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Conserved domains on  [gi|257096042|ref|NP_001157873|]
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receptor-type tyrosine-protein phosphatase O isoform 2 precursor [Mus musculus]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 12877337)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 933-1177 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


:

Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 542.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  933 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 1012
Cdd:cd14614     1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1013 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANA 1092
Cdd:cd14614    81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1093 AESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14614   161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                  ....*
gi 257096042 1173 CVQLM 1177
Cdd:cd14614   241 CVQLM 245
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 444-536 1.76e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 44.41  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  444 EKPQHVSVHVLSSTTALMSWTSSQENyNSTIVS-VVSLTCQKQKESQRLEKqycTQVNSSKPVIENLVPGAQYQVVMYLR 522
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGyVVEYREKGSGDWKEVEV---TPGSETSYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....
gi 257096042  523 KGPLIGPPSDPVTF 536
Cdd:cd00063    78 NGGGESPPSESVTV 91
fn3 pfam00041
Fibronectin type III domain;
735-815 2.35e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.94  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   735 PPKSLFAVNKTQTSVTLLWVE----EGVADFFEVFCQQLGSGhNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDT 810
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 257096042   811 PSVPT 815
Cdd:pfam00041   81 EGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 540-640 1.19e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.10  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  540 PTGIKDLMLYPLGPTAVVLSWTRP--ILGVFRKYVVEMFyfnpTTMTSEWTtyyEIAATVSLTASVRIASLLPAWYYNFR 617
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYR----EKGSGDWK---EVEVTPGSETSYTLTGLKPGTEYEFR 73

                          90       100
                  ....*....|....*....|....*.
gi 257096042  618 VTMVT---WGDPelsccdSSTISFIT 640
Cdd:cd00063    74 VRAVNgggESPP------SESVTVTT 93
 
Name Accession Description Interval E-value
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 933-1177 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 542.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  933 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 1012
Cdd:cd14614     1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1013 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANA 1092
Cdd:cd14614    81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1093 AESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14614   161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                  ....*
gi 257096042 1173 CVQLM 1177
Cdd:cd14614   241 CVQLM 245
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
919-1174 1.77e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 353.89  E-value: 1.77e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042    919 KFSLQFEELKLIGLDIPHFA-ADLPLNRCKNRYTNILPYDFSRVRLvSMNEEEGADYINANYIPGYNSPQEYIATQGPLP 997
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042    998 ETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTE-EPIAYGDITVEMVSEEEEEDWASRHFRINYAD--EAQDV 1074
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   1075 MHFNYTAWPDHGVPPAnaAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMR 1154
Cdd:smart00194  160 THYHYTNWPDHGVPES--PESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|
gi 257096042   1155 SYRMSMVQTEEQYIFIHQCV 1174
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
944-1174 1.66e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 326.12  E-value: 1.66e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   944 NRCKNRYTNILPYDFSRVRLvsMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1023
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  1024 KRRVKCDHYWPFT-EEPIAYGDITVEMVSEEEEE-DWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPPANAaeSILQF 1099
Cdd:pfam00102   79 KGREKCAQYWPEEeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPN--SLLDL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096042  1100 VFTVRQ-QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:pfam00102  157 LRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
943-1170 2.53e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.96  E-value: 2.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  943 LNRCK-NRYTNILPYDFSRVRlvsmneeEGADYINANYIPGYNsPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1021
Cdd:COG5599    40 INGSPlNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1022 NE--KRRVKCDHYWPFTEEPIAYgDITVEMVSEEE-EEDWASRHFRINYAD---EAQDVMHFNYTAWPDHGVPPANAAES 1095
Cdd:COG5599   112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTESIQlRDGIEARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISAEALKN 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096042 1096 ILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE--FVDILGLVSEMRSYR-MSMVQTEEQYIFI 1170
Cdd:COG5599   191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 944-1174 2.03e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 151.69  E-value: 2.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1023
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1024 KRRVKCDHYW-PFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQ--DVMHFNYTAWPDHGVPpaNAAESILQFV 1100
Cdd:PHA02742  130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGAslDIKHFAYEDWPHGGLP--RDPNKFLDFV 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1101 FTVRQQAAKS-----------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 1169
Cdd:PHA02742  208 LAVREADLKAdvdikgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                  ....*
gi 257096042 1170 IHQCV 1174
Cdd:PHA02742  288 CYFIV 292
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 444-536 1.76e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 44.41  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  444 EKPQHVSVHVLSSTTALMSWTSSQENyNSTIVS-VVSLTCQKQKESQRLEKqycTQVNSSKPVIENLVPGAQYQVVMYLR 522
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGyVVEYREKGSGDWKEVEV---TPGSETSYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....
gi 257096042  523 KGPLIGPPSDPVTF 536
Cdd:cd00063    78 NGGGESPPSESVTV 91
fn3 pfam00041
Fibronectin type III domain;
445-531 1.91e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   445 KPQHVSVHVLSSTTALMSWTSSqENYNSTIVSVvSLTCQKQKESQrlekqYCTQVNSSKP----VIENLVPGAQYQVVMY 520
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPP-PDGNGPITGY-EVEYRPKNSGE-----PWNEITVPGTttsvTLTGLKPGTEYEVRVQ 74

                           90
                   ....*....|.
gi 257096042   521 LRKGPLIGPPS 531
Cdd:pfam00041   75 AVNGGGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
735-815 2.35e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.94  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   735 PPKSLFAVNKTQTSVTLLWVE----EGVADFFEVFCQQLGSGhNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDT 810
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 257096042   811 PSVPT 815
Cdd:pfam00041   81 EGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 540-640 1.19e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.10  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  540 PTGIKDLMLYPLGPTAVVLSWTRP--ILGVFRKYVVEMFyfnpTTMTSEWTtyyEIAATVSLTASVRIASLLPAWYYNFR 617
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYR----EKGSGDWK---EVEVTPGSETSYTLTGLKPGTEYEFR 73

                          90       100
                  ....*....|....*....|....*.
gi 257096042  618 VTMVT---WGDPelsccdSSTISFIT 640
Cdd:cd00063    74 VRAVNgggESPP------SESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 733-815 2.84e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.94  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  733 PAPPKSLFAVNKTQTSVTLLWV----EEGVADFFEVFCQQLGSGhNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSH 808
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTppedDGGPITGYVVEYREKGSG-DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ....*..
gi 257096042  809 DTPSVPT 815
Cdd:cd00063    80 GGESPPS 86
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 733-812 3.73e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 40.29  E-value: 3.73e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042    733 PAPPKSLFAVNKTQTSVTLLW--VEEGVADFFEVFCQQLGSGHNGKLQE-PVAVSSHVVTISSLLPATAYNCSVTSFSHD 809
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWepPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 257096042    810 TPS 812
Cdd:smart00060   81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 540-622 1.69e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 38.75  E-value: 1.69e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042    540 PTGIKDLMLYPLGPTAVVLSWTRPILGVFRKYVVEMFYFNpTTMTSEWTTyyeiAATVSLTASVRIASLLPAWYYNFRVT 619
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEY-REEGSEWKE----VNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ...
gi 257096042    620 MVT 622
Cdd:smart00060   76 AVN 78
 
Name Accession Description Interval E-value
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 933-1177 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 542.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  933 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 1012
Cdd:cd14614     1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1013 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANA 1092
Cdd:cd14614    81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1093 AESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14614   161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                  ....*
gi 257096042 1173 CVQLM 1177
Cdd:cd14614   241 CVQLM 245
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 949-1172 2.70e-137

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 415.60  E-value: 2.70e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  949 RYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVK 1028
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1029 CDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAA 1108
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVP--EAPDSLLRFVRLVRDYIK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257096042 1109 KSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14548   159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
919-1174 1.77e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 353.89  E-value: 1.77e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042    919 KFSLQFEELKLIGLDIPHFA-ADLPLNRCKNRYTNILPYDFSRVRLvSMNEEEGADYINANYIPGYNSPQEYIATQGPLP 997
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042    998 ETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTE-EPIAYGDITVEMVSEEEEEDWASRHFRINYAD--EAQDV 1074
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   1075 MHFNYTAWPDHGVPPAnaAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMR 1154
Cdd:smart00194  160 THYHYTNWPDHGVPES--PESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|
gi 257096042   1155 SYRMSMVQTEEQYIFIHQCV 1174
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
944-1174 1.66e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 326.12  E-value: 1.66e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   944 NRCKNRYTNILPYDFSRVRLvsMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1023
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  1024 KRRVKCDHYWPFT-EEPIAYGDITVEMVSEEEEE-DWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPPANAaeSILQF 1099
Cdd:pfam00102   79 KGREKCAQYWPEEeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPN--SLLDL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096042  1100 VFTVRQ-QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:pfam00102  157 LRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 948-1172 2.20e-95

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 304.15  E-value: 2.20e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  948 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1027
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1028 KCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRI---NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVR 1104
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKIcseEQLDAPRLVRHFHYTVWPDHGVP--ETTQSLIQFVRTVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1105 QQAAKS--KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14617   159 DYINRTpgSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 948-1174 3.47e-90

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 290.25  E-value: 3.47e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  948 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1027
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1028 KCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAESILQFVFTVRQ 1105
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTlsVRHFHFTAWPDHGVP--SSTDTLLAFRRLLRQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257096042 1106 --QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14619   159 wlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 942-1174 8.59e-90

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 289.30  E-value: 8.59e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  942 PLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1021
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1022 NEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQF 1099
Cdd:cd14553    81 EERSRVKCDQYWP-TRGTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVP--EHPTPFLAF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257096042 1100 VFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14553   158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 948-1174 4.65e-88

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 284.14  E-value: 4.65e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  948 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1027
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1028 KCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPPANAaeSILQFVFTVRQ 1105
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKErrVKHLHYTAWPDHGIPESTS--SLMAFRELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257096042 1106 --QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14618   159 hvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 974-1172 9.77e-88

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 281.87  E-value: 9.77e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWP-FTEEPIAYGDITVEMVSE 1052
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPeEGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1053 EEEEDWASRHFRINYAD--EAQDVMHFNYTAWPDHGVPPanAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIA 1130
Cdd:cd00047    81 EELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPS--SPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 257096042 1131 LDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd00047   159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 948-1174 7.65e-86

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 277.85  E-value: 7.65e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  948 NRYTNILPYDFSRVRLVSMNEEEgADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1027
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHST-DDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1028 KCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAESILQFVFTVRQ 1105
Cdd:cd14615    80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESrtVRHFHFTSWPDHGVP--ETTDLLINFRHLVRE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257096042 1106 QAAKS--KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14615   157 YMKQNppNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCA 227
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 948-1172 2.27e-84

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 273.71  E-value: 2.27e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  948 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1027
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1028 KCDHYWPFTEEPIA-YGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANAaeSILQFVFTVRQQ 1106
Cdd:cd14616    81 RCHQYWPEDNKPVTvFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSA--PLIHFVKLVRAS 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096042 1107 AAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14616   159 RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 938-1171 1.01e-80

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 265.38  E-value: 1.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  938 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 1017
Cdd:cd14543    23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1018 LTQCNEKRRVKCDHYWPFTEEPIA-YGDITVEMVSEEEEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPPanAAE 1094
Cdd:cd14543   103 TTRVVERGRVKCGQYWPLEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTetDESRQVTHFQFTSWPDFGVPS--SAA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1095 SILQFVFTVRQQAAKS--------KG-----PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMV 1161
Cdd:cd14543   181 ALLDFLGEVRQQQALAvkamgdrwKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSI 260

                         250
                  ....*....|
gi 257096042 1162 QTEEQYIFIH 1171
Cdd:cd14543   261 QTPDQYYFCY 270
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 948-1172 3.49e-77

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 253.86  E-value: 3.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  948 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRr 1026
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1027 VKCDHYWPFtEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPAnaAESILQFVFTVRQ- 1105
Cdd:cd14547    80 EKCAQYWPE-EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEA--AQPLLSLVQEVEEa 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096042 1106 -QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14547   157 rQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 974-1171 1.04e-76

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 251.50  E-value: 1.04e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEE 1053
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP-KEGTETYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHF--------RINYADEAQDVMHFNYTAWPDHGVPPANAaeSILQFvftVRQQAAKSK---GPMIIHCSAGV 1122
Cdd:cd14549    80 VLATYTVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTL--PVLSF---VRKSSAANPpgaGPIVVHCSAGV 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 257096042 1123 GRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1171
Cdd:cd14549   155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 904-1174 2.03e-75

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 251.11  E-value: 2.03e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  904 DFDSYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGY 983
Cdd:cd14626     2 DLADNIERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  984 NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPF--TEepiAYGDITVEMVSEEEEEDWASR 1061
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIrgTE---TYGMIQVTLLDTVELATYSVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1062 HFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIR 1139
Cdd:cd14626   158 TFALykNGSSEKREVRQFQFMAWPDHGVP--EYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMK 235

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 257096042 1140 DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14626   236 HEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 920-1171 1.49e-71

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 239.94  E-value: 1.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  920 FSLQFEELKLIGLDIPHFA--ADLPLNRCKNRYTNILPYDFSRVRLVSM--NEEEGADYINANYIPGYNSPQEYIATQGP 995
Cdd:cd17667     1 FSEDFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  996 LPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRI-NYADEA--- 1071
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTKIHACYTVRRFSIrNTKVKKgqk 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1072 ---------QDVMHFNYTAWPDHGVPpaNAAESILQFVftVRQQAAKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRD 1140
Cdd:cd17667   160 gnpkgrqneRTVIQYHYTQWPDMGVP--EYALPVLTFV--RRSSAARTPemGPVLVHCSAGVGRTGTYIVIDSMLQQIKD 235

                         250       260       270
                  ....*....|....*....|....*....|.
gi 257096042 1141 HEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1171
Cdd:cd17667   236 KSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 932-1176 6.56e-69

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 231.65  E-value: 6.56e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  932 LDIPHFAAdlplnrcKNRYTNILPYDFSRVRLVS-MNEEEGADYINANYIPGYN-SPQEYIATQGPLPETRNDFWKMVLQ 1009
Cdd:cd14612    10 LDIPGHAS-------KDRYKTILPNPQSRVCLRRaGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1010 QKSHIIVMLTQCNEKRRvKCDHYWPFTEEpiAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPp 1089
Cdd:cd14612    83 EECPIIVMITKLKEKKE-KCVHYWPEKEG--TYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTP- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1090 aNAAESILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 1167
Cdd:cd14612   159 -ESAGPLLRLVAEVeeSRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQY 237


                  ....*....
gi 257096042 1168 IFIHQCVQL 1176
Cdd:cd14612   238 QFLHHTLAL 246
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 974-1172 2.70e-68

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 228.29  E-value: 2.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYI-PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSE 1052
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1053 EEEEDWAS--RHFRINYADEA-QDVMHFNYTAWPDHGVPPanAAESILQFVFTVR--QQAAKSKGPMIIHCSAGVGRTGT 1127
Cdd:cd18533    81 EENDDGGFivREFELSKEDGKvKKVYHIQYKSWPDFGVPD--SPEDLLTLIKLKRelNDSASLDPPIIVHCSAGVGRTGT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 257096042 1128 FIALDRLLQHIRDHEFVD---------ILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd18533   159 FIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 899-1174 5.54e-68

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 230.39  E-value: 5.54e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  899 PVQLDDFDSYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 978
Cdd:cd14624     3 PIPILELADHIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  979 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDW 1058
Cdd:cd14624    82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1059 ASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQ 1136
Cdd:cd14624   161 CVRTFALykNGSSEKREVRQFQFTAWPDHGVP--EHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 257096042 1137 HIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14624   239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 899-1174 7.60e-68

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 229.98  E-value: 7.60e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  899 PVQLDDFDSYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 978
Cdd:cd14625     3 PIPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  979 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDW 1058
Cdd:cd14625    82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1059 ASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQ 1136
Cdd:cd14625   161 CVRTFSLhkNGSSEKREVRQFQFTAWPDHGVP--EYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 257096042 1137 HIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14625   239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 938-1178 1.90e-67

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 228.17  E-value: 1.90e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  938 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 1017
Cdd:cd14603    24 AGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILM 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1018 LTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEE-EDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESI 1096
Cdd:cd14603   104 ACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLnEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIP--DSPDCM 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1097 LQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDR-----LLQHIRDHefVDILGLVSEMRSYRMSMVQTEEQYIFIH 1171
Cdd:cd14603   182 LAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLY 259


                  ....*..
gi 257096042 1172 QCVQLMW 1178
Cdd:cd14603   260 HTVAQMF 266
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 944-1174 4.27e-67

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 226.06  E-value: 4.27e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1023
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1024 KRRVKCDHYWPftEEPIAYGDITVEMVSEEEEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVF 1101
Cdd:cd14630    83 VGRVKCVRYWP--DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKkgYHEIREIRQFHFTSWPDHGVP--CYATGLLGFVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257096042 1102 TVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14630   159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 904-1174 6.63e-67

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 226.85  E-value: 6.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  904 DFDSYIKDMAKDSDYKFSLQFEELkLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGY 983
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  984 NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEpiAYGDITVEMVSEEEEEDWASRHF 1063
Cdd:cd14633    80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1064 RINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH 1141
Cdd:cd14633   158 AVEKrgVHEIREIRQFHFTGWPDHGVP--YHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAERE 235

                         250       260       270
                  ....*....|....*....|....*....|...
gi 257096042 1142 EFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14633   236 GVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 939-1172 2.18e-66

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 223.94  E-value: 2.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  939 ADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVML 1018
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1019 TQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPpaNAAESI 1096
Cdd:cd14554    81 TKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDArdGQSRTVRQFQFTDWPEQGVP--KSGEGF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096042 1097 LQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14554   158 IDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 944-1175 1.72e-64

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 219.26  E-value: 1.72e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCKNRYTNILPYDFSRVRLVSM-NEEEGADYINANYIPGYNSP-------QEYIATQGPLPETRNDFWKMVLQQKSHII 1015
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIRNENEGpttdenaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1016 VMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD---VMHFNYTAWPDHGVPpaNA 1092
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPireIWHYQYLSWPDHGVP--SD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1093 AESILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQY 1167
Cdd:cd14544   159 PGGVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQY 238


                  ....*...
gi 257096042 1168 IFIHQCVQ 1175
Cdd:cd14544   239 KFIYVAVA 246
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 973-1174 6.05e-62

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 210.26  E-value: 6.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  973 DYINANY----IPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVE 1048
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1049 MVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 1126
Cdd:cd14541    81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVP--DDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 257096042 1127 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14541   159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAI 206
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 944-1174 3.64e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 208.92  E-value: 3.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCKNRYTNILPYDFSRVRLvsmnEEEGaDYINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1021
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1022 NEKRRVKCDHYWPFT-EEPIAYGD-ITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESIL 1097
Cdd:cd14597    78 VEGGKIKCQRYWPEIlGKTTMVDNrLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTP--SQPEQLL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096042 1098 QFVFTVRQqaAKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14597   156 TFISYMRH--IHKSGPIITHCSAGIGRSGTLICIDVVLGLIsKDLDF-DISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 974-1172 6.66e-61

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 206.99  E-value: 6.66e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWP-FTEEPIAYGDITVEMVSE 1052
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1053 EEEEDWASRHFRINYADE---AQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFI 1129
Cdd:cd14557    81 KICPDYIIRKLNINNKKEkgsGREVTHIQFTSWPDHGVP--EDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 257096042 1130 ALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14557   159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 942-1174 5.16e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 207.04  E-value: 5.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  942 PLNRCKNRYTNILPYDFSRVRLVSM-NEEEGADYINANYI------PGyNSPQEYIATQGPLPETRNDFWKMVLQQKSHI 1014
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRdSNIPGSDYINANYVknqllgPD-ENAKTYIASQGCLEATVNDFWQMAWQENSRV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1015 IVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFR---INYADEAQDVMHFNYTAWPDHGVPPAN 1091
Cdd:cd14606    95 IVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQvspLDNGELIREIWHYQYLSWPDHGVPSEP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1092 AAesILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQ 1166
Cdd:cd14606   175 GG--VLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQ 252


                  ....*...
gi 257096042 1167 YIFIHQCV 1174
Cdd:cd14606   253 YKFIYVAI 260
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 974-1174 6.56e-60

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 204.38  E-value: 6.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMVSEE 1053
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP--DDTEVYGDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIAL 1131
Cdd:cd14555    79 PLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVP--YHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 257096042 1132 DRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14555   157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 974-1174 7.72e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 204.15  E-value: 7.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWP-FTEEP-IAYGDITVEM 1049
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPlICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1050 VSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAakSKGPMIIHCSAGVGRTGT 1127
Cdd:cd14538    81 EKYQSLQDFVIRRISLrdKETGEVHHITHLNFTTWPDHGTP--QSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 257096042 1128 FIALDRLLQHI-RDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14538   157 LITIDVALGLIeRDLPF-DIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 920-1176 9.85e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 205.87  E-value: 9.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  920 FSLQ--FEELKLIGLDIPHFaaDLPLNRCKNRYTNILPYDFSRVRLVSMNEEEG-ADYINANYIPGYNSPQE-YIATQGP 995
Cdd:cd14613     1 FLLQaeFFEIPMNFVDPKEY--DIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYGGEEKvYIATQGP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  996 LPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvKCDHYWPftEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVM 1075
Cdd:cd14613    79 TVNTVGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWP--EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1076 HFNYTAWPDHGVPpaNAAESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSE 1152
Cdd:cd14613   156 HYWYTSWPDQKTP--DNAPPLLQLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQ 233

                         250       260
                  ....*....|....*....|....
gi 257096042 1153 MRSYRMSMVQTEEQYIFIHQCVQL 1176
Cdd:cd14613   234 LRLDRGGMIQTCEQYQFVHHVLSL 257
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 922-1170 2.90e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 205.08  E-value: 2.90e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  922 LQFEEL--KLIGLDIPhfAADLPLNRCKNRYTNILPYDFSRVRLvsmneEEGADYINANY----IPGYNSPQEYIATQGP 995
Cdd:cd14600    18 IQFEQLyrKKPGLAIT--CAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  996 LPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYAD--EAQD 1073
Cdd:cd14600    91 LPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQtgEERT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1074 VMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKgPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEM 1153
Cdd:cd14600   171 VTHLQYVAWPDHGVP--DDSSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKM 247

                         250
                  ....*....|....*..
gi 257096042 1154 RSYRMSMVQTEEQYIFI 1170
Cdd:cd14600   248 RDQRAMMVQTSSQYKFV 264
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 944-1174 4.13e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 205.55  E-value: 4.13e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1023
Cdd:cd14604    57 NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1024 KRRVKCDHYWP-FTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFT 1102
Cdd:cd14604   137 MGRKKCERYWPlYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVP--SSFDSILDMISL 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257096042 1103 VRQQAAKSKGPMIIHCSAGVGRTGTFIALD---RLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14604   215 MRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 899-1174 1.53e-58

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 203.72  E-value: 1.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  899 PVQLDDFDSYIKDMAKDSDYKFSLQFEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 978
Cdd:cd14621     7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  979 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDW 1058
Cdd:cd14621    87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDVTVLVDY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1059 ASRHFRINYADEAQD------VMHFNYTAWPDHGVPPANAAesILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALD 1132
Cdd:cd14621   166 TVRKFCIQQVGDVTNkkpqrlITQFHFTSWPDFGVPFTPIG--MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVID 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 257096042 1133 RLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14621   244 AMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 950-1172 2.21e-58

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 200.94  E-value: 2.21e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  950 YTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKC 1029
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1030 DHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINY-----ADEAQDVMHFNYTAWPDHGVPPANAAesILQFVFTVR 1104
Cdd:cd14620    81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPqlpdgCKAPRLVTQLHFTSWPDFGVPFTPIG--MLKFLKKVK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096042 1105 QQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14620   158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 924-1169 1.12e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 200.64  E-value: 1.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  924 FEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLvsmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDF 1003
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1004 WKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEE-PIAYGD--ITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFN 1078
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkEMIFEDtnLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1079 YTAWPDHGVPPANAaeSILQFVFTVRQQAAKSK--GPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEM 1153
Cdd:cd14608   161 YTTWPDFGVPESPA--SFLNFLFKVRESGSLSPehGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEM 238

                         250
                  ....*....|....*.
gi 257096042 1154 RSYRMSMVQTEEQYIF 1169
Cdd:cd14608   239 RKFRMGLIQTADQLRF 254
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 947-1169 1.22e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 198.77  E-value: 1.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  947 KNRYTNILPYDFSRVRLVSMNEEegADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRR 1026
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1027 VKCDHYWPFTEEP---IAYGDITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPPANAAesILQFVF 1101
Cdd:cd14545    79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAA--FLNFLQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257096042 1102 TVRQQAAKS--KGPMIIHCSAGVGRTGTFIALDRLLQHI--RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 1169
Cdd:cd14545   157 KVRESGSLSsdVGPPVVHCSAGIGRSGTFCLVDTCLVLIekGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 974-1171 7.63e-57

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 195.58  E-value: 7.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEE 1053
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHFRINYAD----------EAQDVMHFNYTAWPDHGVPPANAAesILQFVFTVRQQAAKSKGPMIIHCSAGVG 1123
Cdd:cd17668    80 VLAYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYTQWPDMGVPEYTLP--VLTFVRKASYAKRHAVGPVVVHCSAGVG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 257096042 1124 RTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1171
Cdd:cd17668   158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 938-1172 7.75e-57

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 198.80  E-value: 7.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  938 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 1017
Cdd:cd14627    47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1018 LTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAES 1095
Cdd:cd14627   127 LTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSrtVRQFQFTDWPEQGVP--KSGEG 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257096042 1096 ILQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14627   204 FIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 947-1172 1.35e-56

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 195.52  E-value: 1.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  947 KNRYTNILPYDFSRVRLVSMNEEEG-ADYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEK 1024
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1025 RRvKCDHYWPftEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVR 1104
Cdd:cd14611    82 NE-KCVLYWP--EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTP--DSAQPLLQLMLDVE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1105 Q--QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14611   157 EdrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 938-1172 1.39e-56

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 198.03  E-value: 1.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  938 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 1017
Cdd:cd14628    46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1018 LTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAES 1095
Cdd:cd14628   126 LTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSrtVRQFQFTDWPEQGVP--KSGEG 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257096042 1096 ILQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14628   203 FIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 960-1174 1.87e-56

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 194.85  E-value: 1.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  960 RVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEP 1039
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP--DDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1040 IAYGDITVEMVSEEEEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIH 1117
Cdd:cd14631    79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVP--YHATGLLSFIRRVKLSNPPSAGPIVVH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 257096042 1118 CSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14631   157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 926-1167 9.47e-56

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 195.71  E-value: 9.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  926 ELKLIGLDIPH----FAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRN 1001
Cdd:cd14629    31 EFKLLANSKAHtsrfISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1002 DFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNY 1079
Cdd:cd14629   111 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSrtIRQFQF 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1080 TAWPDHGVPpaNAAESILQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYR 1157
Cdd:cd14629   190 TDWPEQGVP--KTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQR 267

                         250
                  ....*....|
gi 257096042 1158 MSMVQTEEQY 1167
Cdd:cd14629   268 PAMVQTEDQY 277
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 944-1175 1.34e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 193.70  E-value: 1.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCKNRYTNILPYDFSRVRLVSMN-EEEGADYINANYI-PGYNS-------PQEYIATQGPLPETRNDFWKMVLQQKSHI 1014
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1015 IVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEA---QDVMHFNYTAWPDHGVPPAN 1091
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGnteRTVWQYHFRTWPDHGVPSDP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1092 AAesILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQ 1166
Cdd:cd14605   162 GG--VLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQ 239


                  ....*....
gi 257096042 1167 YIFIHQCVQ 1175
Cdd:cd14605   240 YRFIYMAVQ 248
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 947-1174 1.66e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 192.75  E-value: 1.66e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  947 KNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRR 1026
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1027 VKCDHYWPFT-EEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQ 1105
Cdd:cd14602    81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVP--SSIDPILELIWDVRC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257096042 1106 QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH---EFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14602   159 YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 933-1174 4.62e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 192.49  E-value: 4.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  933 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEeegaDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 1012
Cdd:cd14607    13 DYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEN----DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1013 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDIT---VEMVSEEEEEDWASRHFRINYAD--EAQDVMHFNYTAWPDHGV 1087
Cdd:cd14607    89 KAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETgfsVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1088 PPANAaeSILQFVFTVRQQAAKS--KGPMIIHCSAGVGRTGTFIALDR--LLQHIRDHEFVDILGLVSEMRSYRMSMVQT 1163
Cdd:cd14607   169 PESPA--SFLNFLFKVRESGSLSpeHGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQT 246

                         250
                  ....*....|.
gi 257096042 1164 EEQYIFIHQCV 1174
Cdd:cd14607   247 PDQLRFSYMAV 257
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 974-1172 9.18e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 189.56  E-value: 9.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMltQCNEKR--RVKCDHYWP-FTEEPIAYGDITVEMV 1050
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVM--ACREFEmgKKKCERYWPeEGEEQLQFGPFKISLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1051 SEEEE-EDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPanAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFI 1129
Cdd:cd14542    79 KEKRVgPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPS--SVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTIC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 257096042 1130 ALD---RLLQ-HIRDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14542   157 AIDyvwNLLKtGKIPEEF-SLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 974-1174 1.16e-54

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 189.11  E-value: 1.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMVSEE 1053
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP--DDSDTYGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHF---RINYADEaQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIA 1130
Cdd:cd14632    79 TLAEYSVRTFaleRRGYSAR-HEVKQFHFTSWPEHGVP--YHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 257096042 1131 LDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14632   156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 974-1175 1.68e-52

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 182.85  E-value: 1.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEE 1053
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP-EDGSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIAL 1131
Cdd:cd14552    80 DYEDYTLRDFLVtkGKGGSTRTVRQFHFHGWPEVGI-PDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCAL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 257096042 1132 DRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 1175
Cdd:cd14552   159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 973-1175 1.79e-52

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 182.90  E-value: 1.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  973 DYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSE 1052
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWP-SEGSVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1053 EEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAESILQFVFTV-RQQAAKSKGPMIIHCSAGVGRTGTFI 1129
Cdd:cd14622    80 TLLETISIRDFLVTYNQEKQTrlVRQFHFHGWPEIGIP--AEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 257096042 1130 ALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 1175
Cdd:cd14622   158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQ 203
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 974-1172 2.05e-51

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 179.72  E-value: 2.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPiAYGDITVEMVSEE 1053
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW-TYGNLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHFRINYADEAQD------VMHFNYTAWPDHGVPPANAAesILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGT 1127
Cdd:cd14551    80 VLVDYTTRKFCIQKVNRGIGekrvrlVTQFHFTSWPDFGVPFTPIG--MLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 257096042 1128 FIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 949-1175 4.98e-51

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 179.86  E-value: 4.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  949 RYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVK 1028
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1029 CDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQ 1106
Cdd:cd14623    81 CAQYWP-SDGSVSYGDITIELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGWPEVGIP--SDGKGMINIIAAVQKQ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1107 AAKSKG-PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 1175
Cdd:cd14623   158 QQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQ 227
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 974-1171 2.93e-50

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 176.43  E-value: 2.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMVSEE 1053
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG--DEKKTYGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPP-----ANAAESILQFVFTVRQQAAKSKgPMIIHCSAGVGRTG 1126
Cdd:cd14558    79 KSPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEkpkdlVDMIKSIKQKLPYKNSKHGRSV-PIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 257096042 1127 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1171
Cdd:cd14558   158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 974-1174 2.13e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 171.47  E-value: 2.13e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFT-EEPIAYGDITVEMV 1050
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1051 SEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRqqAAKSKGPMIIHCSAGVGRTGTF 1128
Cdd:cd14596    81 NYQALQYFIIRIIKLveKETGENRLIKHLQFTTWPDHGTP--QSSDQLVKFICYMR--KVHNTGPIVVHCSAGIGRAGVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 257096042 1129 IALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 974-1171 1.35e-47

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 169.18  E-value: 1.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQ-CNEKRRVKCDHYWPFTE-EPIAYGDITVEM 1049
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRlVDNYSTAKCADYFPAEEnESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1050 VSEEEEED-WASRHFRINYAdEAQD----VMHFNYTAWPDHGVPPANAA-ESILQFVFTVrqqaAKSKGPMIIHCSAGVG 1123
Cdd:cd17658    81 KKLKHSQHsITLRVLEVQYI-ESEEpplsVLHIQYPEWPDHGVPKDTRSvRELLKRLYGI----PPSAGPIVVHCSAGIG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 257096042 1124 RTGTFIALDRLLQHIR--DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1171
Cdd:cd17658   156 RTGAYCTIHNTIRRILegDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
943-1170 2.53e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.96  E-value: 2.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  943 LNRCK-NRYTNILPYDFSRVRlvsmneeEGADYINANYIPGYNsPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1021
Cdd:COG5599    40 INGSPlNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1022 NE--KRRVKCDHYWPFTEEPIAYgDITVEMVSEEE-EEDWASRHFRINYAD---EAQDVMHFNYTAWPDHGVPPANAAES 1095
Cdd:COG5599   112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTESIQlRDGIEARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISAEALKN 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096042 1096 ILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE--FVDILGLVSEMRSYR-MSMVQTEEQYIFI 1170
Cdd:COG5599   191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 973-1170 1.18e-45

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 163.58  E-value: 1.18e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  973 DYINANYI----PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVE 1048
Cdd:cd14601     1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1049 MVSEEEEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 1126
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNleKNESRPLTQIQYIAWPDHGVP--DDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 257096042 1127 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 1170
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 974-1172 5.20e-45

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 161.42  E-value: 5.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvKCDHYWPfTEEPIAYGDITVEMVSEE 1053
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWP-DEGSGTYGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHFRI----NYADEAQDVMHFNYTAWPDHG-VPPAnaAESILQFVFTVRQ-QAAKSKGPMIIHCSAGVGRTGT 1127
Cdd:cd14556    79 IDEDVISRIFRLqnttRPQEGYRMVQQFQFLGWPRDRdTPPS--KRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSGV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 257096042 1128 FIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14556   157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 974-1172 1.62e-43

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 157.16  E-value: 1.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGY-NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTE--EPIAYGDITVEMV 1050
Cdd:cd14539     1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWP-TErgQALVYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1051 SEEEEEDWASRHFRINYADEAQ--DVMHFNYTAWPDHGVPPANAAesILQFVFTVR---QQAAKSKGPMIIHCSAGVGRT 1125
Cdd:cd14539    80 SVRTTPTHVERIISIQHKDTRLsrSVVHLQFTTWPELGLPDSPNP--LLRFIEEVHshyLQQRSLQTPIVVHCSSGVGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 257096042 1126 GTFIALDRLLQHIR-DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14539   158 GAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 974-1172 3.52e-43

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 156.85  E-value: 3.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGY--NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFT---EEPIAYGDITVE 1048
Cdd:cd14540     1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggeHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1049 MVSEEEEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQF---VFTVRQQAAKSKG------PMIIH 1117
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHtlSGQSRTVWHLQYTDWPDHGCP--EDVSGFLDFleeINSVRRHTNQDVAghnrnpPTLVH 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 257096042 1118 CSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14540   159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYN 213
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 939-1172 9.20e-43

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 158.24  E-value: 9.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  939 ADLPLNRCKNRYTNILPYDFSRVRLVSmNEEEGADYINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSHIIV 1016
Cdd:cd14599    33 ATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1017 MLTQCNEKRRVKCDHYWP---FTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPP-A 1090
Cdd:cd14599   112 MVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQErtVWHLQYTDWPDHGCPEeV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1091 NAAESILQFVFTVRQQA-------AKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQT 1163
Cdd:cd14599   192 QGFLSYLEEIQSVRRHTnsmldstKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQT 271


                  ....*....
gi 257096042 1164 EEQYIFIHQ 1172
Cdd:cd14599   272 IAQYKFVYQ 280
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 944-1169 3.89e-41

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 153.29  E-value: 3.89e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNsPQE--YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1021
Cdd:cd14610    44 NVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHD-PRNpaYIATQGPLPATVADFWQMVWESGCVVIVMLTPL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1022 NEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEE-EEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQ 1098
Cdd:cd14610   123 AENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGVP--ASTRSLLD 199

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257096042 1099 FVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 1169
Cdd:cd14610   200 FRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 944-1174 2.03e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 151.69  E-value: 2.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1023
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1024 KRRVKCDHYW-PFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQ--DVMHFNYTAWPDHGVPpaNAAESILQFV 1100
Cdd:PHA02742  130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGAslDIKHFAYEDWPHGGLP--RDPNKFLDFV 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1101 FTVRQQAAKS-----------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 1169
Cdd:PHA02742  208 LAVREADLKAdvdikgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                  ....*
gi 257096042 1170 IHQCV 1174
Cdd:PHA02742  288 CYFIV 292
PHA02738 PHA02738
hypothetical protein; Provisional
 944-1176 2.86e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 152.00  E-value: 2.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1023
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPA--ERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1024 KRRVKCDHYWPFTEE-PIAYGDITVEMVSEEEEEDWASRHFRINYADEA-QDVMHFNYTAWPDHGVPpaNAAESILQFVF 1101
Cdd:PHA02738  127 NGREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVP--KNTSEFLNFVL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1102 TVRQ------QAAKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 1168
Cdd:PHA02738  205 EVRQcqkelaQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                  ....*...
gi 257096042 1169 FIHQCVQL 1176
Cdd:PHA02738  285 FCYRAVKR 292
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 944-1169 3.89e-38

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 144.41  E-value: 3.89e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNsPQ--EYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1021
Cdd:cd14609    42 NVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHD-PRmpAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1022 NEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEE-EEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQ 1098
Cdd:cd14609   121 VEDGVKQCDRYWP-DEGSSLYHIYEVNLVSEHIwCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGIP--SSTRPLLD 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257096042 1099 FVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 1169
Cdd:cd14609   198 FRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1074-1174 4.41e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.88  E-value: 4.41e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   1074 VMHFNYTAWPDHGVPPAnaAESILQFVFTVR--QQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRD-HEFVDILGLV 1150
Cdd:smart00404    2 VKHYHYTGWPDHGVPES--PDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....
gi 257096042   1151 SEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:smart00404   80 KELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1074-1174 4.41e-38

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 137.88  E-value: 4.41e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   1074 VMHFNYTAWPDHGVPPAnaAESILQFVFTVR--QQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRD-HEFVDILGLV 1150
Cdd:smart00012    2 VKHYHYTGWPDHGVPES--PDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....
gi 257096042   1151 SEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:smart00012   80 KELRSQRPGMVQTEEQYLFLYRAL 103
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 974-1174 5.22e-38

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 141.43  E-value: 5.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSE 1052
Cdd:cd14546     1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-EEGSEVYHIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1053 EE-EEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFI 1129
Cdd:cd14546    80 HIwCDDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIP--ASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 257096042 1130 ALD----RLLQHIRDhefVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14546   158 LIDmvlnRMAKGAKE---IDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 942-1181 9.69e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 144.79  E-value: 9.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  942 PLNRCKNRYTNILPYDFSRV-------------------RLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRND 1002
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1003 FWKMVLQQKSHIIVMLTQCNEKRRvKCDHYWPFTEE-PIAYGDITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNY 1079
Cdd:PHA02746  129 FFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDsELAFGRFVAKILDIIEELSFTKTRLMITdkISDTSREIHHFWF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1080 TAWPDHGVpPANAAEsILQFVFTVRQQAAKSK----------GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGL 1149
Cdd:PHA02746  208 PDWPDNGI-PTGMAE-FLELINKVNEEQAELIkqadndpqtlGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                         250       260       270
                  ....*....|....*....|....*....|..
gi 257096042 1150 VSEMRSYRMSMVQTEEQYIFIHQCVQLMWLRK 1181
Cdd:PHA02746  286 VLKIRKQRHSSVFLPEQYAFCYKALKYAIIEE 317
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 942-1171 1.28e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 135.13  E-value: 1.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  942 PLNRCKNRYTNILPYDFSRVRLVSmNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1021
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1022 NEKR-RVKCDHYWPFTEE-PIAYGDITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVpPANAAESI- 1096
Cdd:PHA02747  128 KGTNgEEKCYQYWCLNEDgNIDMEDFRIETLKTSVRAKYILTLIEITdkILKDSRKISHFQCSEWFEDET-PSDHPDFIk 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1097 -LQFVFTVRQQAAKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 1168
Cdd:PHA02747  207 fIKIIDINRKKSGKLFNpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                  ...
gi 257096042 1169 FIH 1171
Cdd:PHA02747  287 FIQ 289
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 974-1172 6.07e-34

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 130.48  E-value: 6.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPF---TEEPIAYGDITVE 1048
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgsRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1049 MVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPP-ANAAESILQFVFTVRQQAAKS------KGPMIIHCS 1119
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKHLLTGQErtVWHLQYTDWPEHGCPEdLKGFLSYLEEIQSVRRHTNSTidpkspNPPVLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 257096042 1120 AGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14598   161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYK 213
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 974-1172 1.06e-33

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 128.99  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvkCDHYWPfTEEPIAYGDITVEMVSEE 1053
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL--CMQYWP-EKTSCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHFRINYADEAQD----VMHFNYTAWPDH-GVPPANaaESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRT 1125
Cdd:cd14634    78 IDEDIISRIFRICNMARPQDgyriVQHLQYIGWPAYrDTPPSK--RSILKVVRRLekwQEQYDGREGRTVVHCLNGGGRS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 257096042 1126 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14634   156 GTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYE 202
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 974-1174 7.72e-31

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 120.78  E-value: 7.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV-KCDHYWPfteEP--IAYGDITVEMV 1050
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP---EPglQQYGPMEVEFV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1051 SEEEEEDWASRHFRINYADEAQD----VMHFNYTAWPDHGVPPaNAAESILQFVFTVRQ-QAAKSKGPMIIHCSAGVGRT 1125
Cdd:cd14637    78 SGSADEDIVTRLFRVQNITRLQEghlmVRHFQFLRWSAYRDTP-DSKKAFLHLLASVEKwQRESGEGRTVVHCLNGGGRS 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 257096042 1126 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd14637   157 GTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 974-1171 8.08e-31

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 120.90  E-value: 8.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRrvKCDHYWPfTEEPIAYGDITVEMVSEE 1053
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWP-EEGMLRYGPIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHFRINYADEAQD----VMHFNYTAWPDHGVPPAnAAESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRTG 1126
Cdd:cd14636    78 MDCDVISRIFRICNLTRPQEgylmVQQFQYLGWASHREVPG-SKRSFLKLILQVekwQEECDEGEGRTIIHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 257096042 1127 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1171
Cdd:cd14636   157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 974-1172 2.76e-29

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 116.27  E-value: 2.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCdhYWPFTEEPIAYGDITV-----E 1048
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVtlsgeD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1049 MVSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDhgvpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 1126
Cdd:cd14550    79 HSCLSNEIRLIVRDFILesTQDDYVLEVRQFQCPSWPN----PCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 257096042 1127 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14550   155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 974-1172 1.37e-26

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 108.62  E-value: 1.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvkCDHYWPftEEPI-AYGDITVEMVSE 1052
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP--ENGVhRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1053 EEEEDWASRHFRINYADEAQD----VMHFNYTAWPDHGVPPAnAAESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRT 1125
Cdd:cd14635    77 DLEEDIISRIFRIYNAARPQDgyrmVQQFQFLGWPMYRDTPV-SKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 257096042 1126 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1172
Cdd:cd14635   156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 202
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 974-1174 3.34e-25

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 104.69  E-value: 3.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCdHYWPFTEEPIAYGDITVEMVSEE 1053
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 EEEDWASRHFRI-NYADEA-QD-----VMHFNYTAWPDhgvpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 1126
Cdd:cd17669    80 HKCLSNEEKLIIqDFILEAtQDdyvleVRHFQCPKWPN----PDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 257096042 1127 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd17669   156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 974-1174 7.68e-25

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 103.60  E-value: 7.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  974 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQcNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEE 1053
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1054 eeedwasrhfRINYADEAQ-----------------DVMHFNYTAWPDhgvpPANAAESILQFVFTVRQQAAKSKGPMII 1116
Cdd:cd17670    80 ----------RLCLSNEEQiiihdfileatqddyvlEVRHFQCPKWPN----PDAPISSTFELINVIKEEALTRDGPTIV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 257096042 1117 HCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1174
Cdd:cd17670   146 HDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 948-1167 7.87e-18

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 83.99  E-value: 7.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  948 NRYTNIlpydfsrvrlVSMNEEEGADYINANYIPGYNSPQeYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1027
Cdd:cd14559     1 NRFTNI----------QTRVSTPVGKNLNANRVQIGNKNV-AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1028 KCDHYWPFTEEpiaYGDITV--EMVSEEEEEDWASRH---FRINYADEAQDVMHFNYTAWPDHGVPPANAAESILQFVFT 1102
Cdd:cd14559    70 GLPPYFRQSGT---YGSVTVksKKTGKDELVDGLKADmynLKITDGNKTITIPVVHVTNWPDHTAISSEGLKELADLVNK 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257096042 1103 VRQQAA-------------KSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDIlglVSEMRSYRMS-MVQTEEQY 1167
Cdd:cd14559   147 SAEEKRnfykskgssaindKNKLLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRNGkMVQKDEQL 222
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 944-1191 2.79e-15

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 78.08  E-value: 2.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  944 NRCK--NRYTNILPYDFSRVRLVSMNEeegadYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1021
Cdd:PHA02740   51 NKAKdeNLALHITRLLHRRIKLFNDEK-----VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1022 NEKrrvKC-DHYWPFTEEP-IAYGDITVEMVSEEEEEdwasrHFRI------NYADEAQDVMHFNYTAWPDHGVppANAA 1093
Cdd:PHA02740  126 ADK---KCfNQFWSLKEGCvITSDKFQIETLEIIIKP-----HFNLtllsltDKFGQAQKISHFQYTAWPADGF--SHDP 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1094 ESILQFVFTV--------RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEE 1165
Cdd:PHA02740  196 DAFIDFFCNIddlcadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLD 275

                         250       260
                  ....*....|....*....|....*.
gi 257096042 1166 QYIFihqCVQLMWLRKKQQFCISDVI 1191
Cdd:PHA02740  276 DYVF---CYHLIAAYLKEKFDILKFI 298
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1091-1172 3.12e-10

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 58.52  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1091 NAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRdhefvDILGLVSEMRSYR-MSMVQTEEQYIF 1169
Cdd:cd14494    36 DLTLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRpGGIPQTIEQLDF 110


                  ...
gi 257096042 1170 IHQ 1172
Cdd:cd14494   111 LIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1082-1172 7.36e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 58.44  E-value: 7.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1082 WPDHGVPPANAAESILQFVftvrQQAAKSKGPMIIHCSAGVGRTGTFIAldrLLQHIRDHEFVDILGLVSEMRSYRmsmV 1161
Cdd:COG2453    55 IPDFGAPDDEQLQEAVDFI----DEALREGKKVLVHCRGGIGRTGTVAA---AYLVLLGLSAEEALARVRAARPGA---V 124

                          90
                  ....*....|.
gi 257096042 1162 QTEEQYIFIHQ 1172
Cdd:COG2453   125 ETPAQRAFLER 135
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1071-1183 4.61e-06

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 48.88  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1071 AQDVMHFNYtAWPDHGVPPANAAESILQfvftVRQQAAKSKGPMIIHCSAGVGRTGTFIA-----LDRLL--QHIRdheF 1143
Cdd:cd14506    74 RAGIYFYNF-GWKDYGVPSLTTILDIVK----VMAFALQEGGKVAVHCHAGLGRTGVLIAcylvyALRMSadQAIR---L 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 257096042 1144 VdilglvsemRSYRMSMVQTEEQYIFIHQCVQLMWLRKKQ 1183
Cdd:cd14506   146 V---------RSKRPNSIQTRGQVLCVREFAQFLLPLRNV 176
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1083-1172 8.90e-06

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 47.26  E-value: 8.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1083 PDHGVPPANAaesilQFVFTVRQ--QAAKSKGPMIIHCSAGVGRTGTFIAldRLLQHIRDHEFVD-ILGLVsemRSYRMS 1159
Cdd:cd14505    81 PDGGVPSDIA-----QWQELLEEllSALENGKKVLIHCKGGLGRTGLIAA--CLLLELGDTLDPEqAIAAV---RALRPG 150

                          90
                  ....*....|...
gi 257096042 1160 MVQTEEQYIFIHQ 1172
Cdd:cd14505   151 AIQTPKQENFLHQ 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1083-1172 1.18e-05

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 46.50  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042 1083 PDHGVPpanAAESILQFVFTVRQQAAKSKgPMIIHCSAGVGRTGTFIALdrllqHIRDHEFVDILGLVSEMRSYRMSMVQ 1162
Cdd:cd14504    58 EDYTPP---TLEQIDEFLDIVEEANAKNE-AVLVHCLAGKGRTGTMLAC-----YLVKTGKISAVDAINEIRRIRPGSIE 128

                          90
                  ....*....|
gi 257096042 1163 TEEQYIFIHQ 1172
Cdd:cd14504   129 TSEQEKFVIQ 138
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 444-536 1.76e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 44.41  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  444 EKPQHVSVHVLSSTTALMSWTSSQENyNSTIVS-VVSLTCQKQKESQRLEKqycTQVNSSKPVIENLVPGAQYQVVMYLR 522
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGyVVEYREKGSGDWKEVEV---TPGSETSYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....
gi 257096042  523 KGPLIGPPSDPVTF 536
Cdd:cd00063    78 NGGGESPPSESVTV 91
fn3 pfam00041
Fibronectin type III domain;
445-531 1.91e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   445 KPQHVSVHVLSSTTALMSWTSSqENYNSTIVSVvSLTCQKQKESQrlekqYCTQVNSSKP----VIENLVPGAQYQVVMY 520
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPP-PDGNGPITGY-EVEYRPKNSGE-----PWNEITVPGTttsvTLTGLKPGTEYEVRVQ 74

                           90
                   ....*....|.
gi 257096042   521 LRKGPLIGPPS 531
Cdd:pfam00041   75 AVNGGGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
735-815 2.35e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.94  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042   735 PPKSLFAVNKTQTSVTLLWVE----EGVADFFEVFCQQLGSGhNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDT 810
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 257096042   811 PSVPT 815
Cdd:pfam00041   81 EGPPS 85
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 1060-1131 8.78e-05

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 44.29  E-value: 8.78e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257096042 1060 SRHFRINYADEAQDVMHFNYTAWPDHGVPPANAAESIlqfvFTVRQQAAKSKGPMIIHCSAGVGRTGTFIAL 1131
Cdd:cd14529    42 GADERAASEEAAAKIDGVKYVNLPLSATRPTESDVQS----FLLIMDLKLAPGPVLIHCKHGKDRTGLVSAL 109
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 540-640 1.19e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.10  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  540 PTGIKDLMLYPLGPTAVVLSWTRP--ILGVFRKYVVEMFyfnpTTMTSEWTtyyEIAATVSLTASVRIASLLPAWYYNFR 617
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYR----EKGSGDWK---EVEVTPGSETSYTLTGLKPGTEYEFR 73

                          90       100
                  ....*....|....*....|....*.
gi 257096042  618 VTMVT---WGDPelsccdSSTISFIT 640
Cdd:cd00063    74 VRAVNgggESPP------SESVTVTT 93
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1083-1131 2.49e-04

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 43.21  E-value: 2.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 257096042 1083 PDHGVPPanaaESILQ-FVftvrQQAAKSKGPMIIHCSAGVGRTGTFIAL 1131
Cdd:cd14499    88 PDGSTPS----DDIVKkFL----DICENEKGAIAVHCKAGLGRTGTLIAC 129
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 733-815 2.84e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.94  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042  733 PAPPKSLFAVNKTQTSVTLLWV----EEGVADFFEVFCQQLGSGhNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSH 808
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTppedDGGPITGYVVEYREKGSG-DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ....*..
gi 257096042  809 DTPSVPT 815
Cdd:cd00063    80 GGESPPS 86
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 733-812 3.73e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 40.29  E-value: 3.73e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042    733 PAPPKSLFAVNKTQTSVTLLW--VEEGVADFFEVFCQQLGSGHNGKLQE-PVAVSSHVVTISSLLPATAYNCSVTSFSHD 809
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWepPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 257096042    810 TPS 812
Cdd:smart00060   81 GEG 83
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 1061-1129 4.04e-04

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 42.74  E-value: 4.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096042 1061 RHFRI-NYADE-AQDVMHFNYTA----WPDHGVPPAnaaESILQFVFTVRQ-QAAKSKGPMIIHCSAGVGRTGTFI 1129
Cdd:cd14510    54 DHYKVyNLCSErGYDPKYFHNRVervpIDDHNVPTL---DEMLSFTAEVREwMAADPKNVVAIHCKGGKGRTGTMV 126
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 540-622 1.69e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 38.75  E-value: 1.69e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096042    540 PTGIKDLMLYPLGPTAVVLSWTRPILGVFRKYVVEMFYFNpTTMTSEWTTyyeiAATVSLTASVRIASLLPAWYYNFRVT 619
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEY-REEGSEWKE----VNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ...
gi 257096042    620 MVT 622
Cdd:smart00060   76 AVN 78
 
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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