NCBI Conserved Domain Search

Conserved domains on [gi|257096044|ref|NP_001157874|]

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receptor-type tyrosine-protein phosphatase O isoform 3 [Mus musculus]

Protein Classification

R-PTPc-O domain-containing protein( domain architecture ID 12998700)

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 ...

140-384

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: 537.55 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 140 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 219
Cdd:cd14614    1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 220 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANA 299
Cdd:cd14614   81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 300 AESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14614  161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                 ....*
gi 257096044 380 CVQLM 384
Cdd:cd14614  241 CVQLM 245

Name

Accession

Description

Interval

E-value

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

140-384

0e+00

Pssm-ID: 350462 [Multi-domain] Cd Length: 245 Bit Score: 537.55 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 140 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 219
Cdd:cd14614    1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 220 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANA 299
Cdd:cd14614   81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 300 AESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14614  161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                 ....*
gi 257096044 380 CVQLM 384
Cdd:cd14614  241 CVQLM 245

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

126-381

1.60e-119

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 347.72 E-value: 1.60e-119

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044   126 KFSLQFEELKLIGLDIPHFA-ADLPLNRCKNRYTNILPYDFSRVRLvSMNEEEGADYINANYIPGYNSPQEYIATQGPLP 204
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044   205 ETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTE-EPIAYGDITVEMVSEEEEEDWASRHFRINYAD--EAQDV 281
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044   282 MHFNYTAWPDHGVPPAnaAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMR 361
Cdd:smart00194 160 THYHYTNWPDHGVPES--PESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|
gi 257096044   362 SYRMSMVQTEEQYIFIHQCV 381
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAI 257

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

151-381

9.26e-109

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 319.19 E-value: 9.26e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044  151 NRCKNRYTNILPYDFSRVRLvsMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 230
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044  231 KRRVKCDHYWPFT-EEPIAYGDITVEMVSEEEEE-DWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPPANAaeSILQF 306
Cdd:pfam00102  79 KGREKCAQYWPEEeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPN--SLLDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096044  307 VFTVRQ-QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:pfam00102 157 LRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

150-377

3.01e-49

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 168.35 E-value: 3.01e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 150 LNRCK-NRYTNILPYDFSRVRlvsmneeEGADYINANYIPGYNsPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 228
Cdd:COG5599   40 INGSPlNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 229 NE--KRRVKCDHYWPFTEEPIAYgDITVEMV-SEEEEEDWASRHFRINYAD---EAQDVMHFNYTAWPDHGVPPANAAES 302
Cdd:COG5599  112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTeSIQLRDGIEARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISAEALKN 190

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096044 303 ILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE--FVDILGLVSEMRSYR-MSMVQTEEQYIFI 377
Cdd:COG5599  191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268

PHA02742

protein tyrosine phosphatase; Provisional

151-381

9.52e-43

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 151.69 E-value: 9.52e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 230
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 231 KRRVKCDHYW-PFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQ--DVMHFNYTAWPDHGVPpaNAAESILQFV 307
Cdd:PHA02742 130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGAslDIKHFAYEDWPHGGLP--RDPNKFLDFV 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 308 FTVRQQAAKS-----------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 376
Cdd:PHA02742 208 LAVREADLKAdvdikgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                 ....*
gi 257096044 377 IHQCV 381
Cdd:PHA02742 288 CYFIV 292

Name

Accession

Description

Interval

E-value

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

140-384

0e+00

Pssm-ID: 350462 [Multi-domain] Cd Length: 245 Bit Score: 537.55 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 140 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 219
Cdd:cd14614    1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 220 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANA 299
Cdd:cd14614   81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTANA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 300 AESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14614  161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                 ....*
gi 257096044 380 CVQLM 384
Cdd:cd14614  241 CVQLM 245

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

156-379

1.89e-146

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: 414.44 E-value: 1.89e-146

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 156 RYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVK 235
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 236 CDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAA 315
Cdd:cd14548   81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVP--EAPDSLLRFVRLVRDYIK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257096044 316 KSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14548  159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

126-381

1.60e-119

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 347.72 E-value: 1.60e-119

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044   126 KFSLQFEELKLIGLDIPHFA-ADLPLNRCKNRYTNILPYDFSRVRLvSMNEEEGADYINANYIPGYNSPQEYIATQGPLP 204
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044   205 ETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTE-EPIAYGDITVEMVSEEEEEDWASRHFRINYAD--EAQDV 281
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044   282 MHFNYTAWPDHGVPPAnaAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMR 361
Cdd:smart00194 160 THYHYTNWPDHGVPES--PESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|
gi 257096044   362 SYRMSMVQTEEQYIFIHQCV 381
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAI 257

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

151-381

9.26e-109

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 319.19 E-value: 9.26e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044  151 NRCKNRYTNILPYDFSRVRLvsMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 230
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044  231 KRRVKCDHYWPFT-EEPIAYGDITVEMVSEEEEE-DWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPPANAaeSILQF 306
Cdd:pfam00102  79 KGREKCAQYWPEEeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPN--SLLDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096044  307 VFTVRQ-QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:pfam00102 157 LRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

155-379

2.80e-102

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: 302.61 E-value: 2.80e-102

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 155 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 234
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 235 KCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRI---NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVR 311
Cdd:cd14617   81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKIcseEQLDAPRLVRHFHYTVWPDHGVP--ETTQSLIQFVRTVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 312 QQAAKS--KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14617  159 DYINRTpgSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

155-381

3.10e-98

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: 292.56 E-value: 3.10e-98

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 155 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 234
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 235 KCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAESILQFVFTVRQ 312
Cdd:cd14619   81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTlsVRHFHFTAWPDHGVP--SSTDTLLAFRRLLRQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257096044 313 --QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14619  159 wlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

149-381

2.71e-96

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: 287.76 E-value: 2.71e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 149 PLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 228
Cdd:cd14553    1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 229 NEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQF 306
Cdd:cd14553   81 EERSRVKCDQYWP-TRGTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVP--EHPTPFLAF 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257096044 307 VFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14553  158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

155-381

1.20e-95

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: 285.68 E-value: 1.20e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 155 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 234
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 235 KCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPPANAaeSILQFVFTVRQ 312
Cdd:cd14618   81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKErrVKHLHYTAWPDHGIPESTS--SLMAFRELVRE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257096044 313 --QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14618  159 hvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

155-381

5.33e-93

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: 279.01 E-value: 5.33e-93

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 155 NRYTNILPYDFSRVRLVSMNEEEgADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 234
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHST-DDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 235 KCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAESILQFVFTVRQ 312
Cdd:cd14615   80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESrtVRHFHFTSWPDHGVP--ETTDLLINFRHLVRE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257096044 313 QAAKS--KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14615  157 YMKQNppNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCA 227

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

181-379

1.72e-92

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: 276.47 E-value: 1.72e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWP-FTEEPIAYGDITVEMVSE 259
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPeEGGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 260 EEEEDWASRHFRINYAD--EAQDVMHFNYTAWPDHGVPPanAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIA 337
Cdd:cd00047   81 EELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPS--SPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 257096044 338 LDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd00047  159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

155-379

6.26e-91

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: 6.26e-91

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 155 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 234
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 235 KCDHYWPFTEEPIA-YGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANAaeSILQFVFTVRQQ 313
Cdd:cd14616   81 RCHQYWPEDNKPVTvFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSA--PLIHFVKLVRAS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096044 314 AAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14616  159 RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

145-378

2.00e-86

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: 263.84 E-value: 2.00e-86

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 145 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 224
Cdd:cd14543   23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 225 LTQCNEKRRVKCDHYWPFTEEPIA-YGDITVEMVSEEEEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPPanAAE 301
Cdd:cd14543  103 TTRVVERGRVKCGQYWPLEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTetDESRQVTHFQFTSWPDFGVPS--SAA 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 302 SILQFVFTVRQQAAKS--------KG-----PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMV 368
Cdd:cd14543  181 ALLDFLGEVRQQQALAvkamgdrwKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSI 260

                        250
                 ....*....|
gi 257096044 369 QTEEQYIFIH 378
Cdd:cd14543  261 QTPDQYYFCY 270

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

155-379

9.58e-83

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: 252.70 E-value: 9.58e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 155 NRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRr 233
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 234 VKCDHYWPFtEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPAnaAESILQFVFTVRQ- 312
Cdd:cd14547   80 EKCAQYWPE-EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEA--AQPLLSLVQEVEEa 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096044 313 -QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14547  157 rQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

181-378

7.80e-82

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: 249.58 E-value: 7.80e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEE 260
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP-KEGTETYGNIQVTLLSTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHF--------RINYADEAQDVMHFNYTAWPDHGVPPANAaeSILQFvftVRQQAAKSK---GPMIIHCSAGV 329
Cdd:cd14549   80 VLATYTVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTL--PVLSF---VRKSSAANPpgaGPIVVHCSAGV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 257096044 330 GRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 378
Cdd:cd14549  155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

111-381

9.40e-82

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: 251.88 E-value: 9.40e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 111 DFDSYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGY 190
Cdd:cd14626    2 DLADNIERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 191 NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPF--TEepiAYGDITVEMVSEEEEEDWASR 268
Cdd:cd14626   81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIrgTE---TYGMIQVTLLDTVELATYSVR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 269 HFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIR 346
Cdd:cd14626  158 TFALykNGSSEKREVRQFQFMAWPDHGVP--EYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMK 235

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 257096044 347 DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14626  236 HEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

127-378

4.36e-77

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

Pssm-ID: 350505 [Multi-domain] Cd Length: 274 Bit Score: 239.94 E-value: 4.36e-77

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 127 FSLQFEELKLIGLDIPHFA--ADLPLNRCKNRYTNILPYDFSRVRLVSM--NEEEGADYINANYIPGYNSPQEYIATQGP 202
Cdd:cd17667    1 FSEDFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 203 LPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRI-NYADEA--- 278
Cdd:cd17667   81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTKIHACYTVRRFSIrNTKVKKgqk 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 279 ---------QDVMHFNYTAWPDHGVPpaNAAESILQFVftVRQQAAKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRD 347
Cdd:cd17667  160 gnpkgrqneRTVIQYHYTQWPDMGVP--EYALPVLTFV--RRSSAARTPemGPVLVHCSAGVGRTGTYIVIDSMLQQIKD 235

                        250       260       270
                 ....*....|....*....|....*....|.
gi 257096044 348 HEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 378
Cdd:cd17667  236 KSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

139-383

1.64e-74

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: 232.42 E-value: 1.64e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 139 LDIPHFAAdlplnrcKNRYTNILPYDFSRVRLVS-MNEEEGADYINANYIPGYN-SPQEYIATQGPLPETRNDFWKMVLQ 216
Cdd:cd14612   10 LDIPGHAS-------KDRYKTILPNPQSRVCLRRaGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 217 QKSHIIVMLTQCNEKRRvKCDHYWPFTEEpiAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPp 296
Cdd:cd14612   83 EECPIIVMITKLKEKKE-KCVHYWPEKEG--TYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTP- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 297 aNAAESILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 374
Cdd:cd14612  159 -ESAGPLLRLVAEVeeSRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQY 237


                 ....*....
gi 257096044 375 IFIHQCVQL 383
Cdd:cd14612  238 QFLHHTLAL 246

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

106-381

2.76e-74

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: 233.06 E-value: 2.76e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 106 PVQLDDFDSYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 185
Cdd:cd14625    3 PIPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 186 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDW 265
Cdd:cd14625   82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 266 ASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQ 343
Cdd:cd14625  161 CVRTFSLhkNGSSEKREVRQFQFTAWPDHGVP--EYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 257096044 344 HIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14625  239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

106-381

3.83e-74

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: 232.70 E-value: 3.83e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 106 PVQLDDFDSYIKDMAKDSDYKFSLQFEELKlIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 185
Cdd:cd14624    3 PIPILELADHIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 186 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDW 265
Cdd:cd14624   82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 266 ASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQ 343
Cdd:cd14624  161 CVRTFALykNGSSEKREVRQFQFTAWPDHGVP--EHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 257096044 344 HIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14624  239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

181-379

1.10e-72

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: 226.36 E-value: 1.10e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYI-PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSE 259
Cdd:cd18533    1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 260 EEEEDWAS--RHFRINYADEA-QDVMHFNYTAWPDHGVPPanAAESILQFVFTVR--QQAAKSKGPMIIHCSAGVGRTGT 334
Cdd:cd18533   81 EENDDGGFivREFELSKEDGKvKKVYHIQYKSWPDFGVPD--SPEDLLTLIKLKRelNDSASLDPPIIVHCSAGVGRTGT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 257096044 335 FIALDRLLQHIRDHEFVD---------ILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd18533  159 FIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

145-385

9.20e-72

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: 225.86 E-value: 9.20e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 145 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 224
Cdd:cd14603   24 AGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILM 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 225 LTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEE-EDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESI 303
Cdd:cd14603  104 ACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLnEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIP--DSPDCM 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 304 LQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDR-----LLQHIRDHefVDILGLVSEMRSYRMSMVQTEEQYIFIH 378
Cdd:cd14603  182 LAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLY 259


                 ....*..
gi 257096044 379 QCVQLMW 385
Cdd:cd14603  260 HTVAQMF 266

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

151-381

2.76e-71

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: 223.75 E-value: 2.76e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 230
Cdd:cd14630    3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 231 KRRVKCDHYWPftEEPIAYGDITVEMVSEEEEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVF 308
Cdd:cd14630   83 VGRVKCVRYWP--DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKkgYHEIREIRQFHFTSWPDHGVP--CYATGLLGFVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257096044 309 TVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14630  159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

111-381

5.64e-71

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: 224.15 E-value: 5.64e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 111 DFDSYIKDMAKDSDYKFSLQFEELkLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGY 190
Cdd:cd14633    1 DLLQHITQMKCAEGYGFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 191 NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEpiAYGDITVEMVSEEEEEDWASRHF 270
Cdd:cd14633   80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 271 RINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH 348
Cdd:cd14633  158 AVEKrgVHEIREIRQFHFTGWPDHGVP--YHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAERE 235

                        250       260       270
                 ....*....|....*....|....*....|...
gi 257096044 349 EFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
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 ...

146-379

8.79e-71

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: 222.40 E-value: 8.79e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 146 ADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVML 225
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 226 TQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPpaNAAESI 303
Cdd:cd14554   81 TKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDArdGQSRTVRQFQFTDWPEQGVP--KSGEGF 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096044 304 LQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14554  158 IDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

151-382

1.61e-68

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: 216.95 E-value: 1.61e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCKNRYTNILPYDFSRVRLVSM-NEEEGADYINANYIPGYNSP-------QEYIATQGPLPETRNDFWKMVLQQKSHII 222
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIRNENEGpttdenaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 223 VMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD---VMHFNYTAWPDHGVPpaNA 299
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPireIWHYQYLSWPDHGVP--SD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 300 AESILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQY 374
Cdd:cd14544  159 PGGVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQY 238


                 ....*...
gi 257096044 375 IFIHQCVQ 382
Cdd:cd14544  239 KFIYVAVA 246

PTPc-N3_4

cd14541

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

180-381

1.56e-65

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: 207.95 E-value: 1.56e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 180 DYINANY----IPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVE 255
Cdd:cd14541    1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 256 MVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 333
Cdd:cd14541   81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVP--DDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 257096044 334 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14541  159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAI 206

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

181-379

1.53e-64

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: 205.06 E-value: 1.53e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWP-FTEEPIAYGDITVEMVSE 259
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 260 EEEEDWASRHFRINYADE---AQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFI 336
Cdd:cd14557   81 KICPDYIIRKLNINNKKEkgsGREVTHIQFTSWPDHGVP--EDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 257096044 337 ALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14557  159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

127-383

1.85e-64

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: 207.02 E-value: 1.85e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 127 FSLQ--FEELKLIGLDIPHFaaDLPLNRCKNRYTNILPYDFSRVRLVSMNEEEG-ADYINANYIPGYNSPQE-YIATQGP 202
Cdd:cd14613    1 FLLQaeFFEIPMNFVDPKEY--DIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYGGEEKvYIATQGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 203 LPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvKCDHYWPftEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVM 282
Cdd:cd14613   79 TVNTVGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWP--EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 283 HFNYTAWPDHGVPpaNAAESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSE 359
Cdd:cd14613  156 HYWYTSWPDQKTP--DNAPPLLQLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQ 233

                        250       260
                 ....*....|....*....|....
gi 257096044 360 MRSYRMSMVQTEEQYIFIHQCVQL 383
Cdd:cd14613  234 LRLDRGGMIQTCEQYQFVHHVLSL 257

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

151-381

3.75e-64

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: 205.45 E-value: 3.75e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCKNRYTNILPYDFSRVRLvsmnEEEGaDYINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 228
Cdd:cd14597    3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 229 NEKRRVKCDHYWPFT-EEPIAYGD-ITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESIL 304
Cdd:cd14597   78 VEGGKIKCQRYWPEIlGKTTMVDNrLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTP--SQPEQLL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096044 305 QFVFTVRQqaAKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14597  156 TFISYMRH--IHKSGPIITHCSAGIGRSGTLICIDVVLGLIsKDLDF-DISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230

PTPc-N6

cd14606

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...

149-381

5.27e-64

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: 205.88 E-value: 5.27e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 149 PLNRCKNRYTNILPYDFSRVRLVSM-NEEEGADYINANYI------PGyNSPQEYIATQGPLPETRNDFWKMVLQQKSHI 221
Cdd:cd14606   16 PENKSKNRYKNILPFDHSRVILQGRdSNIPGSDYINANYVknqllgPD-ENAKTYIASQGCLEATVNDFWQMAWQENSRV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 222 IVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFR---INYADEAQDVMHFNYTAWPDHGVPPAN 298
Cdd:cd14606   95 IVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQvspLDNGELIREIWHYQYLSWPDHGVPSEP 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 299 AAesILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQ 373
Cdd:cd14606  175 GG--VLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQ 252


                 ....*...
gi 257096044 374 YIFIHQCV 381
Cdd:cd14606  253 YKFIYVAI 260

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

181-381

1.64e-63

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: 202.45 E-value: 1.64e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMVSEE 260
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP--DDTEVYGDIKVTLVETE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIAL 338
Cdd:cd14555   79 PLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVP--YHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 257096044 339 DRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14555  157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199

PTPc-N3

cd14600

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...

129-377

2.09e-63

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: 204.70 E-value: 2.09e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 129 LQFEEL--KLIGLDIPhfAADLPLNRCKNRYTNILPYDFSRVRLvsmneEEGADYINANY----IPGYNSPQEYIATQGP 202
Cdd:cd14600   18 IQFEQLyrKKPGLAIT--CAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 203 LPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYAD--EAQD 280
Cdd:cd14600   91 LPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQtgEERT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 281 VMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKgPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEM 360
Cdd:cd14600  171 VTHLQYVAWPDHGVP--DDSSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKM 247

                        250
                 ....*....|....*..
gi 257096044 361 RSYRMSMVQTEEQYIFI 377
Cdd:cd14600  248 RDQRAMMVQTSSQYKFV 264

R-PTPc-A-1

cd14621

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...

106-381

8.07e-63

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: 8.07e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 106 PVQLDDFDSYIKDMAKDSDYKFSLQFEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINAN 185
Cdd:cd14621    7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 186 YIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDW 265
Cdd:cd14621   87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDVTVLVDY 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 266 ASRHFRINYADEAQD------VMHFNYTAWPDHGVPPANAAesILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALD 339
Cdd:cd14621  166 TVRKFCIQQVGDVTNkkpqrlITQFHFTSWPDFGVPFTPIG--MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVID 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 257096044 340 RLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14621  244 AMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

151-381

1.45e-62

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: 203.24 E-value: 1.45e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 230
Cdd:cd14604   57 NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 231 KRRVKCDHYWP-FTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFT 309
Cdd:cd14604  137 MGRKKCERYWPlYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVP--SSFDSILDMISL 214

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257096044 310 VRQQAAKSKGPMIIHCSAGVGRTGTFIALD---RLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14604  215 MRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

181-381

2.19e-62

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: 199.91 E-value: 2.19e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWP-FTEEP-IAYGDITVEM 256
Cdd:cd14538    1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPlICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 257 VSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAakSKGPMIIHCSAGVGRTGT 334
Cdd:cd14538   81 EKYQSLQDFVIRRISLrdKETGEVHHITHLNFTTWPDHGTP--QSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 257096044 335 FIALDRLLQHI-RDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14538  157 LITIDVALGLIeRDLPF-DIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

157-379

2.86e-62

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: 200.17 E-value: 2.86e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 157 YTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKC 236
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 237 DHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINY-----ADEAQDVMHFNYTAWPDHGVPPANAAesILQFVFTVR 311
Cdd:cd14620   81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPqlpdgCKAPRLVTQLHFTSWPDFGVPFTPIG--MLKFLKKVK 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096044 312 QQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14620  158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

131-376

9.73e-62

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: 9.73e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 131 FEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLvsmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDF 210
Cdd:cd14608    5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 211 WKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEE-PIAYGD--ITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFN 285
Cdd:cd14608   81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkEMIFEDtnLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 286 YTAWPDHGVPPANAaeSILQFVFTVRQQAAKSK--GPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEM 360
Cdd:cd14608  161 YTTWPDFGVPESPA--SFLNFLFKVRESGSLSPehGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEM 238

                        250
                 ....*....|....*.
gi 257096044 361 RSYRMSMVQTEEQYIF 376
Cdd:cd14608  239 RKFRMGLIQTADQLRF 254

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

145-379

2.49e-61

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: 199.96 E-value: 2.49e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 145 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 224
Cdd:cd14627   47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 225 LTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAES 302
Cdd:cd14627  127 LTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSrtVRQFQFTDWPEQGVP--KSGEG 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257096044 303 ILQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14627  204 FIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

145-379

5.97e-61

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: 199.19 E-value: 5.97e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 145 AADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVM 224
Cdd:cd14628   46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 225 LTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAES 302
Cdd:cd14628  126 LTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSrtVRQFQFTDWPEQGVP--KSGEG 202

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257096044 303 ILQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14628  203 FIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281

R-PTPc-Z-1

cd17668

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...

181-378

7.92e-61

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: 7.92e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEE 260
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHFRINYAD----------EAQDVMHFNYTAWPDHGVPPANAAesILQFVFTVRQQAAKSKGPMIIHCSAGVG 330
Cdd:cd17668   80 VLAYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYTQWPDMGVPEYTLP--VLTFVRKASYAKRHAVGPVVVHCSAGVG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 257096044 331 RTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 378
Cdd:cd17668  158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

154-379

7.96e-61

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: 196.29 E-value: 7.96e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 154 KNRYTNILPYDFSRVRLVSMNEEEG-ADYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEK 231
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 232 RRvKCDHYWPftEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVR 311
Cdd:cd14611   82 NE-KCVLYWP--EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTP--DSAQPLLQLMLDVE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 312 Q--QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14611  157 EdrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

154-376

9.83e-61

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: 196.46 E-value: 9.83e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 154 KNRYTNILPYDFSRVRLVSMNEEegADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRR 233
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 234 VKCDHYWPFTEEP---IAYGDITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPPANAAesILQFVF 308
Cdd:cd14545   79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAA--FLNFLQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257096044 309 TVRQQAAKS--KGPMIIHCSAGVGRTGTFIALDRLLQHI--RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 376
Cdd:cd14545  157 KVRESGSLSsdVGPPVVHCSAGIGRSGTFCLVDTCLVLIekGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

167-381

2.68e-60

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

Pssm-ID: 350479 [Multi-domain] Cd Length: 218 Bit Score: 194.85 E-value: 2.68e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 167 RVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEP 246
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP--DDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 247 IAYGDITVEMVSEEEEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIH 324
Cdd:cd14631   79 EVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVP--YHATGLLSFIRRVKLSNPPSAGPIVVH 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 257096044 325 CSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14631  157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

133-374

3.36e-60

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: 196.87 E-value: 3.36e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 133 ELKLIGLDIPH----FAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRN 208
Cdd:cd14629   31 EFKLLANSKAHtsrfISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 209 DFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNY 286
Cdd:cd14629  111 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP-AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSrtIRQFQF 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 287 TAWPDHGVPpaNAAESILQFVFTVRQQAAK--SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYR 364
Cdd:cd14629  190 TDWPEQGVP--KTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQR 267

                        250
                 ....*....|
gi 257096044 365 MSMVQTEEQY 374
Cdd:cd14629  268 PAMVQTEDQY 277

PTPc-N11

cd14605

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...

151-382

2.38e-59

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: 2.38e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCKNRYTNILPYDFSRVRLVSMN-EEEGADYINANYI-PGYNS-------PQEYIATQGPLPETRNDFWKMVLQQKSHI 221
Cdd:cd14605    2 NKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 222 IVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEA---QDVMHFNYTAWPDHGVPPAN 298
Cdd:cd14605   82 IVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGnteRTVWQYHFRTWPDHGVPSDP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 299 AAesILQFVFTV--RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQ 373
Cdd:cd14605  162 GG--VLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQ 239


                 ....*....
gi 257096044 374 YIFIHQCVQ 382
Cdd:cd14605  240 YRFIYMAVQ 248

PTPc-N2

cd14607

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...

140-381

6.14e-59

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: 6.14e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 140 DIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEeegaDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 219
Cdd:cd14607   13 DYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEN----DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 220 HIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDIT---VEMVSEEEEEDWASRHFRINYAD--EAQDVMHFNYTAWPDHGV 294
Cdd:cd14607   89 KAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETgfsVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 295 PPANAaeSILQFVFTVRQQAAKS--KGPMIIHCSAGVGRTGTFIALDR--LLQHIRDHEFVDILGLVSEMRSYRMSMVQT 370
Cdd:cd14607  169 PESPA--SFLNFLFKVRESGSLSpeHGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQT 246

                        250
                 ....*....|.
gi 257096044 371 EEQYIFIHQCV 381
Cdd:cd14607  247 PDQLRFSYMAV 257

PTPc-N22

cd14602

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...

154-381

1.06e-58

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: 191.21 E-value: 1.06e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 154 KNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRR 233
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 234 VKCDHYWPFT-EEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQ 312
Cdd:cd14602   81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVP--SSIDPILELIWDVRC 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257096044 313 QAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH---EFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14602  159 YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

181-381

3.15e-58

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: 3.15e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMVSEE 260
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP--DDSDTYGDIKITLLKTE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHF---RINYADEaQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIA 337
Cdd:cd14632   79 TLAEYSVRTFaleRRGYSAR-HEVKQFHFTSWPEHGVP--YHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 257096044 338 LDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14632  156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199

PTPc-N22_18_12

cd14542

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...

181-379

2.52e-57

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: 186.47 E-value: 2.52e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMltQCNEKR--RVKCDHYWP-FTEEPIAYGDITVEMV 257
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVM--ACREFEmgKKKCERYWPeEGEEQLQFGPFKISLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 258 SEEEE-EDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPanAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFI 336
Cdd:cd14542   79 KEKRVgPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPS--SVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTIC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 257096044 337 ALD---RLLQ-HIRDHEFvDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14542  157 AIDyvwNLLKtGKIPEEF-SLFDLVREMRKQRPAMVQTKEQYELVYR 202

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

181-382

6.76e-56

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: 6.76e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSEE 260
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP-EDGSVSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIAL 338
Cdd:cd14552   80 DYEDYTLRDFLVtkGKGGSTRTVRQFHFHGWPEVGI-PDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCAL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 257096044 339 DRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 382
Cdd:cd14552  159 STVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

180-382

2.04e-55

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: 181.74 E-value: 2.04e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 180 DYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSE 259
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWP-SEGSVTHGEITIEIKND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 260 EEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPpaNAAESILQFVFTV-RQQAAKSKGPMIIHCSAGVGRTGTFI 336
Cdd:cd14622   80 TLLETISIRDFLVTYNQEKQTrlVRQFHFHGWPEIGIP--AEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 257096044 337 ALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 382
Cdd:cd14622  158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQ 203

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

156-382

2.66e-54

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: 179.47 E-value: 2.66e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 156 RYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVK 235
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 236 CDHYWPfTEEPIAYGDITVEMVSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQ 313
Cdd:cd14623   81 CAQYWP-SDGSVSYGDITIELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGWPEVGIP--SDGKGMINIIAAVQKQ 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 314 AAKSKG-PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 382
Cdd:cd14623  158 QQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQ 227

R-PTPc-A-E-1

cd14551

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...

181-379

3.26e-54

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: 178.57 E-value: 3.26e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPiAYGDITVEMVSEE 260
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW-TYGNLRVRVEDTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHFRINYADEAQD------VMHFNYTAWPDHGVPPANAAesILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGT 334
Cdd:cd14551   80 VLVDYTTRKFCIQKVNRGIGekrvrlVTQFHFTSWPDFGVPFTPIG--MLKFLKKVKSANPPRAGPIVVHCSAGVGRTGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 257096044 335 FIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14551  158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

181-378

1.73e-52

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: 174.12 E-value: 1.73e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPftEEPIAYGDITVEMVSEE 260
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG--DEKKTYGDIEVELKDTE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHFRINYA--DEAQDVMHFNYTAWPDHGVPP-----ANAAESILQFVFTVRQQAAKSKgPMIIHCSAGVGRTG 333
Cdd:cd14558   79 KSPTYTVRVFEITHLkrKDSRTVYQYQYHKWKGEELPEkpkdlVDMIKSIKQKLPYKNSKHGRSV-PIVVHCSDGSSRTG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 257096044 334 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 378
Cdd:cd14558  158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

PTPc_plant_PTP1

cd17658

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...

181-378

6.32e-51

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: 169.95 E-value: 6.32e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQ-CNEKRRVKCDHYWPFTE-EPIAYGDITVEM 256
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRlVDNYSTAKCADYFPAEEnESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 257 VSEEEEED-WASRHFRINYAdEAQD----VMHFNYTAWPDHGVPPANAA-ESILQFVFTVrqqaAKSKGPMIIHCSAGVG 330
Cdd:cd17658   81 KKLKHSQHsITLRVLEVQYI-ESEEpplsVLHIQYPEWPDHGVPKDTRSvRELLKRLYGI----PPSAGPIVVHCSAGIG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 257096044 331 RTGTFIALDRLLQHIR--DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 378
Cdd:cd17658  156 RTGAYCTIHNTIRRILegDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

181-381

4.66e-50

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: 168.00 E-value: 4.66e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFT-EEPIAYGDITVEMV 257
Cdd:cd14596    1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 258 SEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRqqAAKSKGPMIIHCSAGVGRTGTF 335
Cdd:cd14596   81 NYQALQYFIIRIIKLveKETGENRLIKHLQFTTWPDHGTP--QSSDQLVKFICYMR--KVHNTGPIVVHCSAGIGRAGVL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 257096044 336 IALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14596  157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

150-377

3.01e-49

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 168.35 E-value: 3.01e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 150 LNRCK-NRYTNILPYDFSRVRlvsmneeEGADYINANYIPGYNsPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 228
Cdd:COG5599   40 INGSPlNRFRDIQPYKETALR-------ANLGYLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 229 NE--KRRVKCDHYWPFTEEPIAYgDITVEMV-SEEEEEDWASRHFRINYAD---EAQDVMHFNYTAWPDHGVPPANAAES 302
Cdd:COG5599  112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTeSIQLRDGIEARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISAEALKN 190

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257096044 303 ILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE--FVDILGLVSEMRSYR-MSMVQTEEQYIFI 377
Cdd:COG5599  191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268

PTPc-N4

cd14601

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...

180-377

6.21e-49

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: 165.12 E-value: 6.21e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 180 DYINANYI----PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVE 255
Cdd:cd14601    1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 256 MVSEEEEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 333
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNleKNESRPLTQIQYIAWPDHGVP--DDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 257096044 334 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 377
Cdd:cd14601  159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV 202

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

181-379

2.19e-47

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: 160.65 E-value: 2.19e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvKCDHYWPfTEEPIAYGDITVEMVSEE 260
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWP-DEGSGTYGPIQVEFVSTT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHFRI----NYADEAQDVMHFNYTAWPDHG-VPPAnaAESILQFVFTVRQ-QAAKSKGPMIIHCSAGVGRTGT 334
Cdd:cd14556   79 IDEDVISRIFRLqnttRPQEGYRMVQQFQFLGWPRDRdTPPS--KRALLKLLSEVEKwQEQSGEGPIVVHCLNGVGRSGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 257096044 335 FIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14556  157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

181-379

3.42e-46

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: 157.55 E-value: 3.42e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGY-NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTE--EPIAYGDITVEMV 257
Cdd:cd14539    1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWP-TErgQALVYGAITVSLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 258 SEEEEEDWASRHFRINYADEAQ--DVMHFNYTAWPDHGVPPANAAesILQFVFTVR---QQAAKSKGPMIIHCSAGVGRT 332
Cdd:cd14539   80 SVRTTPTHVERIISIQHKDTRLsrSVVHLQFTTWPELGLPDSPNP--LLRFIEEVHshyLQQRSLQTPIVVHCSSGVGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 257096044 333 GTFIALDRLLQHIR-DHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14539  158 GAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

PTPc-N14

cd14599

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...

146-379

7.07e-46

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: 159.39 E-value: 7.07e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 146 ADLPLNRCKNRYTNILPYDFSRVRLVSmNEEEGADYINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSHIIV 223
Cdd:cd14599   33 ATLPENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 224 MLTQCNEKRRVKCDHYWP---FTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPP-A 297
Cdd:cd14599  112 MVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQErtVWHLQYTDWPDHGCPEeV 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 298 NAAESILQFVFTVRQQA-------AKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQT 370
Cdd:cd14599  192 QGFLSYLEEIQSVRRHTnsmldstKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQT 271


                 ....*....
gi 257096044 371 EEQYIFIHQ 379
Cdd:cd14599  272 IAQYKFVYQ 280

PTPc-N21_14

cd14540

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

181-379

1.64e-45

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: 156.46 E-value: 1.64e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGY--NSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFT---EEPIAYGDITVE 255
Cdd:cd14540    1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggeHDALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 256 MVSEEEEEDWASRHFRINY--ADEAQDVMHFNYTAWPDHGVPpaNAAESILQF---VFTVRQQAAKSKG------PMIIH 324
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHtlSGQSRTVWHLQYTDWPDHGCP--EDVSGFLDFleeINSVRRHTNQDVAghnrnpPTLVH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 257096044 325 CSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14540  159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYN 213

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

151-376

1.55e-43

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: 1.55e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNsPQE--YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 228
Cdd:cd14610   44 NVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHD-PRNpaYIATQGPLPATVADFWQMVWESGCVVIVMLTPL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 229 NEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEE-EEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQ 305
Cdd:cd14610  123 AENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGVP--ASTRSLLD 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257096044 306 FVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 376
Cdd:cd14610  200 FRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271

PHA02742

protein tyrosine phosphatase; Provisional

151-381

9.52e-43

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 151.69 E-value: 9.52e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 230
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 231 KRRVKCDHYW-PFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQ--DVMHFNYTAWPDHGVPpaNAAESILQFV 307
Cdd:PHA02742 130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGAslDIKHFAYEDWPHGGLP--RDPNKFLDFV 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 308 FTVRQQAAKS-----------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 376
Cdd:PHA02742 208 LAVREADLKAdvdikgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                 ....*
gi 257096044 377 IHQCV 381
Cdd:PHA02742 288 CYFIV 292

PHA02738

hypothetical protein; Provisional

151-383

1.55e-42

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 151.62 E-value: 1.55e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCKNRYTNILPYDFSRVRLVSmnEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNE 230
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSRVILPA--ERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 231 KRRVKCDHYWPFTEE-PIAYGDITVEMVSEEEEEDWASRHFRINYADEA-QDVMHFNYTAWPDHGVPpaNAAESILQFVF 308
Cdd:PHA02738 127 NGREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVP--KNTSEFLNFVL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 309 TVRQ------QAAKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 375
Cdd:PHA02738 205 EVRQcqkelaQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                 ....*...
gi 257096044 376 FIHQCVQL 383
Cdd:PHA02738 285 FCYRAVKR 292

PHA02746

protein tyrosine phosphatase; Provisional

149-388

5.28e-41

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 147.87 E-value: 5.28e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 149 PLNRCKNRYTNILPYDFSRV-------------------RLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRND 209
Cdd:PHA02746  49 KENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 210 FWKMVLQQKSHIIVMLTQCNEKRRvKCDHYWPFTEE-PIAYGDITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNY 286
Cdd:PHA02746 129 FFKLISEHESQVIVSLTDIDDDDE-KCFELWTKEEDsELAFGRFVAKILDIIEELSFTKTRLMITdkISDTSREIHHFWF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 287 TAWPDHGVpPANAAEsILQFVFTVRQQAAKSK----------GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGL 356
Cdd:PHA02746 208 PDWPDNGI-PTGMAE-FLELINKVNEEQAELIkqadndpqtlGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                        250       260       270
                 ....*....|....*....|....*....|..
gi 257096044 357 VSEMRSYRMSMVQTEEQYIFIHQCVQLMWLRK 388
Cdd:PHA02746 286 VLKIRKQRHSSVFLPEQYAFCYKALKYAIIEE 317

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

151-376

2.92e-40

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: 2.92e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNsPQ--EYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 228
Cdd:cd14609   42 NVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHD-PRmpAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 229 NEKRRVKCDHYWPfTEEPIAYGDITVEMVSEEE-EEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQ 305
Cdd:cd14609  121 VEDGVKQCDRYWP-DEGSSLYHIYEVNLVSEHIwCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGIP--SSTRPLLD 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257096044 306 FVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 376
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 ...

181-381

1.09e-39

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: 140.66 E-value: 1.09e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPfTEEPIAYGDITVEMVSE 259
Cdd:cd14546    1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-EEGSEVYHIYEVHLVSE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 260 EE-EEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVPpaNAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFI 336
Cdd:cd14546   80 HIwCDDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIP--ASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 257096044 337 ALD----RLLQHIRDhefVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14546  158 LIDmvlnRMAKGAKE---IDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

281-381

5.19e-38

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 132.87 E-value: 5.19e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044   281 VMHFNYTAWPDHGVPPAnaAESILQFVFTVR--QQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRD-HEFVDILGLV 357
Cdd:smart00404   2 VKHYHYTGWPDHGVPES--PDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTV 79

                           90       100
                   ....*....|....*....|....
gi 257096044   358 SEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRAL 103

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

281-381

5.19e-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: 132.87 E-value: 5.19e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044   281 VMHFNYTAWPDHGVPPAnaAESILQFVFTVR--QQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRD-HEFVDILGLV 357
Cdd:smart00012   2 VKHYHYTGWPDHGVPES--PDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTV 79

                           90       100
                   ....*....|....*....|....
gi 257096044   358 SEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRAL 103

PHA02747

protein tyrosine phosphatase; Provisional

149-378

2.05e-36

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 135.13 E-value: 2.05e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 149 PLNRCKNRYTNILPYDFSRVRLVSmNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 228
Cdd:PHA02747  49 PENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 229 NEKR-RVKCDHYWPFTEE-PIAYGDITVEMVSEEEEEDWASRHFRIN--YADEAQDVMHFNYTAWPDHGVpPANAAESI- 303
Cdd:PHA02747 128 KGTNgEEKCYQYWCLNEDgNIDMEDFRIETLKTSVRAKYILTLIEITdkILKDSRKISHFQCSEWFEDET-PSDHPDFIk 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 304 -LQFVFTVRQQAAKSKG-------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 375
Cdd:PHA02747 207 fIKIIDINRKKSGKLFNpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                 ...
gi 257096044 376 FIH 378
Cdd:PHA02747 287 FIQ 289

PTPc-N21

cd14598

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...

181-379

1.68e-35

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: 1.68e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPF---TEEPIAYGDITVE 255
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgsRHNTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 256 MVSEEEEEDWASRHFRINYADEAQD--VMHFNYTAWPDHGVPP-ANAAESILQFVFTVRQQAAKS------KGPMIIHCS 326
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKHLLTGQErtVWHLQYTDWPEHGCPEdLKGFLSYLEEIQSVRRHTNSTidpkspNPPVLVHCS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 257096044 327 AGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14598  161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYK 213

R-PTPc-T-2

cd14634

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...

181-379

2.74e-35

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: 2.74e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvkCDHYWPfTEEPIAYGDITVEMVSEE 260
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL--CMQYWP-EKTSCCYGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHFRINYADEAQD----VMHFNYTAWPDH-GVPPANaaESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRT 332
Cdd:cd14634   78 IDEDIISRIFRICNMARPQDgyriVQHLQYIGWPAYrDTPPSK--RSILKVVRRLekwQEQYDGREGRTVVHCLNGGGRS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 257096044 333 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14634  156 GTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYE 202

R-PTPc-U-2

cd14637

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...

181-381

1.03e-31

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

Pssm-ID: 350485 [Multi-domain] Cd Length: 207 Bit Score: 119.63 E-value: 1.03e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV-KCDHYWPfteEP--IAYGDITVEMV 257
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP---EPglQQYGPMEVEFV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 258 SEEEEEDWASRHFRINYADEAQD----VMHFNYTAWPDHGVPPaNAAESILQFVFTVRQ-QAAKSKGPMIIHCSAGVGRT 332
Cdd:cd14637   78 SGSADEDIVTRLFRVQNITRLQEghlmVRHFQFLRWSAYRDTP-DSKKAFLHLLASVEKwQRESGEGRTVVHCLNGGGRS 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 257096044 333 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd14637  157 GTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205

R-PTPc-K-2

cd14636

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...

181-378

2.10e-31

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

Pssm-ID: 350484 [Multi-domain] Cd Length: 206 Bit Score: 118.59 E-value: 2.10e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRrvKCDHYWPfTEEPIAYGDITVEMVSEE 260
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWP-EEGMLRYGPIQVECMSCS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHFRINYADEAQD----VMHFNYTAWPDHGVPPAnAAESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRTG 333
Cdd:cd14636   78 MDCDVISRIFRICNLTRPQEgylmVQQFQYLGWASHREVPG-SKRSFLKLILQVekwQEECDEGEGRTIIHCLNGGGRSG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 257096044 334 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 378
Cdd:cd14636  157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201

R5-PTP-2

cd14550

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

181-379

2.06e-30

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: 2.06e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCdhYWPFTEEPIAYGDITV-----E 255
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVtlsgeD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 256 MVSEEEEEDWASRHFRI--NYADEAQDVMHFNYTAWPDhgvpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 333
Cdd:cd14550   79 HSCLSNEIRLIVRDFILesTQDDYVLEVRQFQCPSWPN----PCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 257096044 334 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14550  155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

R-PTPc-M-2

cd14635

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...

181-379

3.71e-27

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: 107.08 E-value: 3.71e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRvkCDHYWPftEEPI-AYGDITVEMVSE 259
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP--ENGVhRHGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 260 EEEEDWASRHFRINYADEAQD----VMHFNYTAWPDHGVPPAnAAESILQFVFTV---RQQAAKSKGPMIIHCSAGVGRT 332
Cdd:cd14635   77 DLEEDIISRIFRIYNAARPQDgyrmVQQFQFLGWPMYRDTPV-SKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 257096044 333 GTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 379
Cdd:cd14635  156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 202

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

181-381

4.88e-26

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: 103.99 E-value: 4.88e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQcNEKRRVKCDHYWPFTEEPIAYGDITVEMVSE- 259
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCEAFTVTLISKd 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 260 ---------EEEEDWASRHFRINYADEaqdVMHFNYTAWPDhgvpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVG 330
Cdd:cd17670   80 rlclsneeqIIIHDFILEATQDDYVLE---VRHFQCPKWPN----PDAPISSTFELINVIKEEALTRDGPTIVHDEFGAV 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 257096044 331 RTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd17670  153 SAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203

R-PTP-Z-2

cd17669

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

181-381

6.06e-26

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: 103.92 E-value: 6.06e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 181 YINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCdHYWPFTEEPIAYGDITVEMVSEE 260
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 261 EEEDWASRHFRI-NYADEA-QD-----VMHFNYTAWPDhgvpPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTG 333
Cdd:cd17669   80 HKCLSNEEKLIIqDFILEAtQDdyvleVRHFQCPKWPN----PDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 257096044 334 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 381
Cdd:cd17669  156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203

PTP_YopH-like

cd14559

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...

155-374

1.65e-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: 83.60 E-value: 1.65e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 155 NRYTNIlpydfsrvrlVSMNEEEGADYINANYIPGYNSPQeYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRV 234
Cdd:cd14559    1 NRFTNI----------QTRVSTPVGKNLNANRVQIGNKNV-AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 235 KCDHYWPFTEEpiaYGDITV--EMVSEEEEEDWASRH---FRINYADEAQDVMHFNYTAWPDHGVPPANAAESILQFVFT 309
Cdd:cd14559   70 GLPPYFRQSGT---YGSVTVksKKTGKDELVDGLKADmynLKITDGNKTITIPVVHVTNWPDHTAISSEGLKELADLVNK 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257096044 310 VRQQAA-------------KSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDIlglVSEMRSYRMS-MVQTEEQY 374
Cdd:cd14559  147 SAEEKRnfykskgssaindKNKLLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRNGkMVQKDEQL 222

PHA02740

protein tyrosine phosphatase; Provisional

151-398

6.12e-15

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 75.00 E-value: 6.12e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 151 NRCK--NRYTNILPYDFSRVRLVSMNEeegadYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQC 228
Cdd:PHA02740  51 NKAKdeNLALHITRLLHRRIKLFNDEK-----VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 229 NEKrrvKC-DHYWPFTEEP-IAYGDITVEMVSEEEEEdwasrHFRI------NYADEAQDVMHFNYTAWPDHGVppANAA 300
Cdd:PHA02740 126 ADK---KCfNQFWSLKEGCvITSDKFQIETLEIIIKP-----HFNLtllsltDKFGQAQKISHFQYTAWPADGF--SHDP 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 301 ESILQFVFTV--------RQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEE 372
Cdd:PHA02740 196 DAFIDFFCNIddlcadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLD 275

                        250       260
                 ....*....|....*....|....*.
gi 257096044 373 QYIFihqCVQLMWLRKKQQFCISDVI 398
Cdd:PHA02740 276 DYVF---CYHLIAAYLKEKFDILKFI 298

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

289-379

2.54e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 58.06 E-value: 2.54e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 289 WPDHGVPPANAAESILQFVftvrQQAAKSKGPMIIHCSAGVGRTGTFIAldrLLQHIRDHEFVDILGLVSEMRSYRmsmV 368
Cdd:COG2453   55 IPDFGAPDDEQLQEAVDFI----DEALREGKKVLVHCRGGIGRTGTVAA---AYLVLLGLSAEEALARVRAARPGA---V 124

                         90
                 ....*....|.
gi 257096044 369 QTEEQYIFIHQ 379
Cdd:COG2453  125 ETPAQRAFLER 135

PTP_DSP_cys

cd14494

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...

298-379

5.24e-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: 56.59 E-value: 5.24e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 298 NAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRdhefvDILGLVSEMRSYR-MSMVQTEEQYIF 376
Cdd:cd14494   36 DLTLAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRpGGIPQTIEQLDF 110


                 ...
gi 257096044 377 IHQ 379
Cdd:cd14494  111 LIK 113

CDKN3-like

cd14505

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...

290-379

2.52e-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: 2.52e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 290 PDHGVPPANAaesilQFVFTVRQ--QAAKSKGPMIIHCSAGVGRTGTFIAldRLLQHIRDHEFVD-ILGLVsemRSYRMS 366
Cdd:cd14505   81 PDGGVPSDIA-----QWQELLEEllSALENGKKVLIHCKGGLGRTGLIAA--CLLLELGDTLDPEqAIAAV---RALRPG 150

                         90
                 ....*....|...
gi 257096044 367 MVQTEEQYIFIHQ 379
Cdd:cd14505  151 AIQTPKQENFLHQ 163

PTP_PTPDC1

cd14506

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...

278-390

2.55e-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: 47.73 E-value: 2.55e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 278 AQDVMHFNYtAWPDHGVPPANAAESILQfvftVRQQAAKSKGPMIIHCSAGVGRTGTFIA-----LDRLL--QHIRdheF 350
Cdd:cd14506   74 RAGIYFYNF-GWKDYGVPSLTTILDIVK----VMAFALQEGGKVAVHCHAGLGRTGVLIAcylvyALRMSadQAIR---L 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 257096044 351 VdilglvsemRSYRMSMVQTEEQYIFIHQCVQLMWLRKKQ 390
Cdd:cd14506  146 V---------RSKRPNSIQTRGQVLCVREFAQFLLPLRNV 176

DUSP23

cd14504

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...

290-379

4.39e-06

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: 46.12 E-value: 4.39e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 290 PDHGVPpanAAESILQFVFTVRQQAAKSKgPMIIHCSAGVGRTGTFIALdrllqHIRDHEFVDILGLVSEMRSYRMSMVQ 369
Cdd:cd14504   58 EDYTPP---TLEQIDEFLDIVEEANAKNE-AVLVHCLAGKGRTGTMLAC-----YLVKTGKISAVDAINEIRRIRPGSIE 128

                         90
                 ....*....|
gi 257096044 370 TEEQYIFIHQ 379
Cdd:cd14504  129 TSEQEKFVIQ 138

TpbA-like

cd14529

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...

267-338

2.51e-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: 2.51e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257096044 267 SRHFRINYADEAQDVMHFNYTAWPDHGVPPANAAESIlqfvFTVRQQAAKSKGPMIIHCSAGVGRTGTFIAL 338
Cdd:cd14529   42 GADERAASEEAAAKIDGVKYVNLPLSATRPTESDVQS----FLLIMDLKLAPGPVLIHCKHGKDRTGLVSAL 109

CDC14_C

cd14499

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...

290-338

1.34e-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: 42.44 E-value: 1.34e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 257096044 290 PDHGVPPanaaESILQ-FVftvrQQAAKSKGPMIIHCSAGVGRTGTFIAL 338
Cdd:cd14499   88 PDGSTPS----DDIVKkFL----DICENEKGAIAVHCKAGLGRTGTLIAC 129

PTP_VSP_TPTE

cd14510

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...

268-336

1.86e-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: 41.96 E-value: 1.86e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257096044 268 RHFRI-NYADE-AQDVMHFNYTA----WPDHGVPPAnaaESILQFVFTVRQ-QAAKSKGPMIIHCSAGVGRTGTFI 336
Cdd:cd14510   54 DHYKVyNLCSErGYDPKYFHNRVervpIDDHNVPTL---DEMLSFTAEVREwMAADPKNVVAIHCKGGKGRTGTMV 126

PRK15375

type III secretion system effector GTPase-activating protein SptP;

197-337

3.91e-04

type III secretion system effector GTPase-activating protein SptP;

Pssm-ID: 185273 [Multi-domain] Cd Length: 535 Bit Score: 42.48 E-value: 3.91e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257096044 197 IATQGPLPETRND----FWKMVLQQKSHIIVMLTQcneKRRVKCDHYWPFTEEPIAYGDI-----TVEMVSEEEEEDWAS 267
Cdd:PRK15375 335 VALAGSYPKNTPDaleaHMKMLLEKECSCLVVLTS---EDQMQAKQLPPYFRGSYTFGEVhtnsqKVSSASQGEAIDQYN 411

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257096044 268 RHFRINYADEAQDVMHFNytAWPDHG-VPPANAAESILQFVFTVRQQAAKSKG------PMIiHCSAGVGRTGTFIA 337
Cdd:PRK15375 412 MQLSCGEKRYTIPVLHVK--NWPDHQpLPSTDQLEYLADRVKNSNQNGAPGRSssdkhlPMI-HCLGGVGRTGTMAA 485

PTP-IVa

cd14500

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...

288-338

4.84e-03

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.

Pssm-ID: 350350 [Multi-domain] Cd Length: 156 Bit Score: 37.59 E-value: 4.84e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 257096044 288 AWPDHGVPPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIAL 338
Cdd:cd14500   65 PFDDGSPPPDDVVDDWLDLLKTRFKEEGKPGACIAVHCVAGLGRAPVLVAI 115

PTPLP-like

cd14495

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...

324-354

7.13e-03

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.

Pssm-ID: 350345 Cd Length: 278 Bit Score: 38.12 E-value: 7.13e-03

                         10        20        30
                 ....*....|....*....|....*....|.
gi 257096044 324 HCSAGVGRTGTFIALDRLLQHIRDHEFVDIL 354
Cdd:cd14495  192 HCRAGKGRTTTFMVMYDMLKNPKDVSFDDII 222

DSPc

smart00195

Dual specificity phosphatase, catalytic domain;

283-337

8.64e-03

Dual specificity phosphatase, catalytic domain;

Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 36.49 E-value: 8.64e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 257096044   283 HFNYTAWP---DHGVPPANAAESILQFVftvrQQAAKSKGPMIIHCSAGVGRTGTFIA 337
Cdd:smart00195  44 DFTYLGVPiddNTETKISPYFPEAVEFI----EDAESKGGKVLVHCQAGVSRSATLII 97

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