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Conserved domains on  [gi|568928360|ref|XP_006502798|]
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disabled homolog 1 isoform X11 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1-110 2.39e-64

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd01215:

Pssm-ID: 473070  Cd Length: 147  Bit Score: 205.95  E-value: 2.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360   1 MMKLKGVVAGArskGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTA 80
Cdd:cd01215   41 MMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTA 117

                         90       100       110
                 ....*....|....*....|....*....|
gi 568928360  81 QAAEPVILDLRDLFQLIYELKQREELEKKA 110
Cdd:cd01215  118 KAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 224-405 2.34e-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: 40.74  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360 224 PPDITSPPTPATPGDAFLPSSSQTLPGSADVFGSMSFGTAAVPS--GYVAMGAVLPSFWGQQPLVQQQIAMGAQPPVAqv 301
Cdd:PRK07764 609 PEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHhpKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPA-- 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360 302 iPGAQPIAWGQPGLFPATQQAWPTVAGQFP-PAAFMPTQTVMPLAAAMFQGPLTPLATVPGTNDSARSSPQSDKPRQKMG 380
Cdd:PRK07764 687 -PAAPAAPAGAAPAQPAPAPAATPPAGQADdPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765

                        170       180
                 ....*....|....*....|....*
gi 568928360 381 KESfkdfQMVQPPPVPSRKPDQPSL 405
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 ...
 1-110 2.39e-64

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: 205.95  E-value: 2.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360   1 MMKLKGVVAGArskGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTA 80
Cdd:cd01215   41 MMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTA 117

                         90       100       110
                 ....*....|....*....|....*....|
gi 568928360  81 QAAEPVILDLRDLFQLIYELKQREELEKKA 110
Cdd:cd01215  118 KAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1-107 1.55e-24

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: 98.93  E-value: 1.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360     1 MMKLKgvvAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGN--HRFVAIK 78
Cdd:smart00462  29 IRKLR---AAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGSsrFACHVFR 105

                           90       100
                   ....*....|....*....|....*....
gi 568928360    79 TAQAAEPVILDLRDLFQLIYELKQREELE 107
Cdd:smart00462 106 CEKAAEDIALAIGQAFQLAYELKLKARSE 134
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
18-97 5.99e-06

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 45.82  E-value: 5.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360   18 KQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIA-KDITDHRAFGYVCGKEGNHRFV--AIKTAQAAEPVILDLRDLF 94
Cdd:pfam00640  51 GTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAdGDPDLMRYFAYIARDKATNKFAchVFESEDGAQDIAQSIGQAF 130


                  ...
gi 568928360   95 QLI 97
Cdd:pfam00640 131 ALA 133
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 224-405 2.34e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360 224 PPDITSPPTPATPGDAFLPSSSQTLPGSADVFGSMSFGTAAVPS--GYVAMGAVLPSFWGQQPLVQQQIAMGAQPPVAqv 301
Cdd:PRK07764 609 PEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHhpKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPA-- 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360 302 iPGAQPIAWGQPGLFPATQQAWPTVAGQFP-PAAFMPTQTVMPLAAAMFQGPLTPLATVPGTNDSARSSPQSDKPRQKMG 380
Cdd:PRK07764 687 -PAAPAAPAGAAPAQPAPAPAATPPAGQADdPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765

                        170       180
                 ....*....|....*....|....*
gi 568928360 381 KESfkdfQMVQPPPVPSRKPDQPSL 405
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 ...
 1-110 2.39e-64

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: 205.95  E-value: 2.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360   1 MMKLKGVVAGArskGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTA 80
Cdd:cd01215   41 MMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTA 117

                         90       100       110
                 ....*....|....*....|....*....|
gi 568928360  81 QAAEPVILDLRDLFQLIYELKQREELEKKA 110
Cdd:cd01215  118 KAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1-107 1.55e-24

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: 98.93  E-value: 1.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360     1 MMKLKgvvAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGN--HRFVAIK 78
Cdd:smart00462  29 IRKLR---AAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGSsrFACHVFR 105

                           90       100
                   ....*....|....*....|....*....
gi 568928360    79 TAQAAEPVILDLRDLFQLIYELKQREELE 107
Cdd:smart00462 106 CEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 2-94 1.15e-14

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: 70.23  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360   2 MKLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRF----VAI 77
Cdd:cd00934   24 EALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAGEEGGSGFrchvFQC 103

                         90
                 ....*....|....*..
gi 568928360  78 KTAQAAEPVILDLRDLF 94
Cdd:cd00934  104 EDEEEAEEILQAIGQAF 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 3-98 4.05e-11

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: 61.14  E-value: 4.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360   3 KLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVC--GKEGNHRFVAIKTA 80
Cdd:cd01273   39 KLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADDKTDKRIFSFIAkdSESEKHLCFVFDSE 118

                         90
                 ....*....|....*...
gi 568928360  81 QAAEPVILDLRDLFQLIY 98
Cdd:cd01273  119 KLAEEITLTIGQAFDLAY 136
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 1-100 3.35e-07

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: 49.59  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360   1 MMKLKgvvagaRSKGEHKQ--KIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYV----------Cgk 68
Cdd:cd01274   40 IQKLK------KSTREMKKipTIILSISYKGVKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYItkdlktdhhyC-- 111

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568928360  69 egnHRFVAIKTAQAAEpVILDLRDLFQLIYEL 100
Cdd:cd01274  112 ---HVFCVLTVDLATE-IILTLGQAFEVAYQL 139
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 5-82 3.09e-06

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: 46.56  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360   5 KGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGN-----HRFVAIK- 78
Cdd:cd13159   29 KTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADANHDKVFAFIATNQDNeklecHAFLCAKr 108


                 ....*
gi 568928360  79 -TAQA 82
Cdd:cd13159  109 kMAQA 113
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
18-97 5.99e-06

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 45.82  E-value: 5.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360   18 KQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIA-KDITDHRAFGYVCGKEGNHRFV--AIKTAQAAEPVILDLRDLF 94
Cdd:pfam00640  51 GTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAdGDPDLMRYFAYIARDKATNKFAchVFESEDGAQDIAQSIGQAF 130


                  ...
gi 568928360   95 QLI 97
Cdd:pfam00640 131 ALA 133
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 9-103 4.01e-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: 43.53  E-value: 4.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360   9 AGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDiTDHRAFGYVCGKEGN-------HRFVAiKTAQ 81
Cdd:cd13157   31 ESLKESGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCR-PAHAQFAFVARNPGGptnrqycHVFVT-RSPR 108

                         90       100
                 ....*....|....*....|..
gi 568928360  82 AAEPVILDLRDLFQLIYeLKQR 103
Cdd:cd13157  109 EAQELNLLLCRAFQLAY-LKQH 129
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 12-78 2.29e-04

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: 41.14  E-value: 2.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568928360  12 RSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCgKEGN------HRFVAIK 78
Cdd:cd01268   44 KASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRNHERAFSYIC-RDGTtrrwmcHCFLAVK 115
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 224-405 2.34e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360 224 PPDITSPPTPATPGDAFLPSSSQTLPGSADVFGSMSFGTAAVPS--GYVAMGAVLPSFWGQQPLVQQQIAMGAQPPVAqv 301
Cdd:PRK07764 609 PEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHhpKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPA-- 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360 302 iPGAQPIAWGQPGLFPATQQAWPTVAGQFP-PAAFMPTQTVMPLAAAMFQGPLTPLATVPGTNDSARSSPQSDKPRQKMG 380
Cdd:PRK07764 687 -PAAPAAPAGAAPAQPAPAPAATPPAGQADdPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPA 765

                        170       180
                 ....*....|....*....|....*
gi 568928360 381 KESfkdfQMVQPPPVPSRKPDQPSL 405
Cdd:PRK07764 766 PAA----APAAAPPPSPPSEEEEMA 786
PHA03247 PHA03247
large tegument protein UL36; Provisional
 169-406 7.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360  169 DVPKSQPVSNSQPLEDFDSRFAAATPNRNLSMDfdELLEATKAVTQLELFGDMSTPPDITSPPTPATPGDAflpSSSQTL 248
Cdd:PHA03247 2754 PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRP--AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAA---SPAGPL 2828

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360  249 PGSADVFGSMSFGTAAVPSGYVAM-GAVLPSF-WGQQPLVQQQIAMGAQP--------PVAQVIPGAQPIAWGQPGLFPA 318
Cdd:PHA03247 2829 PPPTSAQPTAPPPPPGPPPPSLPLgGSVAPGGdVRRRPPSRSPAAKPAAParppvrrlARPAVSRSTESFALPPDQPERP 2908

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928360  319 TQQAWPTVAGQFPPAAFMPTQTVMPLAAAMFQGPLTPLATVPGTNDSARSSPQSDKPRQKMGKESFKDFQMVQP-PPVPS 397
Cdd:PHA03247 2909 PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPaPSREA 2988


                  ....*....
gi 568928360  398 RKPDQPSLT 406
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.
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