NCBI Conserved Domain Search

Conserved domains on [gi|196114970|ref|NP_001124481|]

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tyrosine-protein phosphatase non-receptor type 12 isoform 3 [Homo sapiens]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

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

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

PTP_DSP_cys super family

cl28904

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

1-168

1.18e-137

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.

The actual alignment was detected with superfamily member cd14604:

Pssm-ID: 475123 [Multi-domain] Cd Length: 297 Bit Score: 404.31 E-value: 1.18e-137

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSIL 80
Cdd:cd14604  130 MACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSIL 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  81 DMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 160
Cdd:cd14604  210 DMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289


                 ....*...
gi 196114970 161 AQLFEKQL 168
Cdd:cd14604  290 AQLFEKQL 297

Name

Accession

Description

Interval

E-value

PTPc-N12

cd14604

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

1-168

1.18e-137

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: 404.31 E-value: 1.18e-137

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSIL 80
Cdd:cd14604  130 MACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSIL 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  81 DMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 160
Cdd:cd14604  210 DMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289


                 ....*...
gi 196114970 161 AQLFEKQL 168
Cdd:cd14604  290 AQLFEKQL 297

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1-162

1.83e-63

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 210.59 E-value: 1.83e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970     1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:smart00194  99 MLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRTVTHYHYTNWPDHGVPESPES 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970    79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:smart00194 179 ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEIVKELRSQRPGMVQTEEQYIFLYR 255


                   ....
gi 196114970   159 AIAQ 162
Cdd:smart00194 256 AILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1-162

5.10e-62

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 205.94 E-value: 5.10e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970    1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQART-DYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFD 77
Cdd:pfam00102  72 MLTELEEKGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   78 SILDMISLMRKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELV 156
Cdd:pfam00102 152 SLLDLLRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                  ....*.
gi 196114970  157 HRAIAQ 162
Cdd:pfam00102 229 YDAILE 234

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

2-162

7.51e-21

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 93.23 E-value: 7.51e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   2 ACREFEMGRKKCERYWPLYGEdpitFAPFKISCE---DEQARTDYFIRTLLLEFQN---ESRRLYQFHYVNWPDHDVPSS 75
Cdd:COG5599  110 SDDEISKPKVKMPVYFRQDGE----YGKYEVSSElteSIQLRDGIEARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISA 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  76 fDSILDMISLMRKYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQEMRTQR-HSAVQTKE 151
Cdd:COG5599  186 -EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSE 263

                        170
                 ....*....|..
gi 196114970 152 QY-ELVHRAIAQ 162
Cdd:COG5599  264 QLdVLVKLAEQQ 275

PHA02747

protein tyrosine phosphatase; Provisional

9-157

1.29e-17

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 84.28 E-value: 1.29e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   9 GRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYfIRTLLL---EFQNESRRLYQFHYVNWPDHDVPSS---FDSILDM 82
Cdd:PHA02747 132 GEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKY-ILTLIEitdKILKDSRKISHFQCSEWFEDETPSDhpdFIKFIKI 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  83 ISLMRK-------YQEHEDVPICIHCSAGCGRTGAICAIDYTWN-LLKAGKIPEEFNVFNLiqemRTQRHSAVQTKEQYE 154
Cdd:PHA02747 211 IDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNqLVKRKAICLAKTAEKI----REQRHAGIMNFDDYL 286


                 ...
gi 196114970 155 LVH 157
Cdd:PHA02747 287 FIQ 289

Name

Accession

Description

Interval

E-value

PTPc-N12

cd14604

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

1-168

1.18e-137

Pssm-ID: 350452 [Multi-domain] Cd Length: 297 Bit Score: 404.31 E-value: 1.18e-137

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSIL 80
Cdd:cd14604  130 MACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSIL 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  81 DMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 160
Cdd:cd14604  210 DMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289


                 ....*...
gi 196114970 161 AQLFEKQL 168
Cdd:cd14604  290 AQLFEKQL 297

PTPc-N22_18_12

cd14542

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

1-158

1.75e-109

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: 328.23 E-value: 1.75e-109

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQART-DYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSI 79
Cdd:cd14542   44 MACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKEKRVGpDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPI 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 196114970  80 LDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14542  124 LDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDYVWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

PTPc-N22

cd14602

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

1-164

6.75e-94

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: 289.43 E-value: 6.75e-94

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSIL 80
Cdd:cd14602   71 MACMEFEMGKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPIL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  81 DMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 160
Cdd:cd14602  151 ELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230


                 ....
gi 196114970 161 AQLF 164
Cdd:cd14602  231 IELF 234

PTPc-N18

cd14603

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

1-164

5.12e-75

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: 241.27 E-value: 5.12e-75

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYgEDPITFAPFKIS-CEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSI 79
Cdd:cd14603  103 MACREIEMGKKKCERYWAQE-QEPLQTGPFTITlVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCM 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  80 LDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRA 159
Cdd:cd14603  182 LAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHT 261


                 ....*
gi 196114970 160 IAQLF 164
Cdd:cd14603  262 VAQMF 266

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1-162

1.83e-63

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 210.59 E-value: 1.83e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970     1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:smart00194  99 MLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRTVTHYHYTNWPDHGVPESPES 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970    79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:smart00194 179 ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEIVKELRSQRPGMVQTEEQYIFLYR 255


                   ....
gi 196114970   159 AIAQ 162
Cdd:smart00194 256 AILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1-162

5.10e-62

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 205.94 E-value: 5.10e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970    1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQART-DYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFD 77
Cdd:pfam00102  72 MLTELEEKGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   78 SILDMISLMRKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELV 156
Cdd:pfam00102 152 SLLDLLRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                  ....*.
gi 196114970  157 HRAIAQ 162
Cdd:pfam00102 229 YDAILE 234

PTPc

cd00047

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

1-158

3.11e-56

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: 189.42 E-value: 3.11e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQN--ESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd00047   44 MLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSEEELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPED 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd00047  124 LLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEG---EVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

PTP_fungal

cd18533

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

4-157

2.45e-41

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: 149.32 E-value: 2.45e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   4 REFEMGRKKCERYWPlYGEDPITFAPFKISC--EDEQARTDYFIRTLLLEF-QNESRRLYQFHYVNWPDHDVPSSFDSIL 80
Cdd:cd18533   48 PLVENGREKCDQYWP-SGEYEGEYGDLTVELvsEEENDDGGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  81 DMISLMRK--YQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFN------VFNLIQEMRTQRHSAVQTKEQ 152
Cdd:cd18533  127 TLIKLKRElnDSASLDPPIIVHCSAGVGRTGTFIALDSLLDELKRGLSDSQDLedsedpVYEIVNQLRKQRMSMVQTLRQ 206


                 ....*
gi 196114970 153 YELVH 157
Cdd:cd18533  207 YIFLY 211

PTPc-N20_13

cd14538

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

1-162

1.61e-37

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: 138.66 E-value: 1.61e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITF-APFKISCEDEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFD 77
Cdd:cd14538   46 MVTQDVEGGKVKCHRYWPDSLNKPLICgGRLEVSLEKYQSLQDFVIRRISLRDKetGEVHHITHLNFTTWPDHGTPQSAD 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  78 SILDMISLMRKYqeHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14538  126 PLLRFIRYMRRI--HNSGPIVVHCSAGIGRTGVLITIDVALGLIERDL---PFDIQDIVKDLREQRQGMIQTKDQYIFCY 200


                 ....*
gi 196114970 158 RAIAQ 162
Cdd:cd14538  201 KACLE 205

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

59-162

1.27e-36

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 132.48 E-value: 1.27e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970    59 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLI 136
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 196114970   137 QEMRTQRHSAVQTKEQYELVHRAIAQ 162
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRALLE 105

PTPc_DSPc

smart00012

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

59-162

1.27e-36

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

Pssm-ID: 214469 [Multi-domain] Cd Length: 105 Bit Score: 132.48 E-value: 1.27e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970    59 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLI 136
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 196114970   137 QEMRTQRHSAVQTKEQYELVHRAIAQ 162
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRALLE 105

R3-PTPc

cd14548

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

1-157

3.95e-36

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: 135.17 E-value: 3.95e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPlYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSIL 80
Cdd:cd14548   69 MLTQCMEKGRVKCDHYWP-FDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLL 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 196114970  81 DMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14548  148 RFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDR---LLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221

R5-PTPc-1

cd14549

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

7-157

4.97e-35

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: 131.70 E-value: 4.97e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLYGEDpiTFAPFKISCEDEQARTDYFIRTLLL--------EFQNESRRLYQFHYVNWPDHDVPssfDS 78
Cdd:cd14549   50 ERGRRKCDQYWPKEGTE--TYGNIQVTLLSTEVLATYTVRTFSLknlklkkvKGRSSERVVYQYHYTQWPDHGVP---DY 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRK---YQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYEL 155
Cdd:cd14549  125 TLPVLSFVRKssaANPPGAGPIVVHCSAGVGRTGTYIVID---SMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201


                 ..
gi 196114970 156 VH 157
Cdd:cd14549  202 IH 203

PTPc-N11_6

cd14544

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

1-165

5.64e-35

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: 132.97 E-value: 5.64e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPiTFAPFKISCEDEQARTDYFIRTLLL---EFQNESRRLYQFHYVNWPDHDVPSSFD 77
Cdd:cd14544   82 MTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELQVsklDQGDPIREIWHYQYLSWPDHGVPSDPG 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  78 SILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYEL 155
Cdd:cd14544  161 GVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYKF 240

                        170
                 ....*....|
gi 196114970 156 VHRAIAQLFE 165
Cdd:cd14544  241 IYVAVAQYIE 250

PTPc-N9

cd14543

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

1-157

5.94e-34

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: 130.56 E-value: 5.94e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14543  102 MTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVTHFQFTSWPDFGVPSSAAA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQ-------------EHEDVPICIHCSAGCGRTGAICAIDYTWNLL-KAGKIpeefNVFNLIQEMRTQRH 144
Cdd:cd14543  182 LLDFLGEVRQQQalavkamgdrwkgHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLeDVGTL----NVMQTVRRMRTQRA 257

                        170
                 ....*....|...
gi 196114970 145 SAVQTKEQYELVH 157
Cdd:cd14543  258 FSIQTPDQYYFCY 270

PTPc-N20

cd14596

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

1-160

8.00e-33

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: 125.63 E-value: 8.00e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLeFQNES---RRLYQFHYVNWPDHDVPSSFD 77
Cdd:cd14596   46 MMTREVERGKVKCHRYWPETLQEPMELENYQLRLENYQALQYFIIRIIKL-VEKETgenRLIKHLQFTTWPDHGTPQSSD 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  78 SILDMISLMRKYqeHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14596  125 QLVKFICYMRKV--HNTGPIVVHCSAGIGRAGVLICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCY 199


                 ...
gi 196114970 158 RAI 160
Cdd:cd14596  200 KVV 202

PTPc-KIM

cd14547

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

6-158

1.91e-31

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: 122.12 E-value: 1.91e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   6 FEMGRKKCERYWPLygEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDM--- 82
Cdd:cd14547   75 LTEAKEKCAQYWPE--EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLvqe 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 196114970  83 ISLMRKYQEHEDvPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14547  153 VEEARQTEPHRG-PIVVHCSAGIGRTGCFIATSIGCQQLREeGVV----DVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

R-PTPc-typeIIb-1

cd14555

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

1-160

2.17e-31

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: 121.18 E-value: 2.17e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPlygEDPITFAPFKISCEDEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14555   44 MVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVETEPLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14555  121 LLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKELRSRRVNMVQTEEQYIFIHD 197


                 ..
gi 196114970 159 AI 160
Cdd:cd14555  198 AI 199

PTPc-N4

cd14601

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

1-166

3.53e-31

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: 120.82 E-value: 3.53e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPlYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14601   49 MLTTQVERGRVKCHQYWP-EPSGSSSYGGFQVTCHSEEGNPAYVFREMTLTNLekNESRPLTQIQYIAWPDHGVPDDSSD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14601  128 FLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVLITMETAMCLIECN---QPVYPLDIVRTMRDQRAMMIQTPSQYRFVCE 204


                 ....*...
gi 196114970 159 AIAQLFEK 166
Cdd:cd14601  205 AILKVYEE 212

R-PTPc-A-E-2

cd14552

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

7-160

5.66e-31

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: 120.07 E-value: 5.66e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLYGEdpITFAPFKISCEDEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDSILDMIS 84
Cdd:cd14552   50 ERSQNKCAQYWPEDGS--VSSGDITVELKDQTDYEDYTLRDFLVTKgkGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIA 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 196114970  85 LMRKYQEHE-DVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 160
Cdd:cd14552  128 AVQKQQQQSgNHPITVHCSAGAGRTGTFCALSTVLERVKAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

PTPc-N3_4

cd14541

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

7-166

8.73e-31

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: 119.74 E-value: 8.73e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLYGEDpITFAPFKISCEDEQARTDYFIRTLLLEFQN--ESRRLYQFHYVNWPDHDVPSSFDSILDMIS 84
Cdd:cd14541   55 ERGRVKCHQYWPDLGET-MQFGNLQITCVSEEVTPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVK 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  85 LMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLF 164
Cdd:cd14541  134 RVRQNRVGMVEPTVVHCSAGIGRTGVLITMETAMCLIEAN---EPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVY 210


                 ..
gi 196114970 165 EK 166
Cdd:cd14541  211 EE 212

R-PTP-N-N2

cd14546

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

1-162

1.65e-29

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: 116.00 E-value: 1.65e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWP-----LYGEDPITFAPFKISCEDeqartdYFIRTLLLE--FQNESRRLYQFHYVNWPDHDVP 73
Cdd:cd14546   45 MLTRLQENGVKQCARYWPeegseVYHIYEVHLVSEHIWCDD------YLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIP 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  74 SSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLIQEMRTQRHSAVQTKEQY 153
Cdd:cd14546  119 ASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILIDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQF 196


                 ....*....
gi 196114970 154 ELVHRAIAQ 162
Cdd:cd14546  197 EFVLTAVAE 205

R-PTPc-O

cd14614

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

7-160

1.68e-29

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: 117.30 E-value: 1.68e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPlYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPS--SFDSILDMIS 84
Cdd:cd14614   91 EKRRVKCDHYWP-FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTanAAESILQFVQ 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 196114970  85 LMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 160
Cdd:cd14614  170 MVRQQAVKSKGPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242

PTPc-N1_2

cd14545

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

1-152

3.12e-29

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: 115.95 E-value: 3.12e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITF--APFKISCEDEQARTDYFIRTLLLE--FQNESRRLYQFHYVNWPDHDVPSSF 76
Cdd:cd14545   69 MLNKLMEKGQIKCAQYWPQGEGNAMIFedTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESP 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  77 DSILDMISLMRkyqEH----EDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKiPEEFNVFNLIQEMRTQRHSAVQTKE 151
Cdd:cd14545  149 AAFLNFLQKVR---ESgslsSDVgPPVVHCSAGIGRSGTFCLVDTCLVLIEKGN-PSSVDVKKVLLEMRKYRMGLIQTPD 224


                 .
gi 196114970 152 Q 152
Cdd:cd14545  225 Q 225

PTPc-N13

cd14597

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

1-160

6.05e-29

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: 115.31 E-value: 6.05e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWP-LYGEDPITFAPFKISCEDEQARTDYFIRTLLLE--FQNESRRLYQFHYVNWPDHDVPSSFD 77
Cdd:cd14597   73 MMTQEVEGGKIKCQRYWPeILGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPE 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  78 SILDMISLMRKYqeHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14597  153 QLLTFISYMRHI--HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTEDQYIFCY 227


                 ...
gi 196114970 158 RAI 160
Cdd:cd14597  228 QVI 230

PTPc-N6

cd14606

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

1-165

6.78e-29

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: 116.13 E-value: 6.78e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPiTFAPFKISCEDEQARTDYFIRTLLLEFQNES---RRLYQFHYVNWPDHDVPSSFD 77
Cdd:cd14606   97 MTTREVEKGRNKCVPYWPEVGMQR-AYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGeliREIWHYQYLSWPDHGVPSEPG 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  78 SILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYEL 155
Cdd:cd14606  176 GVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKF 255

                        170
                 ....*....|
gi 196114970 156 VHRAIAQLFE 165
Cdd:cd14606  256 IYVAIAQFIE 265

R-PTPc-T-1

cd14630

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

1-162

7.03e-29

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: 115.12 E-value: 7.03e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPlygEDPITFAPFKISCEDEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14630   76 MVTNLVEVGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREIRQFHFTSWPDHGVPCYATG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14630  153 LLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMVQTEEQYVFVHD 229


                 ....
gi 196114970 159 AIAQ 162
Cdd:cd14630  230 AILE 233

R-PTPc-H

cd14619

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

7-160

9.83e-29

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: 114.60 E-value: 9.83e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLyGEDPITFAPFKISCEDEQARTDYFIRTLLLE--FQNESRRLYQFHYVNWPDHDVPSSFDSILDMIS 84
Cdd:cd14619   76 EAGRVKCEHYWPL-DYTPCTYGHLRVTVVSEEVMENWTVREFLLKqvEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRR 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 196114970  85 LMRKY--QEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 160
Cdd:cd14619  155 LLRQWldQTMSGGPTVVHCSAGVGRTGTLIALDV---LLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229

R-PTPc-K-1

cd14631

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

1-162

1.88e-28

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: 113.58 E-value: 1.88e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPlygEDPITFAPFKISCEDEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14631   58 MVTNLVEVGRVKCYKYWP---DDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14631  135 LLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIFIHD 211


                 ....
gi 196114970 159 AIAQ 162
Cdd:cd14631  212 AILE 215

R-PTPc-LAR-1

cd14553

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

1-160

2.13e-28

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: 113.65 E-value: 2.13e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDpiTFAPFKISCEDEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14553   76 MMTKLEERSRVKCDQYWPTRGTE--TYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVPEHPTP 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14553  154 FLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKT---VDIYGHVTCLRAQRNYMVQTEDQYIFIHD 230


                 ..
gi 196114970 159 AI 160
Cdd:cd14553  231 AL 232

PTPc-N21_14

cd14540

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

1-162

2.97e-27

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: 109.85 E-value: 2.97e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYG--EDPITFAPFKISCEDEQARTDYFIRTLLLEFQNE--SRRLYQFHYVNWPDHDVPSSF 76
Cdd:cd14540   46 MVTAEEEGGREKCFRYWPTLGgeHDALTFGEYKVSTKFSVSSGCYTTTGLRVKHTLSgqSRTVWHLQYTDWPDHGCPEDV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  77 DSILDMISLMRKYQEH--EDV-------PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAV 147
Cdd:cd14540  126 SGFLDFLEEINSVRRHtnQDVaghnrnpPTLVHCSAGVGRTGVVILADLMLYCLDHN---EELDIPRVLALLRHQRMLLV 202

                        170
                 ....*....|....*
gi 196114970 148 QTKEQYELVHRAIAQ 162
Cdd:cd14540  203 QTLAQYKFVYNVLIQ 217

PTPc-N11

cd14605

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

1-165

3.11e-27

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: 110.88 E-value: 3.11e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPlygeDPIT---FAPFKISCEDEQARTDYFIRTLLLEF---QNESRRLYQFHYVNWPDHDVPS 74
Cdd:cd14605   84 MTTKEVERGKSKCVKYWP----DEYAlkeYGVMRVRNVKESAAHDYILRELKLSKvgqGNTERTVWQYHFRTWPDHGVPS 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  75 SFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQ 152
Cdd:cd14605  160 DPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQ 239

                        170
                 ....*....|...
gi 196114970 153 YELVHRAIAQLFE 165
Cdd:cd14605  240 YRFIYMAVQHYIE 252

R-PTPc-A-2

cd14623

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

7-162

3.29e-27

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: 110.13 E-value: 3.29e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLYGEdpITFAPFKISCEDEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWPDHDVPSSFDSILDMIS 84
Cdd:cd14623   75 ERGQEKCAQYWPSDGS--VSYGDITIELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIA 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 196114970  85 LMRKYQEHE-DVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 162
Cdd:cd14623  153 AVQKQQQQSgNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

R-PTPc-J

cd14615

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

1-153

7.46e-27

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: 109.14 E-value: 7.46e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPlyGEDPITFAPFKISCEDEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14615   69 MLTKCVEQGRTKCEEYWP--SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNaqTNESRTVRHFHFTSWPDHGVPETTDL 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 196114970  79 ILDMISLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 153
Cdd:cd14615  147 LINFRHLVREYmkQNPPNSPILVHCSAGVGRTGTFIAID---RLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQY 220

R-PTPc-U-1

cd14632

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

1-162

1.59e-26

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: 107.44 E-value: 1.59e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPlygEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRR--LYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14632   44 MITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKTETLAEYSVRTFALERRGYSARheVKQFHFTSWPEHGVPYHATG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14632  121 LLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRINMIQTEEQYIFIHD 197


                 ....
gi 196114970 159 AIAQ 162
Cdd:cd14632  198 AILE 201

R-PTP-C-2

cd14558

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

7-154

9.07e-26

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: 105.17 E-value: 9.07e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWplyGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQN--ESRRLYQFHYVNWPDHDVPSSFDSILDMIS 84
Cdd:cd14558   50 EGDQEQCAQYW---GDEKKTYGDIEVELKDTEKSPTYTVRVFEITHLKrkDSRTVYQYQYHKWKGEELPEKPKDLVDMIK 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 196114970  85 LMRKYQE------HEDVPICIHCSAGCGRTGAICAIdytWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYE 154
Cdd:cd14558  127 SIKQKLPyknskhGRSVPIVVHCSDGSSRTGIFCAL---WNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQ 199

R-PTPc-Z-1

cd17668

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

7-160

1.13e-25

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: 105.06 E-value: 1.13e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLYGEDpiTFAPFKISCEDEQARTDYFIRTLLL----------EFQNESRRLYQFHYVNWPDHDVPssf 76
Cdd:cd17668   50 EKGRRKCDQYWPADGSE--EYGNFLVTQKSVQVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVP--- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  77 DSILDMISLMRKY---QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 153
Cdd:cd17668  125 EYTLPVLTFVRKAsyaKRHAVGPVVVHCSAGVGRTGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 201


                 ....*..
gi 196114970 154 ELVHRAI 160
Cdd:cd17668  202 VFIHDAL 208

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

1-159

1.72e-25

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: 105.30 E-value: 1.72e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPL--------YGEDPITfapfkiscedEQARTDYFIRtlllEFQ------NESRRLYQFHYVN 66
Cdd:cd14554   79 MLTKLREMGREKCHQYWPAersaryqyFVVDPMA----------EYNMPQYILR----EFKvtdardGQSRTVRQFQFTD 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  67 WPDHDVPSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRH 144
Cdd:cd14554  145 WPEQGVPKSGEGFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVFQTVKLLRTQRP 221

                        170
                 ....*....|....*
gi 196114970 145 SAVQTKEQYELVHRA 159
Cdd:cd14554  222 AMVQTEDQYQFCYRA 236

R-PTPc-E-2

cd14622

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

7-160

2.01e-25

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: 104.32 E-value: 2.01e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPlyGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNE--SRRLYQFHYVNWPDHDVPSSFDSILDMIS 84
Cdd:cd14622   51 EREQEKCVQYWP--SEGSVTHGEITIEIKNDTLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIA 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 196114970  85 LMRKYQEHE-DVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 160
Cdd:cd14622  129 AVQKQQQQTgNHPIVVHCSAGAGRTGTFIALS---NILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202

R-PTPc-Q

cd14616

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

1-158

2.26e-25

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: 104.60 E-value: 2.26e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPlygED--PIT-FAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFD 77
Cdd:cd14616   70 MLTQCFEKGRIRCHQYWP---EDnkPVTvFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSA 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  78 SILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14616  147 PLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDH---LTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223


                 .
gi 196114970 158 R 158
Cdd:cd14616  224 Q 224

R-PTP-N2

cd14610

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

7-162

2.39e-25

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: 106.29 E-value: 2.39e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLYGED-----PITFAPFKISCEDEQARTdYFIRTLLlefQNESRRLYQFHYVNWPDHDVPSSFDSILD 81
Cdd:cd14610  124 ENGVKQCYHYWPDEGSNlyhiyEVNLVSEHIWCEDFLVRS-FYLKNLQ---TNETRTVTQFHFLSWNDQGVPASTRSLLD 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  82 MISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNllKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIA 161
Cdd:cd14610  200 FRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLN--KMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVA 277


                 .
gi 196114970 162 Q 162
Cdd:cd14610  278 E 278

PTPc-N1

cd14608

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

1-162

4.54e-25

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: 105.49 E-value: 4.54e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITF--APFKISCEDEQARTDYFIRTLLLE--FQNESRRLYQFHYVNWPDHDVPSSF 76
Cdd:cd14608   94 MLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVPESP 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  77 DSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYE 154
Cdd:cd14608  174 ASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLR 253


                 ....*...
gi 196114970 155 LVHRAIAQ 162
Cdd:cd14608  254 FSYLAVIE 261

R-PTPc-A-E-1

cd14551

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

7-158

5.16e-25

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: 103.07 E-value: 5.16e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLYGEDpiTFAPFKISCEDEQARTDYFIRTLLLEFQNES------RRLYQFHYVNWPDHDVPSSFDSIL 80
Cdd:cd14551   50 ERKEKKCSQYWPDQGCW--TYGNLRVRVEDTVVLVDYTTRKFCIQKVNRGigekrvRLVTQFHFTSWPDFGVPFTPIGML 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 196114970  81 DMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14551  128 KFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAeGKV----DVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

R-PTPc-M-1

cd14633

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

1-162

1.41e-24

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: 103.97 E-value: 1.41e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPlygEDPITFAPFKISCEDEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14633  113 MVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14633  190 LLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVFIHD 266


                 ....
gi 196114970 159 AIAQ 162
Cdd:cd14633  267 AILE 270

PTPc-N7

cd14612

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

9-162

3.79e-24

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: 101.84 E-value: 3.79e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   9 GRKKCERYWPlygEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISlmrK 88
Cdd:cd14612   97 KKEKCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRLVA---E 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 196114970  89 YQEHEDV-----PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 162
Cdd:cd14612  171 VEESRQTaaspgPIVVHCSAGIGRTGCFIATSIGCQQLKD---TGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLAL 246

R-PTPc-F-1

cd14626

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

1-162

5.10e-24

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: 102.42 E-value: 5.10e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDpiTFAPFKISCEDEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14626  114 MMTRLEEKSRVKCDQYWPIRGTE--TYGMIQVTLLDTVELATYSVRTFALykNGSSEKREVRQFQFMAWPDHGVPEYPTP 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14626  192 ILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHE 268


                 ....
gi 196114970 159 AIAQ 162
Cdd:cd14626  269 ALLE 272

R-PTP-N

cd14609

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

7-162

1.31e-23

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: 101.27 E-value: 1.31e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWP-----LYGEDPITFAPFKISCEDeqartdYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDSI 79
Cdd:cd14609  122 EDGVKQCDRYWPdegssLYHIYEVNLVSEHIWCED------FLVRSFYLKNvqTQETRTLTQFHFLSWPAEGIPSSTRPL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  80 LDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRA 159
Cdd:cd14609  196 LDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQRPGMVRTKDQFEFALTA 273


                 ...
gi 196114970 160 IAQ 162
Cdd:cd14609  274 VAE 276

PTPc-N3

cd14600

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

7-166

2.11e-23

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: 100.31 E-value: 2.11e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPlygeDP---ITFAPFKISCEDEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDSILD 81
Cdd:cd14600  118 ERGRTKCHQYWP----DPpdvMEYGGFRVQCHSEDCTIAYVFREMLLTNtqTGEERTVTHLQYVAWPDHGVPDDSSDFLE 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  82 MISLMRKyQEHEDVPICIHCSAGCGRTGAICAIDYTWNLlkagkIPEEFNVFNL--IQEMRTQRHSAVQTKEQYELVHRA 159
Cdd:cd14600  194 FVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCL-----TERNQPVYPLdiVRKMRDQRAMMVQTSSQYKFVCEA 267


                 ....*..
gi 196114970 160 IAQLFEK 166
Cdd:cd14600  268 ILRVYEE 274

R-PTPc-V

cd14618

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

7-160

4.47e-23

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: 98.48 E-value: 4.47e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLyGEDPITFAPFKISCEDEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWPDHDVPSSFDSILDMIS 84
Cdd:cd14618   76 ENGRVLCDHYWPS-ESTPVSYGHITVHLLAQSSEDEWTRREFKLwhEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRE 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 196114970  85 LMRKY-QEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 160
Cdd:cd14618  155 LVREHvQATKGKgPTLVHCSAGVGRSGTFIALDRLLRQLKEEKV---VDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229

R-PTP-F-2

cd14629

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

7-159

4.96e-23

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: 99.80 E-value: 4.96e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPlyGEDPITFAPFKISCEDEQARTDYFIRtlllEFQ------NESRRLYQFHYVNWPDHDVPSSFDSIL 80
Cdd:cd14629  132 EMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTIRQFQFTDWPEQGVPKTGEGFI 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  81 DMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14629  206 DFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRTQRPAMVQTEDQYQLCYR 282


                 .
gi 196114970 159 A 159
Cdd:cd14629  283 A 283

R-PTP-D-2

cd14628

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

7-159

5.48e-23

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: 99.81 E-value: 5.48e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPlyGEDPITFAPFKISCEDEQARTDYFIRtlllEFQ------NESRRLYQFHYVNWPDHDVPSSFDSIL 80
Cdd:cd14628  131 EMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTVRQFQFTDWPEQGVPKSGEGFI 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  81 DMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14628  205 DFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDQYQFCYR 281


                 .
gi 196114970 159 A 159
Cdd:cd14628  282 A 282

R-PTPc-C-1

cd14557

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

1-158

4.06e-22

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: 94.51 E-value: 4.06e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNE---SRRLYQFHYVNWPDHDVPSSFD 77
Cdd:cd14557   44 MVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEEKICPDYIIRKLNINNKKEkgsGREVTHIQFTSWPDHGVPEDPH 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  78 SILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQRHSAVQTKEQYELV 156
Cdd:cd14557  124 LLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAeGRV----DVYGYVVKLRRQRCLMVQVEAQYILI 199


                 ..
gi 196114970 157 HR 158
Cdd:cd14557  200 HQ 201

R-PTP-S-2

cd14627

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

7-159

8.01e-22

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: 96.34 E-value: 8.01e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPlyGEDPITFAPFKISCEDEQARTDYFIRtlllEFQ------NESRRLYQFHYVNWPDHDVPSSFDSIL 80
Cdd:cd14627  132 EMGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTVRQFQFTDWPEQGVPKSGEGFI 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  81 DMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14627  206 DFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282


                 .
gi 196114970 159 A 159
Cdd:cd14627  283 A 283

R-PTPc-G-1

cd17667

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

7-162

1.82e-21

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: 94.72 E-value: 1.82e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPlyGEDPITFAPFKISCEDEQARTDYFIRTLLLE--------------FQNEsRRLYQFHYVNWPDHDV 72
Cdd:cd17667  108 EKGRRKCDQYWP--TENSEEYGNIIVTLKSTKIHACYTVRRFSIRntkvkkgqkgnpkgRQNE-RTVIQYHYTQWPDMGV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  73 PSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQ 152
Cdd:cd17667  185 PEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVID---SMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQ 261

                        170
                 ....*....|
gi 196114970 153 YELVHRAIAQ 162
Cdd:cd17667  262 YIFIHDALLE 271

PTP-N23

cd14539

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

1-157

4.38e-21

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: 91.68 E-value: 4.38e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14539   45 MLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQSVRTTPTHVERIISIQHkdTRLSRSVVHLQFTTWPELGLPDSPNP 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHED---VPICIHCSAGCGRTGAICAIDYTWNLLKAGK-IPeefNVFNLIQEMRTQRHSAVQTKEQYE 154
Cdd:cd14539  125 LLRFIEEVHSHYLQQRslqTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNgIP---DLPQLVRKMRQQRKYMLQEKEHLK 201


                 ...
gi 196114970 155 LVH 157
Cdd:cd14539  202 FCY 204

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

2-162

7.51e-21

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 93.23 E-value: 7.51e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   2 ACREFEMGRKKCERYWPLYGEdpitFAPFKISCE---DEQARTDYFIRTLLLEFQN---ESRRLYQFHYVNWPDHDVPSS 75
Cdd:COG5599  110 SDDEISKPKVKMPVYFRQDGE----YGKYEVSSElteSIQLRDGIEARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISA 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  76 fDSILDMISLMRKYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQEMRTQR-HSAVQTKE 151
Cdd:COG5599  186 -EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSE 263

                        170
                 ....*....|..
gi 196114970 152 QY-ELVHRAIAQ 162
Cdd:COG5599  264 QLdVLVKLAEQQ 275

PTPc-N2

cd14607

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

1-160

1.64e-20

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: 91.57 E-value: 1.64e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAP--FKISCEDEQARTDYFIRTLLLEFQN--ESRRLYQFHYVNWPDHDVPSSF 76
Cdd:cd14607   93 MLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGVPESP 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  77 DSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDyTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYE 154
Cdd:cd14607  173 ASFLNFLFKVRESGslSPEHGPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLR 251


                 ....*.
gi 196114970 155 LVHRAI 160
Cdd:cd14607  252 FSYMAV 257

R-PTPc-S-1

cd14625

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

1-162

1.96e-20

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: 92.08 E-value: 1.96e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDpiTFAPFKISCEDEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDS 78
Cdd:cd14625  120 MMTKLEEKSRIKCDQYWPSRGTE--TYGMIQVTLLDTIELATFCVRTFSLHKNgsSEKREVRQFQFTAWPDHGVPEYPTP 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14625  198 FLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID---AMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHD 274


                 ....
gi 196114970 159 AIAQ 162
Cdd:cd14625  275 ALLE 278

R-PTPc-E-1

cd14620

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

7-160

2.04e-20

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: 90.39 E-value: 2.04e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLYGedPITFAPFKISCEDEQARTDYFIRTLLLEFQ-----NESRRLYQFHYVNWPDHDVPSSFDSILD 81
Cdd:cd14620   74 ERKEEKCYQYWPDQG--CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLK 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 196114970  82 MISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 160
Cdd:cd14620  152 FLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227

R-PTPc-B

cd14617

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

1-158

2.05e-20

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: 90.36 E-value: 2.05e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLyGEDPITFAPFKISCEDEQARTDYFIRTLLL--EFQNESRRLY-QFHYVNWPDHDVPSSFD 77
Cdd:cd14617   70 MVTQCVEKGRVKCDHYWPA-DQDSLYYGDLIVQMLSESVLPEWTIREFKIcsEEQLDAPRLVrHFHYTVWPDHGVPETTQ 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  78 SILDMISLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYEL 155
Cdd:cd14617  149 SLIQFVRTVRDYinRTPGSGPTVVHCSAGVGRTGTFIALD---RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVY 225


                 ...
gi 196114970 156 VHR 158
Cdd:cd14617  226 LHQ 228

R-PTPc-typeIIb-2

cd14556

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

11-157

2.36e-19

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: 86.69 E-value: 2.36e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  11 KKCERYWPLYGEDpiTFAPFKISCEDEQARTDYFIRTLLL----EFQNESRRLYQFHYVNWPDH-DVPSSFDSILDMISL 85
Cdd:cd14556   53 QSCPQYWPDEGSG--TYGPIQVEFVSTTIDEDVISRIFRLqnttRPQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSE 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 196114970  86 MRKYQEH-EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14556  131 VEKWQEQsGEGPIVVHCLNGVGRSGVFCAISSVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200

R-PTPc-D-1

cd14624

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

7-162

2.46e-19

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: 88.63 E-value: 2.46e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   7 EMGRKKCERYWPLYGEDpiTFAPFKISCEDEQARTDYFIRTLLLeFQN---ESRRLYQFHYVNWPDHDVPSSFDSILDMI 83
Cdd:cd14624  126 ERSRVKCDQYWPSRGTE--TYGLIQVTLLDTVELATYCVRTFAL-YKNgssEKREVRQFQFTAWPDHGVPEHPTPFLAFL 202

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 196114970  84 SLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 162
Cdd:cd14624  203 RRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278

PTPc-N21

cd14598

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

1-165

3.73e-19

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: 86.57 E-value: 3.73e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGE--DPITFAPFKISCEDEQ-----ARTDYFIRTLLlefQNESRRLYQFHYVNWPDHDVP 73
Cdd:cd14598   46 MVTAEEEGGREKSFRYWPRLGSrhNTVTYGRFKITTRFRTdsgcyATTGLKIKHLL---TGQERTVWHLQYTDWPEHGCP 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  74 SS---FDSILDMISLMRKYQ------EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLiqeMRTQRH 144
Cdd:cd14598  123 EDlkgFLSYLEEIQSVRRHTnstidpKSPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDM---LRQQRM 199

                        170       180
                 ....*....|....*....|.
gi 196114970 145 SAVQTKEQYELVHRAIAQLFE 165
Cdd:cd14598  200 MMVQTLSQYTFVYKVLIQFLK 220

PTPc-N5

cd14613

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

11-161

8.09e-19

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: 86.45 E-value: 8.09e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  11 KKCERYWPlygEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLM---R 87
Cdd:cd14613  109 EKCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVeeaR 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 196114970  88 KYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIA 161
Cdd:cd14613  186 QQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256

R-PTPc-A-1

cd14621

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

12-162

4.30e-18

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: 85.46 E-value: 4.30e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  12 KCERYWPLYGedPITFAPFKISCEDEQARTDYFIRTLLLE------FQNESRRLYQFHYVNWPDHDVPSSFDSILDMISL 85
Cdd:cd14621  136 KCAQYWPDQG--CWTYGNIRVSVEDVTVLVDYTVRKFCIQqvgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKK 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 196114970  86 MRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 162
Cdd:cd14621  214 VKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287

PHA02747

protein tyrosine phosphatase; Provisional

9-157

1.29e-17

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 84.28 E-value: 1.29e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   9 GRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYfIRTLLL---EFQNESRRLYQFHYVNWPDHDVPSS---FDSILDM 82
Cdd:PHA02747 132 GEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKY-ILTLIEitdKILKDSRKISHFQCSEWFEDETPSDhpdFIKFIKI 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  83 ISLMRK-------YQEHEDVPICIHCSAGCGRTGAICAIDYTWN-LLKAGKIPEEFNVFNLiqemRTQRHSAVQTKEQYE 154
Cdd:PHA02747 211 IDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNqLVKRKAICLAKTAEKI----REQRHAGIMNFDDYL 286


                 ...
gi 196114970 155 LVH 157
Cdd:PHA02747 287 FIQ 289

R-PTPc-R

cd14611

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

11-157

1.82e-17

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: 81.89 E-value: 1.82e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  11 KKCERYWP----LYGEDPITFAPFKiSCEDeqartdYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILdmiSLM 86
Cdd:cd14611   83 EKCVLYWPekrgIYGKVEVLVNSVK-ECDN------YTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLL---QLM 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 196114970  87 RKYQEHEDV-----PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14611  153 LDVEEDRLAspgrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGV---VDVLSIVCQLRVDRGGMVQTSEQYEFVH 225

PTPc_plant_PTP1

cd17658

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

12-153

2.03e-17

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: 81.36 E-value: 2.03e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  12 KCERYWPLYGEDPITFAPF-----KISCeDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISlm 86
Cdd:cd17658   58 KCADYFPAEENESREFGRIsvtnkKLKH-SQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLK-- 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 196114970  87 RKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQEMRTQRHSAVQTKEQY 153
Cdd:cd17658  135 RLYGIPPSAgPIVVHCSAGIGRTGAYCTIHNTIRRILEGDM-SAVDLSKTVRKFRSQRIGMVQTQDQY 201

PHA02742

protein tyrosine phosphatase; Provisional

1-153

6.88e-17

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 81.97 E-value: 6.88e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRL--YQFHYVNWPDHDVPSSFDS 78
Cdd:PHA02742 123 MITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLdiKHFAYEDWPHGGLPRDPNK 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  79 ILDMISLMRKYQEHEDV-----------PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAV 147
Cdd:PHA02742 203 FLDFVLAVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIVRDLRKQRHNCL 279


                 ....*.
gi 196114970 148 QTKEQY 153
Cdd:PHA02742 280 SLPQQY 285

PTPc-N14

cd14599

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

1-165

1.75e-16

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: 80.43 E-value: 1.75e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYG--EDPITFAPFKISCedeQARTD---YFIRTLLLE--FQNESRRLYQFHYVNWPDHDVP 73
Cdd:cd14599  112 MVTAEEEGGRSKSHRYWPKLGskHSSATYGKFKVTT---KFRTDsgcYATTGLKVKhlLSGQERTVWHLQYTDWPDHGCP 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  74 SSFDSILDMISLMRKYQEHEDV----------PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQR 143
Cdd:cd14599  189 EEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHN---EKVEVPVMLRHLREQR 265

                        170       180
                 ....*....|....*....|..
gi 196114970 144 HSAVQTKEQYELVHRAIAQLFE 165
Cdd:cd14599  266 MFMIQTIAQYKFVYQVLIQFLK 287

PHA02738

hypothetical protein; Provisional

1-160

7.25e-16

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 79.20 E-value: 7.25e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970   1 MACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNES-RRLYQFHYVNWPDHDVPSSFDSI 79
Cdd:PHA02738 120 MLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEF 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  80 LDMISLMRKYQE--HEDV-----------PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSA 146
Cdd:PHA02738 200 LNFVLEVRQCQKelAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACAT---VSIPSIVSSIRNQRYYS 276

                        170
                 ....*....|....
gi 196114970 147 VQTKEQYELVHRAI 160
Cdd:PHA02738 277 LFIPFQYFFCYRAV 290

PHA02746

protein tyrosine phosphatase; Provisional

11-160

5.24e-15

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 76.61 E-value: 5.24e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  11 KKCERYWPLYGEDPITFAPFKISCEDEQARTDyFIRTLLL---EFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISL-- 85
Cdd:PHA02746 152 EKCFELWTKEEDSELAFGRFVAKILDIIEELS-FTKTRLMitdKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKvn 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  86 -----MRKYQEHEDV---PICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:PHA02746 231 eeqaeLIKQADNDPQtlgPIVVHCSAGIGRAGTFCAID---NALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCY 307


                 ...
gi 196114970 158 RAI 160
Cdd:PHA02746 308 KAL 310

R-PTPc-T-2

cd14634

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

13-157

8.18e-14

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: 70.82 E-value: 8.18e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  13 CERYWP-----LYGEDPITFAPFKIsceDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDH-DVPSSFDSILDMISLM 86
Cdd:cd14634   54 CMQYWPektscCYGPIQVEFVSADI---DEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRL 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 196114970  87 RKYQEHEDVP---ICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14634  131 EKWQEQYDGRegrTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVY 201

R-PTPc-K-2

cd14636

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

13-157

4.35e-13

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: 68.51 E-value: 4.35e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  13 CERYWPlyGEDPITFAPFKISCEDEQARTDYFIRTL----LLEFQNESRRLYQFHYVNWPDH-DVPSSFDSILDMISLMR 87
Cdd:cd14636   54 CPQYWP--EEGMLRYGPIQVECMSCSMDCDVISRIFricnLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVE 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 196114970  88 KYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14636  132 KWQEECDEgegRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCY 201

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

61-158

6.08e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 57.67 E-value: 6.08e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  61 QFHYVNWPDHDVPS--SFDSILDMIslMRKYQEHEdvPICIHCSAGCGRTGAICAidyTWnLLKAGKIPEEfnvfnLIQE 138
Cdd:COG2453   49 EYLHLPIPDFGAPDdeQLQEAVDFI--DEALREGK--KVLVHCRGGIGRTGTVAA---AY-LVLLGLSAEE-----ALAR 115

                         90       100
                 ....*....|....*....|
gi 196114970 139 MRTQRHSAVQTKEQYELVHR 158
Cdd:COG2453  116 VRAARPGAVETPAQRAFLER 135

R-PTPc-U-2

cd14637

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

13-153

4.07e-09

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: 56.84 E-value: 4.07e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  13 CERYWPLYGEDpiTFAPFKISCEDEQARTDyfIRTLLLEFQNESRR------LYQFHYVNW-PDHDVPSSFDSILDMISL 85
Cdd:cd14637   57 CLQYWPEPGLQ--QYGPMEVEFVSGSADED--IVTRLFRVQNITRLqeghlmVRHFQFLRWsAYRDTPDSKKAFLHLLAS 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 196114970  86 MRKYQ-EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 153
Cdd:cd14637  133 VEKWQrESGEGRTVVHCLNGGGRSGTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQY 198

R-PTPc-M-2

cd14635

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

13-157

7.52e-09

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: 56.23 E-value: 7.52e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  13 CERYWPLYGEDpiTFAPFKISCEDEQARTDYFIRTLLL----EFQNESRRLYQFHYVNWPDH-DVPSSFDSILDMISLMR 87
Cdd:cd14635   54 CPQYWPENGVH--RHGPIQVEFVSADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVD 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 196114970  88 KYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14635  132 KWQEEYNGgegRTVVHCLNGGGRSGTFCAISIVCEMLRH---QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201

PTP_PTPDC1

cd14506

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

52-157

3.07e-08

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: 54.28 E-value: 3.07e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  52 FQNESRRLYQFhyvNWPDHDVPSsFDSILDMISLMRKYQEhEDVPICIHCSAGCGRTG-AICAIdytwnLLKAGKIPEEf 130
Cdd:cd14506   72 FMRAGIYFYNF---GWKDYGVPS-LTTILDIVKVMAFALQ-EGGKVAVHCHAGLGRTGvLIACY-----LVYALRMSAD- 140

                         90       100
                 ....*....|....*....|....*..
gi 196114970 131 nvfNLIQEMRTQRHSAVQTKEQYELVH 157
Cdd:cd14506  141 ---QAIRLVRSKRPNSIQTRGQVLCVR 164

PTP_YopH-like

cd14559

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

62-155

6.84e-08

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: 53.56 E-value: 6.84e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  62 FHYVNWPDHDVPSSFDSIL--DMISLMRK--------------YQEHEDVPIcIHCSAGCGRTGAICAIdytwnlLKAGK 125
Cdd:cd14559  121 VHVTNWPDHTAISSEGLKElaDLVNKSAEekrnfykskgssaiNDKNKLLPV-IHCRAGVGRTGQLAAA------MELNK 193

                         90       100       110
                 ....*....|....*....|....*....|.
gi 196114970 126 IPEEFNVFNLIQEMRTQR-HSAVQTKEQYEL 155
Cdd:cd14559  194 SPNNLSVEDIVSDMRTSRnGKMVQKDEQLDT 224

PTP_DSP_cys

cd14494

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

77-158

1.63e-07

Pssm-ID: 350344 [Multi-domain] Cd Length: 113 Bit Score: 50.04 E-value: 1.63e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  77 DSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwnLLKAGKIPeefnVFNLIQEMRTQR-HSAVQTKEQYEL 155
Cdd:cd14494   39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACY----LVLLGGMS----AEEAVRIVRLIRpGGIPQTIEQLDF 110


                 ...
gi 196114970 156 VHR 158
Cdd:cd14494  111 LIK 113

DUSP23

cd14504

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

59-156

3.88e-07

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

Pssm-ID: 350354 [Multi-domain] Cd Length: 142 Bit Score: 49.58 E-value: 3.88e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  59 LYQFHYVNW-----PDHDVPSsFDSILDMISLMrKYQEHEDVPICIHCSAGCGRTGAICAIdYtwnLLKAGKIPEEfnvf 133
Cdd:cd14504   44 SDTCPGLRYhhipiEDYTPPT-LEQIDEFLDIV-EEANAKNEAVLVHCLAGKGRTGTMLAC-Y---LVKTGKISAV---- 113

                         90       100
                 ....*....|....*....|...
gi 196114970 134 NLIQEMRTQRHSAVQTKEQYELV 156
Cdd:cd14504  114 DAINEIRRIRPGSIETSEQEKFV 136

PTP_PTEN-like

cd14497

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...

61-113

3.24e-06

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: 47.57 E-value: 3.24e-06

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 196114970  61 QFHYVNWPDHDVPSsFDSILDMISLMRKY-QEHEDVPICIHCSAGCGRTGAICA 113
Cdd:cd14497   62 RVLHYGFPDHHPPP-LGLLLEIVDDIDSWlSEDPNNVAVVHCKAGKGRTGTVIC 114

CDKN3-like

cd14505

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

34-158

1.11e-04

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: 43.02 E-value: 1.11e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  34 CEDEQARTdYFIRTLLLEFQneSRRLYQFHYVnWPDHDVPSSFDSIL----DMISLMRKYQEhedvpICIHCSAGCGRTG 109
Cdd:cd14505   51 CTDGELEE-LGVPDLLEQYQ--QAGITWHHLP-IPDGGVPSDIAQWQelleELLSALENGKK-----VLIHCKGGLGRTG 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 196114970 110 AICAIdytwNLLKAG-KIPEEfnvfNLIQEMRTQRHSAVQTKEQYELVHR 158
Cdd:cd14505  122 LIAAC----LLLELGdTLDPE----QAIAAVRALRPGAIQTPKQENFLHQ 163

PTP_VSP_TPTE

cd14510

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

56-157

1.23e-04

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

Pssm-ID: 350360 [Multi-domain] Cd Length: 177 Bit Score: 43.12 E-value: 1.23e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  56 SRRLYQ---FHY----VNWPDHDVPSsfdsILDMISLMRKYQEH----EDVPICIHCSAGCGRTG-AICAidytWnLLKA 123
Cdd:cd14510   63 SERGYDpkyFHNrverVPIDDHNVPT----LDEMLSFTAEVREWmaadPKNVVAIHCKGGKGRTGtMVCA----W-LIYS 133

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 196114970 124 GKIPEEFNVFNLIQEMRT-----QRHSAVQTKEQYELVH 157
Cdd:cd14510  134 GQFESAKEALEYFGERRTdksvsSKFQGVETPSQSRYVG 172

TpbA-like

cd14529

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

35-114

8.72e-04

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

Pssm-ID: 350378 [Multi-domain] Cd Length: 158 Bit Score: 40.44 E-value: 8.72e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  35 EDEQARTDYFIRTLL-LEFQNESRRLY-------QFHYVN------WPDHDVPSSFDSILDMISlmrkyqehEDVPICIH 100
Cdd:cd14529   24 EDRALLKKLGIKTVIdLRGADERAASEeaaakidGVKYVNlplsatRPTESDVQSFLLIMDLKL--------APGPVLIH 95

                         90
                 ....*....|....
gi 196114970 101 CSAGCGRTGAICAI 114
Cdd:cd14529   96 CKHGKDRTGLVSAL 109

PTP-IVa1

cd18537

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...

63-151

2.38e-03

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.

Pssm-ID: 350513 [Multi-domain] Cd Length: 167 Bit Score: 39.29 E-value: 2.38e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  63 HYVNWP-DHDVPSSFDSILDMISLMR-KYQEHEDVPICIHCSAGCGRTGAICAIdytwNLLKAGKIPEEfnvfnLIQEMR 140
Cdd:cd18537   64 QVLDWPfDDGAPPSNQIVDDWLNLLKvKFREEPGCCIAVHCVAGLGRAPVLVAL----ALIECGMKYED-----AVQFIR 134

                         90
                 ....*....|.
gi 196114970 141 TQRHSAVQTKE 151
Cdd:cd18537  135 QKRRGAFNSKQ 145

PHA02740

protein tyrosine phosphatase; Provisional

11-161

7.14e-03

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 38.79 E-value: 7.14e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  11 KKC-ERYWPLYGEDPITFAPFKISCEdEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWP----DHDVPSSFD---SIL 80
Cdd:PHA02740 128 KKCfNQFWSLKEGCVITSDKFQIETL-EIIIKPHFNLTLLSltDKFGQAQKISHFQYTAWPadgfSHDPDAFIDffcNID 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196114970  81 DMISLMRKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRA 159
Cdd:PHA02740 207 DLCADLEKHKADGKIaPIIIDCIDGISSSAVFCVFDICATEFDKTGM---LSIANALKKVRQKKYGCMNCLDDYVFCYHL 283


                 ..
gi 196114970 160 IA 161
Cdd:PHA02740 284 IA 285

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