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Conserved domains on  [gi|1907171683|ref|XP_036021848|]
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receptor-type tyrosine-protein phosphatase O isoform X3 [Mus musculus]

Protein Classification

FN3 and R-PTPc-O domain-containing protein( domain architecture ID 12877337)

FN3 and R-PTPc-O domain-containing protein

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 ...
 960-1204 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: 542.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  960 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 1039
Cdd:cd14614      1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1040 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANA 1119
Cdd:cd14614     81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1120 AESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14614    161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                   ....*
gi 1907171683 1200 CVQLM 1204
Cdd:cd14614    241 CVQLM 245
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 443-535 1.62e-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: 44.79  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  443 EKPQHVSVHVLSSTTALMSWTSSQENyNSTIVS-VVSLTCQKQKESQRLEKqycTQVNSSKPVIENLVPGAQYQVVMYLR 521
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGyVVEYREKGSGDWKEVEV---TPGSETSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....
gi 1907171683  522 KGPLIGPPSDPVTF 535
Cdd:cd00063     78 NGGGESPPSESVTV 91
fn3 pfam00041
Fibronectin type III domain;
734-814 2.20e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.94  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  734 PPKSLFAVNKTQTSVTLLWVE----EGVADFFEVFCQQLGSGhNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDT 809
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1907171683  810 PSVPT 814
Cdd:pfam00041   81 EGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 539-639 1.12e-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: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  539 PTGIKDLMLYPLGPTAVVLSWTRP--ILGVFRKYVVEMFyfnpTTMTSEWTtyyEIAATVSLTASVRIASLLPAWYYNFR 616
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYR----EKGSGDWK---EVEVTPGSETSYTLTGLKPGTEYEFR 73

                           90       100
                   ....*....|....*....|....*.
gi 1907171683  617 VTMVT---WGDPelsccdSSTISFIT 639
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 ...
 960-1204 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: 542.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  960 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 1039
Cdd:cd14614      1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1040 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANA 1119
Cdd:cd14614     81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1120 AESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14614    161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                   ....*
gi 1907171683 1200 CVQLM 1204
Cdd:cd14614    241 CVQLM 245
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
946-1201 1.67e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 354.66  E-value: 1.67e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683   946 KFSLQFEELKLIGLDIPHFA-ADLPLNRCKNRYTNILPYDFSRVRLvSMNEEEGADYINANYIPGYNSPQEYIATQGPLP 1024
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  1025 ETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTE-EPIAYGDITVEMVSEEEEEDWASRHFRINYAD--EAQDV 1101
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  1102 MHFNYTAWPDHGVPPAnaAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMR 1181
Cdd:smart00194  160 THYHYTNWPDHGVPES--PESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|
gi 1907171683  1182 SYRMSMVQTEEQYIFIHQCV 1201
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
971-1201 1.50e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 326.89  E-value: 1.50e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLvsMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1050
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1051 KRRVKCDHYWPFT-EEPIAYGDITVEMVSEEEEE-DWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPPANAaeSILQF 1126
Cdd:pfam00102   79 KGREKCAQYWPEEeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPN--SLLDL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907171683 1127 VFTVRQ-QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:pfam00102  157 LRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
970-1197 2.65e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.96  E-value: 2.65e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  970 LNRCK-NRYTNILPYDFSRVRlvsmneeEGADYINANYIPGYNsPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1048
Cdd:COG5599     40 INGSPlNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1049 NE--KRRVKCDHYWPFTEEPIAYgDITVEMV-SEEEEEDWASRHFRINYAD---EAQDVMHFNYTAWPDHGVPPANAAES 1122
Cdd:COG5599    112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTeSIQLRDGIEARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISAEALKN 190

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907171683 1123 ILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE--FVDILGLVSEMRSYR-MSMVQTEEQYIFI 1197
Cdd:COG5599    191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 971-1201 1.92e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 152.08  E-value: 1.92e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1050
Cdd:PHA02742    52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1051 KRRVKCDHYW-PFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQ--DVMHFNYTAWPDHGVPpaNAAESILQFV 1127
Cdd:PHA02742   130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGAslDIKHFAYEDWPHGGLP--RDPNKFLDFV 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1128 FTVRQQAAKS-----------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 1196
Cdd:PHA02742   208 LAVREADLKAdvdikgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                   ....*
gi 1907171683 1197 IHQCV 1201
Cdd:PHA02742   288 CYFIV 292
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 443-535 1.62e-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: 44.79  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  443 EKPQHVSVHVLSSTTALMSWTSSQENyNSTIVS-VVSLTCQKQKESQRLEKqycTQVNSSKPVIENLVPGAQYQVVMYLR 521
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGyVVEYREKGSGDWKEVEV---TPGSETSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....
gi 1907171683  522 KGPLIGPPSDPVTF 535
Cdd:cd00063     78 NGGGESPPSESVTV 91
fn3 pfam00041
Fibronectin type III domain;
444-530 1.76e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  444 KPQHVSVHVLSSTTALMSWTSSqENYNSTIVSVvSLTCQKQKESQrlekqYCTQVNSSKP----VIENLVPGAQYQVVMY 519
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPP-PDGNGPITGY-EVEYRPKNSGE-----PWNEITVPGTttsvTLTGLKPGTEYEVRVQ 74

                           90
                   ....*....|.
gi 1907171683  520 LRKGPLIGPPS 530
Cdd:pfam00041   75 AVNGGGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
734-814 2.20e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.94  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  734 PPKSLFAVNKTQTSVTLLWVE----EGVADFFEVFCQQLGSGhNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDT 809
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1907171683  810 PSVPT 814
Cdd:pfam00041   81 EGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 539-639 1.12e-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: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  539 PTGIKDLMLYPLGPTAVVLSWTRP--ILGVFRKYVVEMFyfnpTTMTSEWTtyyEIAATVSLTASVRIASLLPAWYYNFR 616
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYR----EKGSGDWK---EVEVTPGSETSYTLTGLKPGTEYEFR 73

                           90       100
                   ....*....|....*....|....*.
gi 1907171683  617 VTMVT---WGDPelsccdSSTISFIT 639
Cdd:cd00063     74 VRAVNgggESPP------SESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 732-814 2.61e-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: 41.33  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  732 PAPPKSLFAVNKTQTSVTLLWV----EEGVADFFEVFCQQLGSGhNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSH 807
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTppedDGGPITGYVVEYREKGSG-DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   ....*..
gi 1907171683  808 DTPSVPT 814
Cdd:cd00063     80 GGESPPS 86
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 732-811 3.57e-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: 40.68  E-value: 3.57e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683   732 PAPPKSLFAVNKTQTSVTLLW--VEEGVADFFEVFCQQLGSGHNGKLQE-PVAVSSHVVTISSLLPATAYNCSVTSFSHD 808
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWepPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 1907171683   809 TPS 811
Cdd:smart00060   81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 539-621 1.63e-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: 1.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683   539 PTGIKDLMLYPLGPTAVVLSWTRPILGVFRKYVVEMFYFNpTTMTSEWTTyyeiAATVSLTASVRIASLLPAWYYNFRVT 618
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEY-REEGSEWKE----VNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ...
gi 1907171683   619 MVT 621
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 ...
 960-1204 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: 542.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  960 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 1039
Cdd:cd14614      1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1040 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANA 1119
Cdd:cd14614     81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1120 AESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14614    161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                   ....*
gi 1907171683 1200 CVQLM 1204
Cdd:cd14614    241 CVQLM 245
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 976-1199 2.98e-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: 415.99  E-value: 2.98e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  976 RYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVK 1055
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1056 CDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAA 1135
Cdd:cd14548     81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVP--EAPDSLLRFVRLVRDYIK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907171683 1136 KSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14548    159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
946-1201 1.67e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 354.66  E-value: 1.67e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683   946 KFSLQFEELKLIGLDIPHFA-ADLPLNRCKNRYTNILPYDFSRVRLvSMNEEEGADYINANYIPGYNSPQEYIATQGPLP 1024
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  1025 ETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTE-EPIAYGDITVEMVSEEEEEDWASRHFRINYAD--EAQDV 1101
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  1102 MHFNYTAWPDHGVPPAnaAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMR 1181
Cdd:smart00194  160 THYHYTNWPDHGVPES--PESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|
gi 1907171683  1182 SYRMSMVQTEEQYIFIHQCV 1201
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
971-1201 1.50e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 326.89  E-value: 1.50e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLvsMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1050
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1051 KRRVKCDHYWPFT-EEPIAYGDITVEMVSEEEEE-DWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPPANAaeSILQF 1126
Cdd:pfam00102   79 KGREKCAQYWPEEeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPN--SLLDL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907171683 1127 VFTVRQ-QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:pfam00102  157 LRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 975-1199 2.90e-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: 2.90e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  975 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1054
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1055 KCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRI---NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVR 1131
Cdd:cd14617     81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKIcseEQLDAPRLVRHFHYTVWPDHGVP--ETTQSLIQFVRTVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1132 QQAAKS--KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14617    159 DYINRTpgSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 975-1201 5.12e-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: 289.87  E-value: 5.12e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  975 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1054
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1055 KCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAESILQFVFTVRQ 1132
Cdd:cd14619     81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTlsVRHFHFTAWPDHGVP--SSTDTLLAFRRLLRQ 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907171683 1133 --QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14619    159 wlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 969-1201 9.16e-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: 9.16e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  969 PLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1048
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1049 NEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQF 1126
Cdd:cd14553     81 EERSRVKCDQYWP-TRGTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVP--EHPTPFLAF 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907171683 1127 VFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14553    158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 975-1201 5.74e-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: 5.74e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  975 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1054
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1055 KCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPPANAaeSILQFVFTVRQ 1132
Cdd:cd14618     81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKErrVKHLHYTAWPDHGIPESTS--SLMAFRELVRE 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907171683 1133 --QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14618    159 hvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1001-1199 8.78e-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: 282.25  E-value: 8.78e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWP-FTEEPIAYGDITVEMVSE 1079
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPeEGGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1080 EEEEDWASRHFRINYAD--EAQDVMHFNYTAWPDHGVPPanAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIA 1157
Cdd:cd00047     81 EELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPS--SPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907171683 1158 LDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd00047    159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 975-1201 9.01e-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: 278.24  E-value: 9.01e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  975 NRYTNILPYDFSRVRLVSMNEEEgADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1054
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHST-DDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1055 KCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAESILQFVFTVRQ 1132
Cdd:cd14615     80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESrtVRHFHFTSWPDHGVP--ETTDLLINFRHLVRE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907171683 1133 QAAKS--KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14615    157 YMKQNppNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCA 227
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 975-1199 2.58e-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: 2.58e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  975 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1054
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1055 KCDHYWPFTEEPIA-YGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANAaeSILQFVFTVRQQ 1133
Cdd:cd14616     81 RCHQYWPEDNKPVTvFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSA--PLIHFVKLVRAS 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907171683 1134 AAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14616    159 RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 965-1198 1.13e-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: 265.77  E-value: 1.13e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  965 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 1044
Cdd:cd14543     23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1045 LTQCNEKRRVKCDHYWPFTEEPIA-YGDITVEMVSEEEEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPPanAAE 1121
Cdd:cd14543    103 TTRVVERGRVKCGQYWPLEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTetDESRQVTHFQFTSWPDFGVPS--SAA 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1122 SILQFVFTVRQQAAKS--------KG-----PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMV 1188
Cdd:cd14543    181 ALLDFLGEVRQQQALAvkamgdrwKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSI 260

                          250
                   ....*....|
gi 1907171683 1189 QTEEQYIFIH 1198
Cdd:cd14543    261 QTPDQYYFCY 270
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 975-1199 4.12e-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: 4.12e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  975 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRr 1053
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1054 VKCDHYWPFtEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPAnaAESILQFVFTVRQ- 1132
Cdd:cd14547     80 EKCAQYWPE-EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEA--AQPLLSLVQEVEEa 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907171683 1133 -QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14547    157 rQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1001-1198 8.21e-77

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: 252.27  E-value: 8.21e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEE 1080
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP-KEGTETYGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHF--------RINYADEAQDVMHFNYTAWPDHGVPPANAaeSILQFvftVRQQAAKSK---GPMIIHCSAGV 1149
Cdd:cd14549     80 VLATYTVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTL--PVLSF---VRKSSAANPpgaGPIVVHCSAGV 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907171683 1150 GRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1198
Cdd:cd14549    155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 931-1201 2.13e-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: 2.13e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  931 DFDSYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGY 1010
Cdd:cd14626      2 DLADNIERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1011 NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPF--TEepiAYGDITVEMVSEEEEEDWASR 1088
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIrgTE---TYGMIQVTLLDTVELATYSVR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1089 HFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIR 1166
Cdd:cd14626    158 TFALykNGSSEKREVRQFQFMAWPDHGVP--EYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMK 235

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907171683 1167 DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14626    236 HEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 947-1198 1.45e-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: 240.32  E-value: 1.45e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  947 FSLQFEELKLIGLDIPHFA--ADLPLNRCKNRYTNILPYDFSRVRLVSM--NEEEGADYINANYIPGYNSPQEYIATQGP 1022
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1023 LPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRI-NYADEA--- 1098
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTKIHACYTVRRFSIrNTKVKKgqk 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1099 ---------QDVMHFNYTAWPDHGVPpaNAAESILQFVftVRQQAAKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRD 1167
Cdd:cd17667    160 gnpkgrqneRTVIQYHYTQWPDMGVP--EYALPVLTFV--RRSSAARTPemGPVLVHCSAGVGRTGTYIVIDSMLQQIKD 235

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907171683 1168 HEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1198
Cdd:cd17667    236 KSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 959-1203 6.85e-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: 6.85e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  959 LDIPHFAAdlplnrcKNRYTNILPYDFSRVRLVS-MNEEEGADYINANYIPGYN-SPQEYIATQGPLPETRNDFWKMVLQ 1036
Cdd:cd14612     10 LDIPGHAS-------KDRYKTILPNPQSRVCLRRaGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1037 QKSHIIVMLTQCNEKRRvKCDHYWPFTEEpiAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPp 1116
Cdd:cd14612     83 EECPIIVMITKLKEKKE-KCVHYWPEKEG--TYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTP- 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1117 aNAAESILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 1194
Cdd:cd14612    159 -ESAGPLLRLVAEVeeSRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQY 237


                   ....*....
gi 1907171683 1195 IFIHQCVQL 1203
Cdd:cd14612    238 QFLHHTLAL 246
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1001-1199 2.67e-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: 2.67e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYI-PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSE 1079
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1080 EEEEDWAS--RHFRINYADEA-QDVMHFNYTAWPDHGVPPanAAESILQFVFTVR--QQAAKSKGPMIIHCSAGVGRTGT 1154
Cdd:cd18533     81 EENDDGGFivREFELSKEDGKvKKVYHIQYKSWPDFGVPD--SPEDLLTLIKLKRelNDSASLDPPIIVHCSAGVGRTGT 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907171683 1155 FIALDRLLQHIRDHEFVD---------ILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd18533    159 FIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 926-1201 4.52e-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: 230.77  E-value: 4.52e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  926 PVQLDDFDSYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 1005
Cdd:cd14624      3 PIPILELADHIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1006 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDW 1085
Cdd:cd14624     82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1086 ASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQ 1163
Cdd:cd14624    161 CVRTFALykNGSSEKREVRQFQFTAWPDHGVP--EHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907171683 1164 HIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14624    239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 926-1201 7.53e-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: 7.53e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  926 PVQLDDFDSYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 1005
Cdd:cd14625      3 PIPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1006 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDW 1085
Cdd:cd14625     82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1086 ASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQ 1163
Cdd:cd14625    161 CVRTFSLhkNGSSEKREVRQFQFTAWPDHGVP--EYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907171683 1164 HIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14625    239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 965-1205 1.93e-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: 1.93e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  965 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 1044
Cdd:cd14603     24 AGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILM 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1045 LTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEE-EDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESI 1123
Cdd:cd14603    104 ACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLnEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIP--DSPDCM 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1124 LQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDR-----LLQHIRDHefVDILGLVSEMRSYRMSMVQTEEQYIFIH 1198
Cdd:cd14603    182 LAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLY 259


                   ....*..
gi 1907171683 1199 QCVQLMW 1205
Cdd:cd14603    260 HTVAQMF 266
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 971-1201 4.19e-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: 4.19e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1050
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1051 KRRVKCDHYWPftEEPIAYGDITVEMVSEEEEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVF 1128
Cdd:cd14630     83 VGRVKCVRYWP--DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKkgYHEIREIRQFHFTSWPDHGVP--CYATGLLGFVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907171683 1129 TVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14630    159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 931-1201 4.38e-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: 227.62  E-value: 4.38e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  931 DFDSYIKDMAKDSDYKFSLQFEELkLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGY 1010
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1011 NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEpiAYGDITVEMVSEEEEEDWASRHF 1090
Cdd:cd14633     80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTF 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1091 RINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH 1168
Cdd:cd14633    158 AVEKrgVHEIREIRQFHFTGWPDHGVP--YHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAERE 235

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907171683 1169 EFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
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 ...
 966-1199 1.74e-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: 224.33  E-value: 1.74e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  966 ADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVML 1045
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1046 TQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPpaNAAESI 1123
Cdd:cd14554     81 TKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDArdGQSRTVRQFQFTDWPEQGVP--KSGEGF 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907171683 1124 LQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14554    158 IDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 971-1202 1.26e-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: 219.64  E-value: 1.26e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLVSM-NEEEGADYINANYIPGYNSP-------QEYIATQGPLPETRNDFWKMVLQQKSHII 1042
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIRNENEGpttdenaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1043 VMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD---VMHFNYTAWPDHGVPpaNA 1119
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPireIWHYQYLSWPDHGVP--SD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1120 AESILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQY 1194
Cdd:cd14544    159 PGGVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQY 238


                   ....*...
gi 1907171683 1195 IFIHQCVQ 1202
Cdd:cd14544    239 KFIYVAVA 246
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1000-1201 6.03e-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: 6.03e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1000 DYINANY----IPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVE 1075
Cdd:cd14541      1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1076 MVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 1153
Cdd:cd14541     81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVP--DDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907171683 1154 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14541    159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAI 206
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 971-1201 3.01e-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: 209.30  E-value: 3.01e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLvsmnEEEGaDYINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1048
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1049 NEKRRVKCDHYWPFT-EEPIAYGD-ITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESIL 1124
Cdd:cd14597     78 VEGGKIKCQRYWPEIlGKTTMVDNrLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTP--SQPEQLL 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907171683 1125 QFVFTVRQqaAKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
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 ...
 1001-1199 5.04e-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: 207.37  E-value: 5.04e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWP-FTEEPIAYGDITVEMVSE 1079
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1080 EEEEDWASRHFRINYADE---AQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFI 1156
Cdd:cd14557     81 KICPDYIIRKLNINNKKEkgsGREVTHIQFTSWPDHGVP--EDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907171683 1157 ALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14557    159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 969-1201 4.65e-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: 4.65e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  969 PLNRCKNRYTNILPYDFSRVRLVSM-NEEEGADYINANYI------PGyNSPQEYIATQGPLPETRNDFWKMVLQQKSHI 1041
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGRdSNIPGSDYINANYVknqllgPD-ENAKTYIASQGCLEATVNDFWQMAWQENSRV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1042 IVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFR---INYADEAQDVMHFNYTAWPDHGVPPAN 1118
Cdd:cd14606     95 IVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQvspLDNGELIREIWHYQYLSWPDHGVPSEP 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1119 AAesILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQ 1193
Cdd:cd14606    175 GG--VLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQ 252


                   ....*...
gi 1907171683 1194 YIFIHQCV 1201
Cdd:cd14606    253 YKFIYVAI 260
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1001-1201 6.75e-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: 6.75e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMVSEE 1080
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP--DDTEVYGDIKVTLVETE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIAL 1158
Cdd:cd14555     79 PLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVP--YHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907171683 1159 DRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14555    157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1001-1201 7.94e-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: 7.94e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWP-FTEEP-IAYGDITVEM 1076
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPlICGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1077 VSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAakSKGPMIIHCSAGVGRTGT 1154
Cdd:cd14538     81 EKYQSLQDFVIRRISLrdKETGEVHHITHLNFTTWPDHGTP--QSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGV 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907171683 1155 FIALDRLLQHI-RDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14538    157 LITIDVALGLIeRDLPF-DIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 947-1203 9.41e-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: 9.41e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  947 FSLQ--FEELKLIGLDIPHFaaDLPLNRCKNRYTNILPYDFSRVRLVSMNEEEG-ADYINANYIPGYNSPQE-YIATQGP 1022
Cdd:cd14613      1 FLLQaeFFEIPMNFVDPKEY--DIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYGGEEKvYIATQGP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1023 LPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvKCDHYWPftEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVM 1102
Cdd:cd14613     79 TVNTVGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWP--EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1103 HFNYTAWPDHGVPpaNAAESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSE 1179
Cdd:cd14613    156 HYWYTSWPDQKTP--DNAPPLLQLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQ 233

                          250       260
                   ....*....|....*....|....
gi 1907171683 1180 MRSYRMSMVQTEEQYIFIHQCVQL 1203
Cdd:cd14613    234 LRLDRGGMIQTCEQYQFVHHVLSL 257
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 949-1197 2.40e-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: 205.47  E-value: 2.40e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  949 LQFEEL--KLIGLDIPhfAADLPLNRCKNRYTNILPYDFSRVRLvsmneEEGADYINANY----IPGYNSPQEYIATQGP 1022
Cdd:cd14600     18 IQFEQLyrKKPGLAIT--CAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGP 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1023 LPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYAD--EAQD 1100
Cdd:cd14600     91 LPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQtgEERT 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1101 VMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKgPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEM 1180
Cdd:cd14600    171 VTHLQYVAWPDHGVP--DDSSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKM 247

                          250
                   ....*....|....*..
gi 1907171683 1181 RSYRMSMVQTEEQYIFI 1197
Cdd:cd14600    248 RDQRAMMVQTSSQYKFV 264
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 971-1201 4.39e-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: 4.39e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1050
Cdd:cd14604     57 NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1051 KRRVKCDHYWP-FTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFT 1129
Cdd:cd14604    137 MGRKKCERYWPlYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVP--SSFDSILDMISL 214

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907171683 1130 VRQQAAKSKGPMIIHCSAGVGRTGTFIALD---RLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14604    215 MRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 926-1201 1.22e-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: 204.10  E-value: 1.22e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  926 PVQLDDFDSYIKDMAKDSDYKFSLQFEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 1005
Cdd:cd14621      7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1006 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDW 1085
Cdd:cd14621     87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDVTVLVDY 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1086 ASRHFRINYADEAQD------VMHFNYTAWPDHGVPPANAAesILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALD 1159
Cdd:cd14621    166 TVRKFCIQQVGDVTNkkpqrlITQFHFTSWPDFGVPFTPIG--MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVID 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1907171683 1160 RLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14621    244 AMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 977-1199 2.08e-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: 2.08e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  977 YTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKC 1056
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1057 DHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINY-----ADEAQDVMHFNYTAWPDHGVPPANAAesILQFVFTVR 1131
Cdd:cd14620     81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPqlpdgCKAPRLVTQLHFTSWPDFGVPFTPIG--MLKFLKKVK 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907171683 1132 QQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14620    158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 951-1196 1.18e-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: 1.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  951 FEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLvsmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDF 1030
Cdd:cd14608      5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1031 WKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEE-PIAYGD--ITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFN 1105
Cdd:cd14608     81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkEMIFEDtnLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1106 YTAWPDHGVPPANAaeSILQFVFTVRQQAAKSK--GPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEM 1180
Cdd:cd14608    161 YTTWPDFGVPESPA--SFLNFLFKVRESGSLSPehGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEM 238

                          250
                   ....*....|....*.
gi 1907171683 1181 RSYRMSMVQTEEQYIF 1196
Cdd:cd14608    239 RKFRMGLIQTADQLRF 254
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 974-1196 1.31e-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: 1.31e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  974 KNRYTNILPYDFSRVRLVSMNEEegADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRR 1053
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1054 VKCDHYWPFTEEP---IAYGDITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPPANAAesILQFVF 1128
Cdd:cd14545     79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAA--FLNFLQ 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907171683 1129 TVRQQAAKS--KGPMIIHCSAGVGRTGTFIALDRLLQHI--RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 1196
Cdd:cd14545    157 KVRESGSLSsdVGPPVVHCSAGIGRSGTFCLVDTCLVLIekGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 965-1199 4.77e-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: 199.57  E-value: 4.77e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  965 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 1044
Cdd:cd14627     47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1045 LTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAES 1122
Cdd:cd14627    127 LTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSrtVRQFQFTDWPEQGVP--KSGEG 203

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907171683 1123 ILQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14627    204 FIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1001-1198 6.49e-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: 195.97  E-value: 6.49e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEE 1080
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHFRINYAD----------EAQDVMHFNYTAWPDHGVPPANAAesILQFVFTVRQQAAKSKGPMIIHCSAGVG 1150
Cdd:cd17668     80 VLAYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYTQWPDMGVPEYTLP--VLTFVRKASYAKRHAVGPVVVHCSAGVG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907171683 1151 RTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1198
Cdd:cd17668    158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 965-1199 8.53e-57

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: 198.80  E-value: 8.53e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  965 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 1044
Cdd:cd14628     46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1045 LTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAES 1122
Cdd:cd14628    126 LTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSrtVRQFQFTDWPEQGVP--KSGEG 202

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907171683 1123 ILQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14628    203 FIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 974-1199 1.34e-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: 1.34e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  974 KNRYTNILPYDFSRVRLVSMNEEEG-ADYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEK 1051
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1052 RRvKCDHYWPftEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVR 1131
Cdd:cd14611     82 NE-KCVLYWP--EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTP--DSAQPLLQLMLDVE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1132 Q--QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14611    157 EdrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 987-1201 1.68e-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: 195.24  E-value: 1.68e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  987 RVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEP 1066
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP--DDT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1067 IAYGDITVEMVSEEEEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIH 1144
Cdd:cd14631     79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVP--YHATGLLSFIRRVKLSNPPSAGPIVVH 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907171683 1145 CSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14631    157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 953-1194 8.73e-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: 8.73e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  953 ELKLIGLDIPH----FAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRN 1028
Cdd:cd14629     31 EFKLLANSKAHtsrfISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1029 DFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNY 1106
Cdd:cd14629    111 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSrtIRQFQF 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1107 TAWPDHGVPpaNAAESILQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYR 1184
Cdd:cd14629    190 TDWPEQGVP--KTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQR 267

                          250
                   ....*....|
gi 1907171683 1185 MSMVQTEEQY 1194
Cdd:cd14629    268 PAMVQTEDQY 277
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 971-1202 1.41e-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: 1.41e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLVSMN-EEEGADYINANYI-PGYNS-------PQEYIATQGPLPETRNDFWKMVLQQKSHI 1041
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1042 IVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEA---QDVMHFNYTAWPDHGVPPAN 1118
Cdd:cd14605     82 IVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGnteRTVWQYHFRTWPDHGVPSDP 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1119 AAesILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQ 1193
Cdd:cd14605    162 GG--VLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQ 239


                   ....*....
gi 1907171683 1194 YIFIHQCVQ 1202
Cdd:cd14605    240 YRFIYMAVQ 248
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 974-1201 1.71e-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: 1.71e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  974 KNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRR 1053
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1054 VKCDHYWPFT-EEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQ 1132
Cdd:cd14602     81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVP--SSIDPILELIWDVRC 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907171683 1133 QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH---EFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14602    159 YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 960-1201 4.16e-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: 4.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  960 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEeegaDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 1039
Cdd:cd14607     13 DYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEN----DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1040 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDIT---VEMVSEEEEEDWASRHFRINYAD--EAQDVMHFNYTAWPDHGV 1114
Cdd:cd14607     89 KAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETgfsVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGV 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1115 PPANAaeSILQFVFTVRQQAAKS--KGPMIIHCSAGVGRTGTFIALDR--LLQHIRDHEFVDILGLVSEMRSYRMSMVQT 1190
Cdd:cd14607    169 PESPA--SFLNFLFKVRESGSLSpeHGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQT 246

                          250
                   ....*....|.
gi 1907171683 1191 EEQYIFIHQCV 1201
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; ...
 1001-1199 1.09e-54

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: 189.17  E-value: 1.09e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMltQCNEKR--RVKCDHYWP-FTEEPIAYGDITVEMV 1077
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVM--ACREFEmgKKKCERYWPeEGEEQLQFGPFKISLE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1078 SEEEE-EDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPanAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFI 1156
Cdd:cd14542     79 KEKRVgPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPS--SVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTIC 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907171683 1157 ALD---RLLQ-HIRDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14542    157 AIDyvwNLLKtGKIPEEF-SLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1001-1201 1.18e-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: 1.18e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMVSEE 1080
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP--DDSDTYGDIKITLLKTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHF---RINYADEaQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIA 1157
Cdd:cd14632     79 TLAEYSVRTFaleRRGYSAR-HEVKQFHFTSWPEHGVP--YHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIV 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907171683 1158 LDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14632    156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1001-1202 1.76e-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: 1.76e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEE 1080
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP-EDGSVSSGDITVELKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIAL 1158
Cdd:cd14552     80 DYEDYTLRDFLVtkGKGGSTRTVRQFHFHGWPEVGI-PDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCAL 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907171683 1159 DRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 1202
Cdd:cd14552    159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1000-1202 1.82e-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: 1.82e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1000 DYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSE 1079
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWP-SEGSVTHGEITIEIKND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1080 EEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAESILQFVFTV-RQQAAKSKGPMIIHCSAGVGRTGTFI 1156
Cdd:cd14622     80 TLLETISIRDFLVTYNQEKQTrlVRQFHFHGWPEIGIP--AEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFI 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907171683 1157 ALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 1202
Cdd:cd14622    158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQ 203
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1001-1199 1.59e-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: 180.11  E-value: 1.59e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPiAYGDITVEMVSEE 1080
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW-TYGNLRVRVEDTV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHFRINYADEAQD------VMHFNYTAWPDHGVPPANAAesILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGT 1154
Cdd:cd14551     80 VLVDYTTRKFCIQKVNRGIGekrvrlVTQFHFTSWPDFGVPFTPIG--MLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907171683 1155 FIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14551    158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 976-1202 5.06e-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: 5.06e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  976 RYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVK 1055
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1056 CDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQ 1133
Cdd:cd14623     81 CAQYWP-SDGSVSYGDITIELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGWPEVGIP--SDGKGMINIIAAVQKQ 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1134 AAKSKG-PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 1202
Cdd:cd14623    158 QQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQ 227
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1001-1198 3.04e-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: 3.04e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMVSEE 1080
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG--DEKKTYGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPP-----ANAAESILQFVFTVRQQAAKSKgPMIIHCSAGVGRTG 1153
Cdd:cd14558     79 KSPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEkpkdlVDMIKSIKQKLPYKNSKHGRSV-PIVVHCSDGSSRTG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907171683 1154 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1198
Cdd:cd14558    158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1001-1201 2.10e-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: 2.10e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFT-EEPIAYGDITVEMV 1077
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1078 SEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRqqAAKSKGPMIIHCSAGVGRTGTF 1155
Cdd:cd14596     81 NYQALQYFIIRIIKLveKETGENRLIKHLQFTTWPDHGTP--QSSDQLVKFICYMR--KVHNTGPIVVHCSAGIGRAGVL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907171683 1156 IALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14596    157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1001-1198 9.41e-48

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: 169.57  E-value: 9.41e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQ-CNEKRRVKCDHYWPFTE-EPIAYGDITVEM 1076
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRlVDNYSTAKCADYFPAEEnESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1077 VSEEEEED-WASRHFRINYAdEAQD----VMHFNYTAWPDHGVPPANAA-ESILQFVFTVrqqaAKSKGPMIIHCSAGVG 1150
Cdd:cd17658     81 KKLKHSQHsITLRVLEVQYI-ESEEpplsVLHIQYPEWPDHGVPKDTRSvRELLKRLYGI----PPSAGPIVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1151 RTGTFIALDRLLQHIR--DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1198
Cdd:cd17658    156 RTGAYCTIHNTIRRILegDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
970-1197 2.65e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.96  E-value: 2.65e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  970 LNRCK-NRYTNILPYDFSRVRlvsmneeEGADYINANYIPGYNsPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1048
Cdd:COG5599     40 INGSPlNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1049 NE--KRRVKCDHYWPFTEEPIAYgDITVEMV-SEEEEEDWASRHFRINYAD---EAQDVMHFNYTAWPDHGVPPANAAES 1122
Cdd:COG5599    112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTeSIQLRDGIEARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISAEALKN 190

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907171683 1123 ILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE--FVDILGLVSEMRSYR-MSMVQTEEQYIFI 1197
Cdd:COG5599    191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1000-1197 1.22e-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: 1.22e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1000 DYINANYI----PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVE 1075
Cdd:cd14601      1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1076 MVSEEEEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 1153
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNleKNESRPLTQIQYIAWPDHGVP--DDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907171683 1154 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 1197
Cdd:cd14601    159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1001-1199 5.28e-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: 5.28e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvKCDHYWPfTEEPIAYGDITVEMVSEE 1080
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWP-DEGSGTYGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHFRI----NYADEAQDVMHFNYTAWPDHG-VPPAnaAESILQFVFTVRQ-QAAKSKGPMIIHCSAGVGRTGT 1154
Cdd:cd14556     79 IDEDVISRIFRLqnttRPQEGYRMVQQFQFLGWPRDRdTPPS--KRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSGV 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907171683 1155 FIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14556    157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1001-1199 1.63e-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: 1.63e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGY-NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTE--EPIAYGDITVEMV 1077
Cdd:cd14539      1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWP-TErgQALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1078 SEEEEEDWASRHFRINYADEAQ--DVMHFNYTAWPDHGVPPANAAesILQFVFTVR---QQAAKSKGPMIIHCSAGVGRT 1152
Cdd:cd14539     80 SVRTTPTHVERIISIQHKDTRLsrSVVHLQFTTWPELGLPDSPNP--LLRFIEEVHshyLQQRSLQTPIVVHCSSGVGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907171683 1153 GTFIALDRLLQHIR-DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14539    158 GAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1001-1199 3.90e-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: 3.90e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGY--NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFT---EEPIAYGDITVE 1075
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggeHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1076 MVSEEEEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQF---VFTVRQQAAKSKG------PMIIH 1144
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHtlSGQSRTVWHLQYTDWPDHGCP--EDVSGFLDFleeINSVRRHTNQDVAghnrnpPTLVH 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907171683 1145 CSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14540    159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYN 213
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 966-1199 8.67e-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: 8.67e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  966 ADLPLNRCKNRYTNILPYDFSRVRLVSmNEEEGADYINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSHIIV 1043
Cdd:cd14599     33 ATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1044 MLTQCNEKRRVKCDHYWP---FTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPP-A 1117
Cdd:cd14599    112 MVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQErtVWHLQYTDWPDHGCPEeV 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1118 NAAESILQFVFTVRQQA-------AKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQT 1190
Cdd:cd14599    192 QGFLSYLEEIQSVRRHTnsmldstKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQT 271


                   ....*....
gi 1907171683 1191 EEQYIFIHQ 1199
Cdd:cd14599    272 IAQYKFVYQ 280
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 971-1196 3.99e-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: 3.99e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNsPQE--YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1048
Cdd:cd14610     44 NVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHD-PRNpaYIATQGPLPATVADFWQMVWESGCVVIVMLTPL 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1049 NEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEE-EEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQ 1125
Cdd:cd14610    123 AENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGVP--ASTRSLLD 199

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907171683 1126 FVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 1196
Cdd:cd14610    200 FRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 971-1201 1.92e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 152.08  E-value: 1.92e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1050
Cdd:PHA02742    52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1051 KRRVKCDHYW-PFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQ--DVMHFNYTAWPDHGVPpaNAAESILQFV 1127
Cdd:PHA02742   130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGAslDIKHFAYEDWPHGGLP--RDPNKFLDFV 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1128 FTVRQQAAKS-----------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 1196
Cdd:PHA02742   208 LAVREADLKAdvdikgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                   ....*
gi 1907171683 1197 IHQCV 1201
Cdd:PHA02742   288 CYFIV 292
PHA02738 PHA02738
hypothetical protein; Provisional
 971-1203 2.77e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 152.00  E-value: 2.77e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 1050
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPA--ERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1051 KRRVKCDHYWPFTEE-PIAYGDITVEMVSEEEEEDWASRHFRINYADEA-QDVMHFNYTAWPDHGVPpaNAAESILQFVF 1128
Cdd:PHA02738   127 NGREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVP--KNTSEFLNFVL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1129 TVRQ------QAAKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 1195
Cdd:PHA02738   205 EVRQcqkelaQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                   ....*...
gi 1907171683 1196 FIHQCVQL 1203
Cdd:PHA02738   285 FCYRAVKR 292
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1101-1201 3.87e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.88  E-value: 3.87e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  1101 VMHFNYTAWPDHGVPPAnaAESILQFVFTVR--QQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRD-HEFVDILGLV 1177
Cdd:smart00404    2 VKHYHYTGWPDHGVPES--PDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....
gi 1907171683  1178 SEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:smart00404   80 KELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1101-1201 3.87e-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: 3.87e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  1101 VMHFNYTAWPDHGVPPAnaAESILQFVFTVR--QQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRD-HEFVDILGLV 1177
Cdd:smart00012    2 VKHYHYTGWPDHGVPES--PDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....
gi 1907171683  1178 SEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:smart00012   80 KELRSQRPGMVQTEEQYLFLYRAL 103
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 971-1196 3.95e-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: 3.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNsPQ--EYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1048
Cdd:cd14609     42 NVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHD-PRmpAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPL 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1049 NEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEE-EEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQ 1125
Cdd:cd14609    121 VEDGVKQCDRYWP-DEGSSLYHIYEVNLVSEHIwCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGIP--SSTRPLLD 197

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907171683 1126 FVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 1196
Cdd:cd14609    198 FRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1001-1201 5.72e-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: 5.72e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSE 1079
Cdd:cd14546      1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-EEGSEVYHIYEVHLVSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1080 EE-EEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFI 1156
Cdd:cd14546     80 HIwCDDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIP--ASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYI 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907171683 1157 ALD----RLLQHIRDhefVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14546    158 LIDmvlnRMAKGAKE---IDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 969-1208 8.81e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 144.79  E-value: 8.81e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  969 PLNRCKNRYTNILPYDFSRV-------------------RLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRND 1029
Cdd:PHA02746    49 KENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1030 FWKMVLQQKSHIIVMLTQCNEKRRvKCDHYWPFTEE-PIAYGDITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNY 1106
Cdd:PHA02746   129 FFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDsELAFGRFVAKILDIIEELSFTKTRLMITdkISDTSREIHHFWF 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1107 TAWPDHGVpPANAAEsILQFVFTVRQQAAKSK----------GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGL 1176
Cdd:PHA02746   208 PDWPDNGI-PTGMAE-FLELINKVNEEQAELIkqadndpqtlGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1907171683 1177 VSEMRSYRMSMVQTEEQYIFIHQCVQLMWLRK 1208
Cdd:PHA02746   286 VLKIRKQRHSSVFLPEQYAFCYKALKYAIIEE 317
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 969-1198 1.43e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 135.13  E-value: 1.43e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  969 PLNRCKNRYTNILPYDFSRVRLVSmNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1048
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1049 NEKR-RVKCDHYWPFTEE-PIAYGDITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVpPANAAESI- 1123
Cdd:PHA02747   128 KGTNgEEKCYQYWCLNEDgNIDMEDFRIETLKTSVRAKYILTLIEITdkILKDSRKISHFQCSEWFEDET-PSDHPDFIk 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1124 -LQFVFTVRQQAAKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 1195
Cdd:PHA02747   207 fIKIIDINRKKSGKLFNpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                   ...
gi 1907171683 1196 FIH 1198
Cdd:PHA02747   287 FIQ 289
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1001-1199 6.41e-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: 130.10  E-value: 6.41e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPF---TEEPIAYGDITVE 1075
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgsRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1076 MVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPP-ANAAESILQFVFTVRQQAAKS------KGPMIIHCS 1146
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQErtVWHLQYTDWPEHGCPEdLKGFLSYLEEIQSVRRHTNSTidpkspNPPVLVHCS 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907171683 1147 AGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14598    161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYK 213
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1001-1199 1.09e-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: 1.09e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvkCDHYWPfTEEPIAYGDITVEMVSEE 1080
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL--CMQYWP-EKTSCCYGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHFRINYADEAQD----VMHFNYTAWPDH-GVPPANaaESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRT 1152
Cdd:cd14634     78 IDEDIISRIFRICNMARPQDgyriVQHLQYIGWPAYrDTPPSK--RSILKVVRRLekwQEQYDGREGRTVVHCLNGGGRS 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907171683 1153 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14634    156 GTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYE 202
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1001-1198 1.01e-30

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: 120.52  E-value: 1.01e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRrvKCDHYWPfTEEPIAYGDITVEMVSEE 1080
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWP-EEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHFRINYADEAQD----VMHFNYTAWPDHGVPPAnAAESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRTG 1153
Cdd:cd14636     78 MDCDVISRIFRICNLTRPQEgylmVQQFQYLGWASHREVPG-SKRSFLKLILQVekwQEECDEGEGRTIIHCLNGGGRSG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907171683 1154 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 1198
Cdd:cd14636    157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1001-1201 1.04e-30

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: 120.40  E-value: 1.04e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV-KCDHYWPfteEP--IAYGDITVEMV 1077
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP---EPglQQYGPMEVEFV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1078 SEEEEEDWASRHFRINYADEAQD----VMHFNYTAWPDHGVPPaNAAESILQFVFTVRQ-QAAKSKGPMIIHCSAGVGRT 1152
Cdd:cd14637     78 SGSADEDIVTRLFRVQNITRLQEghlmVRHFQFLRWSAYRDTP-DSKKAFLHLLASVEKwQRESGEGRTVVHCLNGGGRS 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907171683 1153 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd14637    157 GTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1001-1199 3.27e-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: 115.88  E-value: 3.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCdhYWPFTEEPIAYGDITV-----E 1075
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVtlsgeD 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1076 MVSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDhgvpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 1153
Cdd:cd14550     79 HSCLSNEIRLIVRDFILesTQDDYVLEVRQFQCPSWPN----PCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAA 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907171683 1154 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14550    155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1001-1199 1.40e-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: 1.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvkCDHYWPftEEPI-AYGDITVEMVSE 1079
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP--ENGVhRHGPIQVEFVSA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1080 EEEEDWASRHFRINYADEAQD----VMHFNYTAWPDHGVPPAnAAESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRT 1152
Cdd:cd14635     77 DLEEDIISRIFRIYNAARPQDgyrmVQQFQFLGWPMYRDTPV-SKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRS 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907171683 1153 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 1199
Cdd:cd14635    156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 202
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1001-1201 3.23e-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: 3.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCdHYWPFTEEPIAYGDITVEMVSEE 1080
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1081 EEEDWASRHFRI-NYADEA-QD-----VMHFNYTAWPDhgvpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 1153
Cdd:cd17669     80 HKCLSNEEKLIIqDFILEAtQDdyvleVRHFQCPKWPN----PDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907171683 1154 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd17669    156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1001-1201 8.26e-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: 8.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1001 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQcNEKRRVKCDHYWPFTEEPIAYGDITVEMVSE- 1079
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKd 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1080 ---------EEEEDWASRHFRINYADEaqdVMHFNYTAWPDhgvpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVG 1150
Cdd:cd17670     80 rlclsneeqIIIHDFILEATQDDYVLE---VRHFQCPKWPN----PDAPISSTFELINVIKEEALTRDGPTIVHDEFGAV 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907171683 1151 RTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 1201
Cdd:cd17670    153 SAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 975-1194 8.22e-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: 8.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  975 NRYTNIlpydfsrvrlVSMNEEEGADYINANYIPGYNSPQeYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 1054
Cdd:cd14559      1 NRFTNI----------QTRVSTPVGKNLNANRVQIGNKNV-AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1055 KCDHYWPFTEEpiaYGDITV--EMVSEEEEEDWASRH---FRINYADEAQDVMHFNYTAWPDHGVPPANAAESILQFVFT 1129
Cdd:cd14559     70 GLPPYFRQSGT---YGSVTVksKKTGKDELVDGLKADmynLKITDGNKTITIPVVHVTNWPDHTAISSEGLKELADLVNK 146

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907171683 1130 VRQQAA-------------KSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDIlglVSEMRSYRMS-MVQTEEQY 1194
Cdd:cd14559    147 SAEEKRnfykskgssaindKNKLLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRNGkMVQKDEQL 222
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 971-1218 2.89e-15

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 78.08  E-value: 2.89e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  971 NRCK--NRYTNILPYDFSRVRLVSMNEeegadYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 1048
Cdd:PHA02740    51 NKAKdeNLALHITRLLHRRIKLFNDEK-----VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1049 NEKrrvKC-DHYWPFTEEP-IAYGDITVEMVSEEEEEdwasrHFRI------NYADEAQDVMHFNYTAWPDHGVppANAA 1120
Cdd:PHA02740   126 ADK---KCfNQFWSLKEGCvITSDKFQIETLEIIIKP-----HFNLtllsltDKFGQAQKISHFQYTAWPADGF--SHDP 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1121 ESILQFVFTV--------RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEE 1192
Cdd:PHA02740   196 DAFIDFFCNIddlcadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLD 275

                          250       260
                   ....*....|....*....|....*.
gi 1907171683 1193 QYIFihqCVQLMWLRKKQQFCISDVI 1218
Cdd:PHA02740   276 DYVF---CYHLIAAYLKEKFDILKFI 298
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1118-1199 3.20e-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: 3.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1118 NAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRdhefvDILGLVSEMRSYR-MSMVQTEEQYIF 1196
Cdd:cd14494     36 DLTLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRpGGIPQTIEQLDF 110


                   ...
gi 1907171683 1197 IHQ 1199
Cdd:cd14494    111 LIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1109-1199 7.53e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 58.44  E-value: 7.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1109 WPDHGVPPANAAESILQFVftvrQQAAKSKGPMIIHCSAGVGRTGTFIAldrLLQHIRDHEFVDILGLVSEMRSYRmsmV 1188
Cdd:COG2453     55 IPDFGAPDDEQLQEAVDFI----DEALREGKKVLVHCRGGIGRTGTVAA---AYLVLLGLSAEEALARVRAARPGA---V 124

                           90
                   ....*....|.
gi 1907171683 1189 QTEEQYIFIHQ 1199
Cdd:COG2453    125 ETPAQRAFLER 135
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1098-1210 4.72e-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: 4.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1098 AQDVMHFNYtAWPDHGVPPANAAESILQfvftVRQQAAKSKGPMIIHCSAGVGRTGTFIA-----LDRLL--QHIRdheF 1170
Cdd:cd14506     74 RAGIYFYNF-GWKDYGVPSLTTILDIVK----VMAFALQEGGKVAVHCHAGLGRTGVLIAcylvyALRMSadQAIR---L 145

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907171683 1171 VdilglvsemRSYRMSMVQTEEQYIFIHQCVQLMWLRKKQ 1210
Cdd:cd14506    146 V---------RSKRPNSIQTRGQVLCVREFAQFLLPLRNV 176
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1110-1199 9.12e-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: 9.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1110 PDHGVPPANAaesilQFVFTVRQ--QAAKSKGPMIIHCSAGVGRTGTFIAldRLLQHIRDHEFVD-ILGLVsemRSYRMS 1186
Cdd:cd14505     81 PDGGVPSDIA-----QWQELLEEllSALENGKKVLIHCKGGLGRTGLIAA--CLLLELGDTLDPEqAIAAV---RALRPG 150

                           90
                   ....*....|...
gi 1907171683 1187 MVQTEEQYIFIHQ 1199
Cdd:cd14505    151 AIQTPKQENFLHQ 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1110-1199 1.21e-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: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1110 PDHGVPpanAAESILQFVFTVRQQAAKSKgPMIIHCSAGVGRTGTFIALdrllqHIRDHEFVDILGLVSEMRSYRMSMVQ 1189
Cdd:cd14504     58 EDYTPP---TLEQIDEFLDIVEEANAKNE-AVLVHCLAGKGRTGTMLAC-----YLVKTGKISAVDAINEIRRIRPGSIE 128

                           90
                   ....*....|
gi 1907171683 1190 TEEQYIFIHQ 1199
Cdd:cd14504    129 TSEQEKFVIQ 138
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 443-535 1.62e-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: 44.79  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  443 EKPQHVSVHVLSSTTALMSWTSSQENyNSTIVS-VVSLTCQKQKESQRLEKqycTQVNSSKPVIENLVPGAQYQVVMYLR 521
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGyVVEYREKGSGDWKEVEV---TPGSETSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|....
gi 1907171683  522 KGPLIGPPSDPVTF 535
Cdd:cd00063     78 NGGGESPPSESVTV 91
fn3 pfam00041
Fibronectin type III domain;
444-530 1.76e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  444 KPQHVSVHVLSSTTALMSWTSSqENYNSTIVSVvSLTCQKQKESQrlekqYCTQVNSSKP----VIENLVPGAQYQVVMY 519
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPP-PDGNGPITGY-EVEYRPKNSGE-----PWNEITVPGTttsvTLTGLKPGTEYEVRVQ 74

                           90
                   ....*....|.
gi 1907171683  520 LRKGPLIGPPS 530
Cdd:pfam00041   75 AVNGGGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
734-814 2.20e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.94  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  734 PPKSLFAVNKTQTSVTLLWVE----EGVADFFEVFCQQLGSGhNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDT 809
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSG-EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1907171683  810 PSVPT 814
Cdd:pfam00041   81 EGPPS 85
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 1087-1158 8.99e-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: 8.99e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907171683 1087 SRHFRINYADEAQDVMHFNYTAWPDHGVPPANAAESIlqfvFTVRQQAAKSKGPMIIHCSAGVGRTGTFIAL 1158
Cdd:cd14529     42 GADERAASEEAAAKIDGVKYVNLPLSATRPTESDVQS----FLLIMDLKLAPGPVLIHCKHGKDRTGLVSAL 109
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 539-639 1.12e-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: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  539 PTGIKDLMLYPLGPTAVVLSWTRP--ILGVFRKYVVEMFyfnpTTMTSEWTtyyEIAATVSLTASVRIASLLPAWYYNFR 616
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYR----EKGSGDWK---EVEVTPGSETSYTLTGLKPGTEYEFR 73

                           90       100
                   ....*....|....*....|....*.
gi 1907171683  617 VTMVT---WGDPelsccdSSTISFIT 639
Cdd:cd00063     74 VRAVNgggESPP------SESVTVTT 93
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1110-1158 2.55e-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: 2.55e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907171683 1110 PDHGVPPanaaESILQ-FVftvrQQAAKSKGPMIIHCSAGVGRTGTFIAL 1158
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 ...
 732-814 2.61e-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: 41.33  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683  732 PAPPKSLFAVNKTQTSVTLLWV----EEGVADFFEVFCQQLGSGhNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSH 807
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTppedDGGPITGYVVEYREKGSG-DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   ....*..
gi 1907171683  808 DTPSVPT 814
Cdd:cd00063     80 GGESPPS 86
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 732-811 3.57e-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: 40.68  E-value: 3.57e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683   732 PAPPKSLFAVNKTQTSVTLLW--VEEGVADFFEVFCQQLGSGHNGKLQE-PVAVSSHVVTISSLLPATAYNCSVTSFSHD 808
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWepPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 1907171683   809 TPS 811
Cdd:smart00060   81 GEG 83
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 1088-1156 4.14e-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: 4.14e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907171683 1088 RHFRI-NYADE-AQDVMHFNYTA----WPDHGVPPAnaaESILQFVFTVRQ-QAAKSKGPMIIHCSAGVGRTGTFI 1156
Cdd:cd14510     54 DHYKVyNLCSErGYDPKYFHNRVervpIDDHNVPTL---DEMLSFTAEVREwMAADPKNVVAIHCKGGKGRTGTMV 126
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 539-621 1.63e-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: 1.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171683   539 PTGIKDLMLYPLGPTAVVLSWTRPILGVFRKYVVEMFYFNpTTMTSEWTTyyeiAATVSLTASVRIASLLPAWYYNFRVT 618
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEY-REEGSEWKE----VNVTPSSTSYTLTGLKPGTEYEFRVR 75


                    ...
gi 1907171683   619 MVT 621
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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