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Conserved domains on  [gi|45549349|ref|NP_572506|]
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uncharacterized protein Dmel_CG12075, isoform A [Drosophila melanogaster]

Protein Classification

PTB domain-containing protein( domain architecture ID 10097123)

PTB (phosphotyrosine-binding) domain-containing protein similar to Ciona intestinalis Not4 protein

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 cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 12-120 5.13e-07

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: 49.43  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549349   12 ASYYVWFLGAEEAKGLRGARVINSVLP--YLVDRSRGQEPLKVTLQVSHKGIKIVQGASKHLI---PHSAITSSVQTDDI 86
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKalAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLlrhPLHRISYCGRDPDN 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 45549349   87 VACVLLLYNPATKCPLHVHAYRCDSETTAEALHL 120
Cdd:cd00934   81 PNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQ 114
 
Name Accession Description Interval E-value
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 12-120 5.13e-07

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: 49.43  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549349   12 ASYYVWFLGAEEAKGLRGARVINSVLP--YLVDRSRGQEPLKVTLQVSHKGIKIVQGASKHLI---PHSAITSSVQTDDI 86
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKalAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLlrhPLHRISYCGRDPDN 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 45549349   87 VACVLLLYNPATKCPLHVHAYRCDSETTAEALHL 120
Cdd:cd00934   81 PNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQ 114
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 12-134 7.09e-05

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: 43.46  E-value: 7.09e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549349      12 ASYYVWFLGAEEAKGLRGARVINSVLPYL--VDRSRGQEPLKVTLQVSHKGIKIVQGASKHLIPHSA---ITSSVQTDDI 86
Cdd:smart00462    4 VSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPlrrISFCAVGPDD 83

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 45549349      87 VACVLLLYNPATKCPLHVHAYRCDSETT--AEALHLQLQILINRPDNQKR 134
Cdd:smart00462   84 LDVFGYIARDPGSSRFACHVFRCEKAAEdiALAIGQAFQLAYELKLKARS 133
 
Name Accession Description Interval E-value
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 12-120 5.13e-07

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: 49.43  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549349   12 ASYYVWFLGAEEAKGLRGARVINSVLP--YLVDRSRGQEPLKVTLQVSHKGIKIVQGASKHLI---PHSAITSSVQTDDI 86
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKalAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLlrhPLHRISYCGRDPDN 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 45549349   87 VACVLLLYNPATKCPLHVHAYRCDSETTAEALHL 120
Cdd:cd00934   81 PNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQ 114
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 13-122 8.82e-07

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: 48.87  E-value: 8.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549349   13 SYYVWFLGAEEAKGLRGarvINSVLPYLVDRS----RGQEPLKVTLQVSHKGIKIVQ-----GASKH-LIPHSAITSSVQ 82
Cdd:cd13160    2 VFTVKYLGRMPARGLWG---IKHTRKPLVDALknlpKGKTLPKTKLEVSSDGVKLEElrggfGSSKTvFFPIHTISYGVQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 45549349   83 tDDI----VACVLLLYNPATKCPLHVHAYRCDSETTAEALHLQL 122
Cdd:cd13160   79 -DLVhtrvFSMIVVGEQDSSNHPFECHAFVCDSRADARNLTYWL 121
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 12-134 7.09e-05

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: 43.46  E-value: 7.09e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549349      12 ASYYVWFLGAEEAKGLRGARVINSVLPYL--VDRSRGQEPLKVTLQVSHKGIKIVQGASKHLIPHSA---ITSSVQTDDI 86
Cdd:smart00462    4 VSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPlrrISFCAVGPDD 83

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 45549349      87 VACVLLLYNPATKCPLHVHAYRCDSETT--AEALHLQLQILINRPDNQKR 134
Cdd:smart00462   84 LDVFGYIARDPGSSRFACHVFRCEKAAEdiALAIGQAFQLAYELKLKARS 133
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 18-85 1.05e-03

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: 39.92  E-value: 1.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549349   18 FLGAEEAKGLRGARVINSVLPYLvdRSRGQEPLKVTLQVSHKGIKIVQGASKHLIPHSAIT--SSVQTDD 85
Cdd:cd13161    8 YLGSVPVKEPKGNDVVMAAVKRL--KDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKdiSFVTVDP 75
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 11-72 1.38e-03

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: 39.98  E-value: 1.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45549349   11 KASYYVWFLGAEEAKGLRGARVINSVLPYLvdRSRGQEPLKVTLQVSHKGIKIVQGASKHLI 72
Cdd:cd01268   14 TCSFPVKYLGCVEVGESRGMQVCEEALKKL--KASRKKPVRAVLWVSGDGLRVVDEKTKGLI 73
 
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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