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Conserved domains on  [gi|23093316|gb|AAF49424|]
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disabled, isoform A [Drosophila melanogaster]

Protein Classification

Dab family PTB domain-containing protein; Tec family PH domain-containing protein( domain architecture ID 12913411)

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| Tec family PH (pleckstrin homology) domain-containing protein similar to the PH domain of tyrosine-protein kinase BTK, a non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling

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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 ...
 35-181 1.13e-87

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: 282.22  E-value: 1.13e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   35 AKHRNDPGRFFGDGVQFKAKLIGILEVGEARGDRMCQEALQDLKMAIRAAGEHKQRITIHVTIDGLRLRDEKTGDSLYHH 114
Cdd:cd01215    2 KTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHHH 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23093316  115 PVHKISFIAQDMTDSRAFGYIFGSpDSGHRFFGIKTDKAASQVVLAMRDLFQVVFELKKKEIEMARQ 181
Cdd:cd01215   82 PVHKISFIARDTTDNRAFGYVCGL-DGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PRK12727 super family cl36170
flagellar biosynthesis protein FlhF;
542-708 2.43e-03

flagellar biosynthesis protein FlhF;


The actual alignment was detected with superfamily member PRK12727:

Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 43.05  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   542 PQQNSANTLTSTASTAASLGQ-LLSTVALN---PDPLPAPISIPTSISHSITPSAELKLLLGHVTNPPNPTgHYYTTEP- 616
Cdd:PRK12727   86 PLKLSANANMSQRQRVASAAEdMIAAMALRqpvSVPRQAPAAAPVRAASIPSPAAQALAHAAAVRTAPRQE-HALSAVPe 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   617 ------PTLNSLENPHPPADPVLLPRDTdPFSPTRKKSDPDPFQESDLFAKLDAFEFEA--PPAVPAPSIPNLATETKAN 688
Cdd:PRK12727  165 qlfadfLTTAPVPRAPVQAPVVAAPAPV-PAIAAALAAHAAYAQDDDEQLDDDGFDLDDalPQILPPAALPPIVVAPAAP 243

                         170       180
                  ....*....|....*....|.
gi 23093316   689 VFNGPLQVQLP-PEKELQLQQ 708
Cdd:PRK12727  244 AALAAVAAAAPaPQNDEELKQ 264
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 35-181 1.13e-87

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: 282.22  E-value: 1.13e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   35 AKHRNDPGRFFGDGVQFKAKLIGILEVGEARGDRMCQEALQDLKMAIRAAGEHKQRITIHVTIDGLRLRDEKTGDSLYHH 114
Cdd:cd01215    2 KTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHHH 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23093316  115 PVHKISFIAQDMTDSRAFGYIFGSpDSGHRFFGIKTDKAASQVVLAMRDLFQVVFELKKKEIEMARQ 181
Cdd:cd01215   82 PVHKISFIARDTTDNRAFGYVCGL-DGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 46-178 2.90e-37

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: 137.45  E-value: 2.90e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316      46 GDGVQFKAKLIGILEVGEARGDRMCQEALQDLKMAIRAAGEHKQRITIHVTIDGLRLRDEKTGDSLYHHPVHKISFIAQD 125
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 23093316     126 MTDSRAFGYIFGSPDSG-HRFFGIKTDKAASQVVLAMRDLFQVVFELKKKEIEM 178
Cdd:smart00462   81 PDDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
51-167 2.65e-08

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 54.68  E-value: 2.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316     51 FKAKLIGILEVGEARG----DRM--CQEALQDLKMAIRAAGEHK-------QRITIHVTIDGLRLRDEKTGDSLYHHPVH 117
Cdd:pfam00640    1 FAVRYLGSVEVPEERApdknTRMqqAREAIRRVKAAKINKIRGLsgetgpgTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 23093316    118 KISFIA-QDMTDSRAFGYIFGSPDSG----HRFfgiKTDKAASQVVLAMRDLFQV 167
Cdd:pfam00640   81 SISFCAdGDPDLMRYFAYIARDKATNkfacHVF---ESEDGAQDIAQSIGQAFAL 132
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
542-708 2.43e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 43.05  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   542 PQQNSANTLTSTASTAASLGQ-LLSTVALN---PDPLPAPISIPTSISHSITPSAELKLLLGHVTNPPNPTgHYYTTEP- 616
Cdd:PRK12727   86 PLKLSANANMSQRQRVASAAEdMIAAMALRqpvSVPRQAPAAAPVRAASIPSPAAQALAHAAAVRTAPRQE-HALSAVPe 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   617 ------PTLNSLENPHPPADPVLLPRDTdPFSPTRKKSDPDPFQESDLFAKLDAFEFEA--PPAVPAPSIPNLATETKAN 688
Cdd:PRK12727  165 qlfadfLTTAPVPRAPVQAPVVAAPAPV-PAIAAALAAHAAYAQDDDEQLDDDGFDLDDalPQILPPAALPPIVVAPAAP 243

                         170       180
                  ....*....|....*....|.
gi 23093316   689 VFNGPLQVQLP-PEKELQLQQ 708
Cdd:PRK12727  244 AALAAVAAAAPaPQNDEELKQ 264
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 35-181 1.13e-87

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: 282.22  E-value: 1.13e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   35 AKHRNDPGRFFGDGVQFKAKLIGILEVGEARGDRMCQEALQDLKMAIRAAGEHKQRITIHVTIDGLRLRDEKTGDSLYHH 114
Cdd:cd01215    2 KTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHHH 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23093316  115 PVHKISFIAQDMTDSRAFGYIFGSpDSGHRFFGIKTDKAASQVVLAMRDLFQVVFELKKKEIEMARQ 181
Cdd:cd01215   82 PVHKISFIARDTTDNRAFGYVCGL-DGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 46-178 2.90e-37

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: 137.45  E-value: 2.90e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316      46 GDGVQFKAKLIGILEVGEARGDRMCQEALQDLKMAIRAAGEHKQRITIHVTIDGLRLRDEKTGDSLYHHPVHKISFIAQD 125
Cdd:smart00462    1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 23093316     126 MTDSRAFGYIFGSPDSG-HRFFGIKTDKAASQVVLAMRDLFQVVFELKKKEIEM 178
Cdd:smart00462   81 PDDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 49-165 4.12e-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: 82.17  E-value: 4.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   49 VQFKAKLIGILEVGEARGDRMCQEALQDLKMAIRAAGEHKQRITIHVTIDGLRLRDEKTGDSLYHHPVHKISFIAQDMTD 128
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 23093316  129 SRAFGYIFGSPD-SGHRFFGIKTDKA--ASQVVLAMRDLF 165
Cdd:cd00934   81 PNVFAFIAGEEGgSGFRCHVFQCEDEeeAEEILQAIGQAF 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 49-180 7.21e-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: 79.24  E-value: 7.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   49 VQFKAKLIGILEVGEARGDRMCQEALQDLKMA--IRAAGEHK-QRITIHVTIDGLRLRDEKTGDSLYHHPVHKISFIAQD 125
Cdd:cd01273   12 VAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFArqLKKSEGAKlPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADD 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 23093316  126 MTDSRAFGYIFGSPDSG-HRFFGIKTDKAASQVVLAMRDLFQVVFelkKKEIEMAR 180
Cdd:cd01273   92 KTDKRIFSFIAKDSESEkHLCFVFDSEKLAEEITLTIGQAFDLAY---RRFLESNG 144
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 51-135 4.71e-16

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: 76.96  E-value: 4.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   51 FKAKLIGILEVGEARGDRMCQEALqdlkMAIRAAGEHKQRITIHVTIDGLRLRDEKTGDSLYHHPVHKISFIAQDMTDSR 130
Cdd:cd01268   17 FPVKYLGCVEVGESRGMQVCEEAL----KKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRNHER 92


                 ....*
gi 23093316  131 AFGYI 135
Cdd:cd01268   93 AFSYI 97
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 51-170 4.24e-09

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: 56.49  E-value: 4.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   51 FKAKLIGILEVGEARGDRMCQEALqdlkMAIRAAGEHKQRITIHVTIDGLRLRDEKTGDSLYHHPVHKISFIAQDMTDSR 130
Cdd:cd13161    4 FEAKYLGSVPVKEPKGNDVVMAAV----KRLKDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 23093316  131 AFGYIFGSPDSG----HRFfgiKTDKAASQVVLAMRDLFQVVFE 170
Cdd:cd13161   80 LFAFISHDPRLGritcHVF---RCKRGAQEICDTIAEAFKAAAE 120
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
51-167 2.65e-08

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 54.68  E-value: 2.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316     51 FKAKLIGILEVGEARG----DRM--CQEALQDLKMAIRAAGEHK-------QRITIHVTIDGLRLRDEKTGDSLYHHPVH 117
Cdd:pfam00640    1 FAVRYLGSVEVPEERApdknTRMqqAREAIRRVKAAKINKIRGLsgetgpgTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 23093316    118 KISFIA-QDMTDSRAFGYIFGSPDSG----HRFfgiKTDKAASQVVLAMRDLFQV 167
Cdd:pfam00640   81 SISFCAdGDPDLMRYFAYIARDKATNkfacHVF---ESEDGAQDIAQSIGQAFAL 132
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 44-135 3.26e-08

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: 55.37  E-value: 3.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   44 FFGDGVQFKAKLIGILEVGEArGDRMcqEALQDLKmAIR----AAGEHKQRITIHVTIDGLRL-------RDEKTGDS-- 110
Cdd:cd01270   24 AFQHGITFQAKYIGSLEVPRP-SSRV--EIVAAMR-RIRyefkAKNIKKKKVTITVSVDGVKVvlrkkkkKKGWTWDEsk 99

                         90       100
                 ....*....|....*....|....*..
gi 23093316  111 --LYHHPVHKISFIAQDMTDSRAFGYI 135
Cdd:cd01270  100 llLMQHPIYRIFYVSHDSQDLKIFSYI 126
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 47-166 2.54e-07

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: 51.56  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   47 DGVQFKAKLIGILEVGEARGDRMCQEALQD-LKMAiRAAGEHKQRITIHVTIDGLRLRDEKTGDSLYHHPVHKISFIAQD 125
Cdd:cd13159    1 DGVTFYLKYLGSTLVEKPKGEGATAEAVKTiIAMA-KASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTAD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 23093316  126 MTDSRAFGYIFGSPDSG----HRFFGIKTdKAASQVVLAMRDLFQ 166
Cdd:cd13159   80 ANHDKVFAFIATNQDNEklecHAFLCAKR-KMAQAVTLTVAQAFN 123
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 38-171 2.10e-05

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: 46.50  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   38 RNDPGRFFGDGVQFKAKLIGILEVGEARGDRMCQEALQDLKMAIRaagEHKQ--RITIHVTIDGLRLRDEKTGDSLYHHP 115
Cdd:cd01274    4 RHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTR---EMKKipTIILSISYKGVKFIDATTKNLICEHE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 23093316  116 VHKISFIAQDMTDSRAFGYIFGSPDSGHRF---FGIKTDKAASQVVLAMRDLFQVVFEL 171
Cdd:cd01274   81 IRNISCACQDPEDLNTFAYITKDLKTDHHYchvFCVLTVDLATEIILTLGQAFEVAYQL 139
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
542-708 2.43e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 43.05  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   542 PQQNSANTLTSTASTAASLGQ-LLSTVALN---PDPLPAPISIPTSISHSITPSAELKLLLGHVTNPPNPTgHYYTTEP- 616
Cdd:PRK12727   86 PLKLSANANMSQRQRVASAAEdMIAAMALRqpvSVPRQAPAAAPVRAASIPSPAAQALAHAAAVRTAPRQE-HALSAVPe 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23093316   617 ------PTLNSLENPHPPADPVLLPRDTdPFSPTRKKSDPDPFQESDLFAKLDAFEFEA--PPAVPAPSIPNLATETKAN 688
Cdd:PRK12727  165 qlfadfLTTAPVPRAPVQAPVVAAPAPV-PAIAAALAAHAAYAQDDDEQLDDDGFDLDDalPQILPPAALPPIVVAPAAP 243

                         170       180
                  ....*....|....*....|.
gi 23093316   689 VFNGPLQVQLP-PEKELQLQQ 708
Cdd:PRK12727  244 AALAAVAAAAPaPQNDEELKQ 264
 
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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