NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568945015|ref|XP_006539678|]
View 

numb-like protein isoform X2 [Mus musculus]

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
PubMed:  15567406|8987385|10610414

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 68-202 1.73e-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: 1.73e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  68 HQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEK 147
Cdd:cd01268    1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568945015 148 VSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLER 202
Cdd:cd01268   81 VSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 291-375 5.66e-40

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: 141.07  E-value: 5.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  291 AAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLSLRLNELPSTLQRRTDF-----------QVKGTVPEMEPPGTg 359
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPSSE- 79

                          90
                  ....*....|....*.
gi 568945015  360 DSDGINALCTQISSSF 375
Cdd:pfam06311  80 QADSISAMCQQISSGL 95
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 263-594 8.60e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 8.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  263 PGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGSfrgfpaLSQKNSPFKRQlslRLNELPSTLQRRT 342
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGR------AAQASSPPQRP---RRRAARPTVGSLT 2696

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  343 DF-QVKGTVPEMEPPGTGDSDGINALCTQISSSFASAGAPAS-GPPPATTGTSAWGEPSVPA-----AAAFQPGHKRTPS 415
Cdd:PHA03247 2697 SLaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAApAPPAVPAGPATPGGPARPArppttAGPPAPAPPAAPA 2776

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  416 EAERWLEEVSQVAKAQQQQQQQQQQQQQQQATSVPPMPTMAPTLQPFSAPVGPFDTAAAQVAVFLPPTHMQPPF------ 489
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsv 2856

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  490 VPAYPGLGYPPMPRVPVVGITPSQMVANAFCSAA---QLQPQPATLLGKAGAFPPPAAPSAPGGQARPRPNGAPWPPEPA 566
Cdd:PHA03247 2857 APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAvsrSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936

                         330       340
                  ....*....|....*....|....*...
gi 568945015  567 PAPAPELDPFEAQWAALEGKPAVEKPSN 594
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
 
Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 68-202 1.73e-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: 1.73e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  68 HQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEK 147
Cdd:cd01268    1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568945015 148 VSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLER 202
Cdd:cd01268   81 VSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 291-375 5.66e-40

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: 141.07  E-value: 5.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  291 AAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLSLRLNELPSTLQRRTDF-----------QVKGTVPEMEPPGTg 359
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPSSE- 79

                          90
                  ....*....|....*.
gi 568945015  360 DSDGINALCTQISSSF 375
Cdd:pfam06311  80 QADSISAMCQQISSGL 95
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
84-199 3.06e-35

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 129.41  E-value: 3.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015   84 FPVRYLGHVEVEESR------GMHVCEDAVKKLKAMGRKS-----------VKSVLWVSADGLRVVDDKTKDLLVDQTIE 146
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKINKirglsgetgpgTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568945015  147 KVSFCAP-DRNLDKAFSYICRDGTTRRWICHCFLAlKDSGERLSHAVGCAFAAC 199
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNKFACHVFES-EDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 81-209 5.86e-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: 5.86e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015    81 TCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVK----SVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRN 156
Cdd:smart00462   3 GVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKepqkVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPD 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568945015   157 LDKAFSYICRDGTTRRWICHCFLALKDSGErLSHAVGCAFAACLERKQRREKE 209
Cdd:smart00462  83 DLDVFGYIARDPGSSRFACHVFRCEKAAED-IALAIGQAFQLAYELKLKARSE 134
PHA03247 PHA03247
large tegument protein UL36; Provisional
 263-594 8.60e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 8.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  263 PGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGSfrgfpaLSQKNSPFKRQlslRLNELPSTLQRRT 342
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGR------AAQASSPPQRP---RRRAARPTVGSLT 2696

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  343 DF-QVKGTVPEMEPPGTGDSDGINALCTQISSSFASAGAPAS-GPPPATTGTSAWGEPSVPA-----AAAFQPGHKRTPS 415
Cdd:PHA03247 2697 SLaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAApAPPAVPAGPATPGGPARPArppttAGPPAPAPPAAPA 2776

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  416 EAERWLEEVSQVAKAQQQQQQQQQQQQQQQATSVPPMPTMAPTLQPFSAPVGPFDTAAAQVAVFLPPTHMQPPF------ 489
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsv 2856

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  490 VPAYPGLGYPPMPRVPVVGITPSQMVANAFCSAA---QLQPQPATLLGKAGAFPPPAAPSAPGGQARPRPNGAPWPPEPA 566
Cdd:PHA03247 2857 APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAvsrSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936

                         330       340
                  ....*....|....*....|....*...
gi 568945015  567 PAPAPELDPFEAQWAALEGKPAVEKPSN 594
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
 
Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 68-202 1.73e-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: 1.73e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  68 HQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEK 147
Cdd:cd01268    1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568945015 148 VSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLER 202
Cdd:cd01268   81 VSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 291-375 5.66e-40

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: 141.07  E-value: 5.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  291 AAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLSLRLNELPSTLQRRTDF-----------QVKGTVPEMEPPGTg 359
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPSSE- 79

                          90
                  ....*....|....*.
gi 568945015  360 DSDGINALCTQISSSF 375
Cdd:pfam06311  80 QADSISAMCQQISSGL 95
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
84-199 3.06e-35

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 129.41  E-value: 3.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015   84 FPVRYLGHVEVEESR------GMHVCEDAVKKLKAMGRKS-----------VKSVLWVSADGLRVVDDKTKDLLVDQTIE 146
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKINKirglsgetgpgTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568945015  147 KVSFCAP-DRNLDKAFSYICRDGTTRRWICHCFLAlKDSGERLSHAVGCAFAAC 199
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNKFACHVFES-EDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 81-209 5.86e-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: 5.86e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015    81 TCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVK----SVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRN 156
Cdd:smart00462   3 GVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKepqkVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPD 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568945015   157 LDKAFSYICRDGTTRRWICHCFLALKDSGErLSHAVGCAFAACLERKQRREKE 209
Cdd:smart00462  83 DLDVFGYIARDPGSSRFACHVFRCEKAAED-IALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 82-196 4.76e-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: 4.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  82 CSFPVRYLGHVEVEESRGMHVCEDAVKKLKAM----GRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNL 157
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAAlkssKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568945015 158 DKAFSYICRDGTTRRWICHCFLALKDS-GERLSHAVGCAF 196
Cdd:cd00934   81 PNVFAFIAGEEGGSGFRCHVFQCEDEEeAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 84-201 1.11e-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: 1.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  84 FPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNLDKAFSY 163
Cdd:cd13161    4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAF 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568945015 164 ICRDGTTRRWICHCFLaLKDSGERLSHAVGCAFAACLE 201
Cdd:cd13161   84 ISHDPRLGRITCHVFR-CKRGAQEICDTIAEAFKAAAE 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 75-196 1.55e-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: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  75 DAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKL-------KAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEK 147
Cdd:cd01273    5 EALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLkfarqlkKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHR 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568945015 148 VSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKdSGERLSHAVGCAF 196
Cdd:cd01273   85 ISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEK-LAEEITLTIGQAF 132
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 83-196 1.96e-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: 1.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  83 SFPVRYLGHVEVEESRGMHVCEDAVKK----LKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNLD 158
Cdd:cd13159    4 TFYLKYLGSTLVEKPKGEGATAEAVKTiiamAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADANHD 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568945015 159 KAFSYICRDGTTRRWICHCFLALKDS-GERLSHAVGCAF 196
Cdd:cd13159   84 KVFAFIATNQDNEKLECHAFLCAKRKmAQAVTLTVAQAF 122
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 86-165 2.46e-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: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  86 VRY----LGHVEVEESRGMHVCEDAVKKLK----AMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNL 157
Cdd:cd01215   16 VRFkaklIGIDEVPAARGDKMCQDAMMKLKgavkAAGEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDTTD 95


                 ....*...
gi 568945015 158 DKAFSYIC 165
Cdd:cd01215   96 NRAFGYVC 103
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 69-182 1.42e-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: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  69 QWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKS---VLWVSADGLRVVDDKTKDLLVDQTI 145
Cdd:cd01274    2 QWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIptiILSISYKGVKFIDATTKNLICEHEI 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568945015 146 EKVSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALK 182
Cdd:cd01274   82 RNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLT 118
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 85-206 9.35e-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: 9.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015   85 PVRYLGHVEVEESRGMHVCEDAVKKLK---AMGRKSVKSVLW-VSADGLRVVDDKTKDLLVDQTIEKVSFCA---PDRNL 157
Cdd:pfam08416   3 RVEHLTTFELDSLTGLQAVEDAIRKLQlldAQGRVWTQEMLLqVSDQGITLTDNETKEELESYPLDSISHCQavlNDGRY 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568945015  158 DKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLERKQRR 206
Cdd:pfam08416  83 NSILALVCQEPGQSKPDVHLFQCDELGAELIAEDIESALSDVRLGKPKK 131
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 83-179 5.72e-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: 5.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  83 SFPVRYLGHVEVEESRGMHVCE----DAVKKLKAmgRKSVKSV-LWVSADGLRVVD-----DKTKDLLVdqTIEKVSFCA 152
Cdd:cd13160    2 VFTVKYLGRMPARGLWGIKHTRkplvDALKNLPK--GKTLPKTkLEVSSDGVKLEElrggfGSSKTVFF--PIHTISYGV 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 568945015 153 PDRNLDKAFSYICR-DGTTRR--WICHCFL 179
Cdd:cd13160   78 QDLVHTRVFSMIVVgEQDSSNhpFECHAFV 107
PHA03247 PHA03247
large tegument protein UL36; Provisional
 263-594 8.60e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 8.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  263 PGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGSfrgfpaLSQKNSPFKRQlslRLNELPSTLQRRT 342
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGR------AAQASSPPQRP---RRRAARPTVGSLT 2696

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  343 DF-QVKGTVPEMEPPGTGDSDGINALCTQISSSFASAGAPAS-GPPPATTGTSAWGEPSVPA-----AAAFQPGHKRTPS 415
Cdd:PHA03247 2697 SLaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAApAPPAVPAGPATPGGPARPArppttAGPPAPAPPAAPA 2776

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  416 EAERWLEEVSQVAKAQQQQQQQQQQQQQQQATSVPPMPTMAPTLQPFSAPVGPFDTAAAQVAVFLPPTHMQPPF------ 489
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsv 2856

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  490 VPAYPGLGYPPMPRVPVVGITPSQMVANAFCSAA---QLQPQPATLLGKAGAFPPPAAPSAPGGQARPRPNGAPWPPEPA 566
Cdd:PHA03247 2857 APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAvsrSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936

                         330       340
                  ....*....|....*....|....*...
gi 568945015  567 PAPAPELDPFEAQWAALEGKPAVEKPSN 594
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 74-209 1.26e-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: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  74 EDAVRKGTCsFPVRYLGHVEVEE--SRGMHVCedAVKKL----KAMGRKSVKSVLWVSADGLRVV-----------DDKT 136
Cdd:cd01270   22 EEAFQHGIT-FQAKYIGSLEVPRpsSRVEIVA--AMRRIryefKAKNIKKKKVTITVSVDGVKVVlrkkkkkkgwtWDES 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568945015 137 KDLLVDQTIEKVSFCAPDRNLDKAFSYICRDGTTRRWICHCFLA-LKDSGERLSHAVGCAFAACLERKQRREKE 209
Cdd:cd01270   99 KLLLMQHPIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSkKKSQAMRIVRTIGQAFEVCHKLSLQHMQG 172
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
 84-195 1.44e-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: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  84 FPVRYLGHVEVEESRGMHVCEDAVKKLKAmGR------KSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNL 157
Cdd:cd13158   13 FIVRFLGSMEVKSDRTSEVIYEAMRQVLA-ARaihnifRMTESHLLVTSDCLRLIDPQTQVTRARFPLADVVQFAAHQEN 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568945015 158 DKAFSYICR----DGTTRRWICHCFLAlKDSGERLSHAVGCA 195
Cdd:cd13158   92 KRLFGFVVRtpegDGEEPSFSCYVFES-NTEGEKICDAIALA 132
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 83-178 1.48e-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: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  83 SFPVRYLGHVEVEE--------SRGMHVCedaVKKLkAMGRKSVKSVLWVSADG-----------LRVVDDKTKDLLVDQ 143
Cdd:cd01272    3 RFAVRSLGWVEMAEedltpgksSVAVNNC---IRQL-SYGRNDIRDTVGRWGEGkdmlmvldddtLKLVDPDDRSVLHSQ 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568945015 144 TIEKVSFCAPDRNLDKAFSYICRDGTTRRWICHCF 178
Cdd:cd01272   79 PIHSIRVWGVGRDNGRDFAYVARDKDTRVLKCHVF 113
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
376-583 2.91e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015 376 ASAGAPASGPPPATTGTSAWGEPSVPAAAAFQPGHKRTPSEAERWLEEVSQVAKAQQQQQQQQQQQQQQQATSVPPMPTM 455
Cdd:PRK12323 377 AAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAA 456

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015 456 APTLQPFSAPVGPFDTAAAQVAvflPPTHMQPPFVPAYPGLGYPPMPRVP--VVGITPSQMVANAFCSAAQLQPQPATLL 533
Cdd:PRK12323 457 APAAAARPAAAGPRPVAAAAAA---APARAAPAAAPAPADDDPPPWEELPpeFASPAPAQPDAAPAGWVAESIPDPATAD 533

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568945015 534 GKAGAFPPPAAPSAPGGQARPRPNGAPWPPEPAPAPAPELDP-FEAQWAAL 583
Cdd:PRK12323 534 PDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDmFDGDWPAL 584
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 70-178 1.92e-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: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  70 WQADEDAVRKGTCSFPVRYLGHVEVEES-RGM--------------HVCEdAVKKLKAMGRKSVKSVLW----------- 123
Cdd:cd01209    3 WLHPDQLGMGPGVSYPVRYVGCIEVLQSmRSLdfntrtqvtreainRVCE-AVGGAKGAKRKRKSKALSsilgksnlqfa 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568945015 124 -------VSADGLRVVDDKTKDLLVDQTIEKVSFCAP-DRNLDKAFSYICRDGTTRRwICHCF 178
Cdd:cd01209   82 gmnisltISTDGLNLVTPDTGQIIANHHMQSISFASGgDPDTYDYVAYVAKDPVNQR-ACHVL 143
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
276-509 4.23e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015 276 GEKGEAGTP-VAAGTTAAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLS---LRLNELPSTLQRRTDFQVKGTVP 351
Cdd:PRK12323 367 QSGGGAGPAtAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAaapARRSPAPEALAAARQASARGPGG 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015 352 EMEPPgtgdsdginalctqisSSFASAGAPASGPPPATTGTSAWGEPSVPAAAAFQPGHKRTPSEAERWLE-----EVSQ 426
Cdd:PRK12323 447 APAPA----------------PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEElppefASPA 510

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015 427 VAKAQQQQQQQQQQQQQQQATSVPPMPTMAPTLQPFSAPVGPFDTAAAQVAVFLPPTHMQPPFVPAYPGLGYPPMPRVPV 506
Cdd:PRK12323 511 PAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAARLPV 590


                 ...
gi 568945015 507 VGI 509
Cdd:PRK12323 591 RGL 593
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 83-178 4.35e-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: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945015  83 SFPVRYLGHVEVEESRGMHVCEDAVKKLKAM---GRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNlDK 159
Cdd:cd13157    3 SRNAQYIGSFPVSGLDVADRADSVRKQLESLkesGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPA-HA 81

                         90       100
                 ....*....|....*....|.
gi 568945015 160 AFSYICRD--GTTRRWICHCF 178
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH