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Conserved domains on  [gi|528479250|ref|XP_005171876|]
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dab, mitogen-responsive phosphoprotein, homolog 2 isoform X1 [Danio rerio]

Protein Classification

PTB_Dab and Med15 domain-containing protein( domain architecture ID 11542635)

PTB_Dab and Med15 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 47-196 1.76e-96

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: 296.47  E-value: 1.76e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  47 EKTDEFLLARFQGDGVRYKAKLIGVDDVQDARGDKMCQDSMMKLKGMAIAArsqGKHKQRIWINISLTGIKIVDEKTGVI 126
Cdd:cd01215    1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGAL 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 127 EHEHVVNKISFIARDVTDNRAFGYVCGAEGQHQFFAIKTAQQAEPLVIDLKDLFQLIFNMKKKEQEAGQK 196
Cdd:cd01215   78 LHHHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PPE super family cl35037
PPE-repeat protein [Function unknown];
398-600 7.77e-06

PPE-repeat protein [Function unknown];


The actual alignment was detected with superfamily member COG5651:

Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 49.12  E-value: 7.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 398 PPVLQAPLCNGSNKQLALFQTNPSTTVQNGGLTALCPPPQNLKPRCARRREKSPGNDLFGsglFAPPAQNESQASNQNAS 477
Cdd:COG5651  171 PPTITNPGGLLGAQNAGSGNTSSNPGFANLGLTGLNQVGIGGLNSGSGPIGLNSGPGNTG---FAGTGAAAGAAAAAAAA 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 478 IPADLFNSTPSSTINAFGSMSLGHAPGTAPVS---------WGQTPTMFPPQAGVQVTIPGPPRPFPQPSAFGGLSAPAW 548
Cdd:COG5651  248 AAAAGAGASAALASLAATLLNASSLGLAATAAssaatnlglAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGAA 327

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528479250 549 GQQGASPFGPPAGTQAWGQPGAAAPVGTWPAPGPVASPFQPNQFAPMMPPNA 600
Cdd:COG5651  328 LGAGAAAAAAGAAAGAGAAAAAAAGGAGGGGGGALGAGGGGGSAGAAAGAAS 379
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 47-196 1.76e-96

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: 296.47  E-value: 1.76e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  47 EKTDEFLLARFQGDGVRYKAKLIGVDDVQDARGDKMCQDSMMKLKGMAIAArsqGKHKQRIWINISLTGIKIVDEKTGVI 126
Cdd:cd01215    1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGAL 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 127 EHEHVVNKISFIARDVTDNRAFGYVCGAEGQHQFFAIKTAQQAEPLVIDLKDLFQLIFNMKKKEQEAGQK 196
Cdd:cd01215   78 LHHHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 59-192 3.16e-26

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: 104.32  E-value: 3.16e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250    59 GDGVRYKAKLIGVDDVQDARGDKMCQDSMMKLKGmaiAARSQGKHKQRIWINISLTGIKIVDEKTGVIEHEHVVNKISFI 138
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRA---AQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFC 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 528479250   139 ARDVTDNRAFGYVCGAEGQ--HQFFAIKTAQQAEPLVIDLKDLFQLIFNMKKKEQE 192
Cdd:smart00462  78 AVGPDDLDVFGYIARDPGSsrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARS 133
PPE COG5651
PPE-repeat protein [Function unknown];
398-600 7.77e-06

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 49.12  E-value: 7.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 398 PPVLQAPLCNGSNKQLALFQTNPSTTVQNGGLTALCPPPQNLKPRCARRREKSPGNDLFGsglFAPPAQNESQASNQNAS 477
Cdd:COG5651  171 PPTITNPGGLLGAQNAGSGNTSSNPGFANLGLTGLNQVGIGGLNSGSGPIGLNSGPGNTG---FAGTGAAAGAAAAAAAA 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 478 IPADLFNSTPSSTINAFGSMSLGHAPGTAPVS---------WGQTPTMFPPQAGVQVTIPGPPRPFPQPSAFGGLSAPAW 548
Cdd:COG5651  248 AAAAGAGASAALASLAATLLNASSLGLAATAAssaatnlglAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGAA 327

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528479250 549 GQQGASPFGPPAGTQAWGQPGAAAPVGTWPAPGPVASPFQPNQFAPMMPPNA 600
Cdd:COG5651  328 LGAGAAAAAAGAAAGAGAAAAAAAGGAGGGGGGALGAGGGGGSAGAAAGAAS 379
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
83-160 1.38e-04

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 42.35  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250   83 CQDSMMKLKgMAIAARSQGKH-----KQRIWINISLTGIKIVDEKTGVIEHEHVVNKISFIA-RDVTDNRAFGYVCGAEG 156
Cdd:pfam00640  26 AREAIRRVK-AAKINKIRGLSgetgpGTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAdGDPDLMRYFAYIARDKA 104


                  ....
gi 528479250  157 QHQF 160
Cdd:pfam00640 105 TNKF 108
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 406-607 2.84e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 44.61  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  406 CNGSNKQLALFQTNPSTTVQNGGLTALCPPPQNLKPRCARRREKSPGNDLFGSGLFAPPAQNES---QASNQNASIpadl 482
Cdd:pfam09606  52 DMSKKAAQQQQPQGGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGgpgTASNLLASL---- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  483 fnSTPSSTINAFGSMSLGHAPGTAPVSwGQTPTMFPPQAGVQVTIPGPPRPFPQPSAFGGLSAPAWGQQGASPFGPPAGT 562
Cdd:pfam09606 128 --GRPQMPMGGAGFPSQMSRVGRMQPG-GQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQM 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 528479250  563 QAWGQPGAAAPVGTWPAPGPVASPFQPNQFAPMMPPNAMMGMQQG 607
Cdd:pfam09606 205 GVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ 249
PHA03378 PHA03378
EBNA-3B; Provisional
 434-599 4.51e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.82  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 434 PPPQNLKPRCARRREKSPGNDLFGSGLFAPPAQNESQASNQNASIPADLFNSTPSstiNAFGSMSLGHAPGTAPVSwGQT 513
Cdd:PHA03378 625 PMPLRPIPMRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPT---GANTMLPIQWAPGTMQPP-PRA 700

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 514 PTMFPPQAGVQVTIPGPPRPFPQPSAFGGLSAPAWGQQGA-SPFGPPAGTQAWGQPGAAAPVgtwPAPGPVASPFQPnqf 592
Cdd:PHA03378 701 PTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAApGRARPPAAAPGRARPPAAAPG---RARPPAAAPGAP--- 774


                 ....*..
gi 528479250 593 APMMPPN 599
Cdd:PHA03378 775 TPQPPPQ 781
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 47-196 1.76e-96

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: 296.47  E-value: 1.76e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  47 EKTDEFLLARFQGDGVRYKAKLIGVDDVQDARGDKMCQDSMMKLKGMAIAArsqGKHKQRIWINISLTGIKIVDEKTGVI 126
Cdd:cd01215    1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGAL 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 127 EHEHVVNKISFIARDVTDNRAFGYVCGAEGQHQFFAIKTAQQAEPLVIDLKDLFQLIFNMKKKEQEAGQK 196
Cdd:cd01215   78 LHHHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 59-192 3.16e-26

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: 104.32  E-value: 3.16e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250    59 GDGVRYKAKLIGVDDVQDARGDKMCQDSMMKLKGmaiAARSQGKHKQRIWINISLTGIKIVDEKTGVIEHEHVVNKISFI 138
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRA---AQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFC 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 528479250   139 ARDVTDNRAFGYVCGAEGQ--HQFFAIKTAQQAEPLVIDLKDLFQLIFNMKKKEQE 192
Cdd:smart00462  78 AVGPDDLDVFGYIARDPGSsrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARS 133
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 62-180 1.20e-20

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: 87.95  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  62 VRYKAKLIGVDDVQDARGDKMCQDSmmkLKGMAIAARSQGKHKQRIWINISLTGIKIVDEKTGVIEHEHVVNKISFIARD 141
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEA---LKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 528479250 142 VTDNRAFGYVCGAEGQHQF----FAIKTAQQAEPLVIDLKDLF 180
Cdd:cd00934   78 PDNPNVFAFIAGEEGGSGFrchvFQCEDEEEAEEILQAIGQAF 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 62-182 7.55e-14

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: 69.23  E-value: 7.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  62 VRYKAKLIGVDDVQDARGDKMCQDSMMKLKGMAIAARSQGKHKQRIWINISLTGIKIVDEKTGVIEHEHVVNKISFIARD 141
Cdd:cd01273   12 VAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADD 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 528479250 142 VTDNRAFGYVC--GAEGQHQFFAIKTAQQAEPLVIDLKDLFQL 182
Cdd:cd01273   92 KTDKRIFSFIAkdSESEKHLCFVFDSEKLAEEITLTIGQAFDL 134
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 64-164 3.44e-10

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: 58.47  E-value: 3.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  64 YKAKLIGVDDVQDARGDKMCQDSMMKLkgmaiaaRSQGKHKQRIWINISLTGIKIVDEKTGVIEHEHVVNKISFIARDVT 143
Cdd:cd01268   17 FPVKYLGCVEVGESRGMQVCEEALKKL-------KASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRN 89

                         90       100
                 ....*....|....*....|....*..
gi 528479250 144 DNRAFGYVCgAEGQ------HQFFAIK 164
Cdd:cd01268   90 HERAFSYIC-RDGTtrrwmcHCFLAVK 115
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 43-191 4.51e-08

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: 52.67  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  43 RKIPEKtdefLLArfqgDGVRYKAKLIGVDDVQDARGDKMCQDSMMKLKgmaiaaRSQGKHKQ--RIWINISLTGIKIVD 120
Cdd:cd01274    4 RHSPEK----LIT----GSVNYEAHYLGSTEIKELRGTESTKKAIQKLK------KSTREMKKipTIILSISYKGVKFID 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528479250 121 EKTGVIEHEHVVNKISFIARDVTDNRAFGYVC-GAEGQHQF---FAIKTAQQAEPLVIDLKDLFQLIFNMKKKEQ 191
Cdd:cd01274   70 ATTKNLICEHEIRNISCACQDPEDLNTFAYITkDLKTDHHYchvFCVLTVDLATEIILTLGQAFEVAYQLALRAQ 144
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 60-159 1.94e-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: 50.41  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  60 DGVRYKAKLIGVDDVQDARGDKMCQDSmmkLKGMAIAARSQGKHKQRIWINISLTGIKIVDEKTGVIEHEHVVNKISFIA 139
Cdd:cd13159    1 DGVTFYLKYLGSTLVEKPKGEGATAEA---VKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCT 77

                         90       100
                 ....*....|....*....|
gi 528479250 140 RDVTDNRAFGYVcGAEGQHQ 159
Cdd:cd13159   78 ADANHDKVFAFI-ATNQDNE 96
PPE COG5651
PPE-repeat protein [Function unknown];
398-600 7.77e-06

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 49.12  E-value: 7.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 398 PPVLQAPLCNGSNKQLALFQTNPSTTVQNGGLTALCPPPQNLKPRCARRREKSPGNDLFGsglFAPPAQNESQASNQNAS 477
Cdd:COG5651  171 PPTITNPGGLLGAQNAGSGNTSSNPGFANLGLTGLNQVGIGGLNSGSGPIGLNSGPGNTG---FAGTGAAAGAAAAAAAA 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 478 IPADLFNSTPSSTINAFGSMSLGHAPGTAPVS---------WGQTPTMFPPQAGVQVTIPGPPRPFPQPSAFGGLSAPAW 548
Cdd:COG5651  248 AAAAGAGASAALASLAATLLNASSLGLAATAAssaatnlglAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGAA 327

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528479250 549 GQQGASPFGPPAGTQAWGQPGAAAPVGTWPAPGPVASPFQPNQFAPMMPPNA 600
Cdd:COG5651  328 LGAGAAAAAAGAAAGAGAAAAAAAGGAGGGGGGALGAGGGGGSAGAAAGAAS 379
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 63-152 2.68e-05

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: 44.16  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  63 RYKAKLIGVDDVQDARGDKMCQDSMMKLkgmaiaaRSQGKHKQRIWINISLTGIKIVDEKTGVIEHEHVVNKISFIARDV 142
Cdd:cd13161    3 VFEAKYLGSVPVKEPKGNDVVMAAVKRL-------KDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDP 75

                         90
                 ....*....|
gi 528479250 143 TDNRAFGYVC 152
Cdd:cd13161   76 KDKKLFAFIS 85
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
83-160 1.38e-04

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 42.35  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250   83 CQDSMMKLKgMAIAARSQGKH-----KQRIWINISLTGIKIVDEKTGVIEHEHVVNKISFIA-RDVTDNRAFGYVCGAEG 156
Cdd:pfam00640  26 AREAIRRVK-AAKINKIRGLSgetgpGTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAdGDPDLMRYFAYIARDKA 104


                  ....
gi 528479250  157 QHQF 160
Cdd:pfam00640 105 TNKF 108
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 406-607 2.84e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 44.61  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  406 CNGSNKQLALFQTNPSTTVQNGGLTALCPPPQNLKPRCARRREKSPGNDLFGSGLFAPPAQNES---QASNQNASIpadl 482
Cdd:pfam09606  52 DMSKKAAQQQQPQGGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGgpgTASNLLASL---- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250  483 fnSTPSSTINAFGSMSLGHAPGTAPVSwGQTPTMFPPQAGVQVTIPGPPRPFPQPSAFGGLSAPAWGQQGASPFGPPAGT 562
Cdd:pfam09606 128 --GRPQMPMGGAGFPSQMSRVGRMQPG-GQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQM 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 528479250  563 QAWGQPGAAAPVGTWPAPGPVASPFQPNQFAPMMPPNAMMGMQQG 607
Cdd:pfam09606 205 GVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ 249
PHA03378 PHA03378
EBNA-3B; Provisional
 434-599 4.51e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.82  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 434 PPPQNLKPRCARRREKSPGNDLFGSGLFAPPAQNESQASNQNASIPADLFNSTPSstiNAFGSMSLGHAPGTAPVSwGQT 513
Cdd:PHA03378 625 PMPLRPIPMRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPT---GANTMLPIQWAPGTMQPP-PRA 700

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479250 514 PTMFPPQAGVQVTIPGPPRPFPQPSAFGGLSAPAWGQQGA-SPFGPPAGTQAWGQPGAAAPVgtwPAPGPVASPFQPnqf 592
Cdd:PHA03378 701 PTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAApGRARPPAAAPGRARPPAAAPG---RARPPAAAPGAP--- 774


                 ....*..
gi 528479250 593 APMMPPN 599
Cdd:PHA03378 775 TPQPPPQ 781
 
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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