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Conserved domains on  [gi|388453673|ref|NP_001253035|]
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amyloid-beta A4 precursor protein-binding family B member 3 [Macaca mulatta]

Protein Classification

Fe65 family protein( domain architecture ID 10648645)

Fe65 family protein contains WW and PTB (phosphotyrosine-binding) domains, similar to human protein protein Fe65-like 2, also called amyloid-beta A4 precursor protein-binding family B member 3, that may modulate the internalization of amyloid-beta precursor protein

Gene Ontology:  GO:0005515|GO:0001540
PubMed:  15567406|8987385|10610414|11812645

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 116-261 8.76e-84

Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


:

Pssm-ID: 269970  Cd Length: 138  Bit Score: 254.92  E-value: 8.76e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673 116 AKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRSRSQPLDGAWGEGQNMLMILKKDAMSLVNPLDHSLIHCQPL 195
Cdd:cd01272    1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 388453673 196 VHIRVWGVGSSKGrdspisapaRDFAFVASDKDSCMLKCHVFRCDVPAKVIASALHGLCAQILSER 261
Cdd:cd01272   81 HSIRVWGVGRDNG---------RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 290-420 1.49e-63

Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The C-terminal PTB domain is responsible for APP binding. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


:

Pssm-ID: 269969  Cd Length: 127  Bit Score: 202.45  E-value: 1.49e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673 290 AVSQAAQKYEALYMGTLPVTKAMGMDVLNEAIGTLTTRGDRNAWVPTMLSVSDSLMTAHPIQAEasteEEPLWQCPVRLV 369
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 388453673 370 TFIGVGRDPHTFGLIADLGRQSFQCAAFWCQPHAGGLSEAVQAACMVQYQK 420
Cdd:cd01271   77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 30-61 1.10e-07

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


:

Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 47.98  E-value: 1.10e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 388453673    30 GLPPGWRKIHDAAG-TYYWHVPSGSTQWQRPAW 61
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKPRE 33
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 116-261 8.76e-84

Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269970  Cd Length: 138  Bit Score: 254.92  E-value: 8.76e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673 116 AKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRSRSQPLDGAWGEGQNMLMILKKDAMSLVNPLDHSLIHCQPL 195
Cdd:cd01272    1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 388453673 196 VHIRVWGVGSSKGrdspisapaRDFAFVASDKDSCMLKCHVFRCDVPAKVIASALHGLCAQILSER 261
Cdd:cd01272   81 HSIRVWGVGRDNG---------RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 290-420 1.49e-63

Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The C-terminal PTB domain is responsible for APP binding. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269969  Cd Length: 127  Bit Score: 202.45  E-value: 1.49e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673 290 AVSQAAQKYEALYMGTLPVTKAMGMDVLNEAIGTLTTRGDRNAWVPTMLSVSDSLMTAHPIQAEasteEEPLWQCPVRLV 369
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 388453673 370 TFIGVGRDPHTFGLIADLGRQSFQCAAFWCQPHAGGLSEAVQAACMVQYQK 420
Cdd:cd01271   77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
119-257 3.28e-45

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 154.44  E-value: 3.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673  119 FAVRSLGWVEVPEEdLAPGKS--SIAVNNCIQQL-AQTRSRSQPLDGAWGEGQNMLMILKKDAMSLVNPLDHSLIHCQPL 195
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVkAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388453673  196 VHIRVWGVGSSKGrdspisapARDFAFVASDKDSCMLKCHVFRCDVPAKVIASALHGLCAQI 257
Cdd:pfam00640  80 VSISFCADGDPDL--------MRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 114-261 7.16e-30

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 113.56  E-value: 7.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673   114 PGAKCFAVRSLGWVEVPEEDlapgkSSIAVNNCIQQLAQTRSrsqpldGAWGEGQNMLMILKKDAMSLVNPLDHSLIHCQ 193
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAAQG------SEKKEPQKVILSISSRGVKLIDEDTKAVLHEH 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388453673   194 PLVHIRVWGVGSSkgrdspisaPARDFAFVASDKDSCMLKCHVFRCDVPAKVIASALHGLCAQILSER 261
Cdd:smart00462  70 PLRRISFCAVGPD---------DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELK 128
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 293-425 4.66e-28

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 108.56  E-value: 4.66e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673   293 QAAQKYEALYMGTLPVTKAMGMDVLNEAIGTL--TTRGDRNAWVPTMLSVSDSLMTAHPIQAEAsteeePLWQCPVRLVT 370
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-----VLHEHPLRRIS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 388453673   371 FIGVGR-DPHTFGLIA-DLGRQSFQCAAFWCQPHAGGLSEAVQAACMVQYQKCLVAS 425
Cdd:smart00462  76 FCAVGPdDLDVFGYIArDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 30-61 1.10e-07

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 47.98  E-value: 1.10e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 388453673    30 GLPPGWRKIHDAAG-TYYWHVPSGSTQWQRPAW 61
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 31-59 2.67e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 46.73  E-value: 2.67e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 388453673   31 LPPGWRKIHDAAG-TYYWHVPSGSTQWQRP 59
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 32-61 1.73e-06

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 44.44  E-value: 1.73e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 388453673  32 PPGWRKIHDAAG-TYYWHVPSGSTQWQRPAW 61
Cdd:cd00201    1 PPGWEERWDPDGrVYYYNHNTKETQWEDPRE 31
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 116-261 8.76e-84

Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269970  Cd Length: 138  Bit Score: 254.92  E-value: 8.76e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673 116 AKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRSRSQPLDGAWGEGQNMLMILKKDAMSLVNPLDHSLIHCQPL 195
Cdd:cd01272    1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 388453673 196 VHIRVWGVGSSKGrdspisapaRDFAFVASDKDSCMLKCHVFRCDVPAKVIASALHGLCAQILSER 261
Cdd:cd01272   81 HSIRVWGVGRDNG---------RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 290-420 1.49e-63

Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The C-terminal PTB domain is responsible for APP binding. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269969  Cd Length: 127  Bit Score: 202.45  E-value: 1.49e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673 290 AVSQAAQKYEALYMGTLPVTKAMGMDVLNEAIGTLTTRGDRNAWVPTMLSVSDSLMTAHPIQAEasteEEPLWQCPVRLV 369
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 388453673 370 TFIGVGRDPHTFGLIADLGRQSFQCAAFWCQPHAGGLSEAVQAACMVQYQK 420
Cdd:cd01271   77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
119-257 3.28e-45

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 154.44  E-value: 3.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673  119 FAVRSLGWVEVPEEdLAPGKS--SIAVNNCIQQL-AQTRSRSQPLDGAWGEGQNMLMILKKDAMSLVNPLDHSLIHCQPL 195
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVkAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388453673  196 VHIRVWGVGSSKGrdspisapARDFAFVASDKDSCMLKCHVFRCDVPAKVIASALHGLCAQI 257
Cdd:pfam00640  80 VSISFCADGDPDL--------MRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 114-261 7.16e-30

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 113.56  E-value: 7.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673   114 PGAKCFAVRSLGWVEVPEEDlapgkSSIAVNNCIQQLAQTRSrsqpldGAWGEGQNMLMILKKDAMSLVNPLDHSLIHCQ 193
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAAQG------SEKKEPQKVILSISSRGVKLIDEDTKAVLHEH 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388453673   194 PLVHIRVWGVGSSkgrdspisaPARDFAFVASDKDSCMLKCHVFRCDVPAKVIASALHGLCAQILSER 261
Cdd:smart00462  70 PLRRISFCAVGPD---------DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELK 128
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 293-425 4.66e-28

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 108.56  E-value: 4.66e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673   293 QAAQKYEALYMGTLPVTKAMGMDVLNEAIGTL--TTRGDRNAWVPTMLSVSDSLMTAHPIQAEAsteeePLWQCPVRLVT 370
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-----VLHEHPLRRIS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 388453673   371 FIGVGR-DPHTFGLIA-DLGRQSFQCAAFWCQPHAGGLSEAVQAACMVQYQKCLVAS 425
Cdd:smart00462  76 FCAVGPdDLDVFGYIArDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 118-251 1.07e-11

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 61.76  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673 118 CFAVRSLGWVEVPEEDlapGKSSIAVNNCIQQLAQTRSRSQPldgawgegQNMLMILKKDAMSLVNPLDHSLIHCQPLVH 197
Cdd:cd00934    2 SFQVKYLGSVEVGSSR---GVDVVEEALKALAAALKSSKRKP--------GPVLLEVSSKGVKLLDLDTKELLLRHPLHR 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 388453673 198 IRVWGVGSSKgrdspisapARDFAFVASDKDSCMLKCHVFRCD--VPAKVIASALH 251
Cdd:cd00934   71 ISYCGRDPDN---------PNVFAFIAGEEGGSGFRCHVFQCEdeEEAEEILQAIG 117
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 30-61 1.10e-07

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 47.98  E-value: 1.10e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 388453673    30 GLPPGWRKIHDAAG-TYYWHVPSGSTQWQRPAW 61
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 31-59 2.67e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 46.73  E-value: 2.67e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 388453673   31 LPPGWRKIHDAAG-TYYWHVPSGSTQWQRP 59
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 32-61 1.73e-06

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 44.44  E-value: 1.73e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 388453673  32 PPGWRKIHDAAG-TYYWHVPSGSTQWQRPAW 61
Cdd:cd00201    1 PPGWEERWDPDGrVYYYNHNTKETQWEDPRE 31
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 296-414 2.92e-04

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 40.57  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673 296 QKYEALYMGTLPVTKAMGMDVLNEAI-GTLTTRGDRNAWVPTM-LSVSDSLMTAHpiqaEASTeEEPLWQCPVRLVTFIG 373
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALkALAAALKSSKRKPGPVlLEVSSKGVKLL----DLDT-KELLLRHPLHRISYCG 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 388453673 374 VGRD-PHTFGLIA-DLGRQSFQCAAFWCQP--HAGGLSEAVQAAC 414
Cdd:cd00934   76 RDPDnPNVFAFIAgEEGGSGFRCHVFQCEDeeEAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 298-413 2.95e-04

Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269983  Cd Length: 120  Bit Score: 40.69  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673 298 YEALYMGTLPVTKAMGMDVLNEAIGTLTTRGdrNAWVPTMLSVSDSLMTAhpiqAEASTeEEPLWQCPVRLVTFIGV-GR 376
Cdd:cd13161    4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDLK--LKPKPVVLVVSSEGIRV----VERLT-GEVLTNVPIKDISFVTVdPK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 388453673 377 DPHTFGLIA---DLGRQSfqCAAFWCQPHAGGLSEAVQAA 413
Cdd:cd13161   77 DKKLFAFIShdpRLGRIT--CHVFRCKRGAQEICDTIAEA 114
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 220-242 4.23e-03

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269922  Cd Length: 129  Bit Score: 37.23  E-value: 4.23e-03
                         10        20
                 ....*....|....*....|...
gi 388453673 220 FAFVASDKDSCMLKCHVFRCDVP 242
Cdd:cd01211   87 FAFTWSHGETAIFQCHVFRCEIP 109
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 118-249 6.33e-03

Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269983  Cd Length: 120  Bit Score: 36.84  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453673 118 CFAVRSLGWVEVPEedlapGKSSIAVNNCIQQLaqtrsRSQPLDGawgegQNMLMILKKDAMSLVNPLDHSLIHCQPLVH 197
Cdd:cd13161    3 VFEAKYLGSVPVKE-----PKGNDVVMAAVKRL-----KDLKLKP-----KPVVLVVSSEGIRVVERLTGEVLTNVPIKD 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 388453673 198 IRVWGVGsskGRDSPIsapardFAFVASDKDSCMLKCHVFRCDVPAKVIASA 249
Cdd:cd13161   68 ISFVTVD---PKDKKL------FAFISHDPRLGRITCHVFRCKRGAQEICDT 110
 
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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