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Conserved domains on  [gi|156396490|ref|XP_001637426|]
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WASH complex subunit 2 [Nematostella vectensis]

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

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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 ...
 27-173 7.30e-69

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: 227.14  E-value: 7.30e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   27 GKDAPLNEEKFRGDGVHFKCKLLGLKEVSGPRGDTICIDAIKKLKQQIKQTGEHKQKIIMAVNLRGIRILDEKSKALVYE 106
Cdd:cd01215     1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156396490  107 HAINKVSFITHDPEDKKIFGYVCSQATGHMLYAIKYDKVAGVITATLYELFQVVFKLRQEAAQRRNA 173
Cdd:cd01215    81 HPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 27-173 7.30e-69

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: 227.14  E-value: 7.30e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   27 GKDAPLNEEKFRGDGVHFKCKLLGLKEVSGPRGDTICIDAIKKLKQQIKQTGEHKQKIIMAVNLRGIRILDEKSKALVYE 106
Cdd:cd01215     1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156396490  107 HAINKVSFITHDPEDKKIFGYVCSQATGHMLYAIKYDKVAGVITATLYELFQVVFKLRQEAAQRRNA 173
Cdd:cd01215    81 HPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 39-167 5.38e-28

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


Pssm-ID: 214675  Cd Length: 134  Bit Score: 110.10  E-value: 5.38e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490     39 GDGVHFKCKLLGLKEVSGPRGDTICIDAIKKLKQQIKQTGEHKQKIIMAVNLRGIRILDEKSKALVYEHAINKVSFITHD 118
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 156396490    119 PEDKKIFGYVCSQATGHML--YAIKYDKVAGVITATLYELFQVVFKLRQEA 167
Cdd:smart00462   81 PDDLDVFGYIARDPGSSRFacHVFRCEKAAEDIALAIGQAFQLAYELKLKA 131
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
62-159 3.28e-08

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 53.52  E-value: 3.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490    62 ICIDAIKKLKQQIKQTGEhKQKIIMAVNLRGIRILDEKSKALVYEHAINKVSFITH-DPEDKKIFGYVCSQATGHML--Y 138
Cdd:pfam00640   33 VKAAKINKIRGLSGETGP-GTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCADgDPDLMRYFAYIARDKATNKFacH 111

                           90       100
                   ....*....|....*....|.
gi 156396490   139 AIKYDKVAGVITATLYELFQV 159
Cdd:pfam00640  112 VFESEDGAQDIAQSIGQAFAL 132
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 27-173 7.30e-69

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: 227.14  E-value: 7.30e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   27 GKDAPLNEEKFRGDGVHFKCKLLGLKEVSGPRGDTICIDAIKKLKQQIKQTGEHKQKIIMAVNLRGIRILDEKSKALVYE 106
Cdd:cd01215     1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156396490  107 HAINKVSFITHDPEDKKIFGYVCSQATGHMLYAIKYDKVAGVITATLYELFQVVFKLRQEAAQRRNA 173
Cdd:cd01215    81 HPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 39-167 5.38e-28

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


Pssm-ID: 214675  Cd Length: 134  Bit Score: 110.10  E-value: 5.38e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490     39 GDGVHFKCKLLGLKEVSGPRGDTICIDAIKKLKQQIKQTGEHKQKIIMAVNLRGIRILDEKSKALVYEHAINKVSFITHD 118
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 156396490    119 PEDKKIFGYVCSQATGHML--YAIKYDKVAGVITATLYELFQVVFKLRQEA 167
Cdd:smart00462   81 PDDLDVFGYIARDPGSSRFacHVFRCEKAAEDIALAIGQAFQLAYELKLKA 131
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 33-133 3.90e-21

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: 90.44  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   33 NEEKFRGDGVHFKCKLLGLKEVSGPRGDTICIDAIKKLKQQIKqtgeHKQKIIMAVNLRGIRILDEKSKALVYEHAINKV 112
Cdd:cd01268     6 DEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRK----KPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKV 81

                          90       100
                  ....*....|....*....|.
gi 156396490  113 SFITHDPEDKKIFGYVCSQAT 133
Cdd:cd01268    82 SFCAPDRNHERAFSYICRDGT 102
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 44-157 8.87e-18

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: 80.25  E-value: 8.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   44 FKCKLLGLKEVSGPRGDTICIDAIKKLKQQIKQTGEHKQKIIMAVNLRGIRILDEKSKALVYEHAINKVSFITHDPEDKK 123
Cdd:cd00934     3 FQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPN 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 156396490  124 IFGYVC--SQATGHMLYAIKYDKV--AGVITATLYELF 157
Cdd:cd00934    83 VFAFIAgeEGGSGFRCHVFQCEDEeeAEEILQAIGQAF 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 42-162 5.82e-17

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: 78.86  E-value: 5.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   42 VHFKCKLLGLKEVSGPRGDTICIDAIKKLK--QQIKQTGEHK-QKIIMAVNLRGIRILDEKSKALVYEHAINKVSFITHD 118
Cdd:cd01273    12 VAYLVKFLGCTEVEQPKGTEVVKEAIRKLKfaRQLKKSEGAKlPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 156396490  119 PEDKKIFGYVC--SQATGHMLYAIKYDKVAGVITATLYELFQVVFK 162
Cdd:cd01273    92 KTDKRIFSFIAkdSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYR 137
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 40-158 3.95e-13

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: 66.97  E-value: 3.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   40 DGVHFKCKLLGLKEVSGPRGDTICIDAIKKLKQQIKQTGEHKQKIIMAVNLRGIRILDEKSKALVYEHAINKVSFITHDP 119
Cdd:cd13159     1 DGVTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 156396490  120 EDKKIFGYV-CSQATGHML---YAIKYDKVAGVITATLYELFQ 158
Cdd:cd13159    81 NHDKVFAFIaTNQDNEKLEchaFLCAKRKMAQAVTLTVAQAFN 123
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 44-138 1.31e-12

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: 65.73  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   44 FKCKLLGLKEVSGPRGDTICIDAIKKLKQQiKQTGehkQKIIMAVNLRGIRILDEKSKALVYEHAINKVSFITHDPEDKK 123
Cdd:cd13161     4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDL-KLKP---KPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKK 79

                          90
                  ....*....|....*
gi 156396490  124 IFGYVCSQATGHMLY 138
Cdd:cd13161    80 LFAFISHDPRLGRIT 94
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 49-128 3.10e-11

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: 62.30  E-value: 3.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   49 LGLKEVSGPRGDTICIDAIKKLKqqiKQTGEHKQ--KIIMAVNLRGIRILDEKSKALVYEHAINKVSFITHDPEDKKIFG 126
Cdd:cd01274    22 LGSTEIKELRGTESTKKAIQKLK---KSTREMKKipTIILSISYKGVKFIDATTKNLICEHEIRNISCACQDPEDLNTFA 98


                  ..
gi 156396490  127 YV 128
Cdd:cd01274    99 YI 100
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
62-159 3.28e-08

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 53.52  E-value: 3.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490    62 ICIDAIKKLKQQIKQTGEhKQKIIMAVNLRGIRILDEKSKALVYEHAINKVSFITH-DPEDKKIFGYVCSQATGHML--Y 138
Cdd:pfam00640   33 VKAAKINKIRGLSGETGP-GTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCADgDPDLMRYFAYIARDKATNKFacH 111

                           90       100
                   ....*....|....*....|.
gi 156396490   139 AIKYDKVAGVITATLYELFQV 159
Cdd:pfam00640  112 VFESEDGAQDIAQSIGQAFAL 132
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 45-135 7.46e-08

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: 52.39  E-value: 7.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   45 KCKLLGLKEVSGPRGDTICiDAIKKLKQQIKQTGEHKQKIIMAVNLRGIRILDEKSKALVYEHAINKVSFITHDPEDKKi 124
Cdd:cd13157     5 NAQYIGSFPVSGLDVADRA-DSVRKQLESLKESGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPAHAQ- 82

                          90
                  ....*....|.
gi 156396490  125 FGYVCSQATGH 135
Cdd:cd13157    83 FAFVARNPGGP 93
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 31-129 1.19e-07

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: 53.06  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156396490   31 PLNEEKFRGDGVHFKCKLLGLKEVSGPRGDTICIDAIKKLKQQIKQTGEHKQKIIMAVNLRGIRILDEK----------- 99
Cdd:cd01270    18 PLHNEEAFQHGITFQAKYIGSLEVPRPSSRVEIVAAMRRIRYEFKAKNIKKKKVTITVSVDGVKVVLRKkkkkkgwtwde 97

                          90       100       110
                  ....*....|....*....|....*....|
gi 156396490  100 SKALVYEHAINKVSFITHDPEDKKIFGYVC 129
Cdd:cd01270    98 SKLLLMQHPIYRIFYVSHDSQDLKIFSYIA 127
 
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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