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Conserved domains on  [gi|564326908|ref|XP_006228627|]
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numb-like protein isoform X1 [Rattus norvegicus]

Protein Classification

numb family protein( domain architecture ID 10101010)

numb family protein similar to protein numb, a membrane associated adaptor protein that is required in determination of cell fate during sensory organ formation in embryos

Gene Ontology:  GO:0050767|GO:0005515

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
91-225 4.20e-101

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF 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: 241298  Cd Length: 135  Bit Score: 303.84  E-value: 4.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  91 HQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEK 170
Cdd:cd01268    1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEK 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564326908 171 VSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLER 225
Cdd:cd01268   81 VSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
314-398 4.23e-39

NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB domain..


:

Pssm-ID: 461874  Cd Length: 95  Bit Score: 138.76  E-value: 4.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  314 AAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLSLRLNELPSTLQRRTDF-----------QVKGTVPEMEPPGTg 382
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPSSE- 79
                          90
                  ....*....|....*.
gi 564326908  383 DSDGISALCTQISSSF 398
Cdd:pfam06311  80 QADSISAMCQQISSGL 95
PHA03247 super family cl33720
large tegument protein UL36; Provisional
286-627 5.52e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  286 PGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGsfRGFPALSQKNSPFKRQLSLRLNEL-----PST 360
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG--RAAQASSPPQRPRRRAARPTVGSLtsladPPP 2703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  361 LQRRTDFQVKGTVPEME-PPGTGDSDGISALCTQISSSFASAGAPV-------PGPPSATTGTSAWGEPSVPAATAfqpg 432
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPlPPGPAAARQASPALPAAPAPPAVPAGPAtpggparPARPPTTAGPPAPAPPAAPAAGP---- 2779
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  433 HKRTPSEAERWLEEvSQVAKAQQQQQQQQQQQQQQQQQQQQQQQQQATSVPPMPTMAPTLQPfsTPVGPFDTAAAQVAVF 512
Cdd:PHA03247 2780 PRRLTRPAVASLSE-SRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP--PPPGPPPPSLPLGGSV 2856
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  513 LP--PTHMQPPFVPAYPGLGYPPMPRVPVVGITPSQMVANAFCSAAQLQPQPATLLGKAGAFPPPTAPSAPGGQARPRPN 590
Cdd:PHA03247 2857 APggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 564326908  591 GapwppepapAPAPELDPFEAQWAALEGKPAVEKPSN 627
Cdd:PHA03247 2937 P---------RPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
 
Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
91-225 4.20e-101

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF 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: 241298  Cd Length: 135  Bit Score: 303.84  E-value: 4.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  91 HQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEK 170
Cdd:cd01268    1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEK 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564326908 171 VSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLER 225
Cdd:cd01268   81 VSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
314-398 4.23e-39

NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB domain..


Pssm-ID: 461874  Cd Length: 95  Bit Score: 138.76  E-value: 4.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  314 AAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLSLRLNELPSTLQRRTDF-----------QVKGTVPEMEPPGTg 382
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPSSE- 79
                          90
                  ....*....|....*.
gi 564326908  383 DSDGISALCTQISSSF 398
Cdd:pfam06311  80 QADSISAMCQQISSGL 95
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
107-222 3.76e-35

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 129.41  E-value: 3.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  107 FPVRYLGHVEVEESR------GMHVCEDAVKKLKAMGRKS-----------VKSVLWVSADGLRVVDDKTKDLLVDQTIE 169
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKINKirglsgetgpgTKVDLFISTDGLKLLNPDTQELIHDHPLV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564326908  170 KVSFCAP-DRNLDKAFSYICRDGTTRRWICHCFLAlKDSGERLSHAVGCAFAAC 222
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNKFACHVFES-EDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
104-232 7.04e-34

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: 125.89  E-value: 7.04e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908   104 TCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVK----SVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRN 179
Cdd:smart00462   3 GVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKepqkVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPD 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564326908   180 LDKAFSYICRDGTTRRWICHCFLALKDSGErLSHAVGCAFAACLERKQRREKE 232
Cdd:smart00462  83 DLDVFGYIARDPGSSRFACHVFRCEKAAED-IALAIGQAFQLAYELKLKARSE 134
PHA03247 PHA03247
large tegument protein UL36; Provisional
286-627 5.52e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  286 PGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGsfRGFPALSQKNSPFKRQLSLRLNEL-----PST 360
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG--RAAQASSPPQRPRRRAARPTVGSLtsladPPP 2703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  361 LQRRTDFQVKGTVPEME-PPGTGDSDGISALCTQISSSFASAGAPV-------PGPPSATTGTSAWGEPSVPAATAfqpg 432
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPlPPGPAAARQASPALPAAPAPPAVPAGPAtpggparPARPPTTAGPPAPAPPAAPAAGP---- 2779
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  433 HKRTPSEAERWLEEvSQVAKAQQQQQQQQQQQQQQQQQQQQQQQQQATSVPPMPTMAPTLQPfsTPVGPFDTAAAQVAVF 512
Cdd:PHA03247 2780 PRRLTRPAVASLSE-SRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP--PPPGPPPPSLPLGGSV 2856
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  513 LP--PTHMQPPFVPAYPGLGYPPMPRVPVVGITPSQMVANAFCSAAQLQPQPATLLGKAGAFPPPTAPSAPGGQARPRPN 590
Cdd:PHA03247 2857 APggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 564326908  591 GapwppepapAPAPELDPFEAQWAALEGKPAVEKPSN 627
Cdd:PHA03247 2937 P---------RPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
 
Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
91-225 4.20e-101

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF 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: 241298  Cd Length: 135  Bit Score: 303.84  E-value: 4.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  91 HQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEK 170
Cdd:cd01268    1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEK 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564326908 171 VSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLER 225
Cdd:cd01268   81 VSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
314-398 4.23e-39

NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB domain..


Pssm-ID: 461874  Cd Length: 95  Bit Score: 138.76  E-value: 4.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  314 AAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLSLRLNELPSTLQRRTDF-----------QVKGTVPEMEPPGTg 382
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPSSE- 79
                          90
                  ....*....|....*.
gi 564326908  383 DSDGISALCTQISSSF 398
Cdd:pfam06311  80 QADSISAMCQQISSGL 95
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
107-222 3.76e-35

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 129.41  E-value: 3.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  107 FPVRYLGHVEVEESR------GMHVCEDAVKKLKAMGRKS-----------VKSVLWVSADGLRVVDDKTKDLLVDQTIE 169
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKINKirglsgetgpgTKVDLFISTDGLKLLNPDTQELIHDHPLV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564326908  170 KVSFCAP-DRNLDKAFSYICRDGTTRRWICHCFLAlKDSGERLSHAVGCAFAAC 222
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNKFACHVFES-EDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
104-232 7.04e-34

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: 125.89  E-value: 7.04e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908   104 TCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVK----SVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRN 179
Cdd:smart00462   3 GVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKepqkVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPD 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564326908   180 LDKAFSYICRDGTTRRWICHCFLALKDSGErLSHAVGCAFAACLERKQRREKE 232
Cdd:smart00462  83 DLDVFGYIARDPGSSRFACHVFRCEKAAED-IALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
105-219 5.18e-26

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: 102.97  E-value: 5.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 105 CSFPVRYLGHVEVEESRGMHVCEDAVKKLKAM----GRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNL 180
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAAlkssKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDN 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564326908 181 DKAFSYICRDGTTRRWICHCFLALKDS-GERLSHAVGCAF 219
Cdd:cd00934   81 PNVFAFIAGEEGGSGFRCHVFQCEDEEeAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
107-224 1.20e-25

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: 101.94  E-value: 1.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 107 FPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNLDKAFSY 186
Cdd:cd13161    4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAF 83
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564326908 187 ICRDGTTRRWICHCFLaLKDSGERLSHAVGCAFAACLE 224
Cdd:cd13161   84 ISHDPRLGRITCHVFR-CKRGAQEICDTIAEAFKAAAE 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
98-219 1.65e-20

Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. 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: 269971  Cd Length: 144  Bit Score: 88.10  E-value: 1.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  98 DAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKL-------KAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEK 170
Cdd:cd01273    5 EALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLkfarqlkKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHR 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 564326908 171 VSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKdSGERLSHAVGCAF 219
Cdd:cd01273   85 ISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEK-LAEEITLTIGQAF 132
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
106-219 2.08e-17

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB 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 contains mammals, insects, and sponges.


Pssm-ID: 269981  Cd Length: 123  Bit Score: 78.53  E-value: 2.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 106 SFPVRYLGHVEVEESRGMHVCEDAVKK----LKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNLD 181
Cdd:cd13159    4 TFYLKYLGSTLVEKPKGEGATAEAVKTiiamAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADANHD 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564326908 182 KAFSYICRDGTTRRWICHCFLALKDS-GERLSHAVGCAF 219
Cdd:cd13159   84 KVFAFIATNQDNEKLECHAFLCAKRKmAQAVTLTVAQAF 122
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
109-188 2.62e-13

Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which binds to the cytoplasmic tails of lipoprotein receptors, such as ApoER2 and VLDLR, via its PTB domain. The dab PTB domain has a preference for unphosphorylated tyrosine within an NPxY motif. Additionally, the Dab PTB domain, which is structurally similar to PH domains, binds to phosphatidlyinositol phosphate 4,5 bisphosphate in a manner characteristic of phosphoinositide binding PH domains. 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: 269926  Cd Length: 147  Bit Score: 67.66  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 109 VRY----LGHVEVEESRGMHVCEDAVKKLK----AMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNL 180
Cdd:cd01215   16 VRFkaklIGIDEVPAARGDKMCQDAMMKLKgavkAAGEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDTTD 95

                 ....*...
gi 564326908 181 DKAFSYIC 188
Cdd:cd01215   96 NRAFGYVC 103
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
92-205 1.51e-12

Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. 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: 269972  Cd Length: 146  Bit Score: 65.38  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  92 QWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKS---VLWVSADGLRVVDDKTKDLLVDQTI 168
Cdd:cd01274    2 QWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIptiILSISYKGVKFIDATTKNLICEHEI 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564326908 169 EKVSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALK 205
Cdd:cd01274   82 RNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLT 118
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
108-229 9.92e-08

Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (pfam00017) domain and a region similar to the tumour suppressor PTEN. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.


Pssm-ID: 429984  Cd Length: 131  Bit Score: 51.19  E-value: 9.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  108 PVRYLGHVEVEESRGMHVCEDAVKKLK---AMGRKSVKSVLW-VSADGLRVVDDKTKDLLVDQTIEKVSFCA---PDRNL 180
Cdd:pfam08416   3 RVEHLTTFELDSLTGLQAVEDAIRKLQlldAQGRVWTQEMLLqVSDQGITLTDNETKEELESYPLDSISHCQavlNDGRY 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 564326908  181 DKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLERKQRR 229
Cdd:pfam08416  83 NSILALVCQEPGQSKPDVHLFQCDELGAELIAEDIESALSDVRLGKPKK 131
PHA03247 PHA03247
large tegument protein UL36; Provisional
286-627 5.52e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  286 PGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGsfRGFPALSQKNSPFKRQLSLRLNEL-----PST 360
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG--RAAQASSPPQRPRRRAARPTVGSLtsladPPP 2703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  361 LQRRTDFQVKGTVPEME-PPGTGDSDGISALCTQISSSFASAGAPV-------PGPPSATTGTSAWGEPSVPAATAfqpg 432
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPlPPGPAAARQASPALPAAPAPPAVPAGPAtpggparPARPPTTAGPPAPAPPAAPAAGP---- 2779
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  433 HKRTPSEAERWLEEvSQVAKAQQQQQQQQQQQQQQQQQQQQQQQQQATSVPPMPTMAPTLQPfsTPVGPFDTAAAQVAVF 512
Cdd:PHA03247 2780 PRRLTRPAVASLSE-SRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP--PPPGPPPPSLPLGGSV 2856
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  513 LP--PTHMQPPFVPAYPGLGYPPMPRVPVVGITPSQMVANAFCSAAQLQPQPATLLGKAGAFPPPTAPSAPGGQARPRPN 590
Cdd:PHA03247 2857 APggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 564326908  591 GapwppepapAPAPELDPFEAQWAALEGKPAVEKPSN 627
Cdd:PHA03247 2937 P---------RPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
106-202 6.25e-05

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB 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 contains insects, ticks, sea urchins, and nematodes.


Pssm-ID: 269982  Cd Length: 125  Bit Score: 43.09  E-value: 6.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 106 SFPVRYLGHVEVEESRGMHVCE----DAVKKLKAmgRKSVKSV-LWVSADGLRVVD-----DKTKDLLVdqTIEKVSFCA 175
Cdd:cd13160    2 VFTVKYLGRMPARGLWGIKHTRkplvDALKNLPK--GKTLPKTkLEVSSDGVKLEElrggfGSSKTVFF--PIHTISYGV 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 564326908 176 PDRNLDKAFSYICR-DGTTRR--WICHCFL 202
Cdd:cd13160   78 QDLVHTRVFSMIVVgEQDSSNhpFECHAFV 107
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
400-616 1.17e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.25  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 400 SAGAPVPGPPSATTGTSAWGEPSVPAATAFQPGHKRTPSEAERWLEEVSQVAKAQQQQQQQQQQQQQQQQQQQQQQQQQA 479
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPA 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 480 TSVPPMPtmAPTLQPFSTPVGPFDTAAAQvavflPPTHMQPPFVPAYPGLGYPPMPRVP--VVGITPSQMVANAFCSAAQ 557
Cdd:PRK12323 452 PAPAAAP--AAAARPAAAGPRPVAAAAAA-----APARAAPAAAPAPADDDPPPWEELPpeFASPAPAQPDAAPAGWVAE 524
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 558 LQPQPATLLGKAGAFPPPTAPSAPGGQARPRPNGAPWPPEPAPAPAPELDP-FEAQWAAL 616
Cdd:PRK12323 525 SIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDmFDGDWPAL 584
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
97-232 1.34e-04

Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) Phosphotyrosine-binding (PTB) domain; CAPON (also known as Nitric oxide synthase 1 adaptor protein, NOS1AP, encodes a cytosolic protein that binds to the signaling molecule, neuronal NOS (nNOS). It contains a N-terminal PTB domain that binds to the small monomeric G protein, Dexras1 and a C-terminal PDZ-binding domain that mediates interactions with nNOS. Included in this cd are C. elegan proteins dystrobrevin, DYB-1, which controls neurotransmitter release and muscle Ca(2+) transients by localizing BK channels and DYstrophin-like phenotype and CAPON related,DYC-1, which is functionally related to dystrophin homolog, DYS-1. Mutations in the dystrophin gene causes Duchenne muscular dystrophy. DYS-1 shares sequence similarity, including key motifs, with their mammalian counterparts. These CAPON-like proteins all have a single PTB 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: 269968  Cd Length: 179  Bit Score: 43.04  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  97 EDAVRKGTCsFPVRYLGHVEVEE--SRGMHVCedAVKKL----KAMGRKSVKSVLWVSADGLRVV-----------DDKT 159
Cdd:cd01270   22 EEAFQHGIT-FQAKYIGSLEVPRpsSRVEIVA--AMRRIryefKAKNIKKKKVTITVSVDGVKVVlrkkkkkkgwtWDES 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564326908 160 KDLLVDQTIEKVSFCAPDRNLDKAFSYICRDGTTRRWICHCFLA-LKDSGERLSHAVGCAFAACLERKQRREKE 232
Cdd:cd01270   99 KLLLMQHPIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSkKKSQAMRIVRTIGQAFEVCHKLSLQHMQG 172
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
106-201 1.45e-04

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: 42.29  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 106 SFPVRYLGHVEVEE--------SRGMHVCedaVKKLkAMGRKSVKSVLWVSADG-----------LRVVDDKTKDLLVDQ 166
Cdd:cd01272    3 RFAVRSLGWVEMAEedltpgksSVAVNNC---IRQL-SYGRNDIRDTVGRWGEGkdmlmvldddtLKLVDPDDRSVLHSQ 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564326908 167 TIEKVSFCAPDRNLDKAFSYICRDGTTRRWICHCF 201
Cdd:cd01272   79 PIHSIRVWGVGRDNGRDFAYVARDKDTRVLKCHVF 113
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
107-218 1.53e-04

Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called DCC-interacting protein (DIP)-13alpha) Phosphotyrosine-binding (PTB) domain; APPL interacts with oncoprotein serine/threonine kinase AKT2, tumor suppressor protein DCC (deleted in colorectal cancer), Rab5, GIPC (GAIP-interacting protein, C terminus), human follicle-stimulating hormone receptor (FSHR), and the adiponectin receptors AdipoR1 and AdipoR2. There are two isoforms of human APPL: APPL1 and APPL2, which share about 50% sequence identity. APPL has a BAR and a PH domain near its N terminus, and the two domains are thought to function as a unit (BAR-PH domain). C-terminal to this is a PTB domain. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. 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.


Pssm-ID: 269980  Cd Length: 135  Bit Score: 41.95  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 107 FPVRYLGHVEVEESRGMHVCEDAVKKLKAmGR------KSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNL 180
Cdd:cd13158   13 FIVRFLGSMEVKSDRTSEVIYEAMRQVLA-ARaihnifRMTESHLLVTSDCLRLIDPQTQVTRARFPLADVVQFAAHQEN 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 564326908 181 DKAFSYICR----DGTTRRWICHCFLAlKDSGERLSHAVGCA 218
Cdd:cd13158   92 KRLFGFVVRtpegDGEEPSFSCYVFES-NTEGEKICDAIALA 132
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
93-201 1.87e-03

Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine kinases, which can interact with phosphoproteins at NPXY motifs. Shc contains an PTB domain followed by an SH2 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 Shc-like subgroup.


Pssm-ID: 269920  Cd Length: 170  Bit Score: 39.50  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908  93 WQADEDAVRKGTCSFPVRYLGHVEVEES-RGM--------------HVCEdAVKKLKAMGRKSVKSVLW----------- 146
Cdd:cd01209    3 WLHPDQLGMGPGVSYPVRYVGCIEVLQSmRSLdfntrtqvtreainRVCE-AVGGAKGAKRKRKSKALSsilgksnlqfa 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564326908 147 -------VSADGLRVVDDKTKDLLVDQTIEKVSFCAP-DRNLDKAFSYICRDGTTRRwICHCF 201
Cdd:cd01209   82 gmnisltISTDGLNLVTPDTGQIIANHHMQSISFASGgDPDTYDYVAYVAKDPVNQR-ACHVL 143
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
482-630 2.24e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 482 VPPMPTMAPTLQPFSTPVGPFDTAAAQVAVFLPPTHMQPPFVPAYPGLGYPPMPRVPVVGITPSQMVAnafcSAAQLQPQ 561
Cdd:PRK12323 390 AAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAA----PAAAARPA 465
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564326908 562 PATLLGKAGAFPPPTAPSAPGGQARPRPNGAPW----PPEPAPAPAPELDPFEAQW-AALEGKPAVEKPSNPFS 630
Cdd:PRK12323 466 AAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPweelPPEFASPAPAQPDAAPAGWvAESIPDPATADPDDAFE 539
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
106-201 3.96e-03

Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal function, muscle regeneration, and cell migration. It binds to actin filaments and interacts with the cytoplasmic tails of beta-integrin via its PTB domain, allowing tensin to link actin filaments to integrin receptors. Tensin functions as a platform for assembly and disassembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules, and also by providing interaction sites for other proteins. In addition to its PTB domain, it contains a C-terminal SH2 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.


Pssm-ID: 269979  Cd Length: 129  Bit Score: 37.75  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326908 106 SFPVRYLGHVEVEESRGMHVCEDAVKKLKAM---GRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNlDK 182
Cdd:cd13157    3 SRNAQYIGSFPVSGLDVADRADSVRKQLESLkesGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPA-HA 81
                         90       100
                 ....*....|....*....|.
gi 564326908 183 AFSYICRD--GTTRRWICHCF 201
Cdd:cd13157   82 QFAFVARNpgGPTNRQYCHVF 102
 
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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