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Conserved domains on  [gi|1676324136|dbj|BBD83807|]
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ced-6, partial [Drosophila fuyamai]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15493994

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 ...
 1-102 6.71e-42

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 cd01273:

Pssm-ID: 473070  Cd Length: 144  Bit Score: 142.03  E-value: 6.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136   1 VAIQEPRTHKILHQFPLYNISYCADEKGVKKFFSFIAKSTKTrdgcdpqtnghangngdgsakveESHECFVFISNKLAS 80
Cdd:cd01273    66 VKIQDPKTKVIMHQFPLHRISFCADDKTDKRIFSFIAKDSES-----------------------EKHLCFVFDSEKLAE 122

                          90       100
                  ....*....|....*....|..
gi 1676324136  81 DITLTIGQAFDLAYRKYMDSTE 102
Cdd:cd01273   123 EITLTIGQAFDLAYRRFLESNG 144
 
Name Accession Description Interval E-value
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 1-102 6.71e-42

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: 142.03  E-value: 6.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136   1 VAIQEPRTHKILHQFPLYNISYCADEKGVKKFFSFIAKSTKTrdgcdpqtnghangngdgsakveESHECFVFISNKLAS 80
Cdd:cd01273    66 VKIQDPKTKVIMHQFPLHRISFCADDKTDKRIFSFIAKDSES-----------------------EKHLCFVFDSEKLAE 122

                          90       100
                  ....*....|....*....|..
gi 1676324136  81 DITLTIGQAFDLAYRKYMDSTE 102
Cdd:cd01273   123 EITLTIGQAFDLAYRRFLESNG 144
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1-102 3.51e-13

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: 65.41  E-value: 3.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136    1 VAIQEPRTHKILHQFPLYNISYCADEKGVKKFFSFIAKSTKTRDgcdpqtnghangngdgsakveesHECFVFISNKLAS 80
Cdd:smart00462  55 VKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGSSR-----------------------FACHVFRCEKAAE 111

                           90       100
                   ....*....|....*....|..
gi 1676324136   81 DITLTIGQAFDLAYRKYMDSTE 102
Cdd:smart00462 112 DIALAIGQAFQLAYELKLKARS 133
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
1-93 1.01e-11

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 61.61  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136   1 VAIQEPRTHKILHQFPLYNISYCAD-EKGVKKFFSFIAKstktrdgcDPQTNGHAngngdgsakveesheCFVFISNKLA 79
Cdd:pfam00640  63 LKLLNPDTQELIHDHPLVSISFCADgDPDLMRYFAYIAR--------DKATNKFA---------------CHVFESEDGA 119

                          90
                  ....*....|....
gi 1676324136  80 SDITLTIGQAFDLA 93
Cdd:pfam00640 120 QDIAQSIGQAFALA 133
 
Name Accession Description Interval E-value
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 1-102 6.71e-42

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: 142.03  E-value: 6.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136   1 VAIQEPRTHKILHQFPLYNISYCADEKGVKKFFSFIAKSTKTrdgcdpqtnghangngdgsakveESHECFVFISNKLAS 80
Cdd:cd01273    66 VKIQDPKTKVIMHQFPLHRISFCADDKTDKRIFSFIAKDSES-----------------------EKHLCFVFDSEKLAE 122

                          90       100
                  ....*....|....*....|..
gi 1676324136  81 DITLTIGQAFDLAYRKYMDSTE 102
Cdd:cd01273   123 EITLTIGQAFDLAYRRFLESNG 144
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1-102 3.51e-13

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: 65.41  E-value: 3.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136    1 VAIQEPRTHKILHQFPLYNISYCADEKGVKKFFSFIAKSTKTRDgcdpqtnghangngdgsakveesHECFVFISNKLAS 80
Cdd:smart00462  55 VKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGSSR-----------------------FACHVFRCEKAAE 111

                           90       100
                   ....*....|....*....|..
gi 1676324136   81 DITLTIGQAFDLAYRKYMDSTE 102
Cdd:smart00462 112 DIALAIGQAFQLAYELKLKARS 133
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 1-90 7.29e-12

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: 61.37  E-value: 7.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136   1 VAIQEPRTHKILHQFPLYNISYCADEKGVKKFFSFIAKstktrdgcdpqtngHANGNGdgsakveesHECFVFISNK--L 78
Cdd:cd00934    52 VKLLDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAG--------------EEGGSG---------FRCHVFQCEDeeE 108

                          90
                  ....*....|..
gi 1676324136  79 ASDITLTIGQAF 90
Cdd:cd00934   109 AEEILQAIGQAF 120
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
1-93 1.01e-11

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 61.61  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136   1 VAIQEPRTHKILHQFPLYNISYCAD-EKGVKKFFSFIAKstktrdgcDPQTNGHAngngdgsakveesheCFVFISNKLA 79
Cdd:pfam00640  63 LKLLNPDTQELIHDHPLVSISFCADgDPDLMRYFAYIAR--------DKATNKFA---------------CHVFESEDGA 119

                          90
                  ....*....|....
gi 1676324136  80 SDITLTIGQAFDLA 93
Cdd:pfam00640 120 QDIAQSIGQAFALA 133
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 8-90 4.31e-08

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains mammals, insects, and sponges.


Pssm-ID: 269981  Cd Length: 123  Bit Score: 50.79  E-value: 4.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136   8 THKILHQFPLYNISYCADEKGVKKFFSFIAKStktrdgcdpqtnghangngdgsaKVEESHECFVFI--SNKLASDITLT 85
Cdd:cd13159    61 TNETILEVSIYRISYCTADANHDKVFAFIATN-----------------------QDNEKLECHAFLcaKRKMAQAVTLT 117


                  ....*
gi 1676324136  86 IGQAF 90
Cdd:cd13159   118 VAQAF 122
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 18-95 3.54e-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: 48.82  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136  18 YNISYCADEKGVKKFFSFIAKSTKTRdgcdpqtnghangngdgsakveeSHECFVF--ISNKLASDITLTIGQAFDLAYR 95
Cdd:cd01274    82 RNISCACQDPEDLNTFAYITKDLKTD-----------------------HHYCHVFcvLTVDLATEIILTLGQAFEVAYQ 138
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 3-95 2.28e-04

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: 40.31  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136   3 IQEPRTHKILHQFPLYNISY-CADEKGvKKFFSFIAKSTKTRdgcdpqtnghangngdgsakveeSHECFVFISNKLASD 81
Cdd:cd13161    51 VVERLTGEVLTNVPIKDISFvTVDPKD-KKLFAFISHDPRLG-----------------------RITCHVFRCKRGAQE 106

                          90
                  ....*....|....
gi 1676324136  82 ITLTIGQAFDLAYR 95
Cdd:cd13161   107 ICDTIAEAFKAAAE 120
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 69-98 3.98e-03

Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine kinases, which can interact with phosphoproteins at NPXY motifs. Shc contains an PTB domain followed by an 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. This cd is part of the Shc-like subgroup.


Pssm-ID: 269920  Cd Length: 170  Bit Score: 37.57  E-value: 3.98e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1676324136  69 ECFVF-ISNKLASDITLTIGQAFDLAYRKYM 98
Cdd:cd01209   139 ACHVLeCGDGLAQDVIATIGQAFELRFKQYL 169
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
 5-89 7.33e-03

Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called DCC-interacting protein (DIP)-13alpha) Phosphotyrosine-binding (PTB) domain; APPL interacts with oncoprotein serine/threonine kinase AKT2, tumor suppressor protein DCC (deleted in colorectal cancer), Rab5, GIPC (GAIP-interacting protein, C terminus), human follicle-stimulating hormone receptor (FSHR), and the adiponectin receptors AdipoR1 and AdipoR2. There are two isoforms of human APPL: APPL1 and APPL2, which share about 50% sequence identity. APPL has a BAR and a PH domain near its N terminus, and the two domains are thought to function as a unit (BAR-PH domain). C-terminal to this is a PTB domain. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. 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: 269980  Cd Length: 135  Bit Score: 36.17  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324136   5 EPRTHKILHQFPLYNISYCADEKGVKKFFSFIAKSTKTRDGcdpqtnghangngdgsakvEESHECFVFISNKLASDITL 84
Cdd:cd13158    67 DPQTQVTRARFPLADVVQFAAHQENKRLFGFVVRTPEGDGE-------------------EPSFSCYVFESNTEGEKICD 127


                  ....*
gi 1676324136  85 TIGQA 89
Cdd:cd13158   128 AIALA 132
 
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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