large tegument protein UL36; Provisional
 50-437 3.05e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556   50 NNQGNASPPAGPSNVPkfgsPKPPVAVKPsseekPDKEPKPPFLKPTGAGQRFGTPA-SLTTRDPEAKVGflKPVGPKPI 128
Cdd:PHA03247 2546 DDAGDPPPPLPPAAPP----AAPDRSVPP-----PRPAPRPSEPAVTSRARRPDAPPqSARPRAPVDDRG--DPRGPAPP 2614

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  129 NLPKEDSKPTFPWPPGNKPSLHSVNQDHDL---KPLGPKSGPTPPtseneqKQAFPKLTGVKGKFMSASQDLE-PKPLFP 204
Cdd:PHA03247 2615 SPLPPDTHAPDPPPPSPSPAANEPDPHPPPtvpPPERPRDDPAPG------RVSRPRRARRLGRAAQASSPPQrPRRRAA 2688

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  205 KPAFGQKPPLSTENSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSENKDHAGEISSLPFPGVVLKPAASRGGPG 284
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  285 LSKNGEEKKEDRKIDAAKNTFQSKINQEELASGTPPARFPKAPSKLTVGGPWGQSQEKEKGDKNSATPKQKPLPPLFTLG 364
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 340545556  365 PPPPKPNRPPNVDLTKFHKTSSGNSTSKGQTSYSTTSLPPPPPSHPASQPPLPASHPSQPPVPSLPPRNIKPP 437
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP 2921
PHA03247 PHA03247
large tegument protein UL36; Provisional
 20-437 3.53e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556   20 PTEDVSV-NSRPF-RVTGPNSSSGiQARKNLFNNQGNASPPAGPSNVPKFGSPKPPVAVKPSSEEKPDKEPKPPFLKPTG 97
Cdd:PHA03247 2562 AAPDRSVpPPRPApRPSEPAVTSR-ARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDP 2640

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556   98 AGQRFGTPASLTTRDPEAKVGFLKPVGPKPINLPKEDSKPTFPWPPGNKPSLHSVNQDHDLKPLGPKSGPTPPTSENeqk 177
Cdd:PHA03247 2641 HPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVS--- 2717

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  178 qAFPKLTGVKgkfmSASQDLEPKPLFPKPafgqKPPLSTENSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSEN 257
Cdd:PHA03247 2718 -ATPLPPGPA----AARQASPALPAAPAP----PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  258 KDHAGEISSLPFPGVVLKPAASRGGPGLSKNGEEkkedrkidAAKNTFQSKINQEELASGTPPARFPkapSKLTVGG--- 334
Cdd:PHA03247 2789 ASLSESRESLPSPWDPADPPAAVLAPAAALPPAA--------SPAGPLPPPTSAQPTAPPPPPGPPP---PSLPLGGsva 2857

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  335 PWGQSQEKEKGDKNSATPKQKPLPPLFTLgppppkpnrppnvdltkfhktssgnstSKGQTSYSTTSLPPPPPSHPASQP 414
Cdd:PHA03247 2858 PGGDVRRRPPSRSPAAKPAAPARPPVRRL---------------------------ARPAVSRSTESFALPPDQPERPPQ 2910

                         410       420
                  ....*....|....*....|...
gi 340545556  415 PLPASHPSQPPVPSLPPRNIKPP 437
Cdd:PHA03247 2911 PQAPPPPQPQPQPPPPPQPQPPP 2933
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 526-572 5.30e-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: 38.60  E-value: 5.30e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 340545556 526 AKACCDVKGGK-NELSFKQGEQIEIIRITDnpEGKWLGRTARGSYGYI 572
Cdd:cd00174    2 ARALYDYEAQDdDELSFKKGDIITVLEKDD--DGWWEGELNGGREGLF 47
SH3_Nck_3 cd11767
Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain ...
 538-579 9.13e-04

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: 38.06  E-value: 9.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 340545556 538 ELSFKQGEQIEIIRITDNPEGKWLGRTARGSYGYIKTTAVEI 579
Cdd:cd11767   15 ELSFEKGERLEIIEKPEDDPDWWKARNALGTTGLVPRNYVEV 56
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 28-254 1.34e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.37  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  28 SRPFRVTGPNSSSGIQARKNLFNNQGNASPPAGPSNVpKFGSPKPPVAVKPSSEEKPDKEPKPPFlKPTGAGQRFGTPAS 107
Cdd:PTZ00449 604 QRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQ-RPSSPERPEGPKIIKSPKPPKSPKPPF-DPKFKEKFYDDYLD 681

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556 108 LTTRDPEAKV---------GFLKPVGPKPINLPKEDSKPTFPWPPGNKPSLHSVNQDHDLKPLGPKSGPTPPTSENeqkq 178
Cdd:PTZ00449 682 AAAKSKETKTtvvldesfeSILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEER---- 757

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 340545556 179 afpkltgvkgKFMSASQDLEPKPLFPKPAFgQKPPLSTENSHEDESPMKNVSSSKGSPAPLGVRSkSGPLKPARED 254
Cdd:PTZ00449 758 ----------TFFHETPADTPLPDILAEEF-KEEDIHAETGEPDEAMKRPDSPSEHEDKPPGDHP-SLPKKRHRLD 821
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
 536-579 3.75e-03

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: 36.15  E-value: 3.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 340545556 536 KNELSFKQGEQIEIIRITDNpEGKWLGRTARGSYGYIKTTAVEI 579
Cdd:cd11763   13 SGELSLRAGEVLTITRQDVG-DGWLEGRNSRGEVGLFPSSYVEI 55
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
 517-578 5.94e-03

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: 36.35  E-value: 5.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 340545556 517 TGPIQVIHLAKACCDV---KGGKNELSFKQGEQIEIIRITDnpEGKWLGRTARGSYGYIKTTAVE 578
Cdd:cd11867   14 NGEIKVLYSTTVLQTLtikKFGSKDLQVKPGESLEVIQHTD--DTKVLCRNEEGKYGYVLRSNLE 76
SH3_Pex13p_fungal cd11771
Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the ...
 536-579 6.09e-03

Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the peroxisomal membrane, contains two transmembrane regions and a C-terminal SH3 domain. It binds to the peroxisomal targeting type I (PTS1) receptor Pex5p and the docking factor Pex14p through its SH3 domain. It is essential for both PTS1 and PTS2 protein import pathways into the peroxisomal matrix. Pex13p binds Pex14p, which contains a PxxP motif, in a classical fashion to the proline-rich ligand binding site of its SH3 domain. It binds the WxxxF/Y motif of Pex5p in a novel site that does not compete with Pex14p binding. 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: 212705 [Multi-domain]  Cd Length: 60  Bit Score: 35.71  E-value: 6.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 340545556 536 KNELSFKQGEQIEIIRITD---NPEGKWLGRTARGSYGYIKTTAVEI 579
Cdd:cd11771   14 EMELSLKKGDIVAVLSKTDplgRDSEWWKGRTRDGRIGWFPSNYVEV 60
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 537-572 6.68e-03

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: 35.26  E-value: 6.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 340545556  537 NELSFKQGEQIEIIRitDNPEGKWLGRTARGSYGYI 572
Cdd:pfam00018  12 DELSFKKGDIIIVLE--KSEDGWWKGRNKGGKEGLI 45
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 104-443 6.99e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  104 TPASLTTRDPEAKVGFLKPVGPKPINLPKEdSKPTFPWPPGNKPSLHSvnqDHDLKPLGPKSGPTPPTSENEQKQAFPKL 183
Cdd:PHA03307   54 TVVAGAAACDRFEPPTGPPPGPGTEAPANE-SRSTPTWSLSTLAPASP---AREGSPTPPGPSSPDPPPPTPPPASPPPS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  184 TGvkgkfmSASQDLEPKPLFPKPAFGQKPPLSTENSHEDESPMKNvSSSKGSPAPLGVRSKSGPLKPAREDSENKDHAGE 263
Cdd:PHA03307  130 PA------PDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAAS-SRQAALPLSSPEETARAPSSPPAEPPPSTPPAAA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  264 ISSLPFPGVVLKPAASRGGPGLSKNGEEKKEDRKIDAAKNTFQSKINQEELASGTPPARFPKAPSKLTVGGPWGqSQEKE 343
Cdd:PHA03307  203 SPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN-GPSSR 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  344 KGDKNSATPKQKPLPPlftlgpPPPKPNRPPNVDLTKFHKTSSGNSTSKGQTSYSTTSLPPPPpshpasqpplPASHPSQ 423
Cdd:PHA03307  282 PGPASSSSSPRERSPS------PSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRG----------AAVSPGP 345

                         330       340
                  ....*....|....*....|
gi 340545556  424 PPVPSLPPRNIKPPFDLKSP 443
Cdd:PHA03307  346 SPSRSPSPSRPPPPADPSSP 365
SH3_Nephrocystin cd11770
Src Homology 3 domain of Nephrocystin (or Nephrocystin-1); Nephrocystin contains an SH3 domain ...
 782-819 9.15e-03

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: 34.98  E-value: 9.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 340545556 782 DLQVKPGESLEVIQTTDDTKVLCRNEEGKYGYVLRSYL 819
Cdd:cd11770   15 DLSFKKGEVLRIISKRADGWWLAENSKGNRGLVPKTYL 52
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 68-259 9.34e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 39.37  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  68 GSPKPPVAVKPSSEEKPDKEPKPPFLKPTGAGQRFGTPASLTTRDPEAKVgflKPVGPKPINLPK-EDSKPTFPWPPGN- 145
Cdd:NF033839 307 KKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKP---QPEKPKPEVKPQpEKPKPEVKPQPETp 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556 146 ----KPSLHSVNQDHDLKPLGPKS--GPTPPTSENEQKQAFPKLT-GVKGKFMSASQDLEPKPLFPKPAFGQKPPL-STE 217
Cdd:NF033839 384 kpevKPQPEKPKPEVKPQPEKPKPevKPQPEKPKPEVKPQPEKPKpEVKPQPEKPKPEVKPQPEKPKPEVKPQPETpKPE 463

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 340545556 218 NSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSENKD 259
Cdd:NF033839 464 VKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSKD 505
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 25-270 9.97e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.75  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556   25 SVNSRPFRVTGPNSSSGIQARKNLFNNQGNASPPAGPSNVPKFGSPKPPVAVKPSSEEKPDKEPKP------PFLKPTGA 98
Cdd:pfam03154 281 SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPpaplsmPHIKPPPT 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556   99 GQRFGTPASLTTRDPEakvgflKPVGPKPINLPKedskpTFPWPPGNKPsLHSVNQDHDLKP------LGPKSGPTPPTS 172
Cdd:pfam03154 361 TPIPQLPNPQSHKHPP------HLSGPSPFQMNS-----NLPPPPALKP-LSSLSTHHPPSAhppplqLMPQSQQLPPPP 428

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340545556  173 EN----EQKQAFPKlTGVKGKFMSASQDLEPKPLFPKPAFGQK----------PPLSTENSHEDESPMKNVSSSKGSPAP 238
Cdd:pfam03154 429 AQppvlTQSQSLPP-PAASHPPTSGLHQVPSQSPFPQHPFVPGgpppitppsgPPTSTSSAMPGIQPPSSASVSSSGPVP 507

                         250       260       270
                  ....*....|....*....|....*....|..
gi 340545556  239 LGVrskSGPLKPAREDSENKDHAGEISSLPFP 270
Cdd:pfam03154 508 AAV---SCPLPPVQIKEEALDEAEEPESPPPP 536
 
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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