NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907154043|ref|XP_036019530|]
View 

disabled homolog 1 isoform X1 [Mus musculus]

Protein Classification

Dab family PTB domain-containing protein( domain architecture ID 10100614)

Dab (Disabled) family PTB (phosphotyrosine-binding) domain-containing protein similar to mammalian disabled homolog 1 and 2, which are adapter proteins that function in neural development and endocytosis, respectively

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  15567406|8987385|10610414
SCOP:  4002427

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_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 25-174 1.63e-92

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: 280.68  E-value: 1.63e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  25 DRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKGVVAGArskGEHKQKIFLTISFGGIKIFDEKTGAL 104
Cdd:cd01215     1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGAL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043 105 QHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTAQAAEPVILDLRDLFQLIYELKQREELEKKA 174
Cdd:cd01215    78 LHHHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 288-469 1.71e-03

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043 288 PPDITSPPTPATPGDAFLPSSSQTLPGSADVFGSMSFGTAAVPS--GYVAMGAVLPSFWGQQPLVQQQIAMGAQPPVAqv 365
Cdd:PRK07764  609 PEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHhpKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPA-- 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043 366 iPGAQPIAWGQPGLFPATQQAWPTVAGQFP-PAAFMPTQTVMPLAAAMFQGPLTPLATVPGTNDSARSSPQSDKPRQKMG 444
Cdd:PRK07764  687 -PAAPAAPAGAAPAQPAPAPAATPPAGQADdPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765

                         170       180
                  ....*....|....*....|....*
gi 1907154043 445 KESfkdfQMVQPPPVPSRKPDQPSL 469
Cdd:PRK07764  766 PAA----APAAAPPPSPPSEEEEMA 786
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 25-174 1.63e-92

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: 280.68  E-value: 1.63e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  25 DRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKGVVAGArskGEHKQKIFLTISFGGIKIFDEKTGAL 104
Cdd:cd01215     1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGAL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043 105 QHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTAQAAEPVILDLRDLFQLIYELKQREELEKKA 174
Cdd:cd01215    78 LHHHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 37-171 3.50e-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: 126.27  E-value: 3.50e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043   37 GEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKgvvAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYI 116
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR---AAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFC 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154043  117 AKDITDHRAFGYVCGKEGN--HRFVAIKTAQAAEPVILDLRDLFQLIYELKQREELE 171
Cdd:smart00462  78 AVGPDDLDVFGYIARDPGSsrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
82-161 6.83e-06

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 45.82  E-value: 6.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  82 KQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIA-KDITDHRAFGYVCGKEGNHRFV--AIKTAQAAEPVILDLRDLF 158
Cdd:pfam00640  51 GTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAdGDPDLMRYFAYIARDKATNKFAchVFESEDGAQDIAQSIGQAF 130


                  ...
gi 1907154043 159 QLI 161
Cdd:pfam00640 131 ALA 133
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 288-469 1.71e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043 288 PPDITSPPTPATPGDAFLPSSSQTLPGSADVFGSMSFGTAAVPS--GYVAMGAVLPSFWGQQPLVQQQIAMGAQPPVAqv 365
Cdd:PRK07764  609 PEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHhpKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPA-- 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043 366 iPGAQPIAWGQPGLFPATQQAWPTVAGQFP-PAAFMPTQTVMPLAAAMFQGPLTPLATVPGTNDSARSSPQSDKPRQKMG 444
Cdd:PRK07764  687 -PAAPAAPAGAAPAQPAPAPAATPPAGQADdPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765

                         170       180
                  ....*....|....*....|....*
gi 1907154043 445 KESfkdfQMVQPPPVPSRKPDQPSL 469
Cdd:PRK07764  766 PAA----APAAAPPPSPPSEEEEMA 786
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 25-174 1.63e-92

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: 280.68  E-value: 1.63e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  25 DRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKGVVAGArskGEHKQKIFLTISFGGIKIFDEKTGAL 104
Cdd:cd01215     1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGAL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043 105 QHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTAQAAEPVILDLRDLFQLIYELKQREELEKKA 174
Cdd:cd01215    78 LHHHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 37-171 3.50e-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: 126.27  E-value: 3.50e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043   37 GEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKgvvAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYI 116
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR---AAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFC 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154043  117 AKDITDHRAFGYVCGKEGN--HRFVAIKTAQAAEPVILDLRDLFQLIYELKQREELE 171
Cdd:smart00462  78 AVGPDDLDVFGYIARDPGSsrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 40-158 2.42e-19

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: 84.10  E-value: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  40 VRYKAKLIGIDEVSAARGDKLCQDSmmkLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKD 119
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEEA---LKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907154043 120 ITDHRAFGYVCGKEGNHRF----VAIKTAQAAEPVILDLRDLF 158
Cdd:cd00934    78 PDNPNVFAFIAGEEGGSGFrchvFQCEDEEEAEEILQAIGQAF 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 40-162 2.35e-15

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: 73.47  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  40 VRYKAKLIGIDEVSAARGDKLCQDSMMKLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKD 119
Cdd:cd01273    12 VAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907154043 120 ITDHRAFGYVC--GKEGNHRFVAIKTAQAAEPVILDLRDLFQLIY 162
Cdd:cd01273    92 KTDKRIFSFIAkdSESEKHLCFVFDSEKLAEEITLTIGQAFDLAY 136
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 25-164 4.84e-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: 63.84  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  25 DRSEATLIKrfkgEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKgvvagaRSKGEHKQ--KIFLTISFGGIKIFDEKTG 102
Cdd:cd01274     4 RHSPEKLIT----GSVNYEAHYLGSTEIKELRGTESTKKAIQKLK------KSTREMKKipTIILSISYKGVKFIDATTK 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907154043 103 ALQHHHAVHEISYIAKDITDHRAFGYV----------CgkegnHRFVAIKTAQAAEpVILDLRDLFQLIYEL 164
Cdd:cd01274    74 NLICEHEIRNISCACQDPEDLNTFAYItkdlktdhhyC-----HVFCVLTVDLATE-IILTLGQAFEVAYQL 139
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 38-142 1.58e-09

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: 56.16  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  38 EGVR-----YKAKLIGIDEVSAARGDKLCQDSMMKLkgvvagaRSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHE 112
Cdd:cd01268     8 EAVRsgtcsFPVKYLGCVEVGESRGMQVCEEALKKL-------KASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEK 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907154043 113 ISYIAKDITDHRAFGYVCgKEGN------HRFVAIK 142
Cdd:cd01268    81 VSFCAPDRNHERAFSYIC-RDGTtrrwmcHCFLAVK 115
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 38-146 2.58e-08

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: 52.33  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  38 EGVRYKAKLIGIDEVSAARGDKLCQDSmmkLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIA 117
Cdd:cd13159     1 DGVTFYLKYLGSTLVEKPKGEGATAEA---VKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCT 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907154043 118 KDITDHRAFGYVCGKEGN-----HRFVAIK--TAQA 146
Cdd:cd13159    78 ADANHDKVFAFIATNQDNeklecHAFLCAKrkMAQA 113
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
82-161 6.83e-06

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 45.82  E-value: 6.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  82 KQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIA-KDITDHRAFGYVCGKEGNHRFV--AIKTAQAAEPVILDLRDLF 158
Cdd:pfam00640  51 GTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAdGDPDLMRYFAYIARDKATNKFAchVFESEDGAQDIAQSIGQAF 130


                  ...
gi 1907154043 159 QLI 161
Cdd:pfam00640 131 ALA 133
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 40-167 1.37e-05

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: 44.68  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  40 VRYKAKLIGIDEVSaargDKLCQDSMMKLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKD 119
Cdd:cd13157     2 VSRNAQYIGSFPVS----GLDVADRADSVRKQLESLKESGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCR 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907154043 120 iTDHRAFGYVCGKEGN-------HRFVAiKTAQAAEPVILDLRDLFQLIYeLKQR 167
Cdd:cd13157    78 -PAHAQFAFVARNPGGptnrqycHVFVT-RSPREAQELNLLLCRAFQLAY-LKQH 129
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 41-130 1.61e-05

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: 44.55  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  41 RYKAKLIGIDEVSAARGDKLCQDSMMKLkgvvagaRSKGEHKQKIFLTISFGGIKIFDEKTGalQHHHAVH--EISYIAK 118
Cdd:cd13161     3 VFEAKYLGSVPVKEPKGNDVVMAAVKRL-------KDLKLKPKPVVLVVSSEGIRVVERLTG--EVLTNVPikDISFVTV 73

                          90
                  ....*....|..
gi 1907154043 119 DITDHRAFGYVC 130
Cdd:cd13161    74 DPKDKKLFAFIS 85
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 288-469 1.71e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043 288 PPDITSPPTPATPGDAFLPSSSQTLPGSADVFGSMSFGTAAVPS--GYVAMGAVLPSFWGQQPLVQQQIAMGAQPPVAqv 365
Cdd:PRK07764  609 PEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHhpKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPA-- 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043 366 iPGAQPIAWGQPGLFPATQQAWPTVAGQFP-PAAFMPTQTVMPLAAAMFQGPLTPLATVPGTNDSARSSPQSDKPRQKMG 444
Cdd:PRK07764  687 -PAAPAAPAGAAPAQPAPAPAATPPAGQADdPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765

                         170       180
                  ....*....|....*....|....*
gi 1907154043 445 KESfkdfQMVQPPPVPSRKPDQPSL 469
Cdd:PRK07764  766 PAA----APAAAPPPSPPSEEEEMA 786
PHA03247 PHA03247
large tegument protein UL36; Provisional
 233-470 4.17e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 4.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  233 DVPKSQPVSNSQPLEDFDSRFAAATPNRNLSMDfdELLEATKAVTQLELFGDMSTPPDITSPPTPATPGDAflpSSSQTL 312
Cdd:PHA03247  2754 PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRP--AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAA---SPAGPL 2828

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  313 PGSADVFGSMSFGTAAVPSGYVAM-GAVLPSF-WGQQPLVQQQIAMGA---QPPVA-----QVIPGAQPIAWGQPGLFPA 382
Cdd:PHA03247  2829 PPPTSAQPTAPPPPPGPPPPSLPLgGSVAPGGdVRRRPPSRSPAAKPAapaRPPVRrlarpAVSRSTESFALPPDQPERP 2908

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154043  383 TQQAWPTVAGQFPPAAFMPTQTVMPLAAAMFQGPLTPLATVPGTNDSARSSPQSDKPRQKMGKESFKDFQMVQP-PPVPS 461
Cdd:PHA03247  2909 PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPaPSREA 2988


                   ....*....
gi 1907154043  462 RKPDQPSLT 470
Cdd:PHA03247  2989 PASSTPPLT 2997
 
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