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Conserved domains on  [gi|54144625|ref|NP_001005743|]
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protein numb homolog isoform 1 [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

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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 ...
 23-168 5.18e-102

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: 306.54  E-value: 5.18e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  23 HQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKffkgffgktgkKAVKAVLWVSADGLRVVDEKT 102
Cdd:cd01268   1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRK-----------KPVRAVLWVSGDGLRVVDEKT 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54144625 103 KDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLER 168
Cdd:cd01268  70 KGLIVDQTIEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 258-338 4.58e-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: 136.06  E-value: 4.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   258 PHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDF-----------PIKNAVPEVEG---E 323
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPsseQ 80

                          90
                  ....*....|....*
gi 54144625   324 AESISSLCSQITNAF 338
Cdd:pfam06311  81 ADSISAMCQQISSGL 95
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 343-524 9.44e-05

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   343 DPF-SSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAHTALAPVAMPVREtnpWAHAPDAANKEIAATCSGTEWGQSS 421
Cdd:PRK10263  308 DPLlNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVA---WQPVPGPQTGEPVIAPAPEGYPQQS 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   422 GAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQgnafltSQPVPVGVVPAL 501
Cdd:PRK10263  385 QYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNA------WQAEEQQSTFAP 458

                         170       180
                  ....*....|....*....|....*
gi 54144625   502 QPAFVPAQSY--PVANGMPYPAPNV 524
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 ...
 23-168 5.18e-102

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: 306.54  E-value: 5.18e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  23 HQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKffkgffgktgkKAVKAVLWVSADGLRVVDEKT 102
Cdd:cd01268   1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRK-----------KPVRAVLWVSGDGLRVVDEKT 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54144625 103 KDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLER 168
Cdd:cd01268  70 KGLIVDQTIEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 258-338 4.58e-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: 136.06  E-value: 4.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   258 PHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDF-----------PIKNAVPEVEG---E 323
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPsseQ 80

                          90
                  ....*....|....*
gi 54144625   324 AESISSLCSQITNAF 338
Cdd:pfam06311  81 ADSISAMCQQISSGL 95
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
39-165 1.19e-37

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 136.34  E-value: 1.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625    39 FPVKYLGHVEVDESR------GMHICEDAVKRLKAE-RKFFKGFFGKTGKKaVKAVLWVSADGLRVVDEKTKDLIVDQTI 111
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAkINKIRGLSGETGPG-TKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 54144625   112 EKVSFCAP-DRNFDRAFSYICRDGTTRRWICHCFMAVKDtGERLSHAVGCAFAAC 165
Cdd:pfam00640  80 VSISFCADgDPDLMRYFAYIARDKATNKFACHVFESEDG-AQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 37-175 5.48e-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: 123.19  E-value: 5.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625     37 CSFPVKYLGHVEVDESRGMHICEDAVKRLKAerkffkgFFGKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSF 116
Cdd:smart00462   4 VSFRVKYLGSVEVPEARGLQVVQEAIRKLRA-------AQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISF 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 54144625    117 CAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGErLSHAVGCAFAACLERKQKREKE 175
Cdd:smart00462  77 CAVGPDDLDVFGYIARDPGSSRFACHVFRCEKAAED-IALAIGQAFQLAYELKLKARSE 134
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 343-524 9.44e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   343 DPF-SSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAHTALAPVAMPVREtnpWAHAPDAANKEIAATCSGTEWGQSS 421
Cdd:PRK10263  308 DPLlNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVA---WQPVPGPQTGEPVIAPAPEGYPQQS 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   422 GAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQgnafltSQPVPVGVVPAL 501
Cdd:PRK10263  385 QYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNA------WQAEEQQSTFAP 458

                         170       180
                  ....*....|....*....|....*
gi 54144625   502 QPAFVPAQSY--PVANGMPYPAPNV 524
Cdd:PRK10263  459 QSTYQTEQTYqqPAAQEPLYQQPQP 483
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 302-585 2.00e-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: 41.10  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   302 PSTMQRKTdfPIKNAVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAH 381
Cdd:pfam17823 123 PSSAAQSL--PAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAAS 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   382 TALAPVaMPVRETNpwahapdaankeIAATCSGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAA 461
Cdd:pfam17823 201 SAPATL-TPARGIS------------TAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAA 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   462 PLQPVLQPPPPTAISQPASPFQGNAfltSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFG- 540
Cdd:pfam17823 268 GTINMGDPHARRLSPAKHMPSDTMA---RNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTn 344

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 54144625   541 ----TAGHPQAAHPHQSPSLVRQQTF-PHYEASSATTSPFFKPPAQHLNG 585
Cdd:pfam17823 345 lavvTTTKAQAKEPSASPVPVLHTSMiPEVEATSPTTQPSPLLPTQGAAG 394
 
Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 23-168 5.18e-102

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: 306.54  E-value: 5.18e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  23 HQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKffkgffgktgkKAVKAVLWVSADGLRVVDEKT 102
Cdd:cd01268   1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRK-----------KPVRAVLWVSGDGLRVVDEKT 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54144625 103 KDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLER 168
Cdd:cd01268  70 KGLIVDQTIEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLSHAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 258-338 4.58e-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: 136.06  E-value: 4.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   258 PHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDF-----------PIKNAVPEVEG---E 323
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPsseQ 80

                          90
                  ....*....|....*
gi 54144625   324 AESISSLCSQITNAF 338
Cdd:pfam06311  81 ADSISAMCQQISSGL 95
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
39-165 1.19e-37

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 136.34  E-value: 1.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625    39 FPVKYLGHVEVDESR------GMHICEDAVKRLKAE-RKFFKGFFGKTGKKaVKAVLWVSADGLRVVDEKTKDLIVDQTI 111
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAkINKIRGLSGETGPG-TKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 54144625   112 EKVSFCAP-DRNFDRAFSYICRDGTTRRWICHCFMAVKDtGERLSHAVGCAFAAC 165
Cdd:pfam00640  80 VSISFCADgDPDLMRYFAYIARDKATNKFACHVFESEDG-AQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 37-175 5.48e-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: 123.19  E-value: 5.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625     37 CSFPVKYLGHVEVDESRGMHICEDAVKRLKAerkffkgFFGKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSF 116
Cdd:smart00462   4 VSFRVKYLGSVEVPEARGLQVVQEAIRKLRA-------AQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISF 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 54144625    117 CAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGErLSHAVGCAFAACLERKQKREKE 175
Cdd:smart00462  77 CAVGPDDLDVFGYIARDPGSSRFACHVFRCEKAAED-IALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 37-162 4.37e-27

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: 106.05  E-value: 4.37e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  37 CSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKgffgktgKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSF 116
Cdd:cd00934   1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSK-------RKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISY 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 54144625 117 CAPDRNFDRAFSYICRDGTTRRWICHCFMAV-KDTGERLSHAVGCAF 162
Cdd:cd00934  74 CGRDPDNPNVFAFIAGEEGGSGFRCHVFQCEdEEEAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 39-167 1.40e-22

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: 93.47  E-value: 1.40e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  39 FPVKYLGHVEVDESRGMHICEDAVKRLKAErkffkgffgktGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCA 118
Cdd:cd13161   4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDL-----------KLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVT 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 54144625 119 PDRNFDRAFSYICRDGTTRRWICHCFMaVKDTGERLSHAVGCAFAACLE 167
Cdd:cd13161  73 VDPKDKKLFAFISHDPRLGRITCHVFR-CKRGAQEICDTIAEAFKAAAE 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 35-162 1.72e-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: 85.41  E-value: 1.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  35 GKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGffgkTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKV 114
Cdd:cd01273  10 GHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKS----EGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRI 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 54144625 115 SFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKdTGERLSHAVGCAF 162
Cdd:cd01273  86 SFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEK-LAEEITLTIGQAF 132
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 38-162 3.20e-18

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: 80.84  E-value: 3.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  38 SFPVKYLGHVEVDESRGMHICEDAVKRLKAERKffkgffgKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFC 117
Cdd:cd13159   4 TFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAK-------ASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYC 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 54144625 118 APDRNFDRAFSYICRDGTTRRWICHCFMAVK-DTGERLSHAVGCAF 162
Cdd:cd13159  77 TADANHDKVFAFIATNQDNEKLECHAFLCAKrKMAQAVTLTVAQAF 122
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 30-131 1.48e-15

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: 74.21  E-value: 1.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  30 EGVRtgkcsFPVKYLGHVEVDESRGMHICEDAVKRLKaerkffkGFFGKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQ 109
Cdd:cd01215  14 DGVR-----FKAKLIGIDEVPAARGDKMCQDAMMKLK-------GAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHHH 81

                        90       100
                ....*....|....*....|..
gi 54144625 110 TIEKVSFCAPDRNFDRAFSYIC 131
Cdd:cd01215  82 PVHKISFIARDTTDNRAFGYVC 103
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 24-148 7.53e-13

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: 66.15  E-value: 7.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  24 QWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKaerkffkgffgkTGKKAVKAV----LWVSADGLRVVD 99
Cdd:cd01274   2 QWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLK------------KSTREMKKIptiiLSISYKGVKFID 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 54144625 100 EKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVK 148
Cdd:cd01274  70 ATTKNLICEHEIRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLT 118
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 38-144 3.11e-05

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: 43.86  E-value: 3.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  38 SFPVKYLGHVEVDESRGM-HICEDAVKRLKAERKffkgffgktGKKAVKAVLWVSADGLRVVDEKTKDLIVDQT---IEK 113
Cdd:cd13160   2 VFTVKYLGRMPARGLWGIkHTRKPLVDALKNLPK---------GKTLPKTKLEVSSDGVKLEELRGGFGSSKTVffpIHT 72

                        90       100       110
                ....*....|....*....|....*....|....
gi 54144625 114 VSFCAPDRNFDRAFSYICR-DGTTRR--WICHCF 144
Cdd:cd13160  73 ISYGVQDLVHTRVFSMIVVgEQDSSNhpFECHAF 106
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 343-524 9.44e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   343 DPF-SSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAHTALAPVAMPVREtnpWAHAPDAANKEIAATCSGTEWGQSS 421
Cdd:PRK10263  308 DPLlNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVA---WQPVPGPQTGEPVIAPAPEGYPQQS 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   422 GAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQgnafltSQPVPVGVVPAL 501
Cdd:PRK10263  385 QYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNA------WQAEEQQSTFAP 458

                         170       180
                  ....*....|....*....|....*
gi 54144625   502 QPAFVPAQSY--PVANGMPYPAPNV 524
Cdd:PRK10263  459 QSTYQTEQTYqqPAAQEPLYQQPQP 483
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 25-144 1.84e-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: 42.58  E-value: 1.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  25 WQTDEEGVRTGKCSFPVKYLGHVEVDES-RGM------HICEDAVKRL------------KAERKFFKGFFGKTGKK-AV 84
Cdd:cd01209   3 WLHPDQLGMGPGVSYPVRYVGCIEVLQSmRSLdfntrtQVTREAINRVceavggakgakrKRKSKALSSILGKSNLQfAG 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54144625  85 KAV-LWVSADGLRVVDEKTKDLIVDQTIEKVSFCA---PDRNFDRAfsYICRDGTTRRwICHCF 144
Cdd:cd01209  83 MNIsLTISTDGLNLVTPDTGQIIANHHMQSISFASggdPDTYDYVA--YVAKDPVNQR-ACHVL 143
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 38-144 2.55e-04

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: 41.52  E-value: 2.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  38 SFPVKYLGHVEVDE--------SRGMHICedaVKRLKAERKFFKGFFGKTGKKavKAVLWVSADG-LRVVDEKTKDLIVD 108
Cdd:cd01272   3 RFAVRSLGWVEMAEedltpgksSVAVNNC---IRQLSYGRNDIRDTVGRWGEG--KDMLMVLDDDtLKLVDPDDRSVLHS 77

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 54144625 109 QTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCF 144
Cdd:cd01272  78 QPIHSIRVWGVGRDNGRDFAYVARDKDTRVLKCHVF 113
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 40-172 6.98e-04

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: 40.02  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625    40 PVKYLGHVEVDESRGMHICEDAVKRLKaerkffkgFFGKTGKKAVKAVLW-VSADGLRVVDEKTKDLIVDQTIEKVSFCA 118
Cdd:pfam08416   3 RVEHLTTFELDSLTGLQAVEDAIRKLQ--------LLDAQGRVWTQEMLLqVSDQGITLTDNETKEELESYPLDSISHCQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 54144625   119 ---PDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKR 172
Cdd:pfam08416  75 avlNDGRYNSILALVCQEPGQSKPDVHLFQCDELGAELIAEDIESALSDVRLGKPKK 131
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 302-585 2.00e-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: 41.10  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   302 PSTMQRKTdfPIKNAVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAH 381
Cdd:pfam17823 123 PSSAAQSL--PAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAAS 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   382 TALAPVaMPVRETNpwahapdaankeIAATCSGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAA 461
Cdd:pfam17823 201 SAPATL-TPARGIS------------TAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAA 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   462 PLQPVLQPPPPTAISQPASPFQGNAfltSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFG- 540
Cdd:pfam17823 268 GTINMGDPHARRLSPAKHMPSDTMA---RNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTn 344

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 54144625   541 ----TAGHPQAAHPHQSPSLVRQQTF-PHYEASSATTSPFFKPPAQHLNG 585
Cdd:pfam17823 345 lavvTTTKAQAKEPSASPVPVLHTSMiPEVEATSPTTQPSPLLPTQGAAG 394
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
418-622 2.84e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  418 GQSSGAASPGLFQAGHRRTPSEAdrwleevsksvrAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGV 497
Cdd:PRK12323 366 GQSGGGAGPATAAAAPVAQPAPA------------AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEAL 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  498 VPALQ--PAFVPAQSYPVANGMPYPAPNVPvvgitpsqmvanvfgtaghPQAAHPHQSPSLVRQQTFPHYEASSATTSPF 575
Cdd:PRK12323 434 AAARQasARGPGGAPAPAPAPAAAPAAAAR-------------------PAAAGPRPVAAAAAAAPARAAPAAAPAPADD 494

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 54144625  576 FKPPAQHLNGSAAFNGVDDGRLASADRHTEV---PTGTCPVDPFEAQWAA 622
Cdd:PRK12323 495 DPPPWEELPPEFASPAPAQPDAAPAGWVAESipdPATADPDDAFETLAPA 544
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 38-175 3.07e-03

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: 39.19  E-value: 3.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  38 SFPVKYLGHVEVDE--SRgMHICEdAVKRLKAErkfFKGffgKTGKKAvKAVLWVSADGLRVVDEKTKD----------- 104
Cdd:cd01270  30 TFQAKYIGSLEVPRpsSR-VEIVA-AMRRIRYE---FKA---KNIKKK-KVTITVSVDGVKVVLRKKKKkkgwtwdeskl 100

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54144625 105 LIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMA-VKDTGERLSHAVGCAFAACLERKQKREKE 175
Cdd:cd01270 101 LLMQHPIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSkKKSQAMRIVRTIGQAFEVCHKLSLQHMQG 172
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 272-635 3.13e-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: 40.91  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   272 ARQGSFRGFPALSQKMSPFKRQLSLRInelPSTMQRKTDFPIKNAvPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMT 351
Cdd:pfam03154 162 AQQQILQTQPPVLQAQSGAASPPSPPP---PGTTQAATAGPTPSA-PSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   352 KPVTVVAPQSPTFQANGTDSAFHVLAKPA-----HTALAPVAMPVRETNPWAHAPDAANKEIAATCSGtewgQSSGAASP 426
Cdd:pfam03154 238 HPQRLPSPHPPLQPMTQPPPPSQVSPQPLpqpslHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSS----QSQVPPGP 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   427 GLFQAGH-RRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPA--------------SPFQGNAFLTSQ 491
Cdd:pfam03154 314 SPAAPGQsQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPnpqshkhpphlsgpSPFQMNSNLPPP 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   492 PV--PVGVVPALQPAFV---PAQSYPVANGMPYPAPNVPVVGITPSQMVAnvfgTAGHPQAAHPHQSPSlvrQQTFPHYE 566
Cdd:pfam03154 394 PAlkPLSSLSTHHPPSAhppPLQLMPQSQQLPPPPAQPPVLTQSQSLPPP----AASHPPTSGLHQVPS---QSPFPQHP 466

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   567 ASSATTSPFFKPPAQHLNGSAAFNGVDDGRLASADRHTEVP-TGTCPVDPFEAQWAALENKSKQRTNPSP 635
Cdd:pfam03154 467 FVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPaAVSCPLPPVQIKEEALDEAEEPESPPPP 536
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 423-589 3.35e-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: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   423 AASPGLFQAGHRRTPSeadrwLEEVSKSVRAQ----QPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVV 498
Cdd:pfam09770 180 AAQPASLPAPSRKMMS-----LEEVEAAMRAQakkpAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQ 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   499 PALQPAFVPA-----QSYPVANGMPYPAP-------NVPVVGITPSQMVAN--VFGTAGHPQAAHPHQSPSLVRQQTFPH 564
Cdd:pfam09770 255 QHPGQGHPVTilqrpQSPQPDPAQPSIQPqaqqfhqQPPPVPVQPTQILQNpnRLSAARVGYPQNPQPGVQPAPAHQAHR 334

                         170       180
                  ....*....|....*....|....*....
gi 54144625   565 YEASSATTSPFFKPPAQHLNGS----AAF 589
Cdd:pfam09770 335 QQGSFGRQAPIITHPQQLAQLSeeekAAY 363
PHA03247 PHA03247
large tegument protein UL36; Provisional
 339-574 4.81e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   339 STPEDPFSSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAHTALAPVAMPVreTNPWAHAPDAANKEIAATCSGTEWG 418
Cdd:PHA03247 2746 AGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL--PSPWDPADPPAAVLAPAAALPPAAS 2823

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   419 QSSGAASPGLFQAGHRRTPSEADRWLEEVSKSV------RAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAF----- 487
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFalppd 2903

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625   488 -LTSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAH--PHQSPSLVRQ--QTF 562
Cdd:PHA03247 2904 qPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAlvPGRVAVPRFRvpQPA 2983

                         250
                  ....*....|..
gi 54144625   563 PHYEASSATTSP 574
Cdd:PHA03247 2984 PSREAPASSTPP 2995
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
 39-161 5.07e-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: 37.71  E-value: 5.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  39 FPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFfgktgkKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCA 118
Cdd:cd13158  13 FIVRFLGSMEVKSDRTSEVIYEAMRQVLAARAIHNIF------RMTESHLLVTSDCLRLIDPQTQVTRARFPLADVVQFA 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 54144625 119 PDRNFDRAFSYICR----DGTTRRWICHCFMAVKDtGERLSHAVGCA 161
Cdd:cd13158  87 AHQENKRLFGFVVRtpegDGEEPSFSCYVFESNTE-GEKICDAIALA 132
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 38-144 6.95e-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: 6.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  38 SFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFfkgffgKTGKKAVkaVLWVSADGLRVVDEKTKDLIVDQTIEKVSFC 117
Cdd:cd13157   3 SRNAQYIGSFPVSGLDVADRADSVRKQLESLKES------GSRGRPV--ILSVSLSGIKICSEDGKVVLMAHALRRVSYS 74

                        90       100
                ....*....|....*....|....*....
gi 54144625 118 APDRNfDRAFSYICRD--GTTRRWICHCF 144
Cdd:cd13157  75 TCRPA-HAQFAFVARNpgGPTNRQYCHVF 102
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
347-522 8.83e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.45  E-value: 8.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  347 SAPMTKPVTVVAPQSPtfqANGTDSAFHVLAKPAHTALAPVAMPVRETNPWAHAPDAANKEIAATcSGTEWGQSSGAASP 426
Cdd:PRK07003 366 GAPGGGVPARVAGAVP---APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP-AAPAPPATADRGDD 441

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144625  427 GLFQAGHRRTPSEADRWLEEVSKSvRAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVVPALQPAF- 505
Cdd:PRK07003 442 AADGDAPVPAKANARASADSRCDE-RDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREd 520

                        170
                 ....*....|....*..
gi 54144625  506 VPAQSYPVANGMPYPAP 522
Cdd:PRK07003 521 APAAAAPPAPEARPPTP 537
 
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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