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Conserved domains on  [gi|122921221|pdb|2NZ6|A]
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Chain A, Receptor-type tyrosine-protein phosphatase eta

Protein Classification

protein-tyrosine phosphatase family protein; phosphatase PAP2/dual specificity phosphatase family protein( domain architecture ID 12998701)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively; bifunctional phosphatase PAP2/dual specificity phosphatase (DSP) family protein containing a C-terminal DSP domain that may dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues in target proteins, and an N-terminal PAP2 domain with similarity to yeast inositol phosphorylceramide synthase (AUR1) that catalyzes the addition of inositol phosphate to ceramide, an essential step in sphingolipid synthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 74-302 1.25e-180

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: 497.42  E-value: 1.25e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       74 NRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTK 153
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      154 CEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 233
Cdd:cd14615  81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2NZ6_A      234 SPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14615 161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
 
Name Accession Description Interval E-value
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 74-302 1.25e-180

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: 497.42  E-value: 1.25e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       74 NRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTK 153
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      154 CEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 233
Cdd:cd14615  81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2NZ6_A      234 SPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14615 161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
45-302 6.05e-125

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 357.74  E-value: 6.05e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A          45 GFAEEYEDLKLVGISQPKYA-AELAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 123
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A         124 TLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLR 201
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A         202 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSppESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRM 281
Cdd:smart00194 161 HYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                          250       260
                   ....*....|....*....|.
2NZ6_A         282 HRPLMVQTEDQYVFLNQCVLD 302
Cdd:smart00194 239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
70-302 3.19e-114

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 329.59  E-value: 3.19e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A         70 NRGKNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQ 149
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A        150 GRTKCEEYWPSK--QAQDYGDITVAMTSE-IVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 226
Cdd:pfam00102  80 GREKCAQYWPEEegESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2NZ6_A        227 VRDYmKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:pfam00102 160 VRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
66-296 7.89e-47

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.10  E-value: 7.89e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       66 ELAENRGKNRYNNVLPYDISRVKlsvqthSTDDYINANYMPGYhSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTK 145
Cdd:COG5599  38 QNINGSPLNRFRDIQPYKETALR------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      146 CVE--QGRTKCEEYWPskQAQDYG--DITVAMTSEIVL-PEWTIRDFTVKNIQTS-ESHPLRQFHFTSWPDHGVPDTTdL 219
Cdd:COG5599 111 DDEisKPKVKMPVYFR--QDGEYGkyEVSSELTESIQLrDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAISAE-A 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      220 LINFRYLVRDYMK-QSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR-PLMVQTEDQYVF 295
Cdd:COG5599 188 LKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDV 267


                .
2NZ6_A      296 L 296
Cdd:COG5599 268 L 268
PHA02738 PHA02738
hypothetical protein; Provisional
 63-295 7.24e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 157.78  E-value: 7.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A        63 YAAELAeNRGKNRYNNVLPYDISRVKLSVQtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIM 142
Cdd:PHA02738  43 FNAEKK-NRKLNRYLDAVCFDHSRVILPAE-RNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVM 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       143 LTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEIVLPEWtIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLL 220
Cdd:PHA02738 121 LCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHY-VKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEF 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       221 INFRYLVRDYMKQSPPES-----------PILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQT 289
Cdd:PHA02738 200 LNFVLEVRQCQKELAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFI 279


                 ....*.
2NZ6_A       290 EDQYVF 295
Cdd:PHA02738 280 PFQYFF 285
 
Name Accession Description Interval E-value
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 74-302 1.25e-180

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: 497.42  E-value: 1.25e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       74 NRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTK 153
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      154 CEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 233
Cdd:cd14615  81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2NZ6_A      234 SPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14615 161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 75-298 1.47e-143

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: 403.66  E-value: 1.47e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       75 RYNNVLPYDISRVKLSVQT-HSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTK 153
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINeEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      154 CEEYWPSKQAQ-DYGDITVAMTSEIVLPEWTIRDFTVKNIQtsESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMK 232
Cdd:cd14548  81 CDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
2NZ6_A      233 QspPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:cd14548 159 Q--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
45-302 6.05e-125

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 357.74  E-value: 6.05e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A          45 GFAEEYEDLKLVGISQPKYA-AELAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 123
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A         124 TLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLR 201
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A         202 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSppESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRM 281
Cdd:smart00194 161 HYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                          250       260
                   ....*....|....*....|.
2NZ6_A         282 HRPLMVQTEDQYVFLNQCVLD 302
Cdd:smart00194 239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
70-302 3.19e-114

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 329.59  E-value: 3.19e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A         70 NRGKNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQ 149
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A        150 GRTKCEEYWPSK--QAQDYGDITVAMTSE-IVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 226
Cdd:pfam00102  80 GREKCAQYWPEEegESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2NZ6_A        227 VRDYmKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:pfam00102 160 VRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 74-304 6.56e-112

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: 323.76  E-value: 6.56e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       74 NRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRT 152
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKpIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      153 KCEEYWP-SKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYM 231
Cdd:cd14619  81 KCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2NZ6_A      232 KQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIV 304
Cdd:cd14619 161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 74-298 8.08e-109

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: 315.70  E-value: 8.08e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       74 NRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRT 152
Cdd:cd14617   1 NRYNNILPYDSTRVKLSnVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      153 KCEEYWPSKQ-AQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPL-RQFHFTSWPDHGVPDTTDLLINFRYLVRDY 230
Cdd:cd14617  81 KCDHYWPADQdSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLvRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
2NZ6_A      231 MKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:cd14617 161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 99-298 2.99e-101

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: 295.35  E-value: 2.99e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSE 176
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPleYGDITVTLVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      177 IVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYmkQSPPESPILVHSSAGVGRTGTFIA 256
Cdd:cd00047  81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKE--ARKPNGPIVVHCSAGVGRTGTFIA 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
2NZ6_A      257 IDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:cd00047 159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 74-301 1.74e-100

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: 294.93  E-value: 1.74e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       74 NRYNNVLPYDISRVKLSV---QTHStdDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQG 150
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQlggEPHS--DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      151 RTKCEEYWPSKQAQ-DYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 229
Cdd:cd14618  79 RVLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2NZ6_A      230 YMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 301
Cdd:cd14618 159 HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 70-306 4.60e-100

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: 293.92  E-value: 4.60e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       70 NRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVE 148
Cdd:cd14553   3 NKPKNRYANVIAYDHSRVILQpIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      149 QGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVR 228
Cdd:cd14553  83 RSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2NZ6_A      229 DYmkqSPPES-PILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIVRS 306
Cdd:cd14553 163 AC---NPPDAgPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 61-301 6.50e-96

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: 283.70  E-value: 6.50e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       61 PKYAAELAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 139
Cdd:cd14614   3 PHFAADLPVNRCKNRYTNILPYDFSRVKLvSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      140 IIMLTKCVEQGRTKCEEYWP-SKQAQDYGDITVAMTSEIVLPEWTIRDFTVKniQTSESHPLRQFHFTSWPDHGVP--DT 216
Cdd:cd14614  83 IVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPtaNA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      217 TDLLINFRYLVRDYMKQSPpeSPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 296
Cdd:cd14614 161 AESILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238


                ....*
2NZ6_A      297 NQCVL 301
Cdd:cd14614 239 HQCVQ 243
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 99-296 5.23e-94

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: 277.31  E-value: 5.23e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIV 178
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      179 LPEWTIRDFTVKNIQTSESHP------LRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQSPPES-PILVHSSAGVGRT 251
Cdd:cd14549  81 LATYTVRTFSLKNLKLKKVKGrsservVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPPGAgPIVVHCSAGVGRT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
2NZ6_A      252 GTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 296
Cdd:cd14549 158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 45-295 1.27e-91

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: 273.86  E-value: 1.27e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       45 GFAEEYEDLKLVGISQPKYAAELAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 123
Cdd:cd14543   4 GIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPkRNGDERTDYINANFMDGYKQKNAYIATQGPLPK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      124 TLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQ--AQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLR 201
Cdd:cd14543  84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVT 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      202 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQS-----------PPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTV 270
Cdd:cd14543 164 HFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTL 243

                       250       260
                ....*....|....*....|....*
2NZ6_A      271 DVYGIVYDLRMHRPLMVQTEDQYVF 295
Cdd:cd14543 244 NVMQTVRRMRTQRAFSIQTPDQYYF 268
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 36-304 8.02e-83

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: 251.49  E-value: 8.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       36 KKQQADSNCGFAEEYEDLKlVGISQPKYAAELAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDF 114
Cdd:cd14626   8 ERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILtSVDGVPGSDYINANYIDGYRKQNAY 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      115 IATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQT 194
Cdd:cd14626  87 IATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGS 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      195 SESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQSPPES-PILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVY 273
Cdd:cd14626 167 SEKREVRQFQFMAWPDHGVPEYPTPILAF---LRRVKACNPPDAgPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIY 243

                       250       260       270
                ....*....|....*....|....*....|.
2NZ6_A      274 GIVYDLRMHRPLMVQTEDQYVFLNQCVLDIV 304
Cdd:cd14626 244 GHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 74-298 2.49e-80

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: 243.07  E-value: 2.49e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       74 NRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEqGR 151
Cdd:cd14547   1 NRYKTILPNEHSRVCLpSVDDDPLSSYINANYIRGYDGEeKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      152 TKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNiqTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYM 231
Cdd:cd14547  80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEAR 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2NZ6_A      232 KQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:cd14547 158 QTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 65-301 5.05e-80

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: 242.82  E-value: 5.05e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       65 AELAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIML 143
Cdd:cd14554   1 ANLPCNKFKNRLVNILPYESTRVCLQpIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      144 TKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINF 223
Cdd:cd14554  81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2NZ6_A      224 RYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 301
Cdd:cd14554 161 IGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 69-302 2.93e-79

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: 241.08  E-value: 2.93e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       69 ENRGKNRYNNVLPYDISRVKLSV---QTHStdDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTK 145
Cdd:cd14630   2 ENRNKNRYGNIISYDHSRVRLQLldgDPHS--DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      146 CVEQGRTKCEEYWPSkQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFry 225
Cdd:cd14630  80 LVEVGRVKCVRYWPD-DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF-- 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2NZ6_A      226 lVRDYMKQSPPES-PILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14630 157 -VRQVKFLNPPDAgPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 46-304 6.47e-79

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: 241.48  E-value: 6.47e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       46 FAEEYEDLKLVgISQPKYAAELA---ENRGKNRYNNVLPYDISRVKLSV-----QTHStdDYINANYMPGYHSKKDFIAT 117
Cdd:cd17667   1 FSEDFEEVQRC-TADMNITAEHSnhpDNKHKNRYINILAYDHSRVKLRPlpgkdSKHS--DYINANYVDGYNKAKAYIAT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      118 QGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQT--- 194
Cdd:cd17667  78 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVkkg 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      195 SESHP--------LRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIEN 266
Cdd:cd17667 158 QKGNPkgrqnertVIQYHYTQWPDMGVPEYALPVLTF--VRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKD 235

                       250       260       270
                ....*....|....*....|....*....|....*...
2NZ6_A      267 ENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIV 304
Cdd:cd17667 236 KSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 26-304 4.85e-77

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: 236.91  E-value: 4.85e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       26 IRVENFEAYFKKQQADSNCGFAEEYEDLKlVGISQPKYAAELAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANY 104
Cdd:cd14625   4 IPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILqPIEGIMGSDYINANY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      105 MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTI 184
Cdd:cd14625  83 IDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFCV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      185 RDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQSPPES-PILVHSSAGVGRTGTFIAIDRLIYQ 263
Cdd:cd14625 163 RTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAF---LRRVKTCNPPDAgPIVVHCSAGVGRTGCFIVIDAMLER 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
2NZ6_A      264 IENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIV 304
Cdd:cd14625 240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 74-298 5.04e-77

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: 234.80  E-value: 5.04e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       74 NRYNNVLPYDISRVKLSVQTHST-DDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRT 152
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      153 KCEEYWP--SKQAQDYGDITVAMTSEIVLPEWTIRDFTVKniQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRdy 230
Cdd:cd14616  81 RCHQYWPedNKPVTVFGDIVITKLMEDVQIDWTIRDLKIE--RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR-- 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
2NZ6_A      231 MKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:cd14616 157 ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 34-304 1.06e-76

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: 236.17  E-value: 1.06e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       34 YFKKQQADSNCGFAEEYEDLKlVGISQPKYAAELAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKK 112
Cdd:cd14624  12 HIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSaIEGIPGSDYINANYIDGYRKQN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      113 DFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNI 192
Cdd:cd14624  91 AYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKN 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      193 QTSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQSPPES-PILVHSSAGVGRTGTFIAIDRLIYQIENENTVD 271
Cdd:cd14624 171 GSSEKREVRQFQFTAWPDHGVPEHPTPFLAF---LRRVKTCNPPDAgPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVD 247

                       250       260       270
                ....*....|....*....|....*....|...
2NZ6_A      272 VYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIV 304
Cdd:cd14624 248 IYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 45-302 2.88e-76

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: 234.55  E-value: 2.88e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       45 GFAEEYEDLkLVGISQPKYAAELAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 123
Cdd:cd14633  16 GFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLqPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      124 TLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSkQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQF 203
Cdd:cd14633  95 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQF 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      204 HFTSWPDHGVPDTTDLLINFrylVRDYMKQSPPES-PILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMH 282
Cdd:cd14633 174 HFTGWPDHGVPYHATGLLGF---VRQVKSKSPPNAgPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSR 250

                       250       260
                ....*....|....*....|
2NZ6_A      283 RPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14633 251 RVNMVQTEEQYVFIHDAILE 270
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 28-302 1.36e-73

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: 228.75  E-value: 1.36e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       28 VENFEAYFKKQQADSNCGFAEEYEDLKLVGISQPKYAAELAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMP 106
Cdd:cd14621  10 VDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLtPVEGVPDSDYINASFIN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      107 GYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRD 186
Cdd:cd14621  90 GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRK 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      187 FTVKNI-QTSESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPpeSPILVHSSAGVGRTGTFIAIDRLIY 262
Cdd:cd14621 170 FCIQQVgDVTNKKPQRlitQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYA--GAIVVHCSAGVGRTGTFIVIDAMLD 247

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
2NZ6_A      263 QIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14621 248 MMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 99-302 1.63e-73

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: 225.18  E-value: 1.63e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPsKQAQDYGDITVAMTSEIV 178
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      179 LPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQSPPES-PILVHSSAGVGRTGTFIAI 257
Cdd:cd14555  80 LAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGF---IRRVKASNPPSAgPIVVHCSAGAGRTGCYIVI 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
2NZ6_A      258 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14555 157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 99-298 3.16e-71

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: 219.31  E-value: 3.16e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPS--KQAQDYGDITVAMTSE 176
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      177 IVLPEWTIRDFTVKNIQTSES-HPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYmkQSPPESPILVHSSAGVGRTGTFI 255
Cdd:cd14557  81 KICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF--NNFFSGPIVVHCSAGVGRTGTYI 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
2NZ6_A      256 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:cd14557 159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 99-302 3.95e-71

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: 219.15  E-value: 3.95e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPsKQAQDYGDITVAMTSEIV 178
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      179 LPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQSPPES-PILVHSSAGVGRTGTFIAI 257
Cdd:cd14632  80 LAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAF---IRRVKASTPPDAgPVVVHCSAGAGRTGCYIVL 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
2NZ6_A      258 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14632 157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 99-297 1.51e-69

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: 215.23  E-value: 1.51e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIV 178
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      179 LPEWTIRDFTVKNIQT--------SESHPLRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQSPPESPILVHSSAGVGR 250
Cdd:cd17668  81 LAYYTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTF--VRKASYAKRHAVGPVVVHCSAGVGR 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
2NZ6_A      251 TGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 297
Cdd:cd17668 159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 64-306 2.06e-69

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: 217.67  E-value: 2.06e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       64 AAELAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIM 142
Cdd:cd14629  47 SANLPCNKFKNRLVNIMPYELTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      143 LTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLIN 222
Cdd:cd14629 127 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      223 FRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14629 207 FIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286


                ....
2NZ6_A      303 IVRS 306
Cdd:cd14629 287 YLGS 290
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 64-306 3.21e-69

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: 217.29  E-value: 3.21e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       64 AAELAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIM 142
Cdd:cd14627  47 SANLPCNKFKNRLVNIMPYETTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      143 LTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLIN 222
Cdd:cd14627 127 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      223 FRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14627 207 FIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286


                ....
2NZ6_A      303 IVRS 306
Cdd:cd14627 287 YLGS 290
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 26-306 5.92e-69

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: 216.52  E-value: 5.92e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       26 IRVENFEAYFKK----QQADSNCGFAEEYEDLKLVGISQPKY-AAELAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDY 99
Cdd:cd14628   3 VPARNLYAYIQKltqiETGENVTGMELEFKRLASSKAHTSRFiSANLPCNKFKNRLVNIMPYESTRVCLQpIRGVEGSDY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      100 INANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVL 179
Cdd:cd14628  83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNM 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      180 PEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDR 259
Cdd:cd14628 163 PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSI 242

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
2NZ6_A      260 LIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIVRS 306
Cdd:cd14628 243 VLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 76-302 1.18e-68

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: 213.65  E-value: 1.18e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       76 YNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKC 154
Cdd:cd14620   1 YPNILPYDHSRVILSqLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      155 EEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVRDYm 231
Cdd:cd14620  81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRlvtQLHFTSWPDFGVPFTPIGMLKFLKKVKSV- 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2NZ6_A      232 kqSPPES-PILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14620 160 --NPVHAgPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 99-296 1.28e-68

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


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 212.88  E-value: 1.28e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYM-PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQD-YGDITVAM--T 174
Cdd:cd18533   1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGeYGDLTVELvsE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      175 SEIVLPEWTIRDFTVKNiQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPPESPILVHSSAGVGRTGTF 254
Cdd:cd18533  81 EENDDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTF 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
2NZ6_A      255 IAIDRLIYQIEN--------ENTVD-VYGIVYDLRMHRPLMVQTEDQYVFL 296
Cdd:cd18533 160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFL 210
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 99-301 2.90e-68

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: 211.85  E-value: 2.90e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYM--PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWP---SKQAQDYGDITVAM 173
Cdd:cd14538   1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslNKPLICGGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      174 TSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRdYMKQSPPESPILVHSSAGVGRTGT 253
Cdd:cd14538  81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRF---IR-YMRRIHNSGPIVVHCSAGIGRTGV 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
2NZ6_A      254 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 301
Cdd:cd14538 157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 99-300 4.58e-68

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: 211.36  E-value: 4.58e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIV 178
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      179 LPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSpPESPILVHSSAGVGRTGTFIAID 258
Cdd:cd14552  81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS-GNHPITVHCSAGAGRTGTFCALS 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
2NZ6_A      259 RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 300
Cdd:cd14552 160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 73-295 1.86e-67

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: 210.71  E-value: 1.86e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       73 KNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRT 152
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQGDND-YINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      153 KCEEYWPSKQAQDY----GDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVR 228
Cdd:cd14545  80 KCAQYWPQGEGNAMifedTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVR 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2NZ6_A      229 DYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENT--VDVYGIVYDLRMHRPLMVQTEDQYVF 295
Cdd:cd14545 160 ESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 65-305 5.66e-67

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: 210.86  E-value: 5.66e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       65 AELAENRGKNRYNNVLPYDISRVKLsvqtHSTDDYINANYM----PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAI 140
Cdd:cd14600  35 AKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      141 IMLTKCVEQGRTKCEEYWPSKQ-AQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDL 219
Cdd:cd14600 111 VMLTTLTERGRTKCHQYWPDPPdVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      220 LINFRYLVRDYMKQSppeSPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 299
Cdd:cd14600 191 FLEFVNYVRSKRVEN---EPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267


                ....*.
2NZ6_A      300 VLDIVR 305
Cdd:cd14600 268 ILRVYE 273
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 46-295 7.68e-67

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: 210.65  E-value: 7.68e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       46 FAEEYEDLKLVGISQPKYAAELAENRGKNRYNNVLPYDISRVKLSVQThstDDYINANYMPGYHSKKDFIATQGPLPNTL 125
Cdd:cd14608   1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED---NDYINASLIKMEEAQRSYILTQGPLPNTC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      126 KDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQ----DYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLR 201
Cdd:cd14608  78 GHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKemifEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREIL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      202 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDR---LIYQIENENTVDVYGIVYD 278
Cdd:cd14608 158 HFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLE 237

                       250
                ....*....|....*..
2NZ6_A      279 LRMHRPLMVQTEDQYVF 295
Cdd:cd14608 238 MRKFRMGLIQTADQLRF 254
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 99-298 8.02e-67

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: 208.05  E-value: 8.02e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSE 176
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      177 ivlpEWTIRDFTVKNIQ---TSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYmkQSPPESPILVHSSAGVGRTGT 253
Cdd:cd14542  81 ----KRVGPDFLIRTLKvtfQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGT 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
2NZ6_A      254 FIAIDR----LIYQIENENtVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:cd14542 155 ICAIDYvwnlLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 70-296 1.46e-66

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: 208.86  E-value: 1.46e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       70 NRGKNRYNNVLPYDISRVKLSVQTHST--DDYINANYM-----PGYHSK--KDFIATQGPLPNTLKDFWRMVWEKNVYAI 140
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRDPNVpgSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      141 IMLTKCVEQGRTKCEEYWPSK-QAQDYGDITVAMTSEIVLPEWTIRDFTVKNI-QTSESHPLRQFHFTSWPDHGVPDTTD 218
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWPDEgMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDPG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      219 LLINFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENEN---TVDVYGIVYDLRMHRPLMVQTEDQYVF 295
Cdd:cd14544 161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                .
2NZ6_A      296 L 296
Cdd:cd14544 241 I 241
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 61-307 2.00e-66

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: 210.17  E-value: 2.00e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       61 PKYAAELAENRGKNRYNNVLPYDISRVKLSVQTHSTD-DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 139
Cdd:cd14604  48 PTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDsDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAI 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      140 IIMLTKCVEQGRTKCEEYWP--SKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQtsESHPLRQFHFTSWPDHGVPDTT 217
Cdd:cd14604 128 IVMACREFEMGRKKCERYWPlyGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQN--ETRRLYQFHYVNWPDHDVPSSF 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      218 DLLINFRYLVRDYmkQSPPESPILVHSSAGVGRTGTFIAID---RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYV 294
Cdd:cd14604 206 DSILDMISLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYE 283

                       250
                ....*....|...
2NZ6_A      295 FLNQCVLDIVRSQ 307
Cdd:cd14604 284 LVHRAIAQLFEKQ 296
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 73-296 3.20e-66

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: 208.15  E-value: 3.20e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       73 KNRYNNVLPYDISRVKLSVQTHS--TDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKcVEQ 149
Cdd:cd14612  18 KDRYKTILPNPQSRVCLRRAGSQeeEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITK-LKE 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      150 GRTKCEEYWPSKQAQdYGDITVAMTSEIVLPEWTIRDFTVKniQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 229
Cdd:cd14612  97 KKEKCVHYWPEKEGT-YGRFEIRVQDMKECDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEE 173

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2NZ6_A      230 YMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 296
Cdd:cd14612 174 SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 69-300 3.30e-66

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: 208.53  E-value: 3.30e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       69 ENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCV 147
Cdd:cd14603  29 ENVKKNRYKDILPYDQTRVILSlLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREI 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      148 EQGRTKCEEYWPSKQAQ-DYGDITVAMTSEIVL-PEWTIRDFTVKNIQtsESHPLRQFHFTSWPDHGVPDTTDLLINFRY 225
Cdd:cd14603 109 EMGKKKCERYWAQEQEPlQTGPFTITLVKEKRLnEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPDSPDCMLAMIE 186

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2NZ6_A      226 LVRDYMKQSPpeSPILVHSSAGVGRTGTFIAID---RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 300
Cdd:cd14603 187 LARRLQGSGP--EPLCVHCSAGCGRTGVICTVDyvrQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTV 262
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 98-301 5.36e-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: 203.71  E-value: 5.36e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       98 DYINANY----MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPS-KQAQDYGDITVA 172
Cdd:cd14541   1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      173 MTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRdyMKQSPPESPILVHSSAGVGRTG 252
Cdd:cd14541  81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR--QNRVGMVEPTVVHCSAGIGRTG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
2NZ6_A      253 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 301
Cdd:cd14541 159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 75-300 1.01e-64

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: 203.74  E-value: 1.01e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       75 RYNNVLPYDISRVKLSVQT-HSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTK 153
Cdd:cd14623   1 RVLQIIPYEFNRVIIPVKRgEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      154 CEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 233
Cdd:cd14623  81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2NZ6_A      234 SpPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 300
Cdd:cd14623 161 S-GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 69-304 3.52e-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: 202.37  E-value: 3.52e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       69 ENRGKNRYNNVLPYDISRVKLSVQthstDDYINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKC 146
Cdd:cd14597   2 ENRKKNRYKNILPYDTTRVPLGDE----GGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      147 VEQGRTKCEEYWP-----SKQAQDYGDITVAMTSEivLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLI 221
Cdd:cd14597  78 VEGGKIKCQRYWPeilgkTTMVDNRLQLTLVRMQQ--LKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      222 NFrylvRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 301
Cdd:cd14597 156 TF----ISYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231


                ...
2NZ6_A      302 DIV 304
Cdd:cd14597 232 YVL 234
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 98-302 5.69e-64

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: 201.00  E-value: 5.69e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       98 DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEI 177
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      178 VLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSpPESPILVHSSAGVGRTGTFIAI 257
Cdd:cd14622  81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT-GNHPIVVHCSAGAGRTGTFIAL 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
2NZ6_A      258 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14622 160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 99-298 7.55e-64

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: 200.52  E-value: 7.55e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIV 178
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      179 LPEWTIRDFTVKNIQ--TSESHP--LRQFHFTSWPDHGVPDTTDLLINFRYLVrdyMKQSPPES-PILVHSSAGVGRTGT 253
Cdd:cd14551  81 LVDYTTRKFCIQKVNrgIGEKRVrlVTQFHFTSWPDFGVPFTPIGMLKFLKKV---KSANPPRAgPIVVHCSAGVGRTGT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
2NZ6_A      254 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:cd14551 158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 73-303 2.02e-63

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: 200.45  E-value: 2.02e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       73 KNRYNNVLPYDISRVKLSVQTHSTD-DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGR 151
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDsDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      152 TKCEEYW--PSKQAQDYGDITVAMTSEIVLPEWTIRdfTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 229
Cdd:cd14602  81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2NZ6_A      230 YmkQSPPESPILVHSSAGVGRTGTFIAID---RLIYQ-IENENtVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDI 303
Cdd:cd14602 159 Y--QEDDSVPICIHCSAGCGRTGVICAIDytwMLLKDgIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 64-295 1.92e-62

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: 199.49  E-value: 1.92e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       64 AAELAENRGKNRYNNVLPYDISRVKLSVQTH-STDDYINAN-------YMPGYhskkdfIATQGPLPNTLKDFWRMVWEK 135
Cdd:cd14609  36 TAQGEANVKKNRNPDFVPYDHARIKLKAESNpSRSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWEN 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      136 NVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSE-IVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVP 214
Cdd:cd14609 110 GCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEhIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIP 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      215 DTTDLLINFRYLV-RDYMKQSppeSPILVHSSAGVGRTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQ 292
Cdd:cd14609 190 SSTRPLLDFRRKVnKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQ 266


                ...
2NZ6_A      293 YVF 295
Cdd:cd14609 267 FEF 269
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 91-302 2.72e-62

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: 197.17  E-value: 2.72e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       91 VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPsKQAQDYGDIT 170
Cdd:cd14631   7 VEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      171 VAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQSPPESPILVHSSAGVGR 250
Cdd:cd14631  86 VTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSF--IRRVKLSNPPSAGPIVVHCSAGAGR 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
2NZ6_A      251 TGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14631 164 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 69-300 1.90e-61

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: 196.01  E-value: 1.90e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       69 ENRGKNRYNNVLPYDISRVKLsvqtHSTD------DYINANY-MPGYHS-------KKDFIATQGPLPNTLKDFWRMVWE 134
Cdd:cd14605   1 ENKNKNRYKNILPFDHTRVVL----HDGDpnepvsDYINANIiMPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      135 KNVYAIIMLTKCVEQGRTKCEEYWPSKQA-QDYGDITVAMTSEIVLPEWTIRDFTVKNI-QTSESHPLRQFHFTSWPDHG 212
Cdd:cd14605  77 ENSRVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      213 VPDTTDLLINFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENT---VDVYGIVYDLRMHRPLMVQT 289
Cdd:cd14605 157 VPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQT 236

                       250
                ....*....|.
2NZ6_A      290 EDQYVFLNQCV 300
Cdd:cd14605 237 EAQYRFIYMAV 247
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 73-298 2.38e-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: 194.75  E-value: 2.38e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       73 KNRYNNVLPYDISRVKLSVQ--THSTDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQ 149
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKnsNDSLSTYINANYIRGYGGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      150 GRtKCEEYWPSKQAQdYGDITVAMTSEIVLPEWTIRDFTVKniQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 229
Cdd:cd14611  82 NE-KCVLYWPEKRGI-YGKVEVLVNSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2NZ6_A      230 YMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:cd14611 158 DRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 50-295 4.85e-61

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: 195.18  E-value: 4.85e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       50 YEDLKLVGISQPKYAAELAENRGKNRYNNVLPYDISRVKLSvqtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFW 129
Cdd:cd14607   4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ---NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      130 RMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQD--YGD--ITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHF 205
Cdd:cd14607  81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      206 TSWPDHGVPDTTDLLINFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR 283
Cdd:cd14607 161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYR 240

                       250
                ....*....|..
2NZ6_A      284 PLMVQTEDQYVF 295
Cdd:cd14607 241 MGLIQTPDQLRF 252
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 65-295 1.17e-60

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: 194.89  E-value: 1.17e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       65 AELAENRGKNRYNNVLPYDISRVKLSVQ-THSTDDYINANYMPGYHSKKD-FIATQGPLPNTLKDFWRMVWEKNVYAIIM 142
Cdd:cd14610  39 AQREENVQKNRSLAVLPYDHSRIILKAEnSHSHSDYINASPIMDHDPRNPaYIATQGPLPATVADFWQMVWESGCVVIVM 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      143 LTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSE-IVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLI 221
Cdd:cd14610 119 LTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEhIWCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLL 198

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2NZ6_A      222 NFRYLVRD-YMKQSppeSPILVHSSAGVGRTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 295
Cdd:cd14610 199 DFRRKVNKcYRGRS---CPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 99-296 7.91e-59

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: 187.60  E-value: 7.91e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQaQDYGDITVAMTSEIV 178
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEK-KTYGDIEVELKDTEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      179 LPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPPES----PILVHSSAGVGRTGTF 254
Cdd:cd14558  80 SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHgrsvPIVVHCSDGSSRTGIF 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
2NZ6_A      255 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 296
Cdd:cd14558 160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFL 201
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 98-305 3.16e-58

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: 186.30  E-value: 3.16e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       98 DYINANYM----PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQ-DYGDITVA 172
Cdd:cd14601   1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSsSYGGFQVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      173 MTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDymKQSPPESPILVHSSAGVGRTG 252
Cdd:cd14601  81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRTG 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
2NZ6_A      253 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIVR 305
Cdd:cd14601 159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 73-297 2.20e-57

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: 185.84  E-value: 2.20e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       73 KNRYNNVLPYDISRVKLSvqTHSTDD----YINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKcV 147
Cdd:cd14613  28 KNRYKTILPNPHSRVCLT--SPDQDDplssYINANYIRGYGGEeKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN-I 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      148 EQGRTKCEEYWPSKQAQdYGDITVAMTSEIVLPEWTIRDFTVKNiqTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLV 227
Cdd:cd14613 105 EEMNEKCTEYWPEEQVT-YEGIEITVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEV 181

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2NZ6_A      228 RDYMKQSPPE-SPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 297
Cdd:cd14613 182 EEARQQAEPNcGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 69-306 3.79e-57

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: 185.47  E-value: 3.79e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       69 ENRGKNRYNNVLPYDISRVKLSVQTHST--DDYINANY-----MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAII 141
Cdd:cd14606  17 ENKSKNRYKNILPFDHSRVILQGRDSNIpgSDYINANYvknqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      142 MLTKCVEQGRTKCEEYWPSKQAQ-DYGDITVAMTSEIVLPEWTIRDFTVKNIQTSES-HPLRQFHFTSWPDHGVPDTTDL 219
Cdd:cd14606  97 MTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPGG 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      220 LINFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENT---VDVYGIVYDLRMHRPLMVQTEDQYVFL 296
Cdd:cd14606 177 VLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFI 256

                       250
                ....*....|
2NZ6_A      297 NQCVLDIVRS 306
Cdd:cd14606 257 YVAIAQFIET 266
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 99-305 3.16e-55

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: 178.40  E-value: 3.16e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPS--KQAQDYGDITVAMT 174
Cdd:cd14596   1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlQEPMELENYQLRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      175 SEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRdYMKQSPPESPILVHSSAGVGRTGTF 254
Cdd:cd14596  81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKF---IC-YMRKVHNTGPIVVHCSAGIGRAGVL 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
2NZ6_A      255 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIVR 305
Cdd:cd14596 157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 99-300 3.07e-54

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: 176.10  E-value: 3.07e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANY-------MPGYhskkdfIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITV 171
Cdd:cd14546   1 YINASTiydhdprNPAY------IATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      172 AMTSE-IVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLV-RDYMKQSppeSPILVHSSAGVG 249
Cdd:cd14546  75 HLVSEhIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
2NZ6_A      250 RTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 300
Cdd:cd14546 152 RTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 99-295 5.88e-52

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: 169.87  E-value: 5.88e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGY-HSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTS 175
Cdd:cd14539   1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      176 EIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD-YMKQSPPESPILVHSSAGVGRTGTF 254
Cdd:cd14539  81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShYLQQRSLQTPIVVHCSSGVGRTGAF 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
2NZ6_A      255 IAIDRLIYQIENEN-TVDVYGIVYDLRMHRPLMVQTEDQYVF 295
Cdd:cd14539 161 CLLYAAVQEIEAGNgIPDLPQLVRKMRQQRKYMLQEKEHLKF 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 99-296 1.46e-51

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: 168.74  E-value: 1.46e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKcVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIV 178
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      179 LPEWTIRDFTVKNI-QTSESHPL-RQFHFTSWPDHG-VPDTTDLLINFRYLVRDYMKQSpPESPILVHSSAGVGRTGTFI 255
Cdd:cd14556  80 DEDVISRIFRLQNTtRPQEGYRMvQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQS-GEGPIVVHCLNGVGRSGVFC 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
2NZ6_A      256 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 296
Cdd:cd14556 159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFC 199
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 99-301 2.48e-51

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: 168.79  E-value: 2.48e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPS----KQAQDYGDITVA 172
Cdd:cd14540   1 YINASHitATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggeHDALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      173 MTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINF--------RYLVRDYMKQSPPeSPILVHS 244
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvrRHTNQDVAGHNRN-PPTLVHC 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
2NZ6_A      245 SAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 301
Cdd:cd14540 160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 65-305 4.66e-49

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: 165.17  E-value: 4.66e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       65 AELAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKD--FIATQGPLPNTLKDFWRMVWEKNVYAIIM 142
Cdd:cd14599  33 ATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      143 LTKCVEQGRTKCEEYWP---SKQ-AQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTD 218
Cdd:cd14599 113 VTAEEEGGRSKSHRYWPklgSKHsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQ 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      219 LLINFRYLVRDYMKQSPPES--------PILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTE 290
Cdd:cd14599 193 GFLSYLEEIQSVRRHTNSMLdstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTI 272

                       250
                ....*....|....*
2NZ6_A      291 DQYVFLNQCVLDIVR 305
Cdd:cd14599 273 AQYKFVYQVLIQFLK 287
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 99-295 3.86e-48

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 160.32  E-value: 3.86e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYM--PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRT-KCEEYWPSK--QAQDYGDITVAM 173
Cdd:cd17658   1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      174 ----TSEIVLpewTIRDFTVKNIQTSEShPLRQFH--FTSWPDHGVPDTTDLLinfRYLVRDYMKQSPPESPILVHSSAG 247
Cdd:cd17658  81 kklkHSQHSI---TLRVLEVQYIESEEP-PLSVLHiqYPEWPDHGVPKDTRSV---RELLKRLYGIPPSAGPIVVHCSAG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
2NZ6_A      248 VGRTGTFIAIDRLIYQI--ENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 295
Cdd:cd17658 154 IGRTGAYCTIHNTIRRIleGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
66-296 7.89e-47

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.10  E-value: 7.89e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       66 ELAENRGKNRYNNVLPYDISRVKlsvqthSTDDYINANYMPGYhSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTK 145
Cdd:COG5599  38 QNINGSPLNRFRDIQPYKETALR------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      146 CVE--QGRTKCEEYWPskQAQDYG--DITVAMTSEIVL-PEWTIRDFTVKNIQTS-ESHPLRQFHFTSWPDHGVPDTTdL 219
Cdd:COG5599 111 DDEisKPKVKMPVYFR--QDGEYGkyEVSSELTESIQLrDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAISAE-A 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      220 LINFRYLVRDYMK-QSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR-PLMVQTEDQYVF 295
Cdd:COG5599 188 LKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDV 267


                .
2NZ6_A      296 L 296
Cdd:COG5599 268 L 268
PHA02738 PHA02738
hypothetical protein; Provisional
 63-295 7.24e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 157.78  E-value: 7.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A        63 YAAELAeNRGKNRYNNVLPYDISRVKLSVQtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIM 142
Cdd:PHA02738  43 FNAEKK-NRKLNRYLDAVCFDHSRVILPAE-RNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVM 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       143 LTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEIVLPEWtIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLL 220
Cdd:PHA02738 121 LCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHY-VKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEF 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       221 INFRYLVRDYMKQSPPES-----------PILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQT 289
Cdd:PHA02738 200 LNFVLEVRQCQKELAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFI 279


                 ....*.
2NZ6_A       290 EDQYVF 295
Cdd:PHA02738 280 PFQYFF 285
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 69-296 5.08e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 155.54  E-value: 5.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A        69 ENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIML--TKC 146
Cdd:PHA02747  50 ENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLtpTKG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       147 VeQGRTKCEEYW-PSKQAQ-DYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFR 224
Cdd:PHA02747 130 T-NGEEKCYQYWcLNEDGNiDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFI 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       225 YLV----RDYMKQSPPE----SPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 296
Cdd:PHA02747 209 KIIdinrKKSGKLFNPKdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFI 288
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 69-301 5.08e-44

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 152.46  E-value: 5.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A        69 ENRGKNRYNNVLPYDISRVKLSVQThSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVE 148
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILKIED-GGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       149 QGRTKCEEYWPSKQAQD--YGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 226
Cdd:PHA02742 130 DGKEACYPYWMPHERGKatHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       227 VRDYM---------KQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 297
Cdd:PHA02742 210 VREADlkadvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                 ....
2NZ6_A       298 QCVL 301
Cdd:PHA02742 290 FIVL 293
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 99-296 7.07e-44

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: 149.01  E-value: 7.07e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCveQGRTKCEEYWPSK-QAQDYGDITVAMTSEI 177
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN--ELNEDEPIYWPTKeKPLECETFKVTLSGED 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      178 VLPEW-----TIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLliNFRYLVRDYMKQSppESPILVHSSAGVGRTG 252
Cdd:cd14550  79 HSCLSneirlIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVF--ELINTVQEWAQQR--DGPIVVHDRYGGVQAA 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
2NZ6_A      253 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 296
Cdd:cd14550 155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
199-302 1.34e-41

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 139.80  E-value: 1.34e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A         199 PLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENE-NTVDVYGIVY 277
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
2NZ6_A         278 DLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 199-302 1.34e-41

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: 139.80  E-value: 1.34e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A         199 PLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENE-NTVDVYGIVY 277
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
2NZ6_A         278 DLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 99-305 1.39e-38

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: 135.87  E-value: 1.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKK--DFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQD----YG--DIT 170
Cdd:cd14598   1 YINASHIKVTVGGKewDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGrfKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      171 VAMTSEIVLpeWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDttDLLINFRYL-----VRDYMKQS----PPESPIL 241
Cdd:cd14598  81 TRFRTDSGC--YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPE--DLKGFLSYLeeiqsVRRHTNSTidpkSPNPPVL 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
2NZ6_A      242 VHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIVR 305
Cdd:cd14598 157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 69-295 2.84e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 137.85  E-value: 2.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A        69 ENRGKNRYNNVLPYDISRVKLSVQTHST--------------------DDYINANYMPGYHSKKDFIATQGPLPNTLKDF 128
Cdd:PHA02746  50 ENLKKNRFHDIPCWDHSRVVINAHESLKmfdvgdsdgkkievtsednaENYIHANFVDGFKEANKFICAQGPKEDTSEDF 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       129 WRMVWEKNVYAIIMLTKcVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFT 206
Cdd:PHA02746 130 FKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSElaFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFP 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       207 SWPDHGVPDTTDLLINFRYLVRDYMK--------QSPPESPILVHSSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYD 278
Cdd:PHA02746 209 DWPDNGIPTGMAEFLELINKVNEEQAelikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLK 288

                        250
                 ....*....|....*..
2NZ6_A       279 LRMHRPLMVQTEDQYVF 295
Cdd:PHA02746 289 IRKQRHSSVFLPEQYAF 305
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 99-301 1.10e-34

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: 125.11  E-value: 1.10e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCeEYWPSK-QAQDYGDITVAMTSEI 177
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKdEPINCETFKVTLIAEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      178 VL-----PEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVP-DTTDLLINfryLVRDymKQSPPESPILVHSSAGVGRT 251
Cdd:cd17669  80 HKclsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELIS---IIKE--EAANRDGPMIVHDEHGGVTA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
2NZ6_A      252 GTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 301
Cdd:cd17669 155 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 99-301 1.81e-34

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: 124.79  E-value: 1.81e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKcvEQGRTKCEE-YWPSK-QAQDYGDITVAMTSE 176
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSReESMNCEAFTVTLISK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      177 IVL-----PEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVP-DTTDLLINF---RYLVRDymkqsppeSPILVHSSAG 247
Cdd:cd17670  79 DRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVikeEALTRD--------GPTIVHDEFG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
2NZ6_A      248 VGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 301
Cdd:cd17670 151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 99-302 5.82e-33

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 120.78  E-value: 5.82e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRT-KCEEYWPSKQAQDYGDITVAMTSEI 177
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      178 VLPEWTIRDFTVKNI-QTSESHPL-RQFHFTSW-PDHGVPDTTDLLINFRYLVRDYMKQSpPESPILVHSSAGVGRTGTF 254
Cdd:cd14637  81 ADEDIVTRLFRVQNItRLQEGHLMvRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRES-GEGRTVVHCLNGGGRSGTY 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
2NZ6_A      255 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14637 160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 99-302 7.20e-33

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 120.51  E-value: 7.20e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTkcvEQGRTK-CEEYWPSKQAQDYGDITVAMTSEI 177
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWPEKTSCCYGPIQVEFVSAD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      178 VLPEWTIRDFTVKNIQTSES--HPLRQFHFTSWPDH--GVPDTTDLLINFRYLVRDYMKQSPPESPILVHSSAGVGRTGT 253
Cdd:cd14634  78 IDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrdTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
2NZ6_A      254 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14634 158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 99-295 6.45e-30

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 112.81  E-value: 6.45e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKC-VEQGrtkCEEYWPSKQAQDYGDITVAMTSEI 177
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      178 VLPEWTIRDFTVKNIQTSESHPL--RQFHFTSWPDH-GVPDTTDLLINFRYLVRDYMKQSPP-ESPILVHSSAGVGRTGT 253
Cdd:cd14636  78 MDCDVISRIFRICNLTRPQEGYLmvQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgEGRTIIHCLNGGGRSGM 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
2NZ6_A      254 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 295
Cdd:cd14636 158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 99-302 7.72e-28

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: 107.47  E-value: 7.72e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       99 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKcVEQGRTkCEEYWPSKQAQDYGDITVAMTSEIV 178
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWPENGVHRHGPIQVEFVSADL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      179 LPEWTIRDFTVKNIQTSES--HPLRQFHFTSWPDHgvPDTTDLLINFRYLVRDYMKQSPP----ESPILVHSSAGVGRTG 252
Cdd:cd14635  79 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMY--RDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGGRSG 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
2NZ6_A      253 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 302
Cdd:cd14635 157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 74-296 1.98e-17

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: 79.75  E-value: 1.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       74 NRYNNVLpydiSRVKLSVQTHstddyINANYMPgYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTK 153
Cdd:cd14559   1 NRFTNIQ----TRVSTPVGKN-----LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKG 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      154 CEEYWpsKQAQDYGDITVamTSEIVLPEWTIRDFTVK--NIQTSES---HPLRQFHFTSWPDHGVPDTTDLL-------- 220
Cdd:cd14559  71 LPPYF--RQSGTYGSVTV--KSKKTGKDELVDGLKADmyNLKITDGnktITIPVVHVTNWPDHTAISSEGLKeladlvnk 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      221 -----INFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIdrlIYQIENENTVDVYGIVYDLRMHR-PLMVQTEDQYV 294
Cdd:cd14559 147 saeekRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLAAA---MELNKSPNNLSVEDIVSDMRTSRnGKMVQKDEQLD 223


                ..
2NZ6_A      295 FL 296
Cdd:cd14559 224 TL 225
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 26-298 2.21e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 66.53  E-value: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A        26 IRVENFEAYFKKqqADSNCGFAEEYEDLKLVGISQPKYAAELAENRGKNRyNNVLP---YDISRVKLsvqtHSTDDYINA 102
Cdd:PHA02740   9 INGMDFINFINK--PDLLSCIIKEYRAIVPEHEDEANKACAQAENKAKDE-NLALHitrLLHRRIKL----FNDEKVLDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       103 NYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQgrtKC-EEYWPSKQ--AQDYGDITVAMTSEIVL 179
Cdd:PHA02740  82 RFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEgcVITSDKFQIETLEIIIK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A       180 PEWTIRDFTVKNiQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPPES------PILVHSSAGVGRTGT 253
Cdd:PHA02740 159 PHFNLTLLSLTD-KFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHKadgkiaPIIIDCIDGISSSAV 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
2NZ6_A       254 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:PHA02740 238 FCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYH 282
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
191-298 5.36e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 48.04  E-value: 5.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      191 NIQTSESHPLRQFHFTsWPDHGVPDTTDllinFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDrLIYQ-IENENT 269
Cdd:COG2453  39 LLGLLEEAGLEYLHLP-IPDFGAPDDEQ----LQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAY-LVLLgLSAEEA 112

                        90       100
                ....*....|....*....|....*....
2NZ6_A      270 VDVygivydLRMHRPLMVQTEDQYVFLNQ 298
Cdd:COG2453 113 LAR------VRAARPGAVETPAQRAFLER 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 222-296 1.09e-06

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: 46.57  E-value: 1.09e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2NZ6_A      222 NFRYLVRDYMKQSPPESPILVHSSAGVGRTGTFIAIDRLIYQieNENTVDVYGIVYDLRMHRplMVQTEDQYVFL 296
Cdd:cd14494  41 MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEAVRIVRLIRPGG--IPQTIEQLDFL 111
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 208-256 1.66e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 38.33  E-value: 1.66e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
2NZ6_A      208 WPDHGVPdTTDLLINFRYLVRDYMKQSPpESPILVHSSAGVGRTGTFIA 256
Cdd:cd14497  68 FPDHHPP-PLGLLLEIVDDIDSWLSEDP-NNVAVVHCKAGKGRTGTVIC 114
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 203-296 2.18e-03

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: 38.48  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      203 FHFTSWPDHGVPDTTDLLINFRylVRDYMKQSppESPILVHSSAGVGRTGTFIAIdRLIYqIENENTVDVYGIVydlRMH 282
Cdd:cd14506  79 FYNFGWKDYGVPSLTTILDIVK--VMAFALQE--GGKVAVHCHAGLGRTGVLIAC-YLVY-ALRMSADQAIRLV---RSK 149

                        90
                ....*....|....
2NZ6_A      283 RPLMVQTEDQYVFL 296
Cdd:cd14506 150 RPNSIQTRGQVLCV 163
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 196-298 2.87e-03

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: 37.63  E-value: 2.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2NZ6_A      196 ESHPLRQFHFtSWPDHGVPDTTD----LLINFRYLVRDYMKqsppespILVHSSAGVGRTGTFIAidRLIYQIENENTVD 271
Cdd:cd14505  69 QQAGITWHHL-PIPDGGVPSDIAqwqeLLEELLSALENGKK-------VLIHCKGGLGRTGLIAA--CLLLELGDTLDPE 138

                        90       100
                ....*....|....*....|....*..
2NZ6_A      272 VygIVYDLRMHRPLMVQTEDQYVFLNQ 298
Cdd:cd14505 139 Q--AIAAVRALRPGAIQTPKQENFLHQ 163
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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