NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|20070356|ref|NP_003735|]
View 

protein numb homolog isoform 3 [Homo sapiens]

Protein Classification

numb family protein( domain architecture ID 10101010)

numb family protein similar to protein numb, a membrane associated adaptor protein that is required in determination of cell fate during sensory organ formation in embryos

Gene Ontology:  GO:0050767|GO:0005515
PubMed:  15567406|8987385|10610414

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 23-157 1.85e-104

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: 312.32  E-value: 1.85e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  23 HQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKATGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEK 102
Cdd:cd01268   1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20070356 103 VSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLER 157
Cdd:cd01268  81 VSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 247-327 7.54e-38

NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB domain..


:

Pssm-ID: 461874  Cd Length: 95  Bit Score: 135.29  E-value: 7.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   247 PHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDF-----------PIKNAVPEVEG---E 312
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPsseQ 80

                          90
                  ....*....|....*
gi 20070356   313 AESISSLCSQITNAF 327
Cdd:pfam06311  81 ADSISAMCQQISSGL 95
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 332-513 1.20e-04

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   332 DPF-SSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAHTALAPVAMPVREtnpWAHAPDAANKEIAATCSGTEWGQSS 410
Cdd:PRK10263  308 DPLlNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVA---WQPVPGPQTGEPVIAPAPEGYPQQS 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   411 GAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQgnafltSQPVPVGVVPAL 490
Cdd:PRK10263  385 QYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNA------WQAEEQQSTFAP 458

                         170       180
                  ....*....|....*....|....*
gi 20070356   491 QPAFVPAQSY--PVANGMPYPAPNV 513
Cdd:PRK10263  459 QSTYQTEQTYqqPAAQEPLYQQPQP 483
 
Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 23-157 1.85e-104

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: 312.32  E-value: 1.85e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  23 HQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKATGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEK 102
Cdd:cd01268   1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20070356 103 VSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLER 157
Cdd:cd01268  81 VSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 247-327 7.54e-38

NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB domain..


Pssm-ID: 461874  Cd Length: 95  Bit Score: 135.29  E-value: 7.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   247 PHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDF-----------PIKNAVPEVEG---E 312
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPsseQ 80

                          90
                  ....*....|....*
gi 20070356   313 AESISSLCSQITNAF 327
Cdd:pfam06311  81 ADSISAMCQQISSGL 95
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
39-154 6.76e-36

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 131.33  E-value: 6.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356    39 FPVKYLGHVEVDESR------GMHICEDAVKRLKATGKKA-----------VKAVLWVSADGLRVVDEKTKDLIVDQTIE 101
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKINKirglsgetgpgTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 20070356   102 KVSFCAP-DRNFDRAFSYICRDGTTRRWICHCFMAVKDtGERLSHAVGCAFAAC 154
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNKFACHVFESEDG-AQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 37-164 1.81e-33

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: 124.73  E-value: 1.81e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356     37 CSFPVKYLGHVEVDESRGMHICEDAVKRLKAT----GKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNF 112
Cdd:smart00462   4 VSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAqgseKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDD 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 20070356    113 DRAFSYICRDGTTRRWICHCFMAVKDTGErLSHAVGCAFAACLERKQKREKE 164
Cdd:smart00462  84 LDVFGYIARDPGSSRFACHVFRCEKAAED-IALAIGQAFQLAYELKLKARSE 134
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 332-513 1.20e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   332 DPF-SSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAHTALAPVAMPVREtnpWAHAPDAANKEIAATCSGTEWGQSS 410
Cdd:PRK10263  308 DPLlNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVA---WQPVPGPQTGEPVIAPAPEGYPQQS 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   411 GAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQgnafltSQPVPVGVVPAL 490
Cdd:PRK10263  385 QYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNA------WQAEEQQSTFAP 458

                         170       180
                  ....*....|....*....|....*
gi 20070356   491 QPAFVPAQSY--PVANGMPYPAPNV 513
Cdd:PRK10263  459 QSTYQTEQTYqqPAAQEPLYQQPQP 483
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 412-578 3.36e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 40.79  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   412 AASPGLFQAGHRRTPSeadrwLEEVSKSVRAQ----QPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVV 487
Cdd:pfam09770 180 AAQPASLPAPSRKMMS-----LEEVEAAMRAQakkpAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQ 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   488 PALQPAFVPA-----QSYPVANGMPYPAP-------NVPVVGITPSQMVAN--VFGTAGHPQAAHPHQSPSLVRQQTFPH 553
Cdd:pfam09770 255 QHPGQGHPVTilqrpQSPQPDPAQPSIQPqaqqfhqQPPPVPVQPTQILQNpnRLSAARVGYPQNPQPGVQPAPAHQAHR 334

                         170       180
                  ....*....|....*....|....*....
gi 20070356   554 YEASSATTSPFFKPPAQHLNGS----AAF 578
Cdd:pfam09770 335 QQGSFGRQAPIITHPQQLAQLSeeekAAY 363
 
Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 23-157 1.85e-104

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: 312.32  E-value: 1.85e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  23 HQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKATGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEK 102
Cdd:cd01268   1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20070356 103 VSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLER 157
Cdd:cd01268  81 VSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 247-327 7.54e-38

NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB domain..


Pssm-ID: 461874  Cd Length: 95  Bit Score: 135.29  E-value: 7.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   247 PHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDF-----------PIKNAVPEVEG---E 312
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPsseQ 80

                          90
                  ....*....|....*
gi 20070356   313 AESISSLCSQITNAF 327
Cdd:pfam06311  81 ADSISAMCQQISSGL 95
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
39-154 6.76e-36

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 131.33  E-value: 6.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356    39 FPVKYLGHVEVDESR------GMHICEDAVKRLKATGKKA-----------VKAVLWVSADGLRVVDEKTKDLIVDQTIE 101
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKINKirglsgetgpgTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 20070356   102 KVSFCAP-DRNFDRAFSYICRDGTTRRWICHCFMAVKDtGERLSHAVGCAFAAC 154
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNKFACHVFESEDG-AQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 37-164 1.81e-33

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: 124.73  E-value: 1.81e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356     37 CSFPVKYLGHVEVDESRGMHICEDAVKRLKAT----GKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNF 112
Cdd:smart00462   4 VSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAqgseKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDD 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 20070356    113 DRAFSYICRDGTTRRWICHCFMAVKDTGErLSHAVGCAFAACLERKQKREKE 164
Cdd:smart00462  84 LDVFGYIARDPGSSRFACHVFRCEKAAED-IALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 37-151 1.11e-26

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: 104.90  E-value: 1.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  37 CSFPVKYLGHVEVDESRGMHICEDAVKRLKAT----GKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNF 112
Cdd:cd00934   1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAAlkssKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 20070356 113 DRAFSYICRDGTTRRWICHCFMAV-KDTGERLSHAVGCAF 151
Cdd:cd00934  81 PNVFAFIAGEEGGSGFRCHVFQCEdEEEAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 39-156 1.39e-25

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: 101.94  E-value: 1.39e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  39 FPVKYLGHVEVDESRGMHICEDAVKRLKATGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSY 118
Cdd:cd13161   4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAF 83

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 20070356 119 ICRDGTTRRWICHCFMaVKDTGERLSHAVGCAFAACLE 156
Cdd:cd13161  84 ISHDPRLGRITCHVFR-CKRGAQEICDTIAEAFKAAAE 120
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 38-151 1.50e-19

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: 84.69  E-value: 1.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  38 SFPVKYLGHVEVDESRGMHICEDAVKR----LKATGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFD 113
Cdd:cd13159   4 TFYLKYLGSTLVEKPKGEGATAEAVKTiiamAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADANHD 83

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 20070356 114 RAFSYICRDGTTRRWICHCFMAVK-DTGERLSHAVGCAF 151
Cdd:cd13159  84 KVFAFIATNQDNEKLECHAFLCAKrKMAQAVTLTVAQAF 122
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 35-151 2.81e-19

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: 84.64  E-value: 2.81e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  35 GKCSFPVKYLGHVEVDESRGMHICEDAVKRL-------KATGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCA 107
Cdd:cd01273  10 GHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLkfarqlkKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCA 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 20070356 108 PDRNFDRAFSYICRDGTTRRWICHCFMAVKdTGERLSHAVGCAF 151
Cdd:cd01273  90 DDKTDKRIFSFIAKDSESEKHLCFVFDSEK-LAEEITLTIGQAF 132
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 30-120 3.46e-16

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: 75.75  E-value: 3.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  30 EGVRtgkcsFPVKYLGHVEVDESRGMHICEDAVKRLK----ATGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSF 105
Cdd:cd01215  14 DGVR-----FKAKLIGIDEVPAARGDKMCQDAMMKLKgavkAAGEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISF 88

                        90
                ....*....|....*
gi 20070356 106 CAPDRNFDRAFSYIC 120
Cdd:cd01215  89 IARDTTDNRAFGYVC 103
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 24-137 2.47e-14

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: 70.39  E-value: 2.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  24 QWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKaTGKKAVKAV----LWVSADGLRVVDEKTKDLIVDQT 99
Cdd:cd01274   2 QWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLK-KSTREMKKIptiiLSISYKGVKFIDATTKNLICEHE 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 20070356 100 IEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVK 137
Cdd:cd01274  81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLT 118
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 38-133 9.23e-06

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: 45.40  E-value: 9.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  38 SFPVKYLGHVEVDESRGM-HICEDAVKRLK--ATGKKAVKAVLWVSADGLRVVDEKTKDLIVDQT---IEKVSFCAPDRN 111
Cdd:cd13160   2 VFTVKYLGRMPARGLWGIkHTRKPLVDALKnlPKGKTLPKTKLEVSSDGVKLEELRGGFGSSKTVffpIHTISYGVQDLV 81

                        90       100
                ....*....|....*....|....*
gi 20070356 112 FDRAFSYICR-DGTTRR--WICHCF 133
Cdd:cd13160  82 HTRVFSMIVVgEQDSSNhpFECHAF 106
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 40-161 4.14e-05

Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (pfam00017) domain and a region similar to the tumour suppressor PTEN. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.


Pssm-ID: 429984  Cd Length: 131  Bit Score: 43.49  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356    40 PVKYLGHVEVDESRGMHICEDAVKRLKATGKK----AVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCA---PDRNF 112
Cdd:pfam08416   3 RVEHLTTFELDSLTGLQAVEDAIRKLQLLDAQgrvwTQEMLLQVSDQGITLTDNETKEELESYPLDSISHCQavlNDGRY 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 20070356   113 DRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKR 161
Cdd:pfam08416  83 NSILALVCQEPGQSKPDVHLFQCDELGAELIAEDIESALSDVRLGKPKK 131
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 38-133 8.49e-05

Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. 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: 269970  Cd Length: 138  Bit Score: 43.06  E-value: 8.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  38 SFPVKYLGHVEVDE--------SRGMHICedaVKRLkATGKKAVKAVLWVSADG-----------LRVVDEKTKDLIVDQ 98
Cdd:cd01272   3 RFAVRSLGWVEMAEedltpgksSVAVNNC---IRQL-SYGRNDIRDTVGRWGEGkdmlmvldddtLKLVDPDDRSVLHSQ 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 20070356  99 TIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCF 133
Cdd:cd01272  79 PIHSIRVWGVGRDNGRDFAYVARDKDTRVLKCHVF 113
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 332-513 1.20e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   332 DPF-SSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAHTALAPVAMPVREtnpWAHAPDAANKEIAATCSGTEWGQSS 410
Cdd:PRK10263  308 DPLlNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVA---WQPVPGPQTGEPVIAPAPEGYPQQS 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   411 GAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQgnafltSQPVPVGVVPAL 490
Cdd:PRK10263  385 QYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNA------WQAEEQQSTFAP 458

                         170       180
                  ....*....|....*....|....*
gi 20070356   491 QPAFVPAQSY--PVANGMPYPAPNV 513
Cdd:PRK10263  459 QSTYQTEQTYqqPAAQEPLYQQPQP 483
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 38-164 2.42e-04

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: 42.27  E-value: 2.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  38 SFPVKYLGHVEVDE--SRgMHICEdAVKRL----KATGKKAVKAVLWVSADGLRVVDEKTKD-----------LIVDQTI 100
Cdd:cd01270  30 TFQAKYIGSLEVPRpsSR-VEIVA-AMRRIryefKAKNIKKKKVTITVSVDGVKVVLRKKKKkkgwtwdesklLLMQHPI 107

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20070356 101 EKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMA-VKDTGERLSHAVGCAFAACLERKQKREKE 164
Cdd:cd01270 108 YRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSkKKSQAMRIVRTIGQAFEVCHKLSLQHMQG 172
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 25-133 8.67e-04

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: 40.66  E-value: 8.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  25 WQTDEEGVRTGKCSFPVKYLGHVEVDES-RGM--------------HICEdAVKRLKATGKKAVKAVLW----------- 78
Cdd:cd01209   3 WLHPDQLGMGPGVSYPVRYVGCIEVLQSmRSLdfntrtqvtreainRVCE-AVGGAKGAKRKRKSKALSsilgksnlqfa 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20070356  79 -------VSADGLRVVDEKTKDLIVDQTIEKVSFCA---PDRNFDRAfsYICRDGTTRRwICHCF 133
Cdd:cd01209  82 gmnisltISTDGLNLVTPDTGQIIANHHMQSISFASggdPDTYDYVA--YVAKDPVNQR-ACHVL 143
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 412-578 3.36e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 40.79  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   412 AASPGLFQAGHRRTPSeadrwLEEVSKSVRAQ----QPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVV 487
Cdd:pfam09770 180 AAQPASLPAPSRKMMS-----LEEVEAAMRAQakkpAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQ 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   488 PALQPAFVPA-----QSYPVANGMPYPAP-------NVPVVGITPSQMVAN--VFGTAGHPQAAHPHQSPSLVRQQTFPH 553
Cdd:pfam09770 255 QHPGQGHPVTilqrpQSPQPDPAQPSIQPqaqqfhqQPPPVPVQPTQILQNpnRLSAARVGYPQNPQPGVQPAPAHQAHR 334

                         170       180
                  ....*....|....*....|....*....
gi 20070356   554 YEASSATTSPFFKPPAQHLNGS----AAF 578
Cdd:pfam09770 335 QQGSFGRQAPIITHPQQLAQLSeeekAAY 363
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
407-611 3.87e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  407 GQSSGAASPGLFQAGHRRTPSEAdrwleevsksvrAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGV 486
Cdd:PRK12323 366 GQSGGGAGPATAAAAPVAQPAPA------------AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEAL 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  487 VPALQ--PAFVPAQSYPVANGMPYPAPNVPvvgitpsqmvanvfgtaghPQAAHPHQSPSLVRQQTFPHYEASSATTSPF 564
Cdd:PRK12323 434 AAARQasARGPGGAPAPAPAPAAAPAAAAR-------------------PAAAGPRPVAAAAAAAPARAAPAAAPAPADD 494

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 20070356  565 FKPPAQHLNGSAAFNGVDDGRLASADRHTEV---PTGTCPVDPFEAQWAA 611
Cdd:PRK12323 495 DPPPWEELPPEFASPAPAQPDAAPAGWVAESipdPATADPDDAFETLAPA 544
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 291-574 3.97e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 40.33  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   291 PSTMQRKTdfPIKNAVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAH 370
Cdd:pfam17823 123 PSSAAQSL--PAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAAS 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   371 TALAPVaMPVRETNpwahapdaankeIAATCSGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAA 450
Cdd:pfam17823 201 SAPATL-TPARGIS------------TAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAA 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   451 PLQPVLQPPPPTAISQPASPFQGNAfltSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFG- 529
Cdd:pfam17823 268 GTINMGDPHARRLSPAKHMPSDTMA---RNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTn 344

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 20070356   530 ----TAGHPQAAHPHQSPSLVRQQTF-PHYEASSATTSPFFKPPAQHLNG 574
Cdd:pfam17823 345 lavvTTTKAQAKEPSASPVPVLHTSMiPEVEATSPTTQPSPLLPTQGAAG 394
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 261-624 6.16e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.75  E-value: 6.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   261 ARQGSFRGFPALSQKMSPFKRQLSLRInelPSTMQRKTDFPIKNAvPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMT 340
Cdd:pfam03154 162 AQQQILQTQPPVLQAQSGAASPPSPPP---PGTTQAATAGPTPSA-PSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   341 KPVTVVAPQSPTFQANGTDSAFHVLAKPA-----HTALAPVAMPVRETNPWAHAPDAANKEIAATCSGtewgQSSGAASP 415
Cdd:pfam03154 238 HPQRLPSPHPPLQPMTQPPPPSQVSPQPLpqpslHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSS----QSQVPPGP 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   416 GLFQAGH-RRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPA--------------SPFQGNAFLTSQ 480
Cdd:pfam03154 314 SPAAPGQsQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPnpqshkhpphlsgpSPFQMNSNLPPP 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   481 PV--PVGVVPALQPAFV---PAQSYPVANGMPYPAPNVPVVGITPSQMVAnvfgTAGHPQAAHPHQSPSlvrQQTFPHYE 555
Cdd:pfam03154 394 PAlkPLSSLSTHHPPSAhppPLQLMPQSQQLPPPPAQPPVLTQSQSLPPP----AASHPPTSGLHQVPS---QSPFPQHP 466

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   556 ASSATTSPFFKPPAQHLNGSAAFNGVDDGRLASADRHTEVP-TGTCPVDPFEAQWAALENKSKQRTNPSP 624
Cdd:pfam03154 467 FVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPaAVSCPLPPVQIKEEALDEAEEPESPPPP 536
PHA03247 PHA03247
large tegument protein UL36; Provisional
 328-563 6.17e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   328 STPEDPFSSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAHTALAPVAMPVreTNPWAHAPDAANKEIAATCSGTEWG 407
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL--PSPWDPADPPAAVLAPAAALPPAAS 2823

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   408 QSSGAASPGLFQAGHRRTPSEADRWLEEVSKSV------RAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAF----- 476
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFalppd 2903

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356   477 -LTSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAH--PHQSPSLVRQ--QTF 551
Cdd:PHA03247 2904 qPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAlvPGRVAVPRFRvpQPA 2983

                         250
                  ....*....|..
gi 20070356   552 PHYEASSATTSP 563
Cdd:PHA03247 2984 PSREAPASSTPP 2995
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 38-133 6.20e-03

Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal function, muscle regeneration, and cell migration. It binds to actin filaments and interacts with the cytoplasmic tails of beta-integrin via its PTB domain, allowing tensin to link actin filaments to integrin receptors. Tensin functions as a platform for assembly and disassembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules, and also by providing interaction sites for other proteins. In addition to its PTB domain, it contains a C-terminal SH2 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269979  Cd Length: 129  Bit Score: 37.36  E-value: 6.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  38 SFPVKYLGHVEVDESRGMHICEDAVKRLKA--TGKKAVKAV-LWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNfDR 114
Cdd:cd13157   3 SRNAQYIGSFPVSGLDVADRADSVRKQLESlkESGSRGRPViLSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPA-HA 81

                        90       100
                ....*....|....*....|.
gi 20070356 115 AFSYICRD--GTTRRWICHCF 133
Cdd:cd13157  82 QFAFVARNpgGPTNRQYCHVF 102
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
 39-150 9.52e-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: 36.94  E-value: 9.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070356  39 FPVKYLGHVEVDESRGMHICEDAVKRLKATgkKAVKAV-------LWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRN 111
Cdd:cd13158  13 FIVRFLGSMEVKSDRTSEVIYEAMRQVLAA--RAIHNIfrmteshLLVTSDCLRLIDPQTQVTRARFPLADVVQFAAHQE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 20070356 112 FDRAFSYICR----DGTTRRWICHCFMAVKDtGERLSHAVGCA 150
Cdd:cd13158  91 NKRLFGFVVRtpegDGEEPSFSCYVFESNTE-GEKICDAIALA 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH