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Conserved domains on  [gi|1907161252|ref|XP_036020805|]
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tyrosine-protein phosphatase non-receptor type 12 isoform X2 [Mus musculus]

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 ...
 43-312 0e+00

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: 631.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  43 SNNCKRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQG 122
Cdd:cd14604    28 ASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 123 PLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRR 202
Cdd:cd14604   108 PLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRR 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 203 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQE 282
Cdd:cd14604   188 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQE 267

                         250       260       270
                  ....*....|....*....|....*....|
gi 1907161252 283 MRTQRHSAVQTKEQYELVHRAIAQLFEKQL 312
Cdd:cd14604   268 MRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
 
Name Accession Description Interval E-value
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 43-312 0e+00

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: 631.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  43 SNNCKRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQG 122
Cdd:cd14604    28 ASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 123 PLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRR 202
Cdd:cd14604   108 PLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRR 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 203 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQE 282
Cdd:cd14604   188 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQE 267

                         250       260       270
                  ....*....|....*....|....*....|
gi 1907161252 283 MRTQRHSAVQTKEQYELVHRAIAQLFEKQL 312
Cdd:cd14604   268 MRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
63-306 9.92e-117

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 352.35  E-value: 9.92e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252   63 PTATGEKEENVKKNRYKDILPFDHSRVKLTlKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVI 142
Cdd:smart00194  18 SCTVAAFPENRDKNRYKDVLPYDHTRVKLK-PPPGEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  143 IVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSF 220
Cdd:smart00194  97 IVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRTVTHYHYTNWPDHGVPESP 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  221 DSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELV 300
Cdd:smart00194 177 ESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEIVKELRSQRPGMVQTEEQYIFL 253


                   ....*.
gi 1907161252  301 HRAIAQ 306
Cdd:smart00194 254 YRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
72-306 3.43e-111

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 336.91  E-value: 3.43e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  72 NVKKNRYKDILPFDHSRVKLTlkTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFE 151
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 152 MGRKKCERYWPLYGEDPITFAPFKISCENEQART-DYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDSILDMIS 228
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907161252 229 LMRKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:pfam00102 159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 65-301 1.22e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 168.64  E-value: 1.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  65 ATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQdSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIV 144
Cdd:PHA02747   44 ANFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 145 MAC-REFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYfIRTLLL---EFQNESRRLYQFHYVNWPDHDVPSS- 219
Cdd:PHA02747  123 MLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKY-ILTLIEitdKILKDSRKISHFQCSEWFEDETPSDh 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 220 --FDSILDMISLMRK-------YQEHEDVPICIHCSAGCGRTGAICAIDYTWN-LLKAGKIPEEFNVFNLiqemRTQRHS 289
Cdd:PHA02747  202 pdFIKFIKIIDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNqLVKRKAICLAKTAEKI----REQRHA 277

                         250
                  ....*....|..
gi 1907161252 290 AVQTKEQYELVH 301
Cdd:PHA02747  278 GIMNFDDYLFIQ 289
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
58-306 8.46e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 156.79  E-value: 8.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  58 TEKIYPTATGEKEE----NVKKNRYKDILPFDHSRVkltlktpSQDSDYINANFIKgVYGPKAYVATQGPLANTVIDFWR 133
Cdd:COG5599    24 TNELAPSHNDPQYLqninGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQ-VIGNHRYIATQYPLEEQLEDFFQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 134 MIWEYNVVIIVM--ACREFEMGRKKCERYWPLYGEdpitFAPFKISCE---NEQARTDYFIRTLLLEFQN---ESRRLYQ 205
Cdd:COG5599    96 MLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGE----YGKYEVSSElteSIQLRDGIEARTYVLTIKGtgqKKIEIPV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 206 FHYVNWPDHDVPSSfDSILDMISLMRKYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQE 282
Cdd:COG5599   172 LHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVID 249

                         250       260
                  ....*....|....*....|....*.
gi 1907161252 283 MRTQR-HSAVQTKEQY-ELVHRAIAQ 306
Cdd:COG5599   250 MRTSRnGGMVQTSEQLdVLVKLAEQQ 275
 
Name Accession Description Interval E-value
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 43-312 0e+00

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: 631.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  43 SNNCKRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQG 122
Cdd:cd14604    28 ASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 123 PLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRR 202
Cdd:cd14604   108 PLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRR 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 203 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQE 282
Cdd:cd14604   188 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQE 267

                         250       260       270
                  ....*....|....*....|....*....|
gi 1907161252 283 MRTQRHSAVQTKEQYELVHRAIAQLFEKQL 312
Cdd:cd14604   268 MRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 75-308 4.04e-149

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: 434.65  E-value: 4.04e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  75 KNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGR 154
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 155 KKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQ 234
Cdd:cd14602    81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907161252 235 EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLF 308
Cdd:cd14602   161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 102-302 7.42e-146

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: 424.91  E-value: 7.42e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENE 181
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QART-DYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDY 260
Cdd:cd14542    81 KRVGpDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907161252 261 TWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 302
Cdd:cd14542   161 VWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 49-308 6.77e-126

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: 376.09  E-value: 6.77e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  49 LRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTV 128
Cdd:cd14603     7 IRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 129 IDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYgEDPITFAPFKIS-CENEQARTDYFIRTLLLEFQNESRRLYQFH 207
Cdd:cd14603    87 LDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQE-QEPLQTGPFTITlVKEKRLNEEVILRTLKVTFQKESRSVSHFQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 208 YVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQR 287
Cdd:cd14603   166 YMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQR 245

                         250       260
                  ....*....|....*....|.
gi 1907161252 288 HSAVQTKEQYELVHRAIAQLF 308
Cdd:cd14603   246 PAAVQTEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
63-306 9.92e-117

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 352.35  E-value: 9.92e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252   63 PTATGEKEENVKKNRYKDILPFDHSRVKLTlKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVI 142
Cdd:smart00194  18 SCTVAAFPENRDKNRYKDVLPYDHTRVKLK-PPPGEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  143 IVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSF 220
Cdd:smart00194  97 IVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSETRTVTHYHYTNWPDHGVPESP 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  221 DSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELV 300
Cdd:smart00194 177 ESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEIVKELRSQRPGMVQTEEQYIFL 253


                   ....*.
gi 1907161252  301 HRAIAQ 306
Cdd:smart00194 254 YRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
72-306 3.43e-111

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 336.91  E-value: 3.43e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  72 NVKKNRYKDILPFDHSRVKLTlkTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFE 151
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 152 MGRKKCERYWPLYGEDPITFAPFKISCENEQART-DYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDSILDMIS 228
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907161252 229 LMRKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:pfam00102 159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 102-302 9.79e-88

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


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 274.55  E-value: 9.79e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENE 181
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLLEFQN--ESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAID 259
Cdd:cd00047    81 EELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907161252 260 YTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 302
Cdd:cd00047   161 ILLERLEAEG---EVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 77-301 7.29e-75

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: 241.49  E-value: 7.29e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  77 RYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKK 156
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 157 CERYWPlYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEH 236
Cdd:cd14548    81 CDHYWP-FDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907161252 237 EDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 301
Cdd:cd14548   160 EKGPTIVHCSAGVGRTGTFIALDR---LLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 72-301 1.21e-74

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: 243.04  E-value: 1.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  72 NVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFE 151
Cdd:cd14543    29 NQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 152 MGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISL 229
Cdd:cd14543   109 RGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIhnTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGE 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 230 MRKYQ-------------EHEDVPICIHCSAGCGRTGAICAIDYTWNLL-KAGKIpeefNVFNLIQEMRTQRHSAVQTKE 295
Cdd:cd14543   189 VRQQQalavkamgdrwkgHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLeDVGTL----NVMQTVRRMRTQRAFSIQTPD 264


                  ....*.
gi 1907161252 296 QYELVH 301
Cdd:cd14543   265 QYYFCY 270
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 72-309 5.23e-70

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: 230.04  E-value: 5.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  72 NVKKNRYKDILPFDHSRVKLTLKTPSQD-SDYINANFIK------GVYGP-KAYVATQGPLANTVIDFWRMIWEYNVVII 143
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIRnenegpTTDENaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 144 VMACREFEMGRKKCERYWPLYGEDPiTFAPFKISCENEQARTDYFIRTLLL---EFQNESRRLYQFHYVNWPDHDVPSSF 220
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELQVsklDQGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 221 DSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYE 298
Cdd:cd14544   160 GGVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYK 239

                         250
                  ....*....|.
gi 1907161252 299 LVHRAIAQLFE 309
Cdd:cd14544   240 FIYVAVAQYIE 250
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 76-302 9.34e-70

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: 228.05  E-value: 9.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  76 NRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYG-PKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMgR 154
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 155 KKCERYWPLygEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDM---ISLMR 231
Cdd:cd14547    80 EKCAQYWPE--EENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLvqeVEEAR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907161252 232 KYQEHEDvPICIHCSAGCGRTGAICAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQRHSAVQTKEQYELVHR 302
Cdd:cd14547   158 QTEPHRG-PIVVHCSAGIGRTGCFIATSIGCQQLREeGVV----DVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 102-301 8.54e-66

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: 217.12  E-value: 8.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIK-GVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPlYGEDPITFAPFKISC-- 178
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVELvs 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 179 ENEQARTDYFIRTLLLEF-QNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRK--YQEHEDVPICIHCSAGCGRTGAI 255
Cdd:cd18533    80 EEENDDGGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907161252 256 CAIDYTWNLLKAGKIPEEFN------VFNLIQEMRTQRHSAVQTKEQYELVH 301
Cdd:cd18533   160 IALDSLLDELKRGLSDSQDLedsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 70-304 1.12e-64

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: 214.95  E-value: 1.12e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  70 EENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACRE 149
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 150 FEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWPDHDVPSSFDSILDMI 227
Cdd:cd14553    81 EERSRVKCDQYWPTRGTE--TYGLIQVTLLDTVELATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161252 228 SLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14553   159 RRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKT---VDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 102-301 1.65e-63

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: 210.67  E-value: 1.65e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENE 181
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE--TYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLL--------EFQNESRRLYQFHYVNWPDHDVPssfDSILDMISLMRK---YQEHEDVPICIHCSAGCG 250
Cdd:cd14549    79 EVLATYTVRTFSLknlklkkvKGRSSERVVYQYHYTQWPDHGVP---DYTLPVLSFVRKssaANPPGAGPIVVHCSAGVG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907161252 251 RTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 301
Cdd:cd14549   156 RTGTYIVID---SMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 76-297 4.06e-63

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: 210.44  E-value: 4.06e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  76 NRYKDILPFDHSRVKLTLKTPSQDsDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRK 155
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTD-DYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 156 KCERYWPlyGEDPITFAPFKISCENEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY 233
Cdd:cd14615    80 KCEEYWP--SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNaqTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907161252 234 --QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 297
Cdd:cd14615   158 mkQNPPNSPILVHCSAGVGRTGTFIAID---RLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQY 220
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 76-304 1.06e-62

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: 209.75  E-value: 1.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  76 NRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRK 155
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 156 KCERYWPLyGEDPITFAPFKISCENEQARTDYFIRTLLLE--FQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY 233
Cdd:cd14619    81 KCEHYWPL-DYTPCTYGHLRVTVVSEEVMENWTVREFLLKqvEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907161252 234 --QEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14619   160 ldQTMSGGPTVVHCSAGVGRTGTLIALDV---LLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 70-306 1.73e-61

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: 206.41  E-value: 1.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  70 EENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACRE 149
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 150 FEMGRKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDSILDMI 227
Cdd:cd14630    81 VEVGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907161252 228 SLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14630   158 RQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 67-309 5.42e-61

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: 206.27  E-value: 5.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  67 GEKEENVKKNRYKDILPFDHSRVKLTLKTPS-QDSDYINANFIKG-VYG----PKAYVATQGPLANTVIDFWRMIWEYNV 140
Cdd:cd14606    13 GQRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNqLLGpdenAKTYIASQGCLEATVNDFWQMAWQENS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 141 VIIVMACREFEMGRKKCERYWPLYGEDPiTFAPFKISCENEQARTDYFIRTLLLEFQNES---RRLYQFHYVNWPDHDVP 217
Cdd:cd14606    93 RVIVMTTREVEKGRNKCVPYWPEVGMQR-AYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGeliREIWHYQYLSWPDHGVP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 218 SSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKE 295
Cdd:cd14606   172 SEPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEA 251

                         250
                  ....*....|....
gi 1907161252 296 QYELVHRAIAQLFE 309
Cdd:cd14606   252 QYKFIYVAIAQFIE 265
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 70-304 1.15e-60

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: 204.29  E-value: 1.15e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  70 EENVKKNRYKDILPFDHSRVKLtlktpSQDSDYINANFIKGVYGPK--AYVATQGPLANTVIDFWRMIWEYNVVIIVMAC 147
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 148 REFEMGRKKCERYWP-LYGEDPITFAPFKISCENEQARTDYFIRTLLLE--FQNESRRLYQFHYVNWPDHDVPSSFDSIL 224
Cdd:cd14597    76 QEVEGGKIKCQRYWPeILGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 225 DMISLMRKYqeHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14597   156 TFISYMRHI--HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 72-304 1.24e-60

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: 204.35  E-value: 1.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  72 NVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFE 151
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 152 MGRKKCERYWPlYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPS--SFDSILDMISL 229
Cdd:cd14614    92 KRRVKCDHYWP-FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTanAAESILQFVQM 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907161252 230 MRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14614   171 VRQQAVKSKGPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 102-306 1.55e-59

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: 200.29  E-value: 1.55e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKA--YVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITF-APFKISC 178
Cdd:cd14538     1 YINASHIRIPVGGDTyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICgGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 179 ENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYqeHEDVPICIHCSAGCGRTGAIC 256
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKetGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI--HNSGPIVVHCSAGIGRTGVLI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907161252 257 AIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14538   159 TIDVALGLIERDL---PFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 75-296 4.83e-58

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 196.84  E-value: 4.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  75 KNRYKDILPFDHSRVKLTLKtpSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGR 154
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLK--QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 155 KKCERYWPLYGEDPITF--APFKISCENEQARTDYFIRTLLLE--FQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLM 230
Cdd:cd14545    79 IKCAQYWPQGEGNAMIFedTGLKVTLLSEEDKSYYTVRTLELEnlKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907161252 231 RkyqEH----EDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKiPEEFNVFNLIQEMRTQRHSAVQTKEQ 296
Cdd:cd14545   159 R---ESgslsSDVgPPVVHCSAGIGRSGTFCLVDTCLVLIEKGN-PSSVDVKKVLLEMRKYRMGLIQTPDQ 225
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 71-309 6.03e-58

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: 197.55  E-value: 6.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  71 ENVKKNRYKDILPFDHSRVKLTLKTPS-QDSDYINANFIKGVYG--------PKAYVATQGPLANTVIDFWRMIWEYNVV 141
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDGDPNePVSDYINANIIMPEFEtkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 142 IIVMACREFEMGRKKCERYWPlygeDPIT---FAPFKISCENEQARTDYFIRTLLLEF---QNESRRLYQFHYVNWPDHD 215
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWP----DEYAlkeYGVMRVRNVKESAAHDYILRELKLSKvgqGNTERTVWQYHFRTWPDHG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 216 VPSSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 293
Cdd:cd14605   157 VPSDPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQT 236

                         250
                  ....*....|....*.
gi 1907161252 294 KEQYELVHRAIAQLFE 309
Cdd:cd14605   237 EAQYRFIYMAVQHYIE 252
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 63-306 1.68e-57

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: 197.19  E-value: 1.68e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  63 PTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVI 142
Cdd:cd14633    31 PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 143 IVMACREFEMGRKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSF 220
Cdd:cd14633   111 IIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 221 DSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELV 300
Cdd:cd14633   188 TGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVFI 264


                  ....*.
gi 1907161252 301 HRAIAQ 306
Cdd:cd14633   265 HDAILE 270
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 72-303 1.87e-57

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: 195.82  E-value: 1.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  72 NVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFE 151
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 152 MGRKKCERYWPL--------YGEDPITfapfkiscenEQARTDYFIRtlllEFQ------NESRRLYQFHYVNWPDHDVP 217
Cdd:cd14554    86 MGREKCHQYWPAersaryqyFVVDPMA----------EYNMPQYILR----EFKvtdardGQSRTVRQFQFTDWPEQGVP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 218 SSFDSILDMISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKE 295
Cdd:cd14554   152 KSGEGFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVFQTVKLLRTQRPAMVQTED 228


                  ....*...
gi 1907161252 296 QYELVHRA 303
Cdd:cd14554   229 QYQFCYRA 236
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 64-306 2.03e-56

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 194.50  E-value: 2.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  64 TATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGvYGPK--AYVATQGPLANTVIDFWRMIWEYNVV 141
Cdd:cd14610    36 TNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 142 IIVMACREFEMGRKKCERYWPLYGED-----PITFAPFKISCEneqartDYFIRTLLLEF--QNESRRLYQFHYVNWPDH 214
Cdd:cd14610   115 VIVMLTPLAENGVKQCYHYWPDEGSNlyhiyEVNLVSEHIWCE------DFLVRSFYLKNlqTNETRTVTQFHFLSWNDQ 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 215 DVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNllKAGKIPEEFNVFNLIQEMRTQRHSAVQTK 294
Cdd:cd14610   189 GVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLN--KMAKGAKEIDIAATLEHLRDQRPGMVQTK 266

                         250
                  ....*....|..
gi 1907161252 295 EQYELVHRAIAQ 306
Cdd:cd14610   267 EQFEFALTAVAE 278
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 65-306 1.97e-55

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: 191.79  E-value: 1.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  65 ATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGvYGPK--AYVATQGPLANTVIDFWRMIWEYNVVI 142
Cdd:cd14609    35 STAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWENGCTV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 143 IVMACREFEMGRKKCERYWP-----LYGEDPITFAPFKISCEneqartDYFIRTLLLEF--QNESRRLYQFHYVNWPDHD 215
Cdd:cd14609   114 IVMLTPLVEDGVKQCDRYWPdegssLYHIYEVNLVSEHIWCE------DFLVRSFYLKNvqTQETRTLTQFHFLSWPAEG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 216 VPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLIQEMRTQRHSAVQTKE 295
Cdd:cd14609   188 IPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQRPGMVRTKD 265

                         250
                  ....*....|.
gi 1907161252 296 QYELVHRAIAQ 306
Cdd:cd14609   266 QFEFALTAVAE 276
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 71-306 3.31e-55

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: 191.02  E-value: 3.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  71 ENVKKNRYKDILPFDHSRVKLTlKTPSQDS---DYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMAC 147
Cdd:cd17667    26 DNKHKNRYINILAYDHSRVKLR-PLPGKDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 148 REFEMGRKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRTLLLE--------------FQNEsRRLYQFHYVNWPD 213
Cdd:cd17667   105 NLVEKGRRKCDQYWP--TENSEEYGNIIVTLKSTKIHACYTVRRFSIRntkvkkgqkgnpkgRQNE-RTVIQYHYTQWPD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 214 HDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 293
Cdd:cd17667   182 MGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVID---SMLQQIKDKSTVNVLGFLKHIRTQRNYLVQT 258

                         250
                  ....*....|...
gi 1907161252 294 KEQYELVHRAIAQ 306
Cdd:cd17667   259 EEQYIFIHDALLE 271
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 76-304 4.45e-55

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: 189.00  E-value: 4.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  76 NRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRK 155
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 156 KCERYWPLyGEDPITFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY 233
Cdd:cd14618    81 LCDHYWPS-ESTPVSYGHITVHLLAQSSEDEWTRREFKLwhEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907161252 234 -QEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14618   160 vQATKGKgPTLVHCSAGVGRSGTFIALDRLLRQLKEEKV---VDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 75-306 8.04e-55

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: 188.89  E-value: 8.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  75 KNRYKDILPFDHSRVKL-TLKTPSQDSDYINANFIKGVYG-PKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEm 152
Cdd:cd14612    18 KDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDGkEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 153 GRKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISlmrK 232
Cdd:cd14612    97 KKEKCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRLVA---E 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907161252 233 YQEHEDV-----PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14612   171 VEESRQTaaspgPIVVHCSAGIGRTGCFIATSIGCQQLKD---TGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLAL 246
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 62-306 2.85e-54

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: 188.31  E-value: 2.85e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  62 YPTATGEKEENVKKNRYKDILPFDHSRVKLTLktpsQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVV 141
Cdd:cd14608    15 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 142 IIVMACREFEMGRKKCERYWPLYGEDPITF--APFKISCENEQARTDYFIRTLLLE--FQNESRRLYQFHYVNWPDHDVP 217
Cdd:cd14608    91 GVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 218 SSFDSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKE 295
Cdd:cd14608   171 ESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTAD 250

                         250
                  ....*....|.
gi 1907161252 296 QYELVHRAIAQ 306
Cdd:cd14608   251 QLRFSYLAVIE 261
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 43-306 7.27e-54

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: 187.17  E-value: 7.27e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  43 SNNCKRLR-----RLSTKYrtEKIYPTA--TGEK---EENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVY 112
Cdd:cd14626     4 ADNIERLKandglKFSQEY--ESIDPGQqfTWENsnlEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 113 GPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTL 192
Cdd:cd14626    82 KQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE--TYGMIQVTLLDTVELATYSVRTF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 193 LL--EFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKI 270
Cdd:cd14626   160 ALykNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERMKH 236

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907161252 271 PEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14626   237 EKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 76-302 1.85e-53

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: 184.34  E-value: 1.85e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  76 NRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRK 155
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 156 KCERYWPlygED--PIT-FAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRK 232
Cdd:cd14616    81 RCHQYWP---EDnkPVTvFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 233 YQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 302
Cdd:cd14616   158 SRAHDNTPMIVHCSAGVGRTGVFIALDH---LTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 102-304 3.97e-53

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 182.47  E-value: 3.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEdpITFAPFKISCENE 181
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS--VSSGDITVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHE-DVPICIHCSAGCGRTGAICAI 258
Cdd:cd14552    79 TDYEDYTLRDFLVTKgkGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRTGTFCAL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907161252 259 DYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14552   159 STVLERVKAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 102-304 9.79e-53

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: 181.65  E-value: 9.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPlygEDPITFAPFKISCENE 181
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP---DDTEVYGDIKVTLVET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAID 259
Cdd:cd14555    78 EPLAEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907161252 260 YTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14555   158 IMLDMAEREGV---VDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 101-310 2.33e-52

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: 180.60  E-value: 2.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 101 DYINANF----IKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpITFAPFKI 176
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGET-MQFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 177 SCENEQARTDYFIRTLLLEFQN--ESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGA 254
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907161252 255 ICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEK 310
Cdd:cd14541   160 LITMETAMCLIEAN---EPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVYEE 212
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 77-306 1.75e-51

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 179.09  E-value: 1.75e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  77 RYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKK 156
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 157 CERYWPLYGEdpITFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQ 234
Cdd:cd14623    81 CAQYWPSDGS--VSYGDITIELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907161252 235 EHE-DVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14623   159 QQSgNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 72-303 4.47e-51

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: 180.31  E-value: 4.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  72 NVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFE 151
Cdd:cd14628    52 NKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 152 MGRKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRtlllEFQ------NESRRLYQFHYVNWPDHDVPSSFDSILD 225
Cdd:cd14628   132 MGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTVRQFQFTDWPEQGVPKSGEGFID 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 226 MISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRA 303
Cdd:cd14628   206 FIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDQYQFCYRA 282
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 102-304 9.04e-51

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: 176.09  E-value: 9.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKA--YVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCE 179
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 180 NEQARTDYFIRTLLLeFQNES---RRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYqeHEDVPICIHCSAGCGRTGAIC 256
Cdd:cd14596    81 NYQALQYFIIRIIKL-VEKETgenRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKV--HNTGPIVVHCSAGIGRAGVLI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907161252 257 AIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14596   158 CVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 76-302 9.38e-51

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: 177.03  E-value: 9.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  76 NRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRK 155
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 156 KCERYWPLyGEDPITFAPFKISCENEQARTDYFIRTLLL--EFQNESRRLY-QFHYVNWPDHDVPSSFDSILDMISLMRK 232
Cdd:cd14617    81 KCDHYWPA-DQDSLYYGDLIVQMLSESVLPEWTIREFKIcsEEQLDAPRLVrHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907161252 233 Y--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 302
Cdd:cd14617   160 YinRTPGSGPTVVHCSAGVGRTGTFIALD---RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 73-305 2.32e-50

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: 176.98  E-value: 2.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  73 VKKNRYKDILPFDHSRVKLTlkTPSQD---SDYINANFIKGvYG--PKAYVATQGPLANTVIDFWRMIWEYNVVIIVMAC 147
Cdd:cd14613    26 VRKNRYKTILPNPHSRVCLT--SPDQDdplSSYINANYIRG-YGgeEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMIT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 148 REFEMGrKKCERYWPlygEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMI 227
Cdd:cd14613   103 NIEEMN-EKCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 228 SLM---RKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14613   179 QEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255


                  .
gi 1907161252 305 A 305
Cdd:cd14613   256 S 256
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 102-304 3.00e-50

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: 174.78  E-value: 3.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENE 181
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLL----------EFQNESRRLYQFHYVNWPDHDVPssfDSILDMISLMRK---YQEHEDVPICIHCSAG 248
Cdd:cd17668    79 QVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVP---EYTLPVLTFVRKasyAKRHAVGPVVVHCSAG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907161252 249 CGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd17668   156 VGRTGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 71-310 4.15e-50

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: 176.96  E-value: 4.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  71 ENVKKNRYKDILPFDHSRVKLtlktpSQDSDYINANFIK----GVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMA 146
Cdd:cd14600    39 QNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 147 CREFEMGRKKCERYWPlygeDP---ITFAPFKISCENEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFD 221
Cdd:cd14600   114 TTLTERGRTKCHQYWP----DPpdvMEYGGFRVQCHSEDCTIAYVFREMLLTNtqTGEERTVTHLQYVAWPDHGVPDDSS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 222 SILDMISLMRKyQEHEDVPICIHCSAGCGRTGAICAIDYTWNLlkagkIPEEFNVFNL--IQEMRTQRHSAVQTKEQYEL 299
Cdd:cd14600   190 DFLEFVNYVRS-KRVENEPVLVHCSAGIGRTGVLVTMETAMCL-----TERNQPVYPLdiVRKMRDQRAMMVQTSSQYKF 263

                         250
                  ....*....|.
gi 1907161252 300 VHRAIAQLFEK 310
Cdd:cd14600   264 VCEAILRVYEE 274
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 72-303 4.86e-50

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: 177.23  E-value: 4.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  72 NVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFE 151
Cdd:cd14629    53 NKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 152 MGRKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRtlllEFQ------NESRRLYQFHYVNWPDHDVPSSFDSILD 225
Cdd:cd14629   133 MGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 226 MISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRA 303
Cdd:cd14629   207 FIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRTQRPAMVQTEDQYQLCYRA 283
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 72-303 2.36e-49

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: 175.31  E-value: 2.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  72 NVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFE 151
Cdd:cd14627    53 NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 152 MGRKKCERYWPlyGEDPITFAPFKISCENEQARTDYFIRtlllEFQ------NESRRLYQFHYVNWPDHDVPSSFDSILD 225
Cdd:cd14627   133 MGREKCHQYWP--AERSARYQYFVVDPMAEYNMPQYILR----EFKvtdardGQSRTVRQFQFTDWPEQGVPKSGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 226 MISLMRKYQEH--EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRA 303
Cdd:cd14627   207 FIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDEYQFCYQA 283
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 100-306 2.52e-49

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: 172.90  E-value: 2.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 100 SDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPlygEDPITFAPFKISCE 179
Cdd:cd14631    13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DDTEVYGDFKVTCV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 180 NEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICA 257
Cdd:cd14631    90 EMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIV 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907161252 258 IDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14631   170 IDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 102-306 2.79e-49

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: 172.24  E-value: 2.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGvYGPK--AYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWP-----LYGEDPITFAPF 174
Cdd:cd14546     1 YINASTIYD-HDPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPeegseVYHIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 175 KISCEneqartDYFIRTLLLE--FQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRT 252
Cdd:cd14546    80 HIWCD------DYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907161252 253 GAICAIDYTWNLLKAGKipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14546   154 GTYILIDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 101-310 1.22e-48

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: 170.51  E-value: 1.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 101 DYINANFIKGVYGPKA----YVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPlYGEDPITFAPFKI 176
Cdd:cd14601     1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 177 SCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGA 254
Cdd:cd14601    80 TCHSEEGNPAYVFREMTLTNLekNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907161252 255 ICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEK 310
Cdd:cd14601   160 LITMETAMCLIECN---QPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 69-306 1.91e-48

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: 172.90  E-value: 1.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  69 KEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACR 148
Cdd:cd14621    49 KEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTN 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 149 EFEMGRKKCERYWPLYGedPITFAPFKISCENEQARTDYFIRTLLLE------FQNESRRLYQFHYVNWPDHDVPSSFDS 222
Cdd:cd14621   129 LKERKECKCAQYWPDQG--CWTYGNIRVSVEDVTVLVDYTVRKFCIQqvgdvtNKKPQRLITQFHFTSWPDFGVPFTPIG 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 223 ILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHR 302
Cdd:cd14621   207 MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQRCQMVQTDMQYVFIYQ 283


                  ....
gi 1907161252 303 AIAQ 306
Cdd:cd14621   284 ALLE 287
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 102-306 2.47e-48

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: 169.94  E-value: 2.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKA--YVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYG--EDPITFAPFKIS 177
Cdd:cd14540     1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgeHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 178 CENEQARTDYFIRTLLLEFQNE--SRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEH--EDV-------PICIHCS 246
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSgqSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHtnQDVaghnrnpPTLVHCS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 247 AGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHN---EELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 102-298 1.16e-47

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: 167.57  E-value: 1.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWplyGEDPITFAPFKISCENE 181
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYW---GDEKKTYGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLLEFQN--ESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQE------HEDVPICIHCSAGCGRTG 253
Cdd:cd14558    78 EKSPTYTVRVFEITHLKrkDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPyknskhGRSVPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907161252 254 AICAIdytWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYE 298
Cdd:cd14558   158 IFCAL---WNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQ 199
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 62-304 2.45e-47

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: 168.61  E-value: 2.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  62 YPTATGEKEENVKKNRYKDILPFDHSRVKLTlktpSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVV 141
Cdd:cd14607    14 YPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 142 IIVMACREFEMGRKKCERYWPLYGEDPITFAP--FKISCENEQARTDYFIRTLLLEFQN--ESRRLYQFHYVNWPDHDVP 217
Cdd:cd14607    90 AVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGVP 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 218 SSFDSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDyTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKE 295
Cdd:cd14607   170 ESPASFLNFLFKVRESGslSPEHGPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPD 248


                  ....*....
gi 1907161252 296 QYELVHRAI 304
Cdd:cd14607   249 QLRFSYMAV 257
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 65-301 1.22e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 168.64  E-value: 1.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  65 ATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQdSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIV 144
Cdd:PHA02747   44 ANFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 145 MAC-REFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYfIRTLLL---EFQNESRRLYQFHYVNWPDHDVPSS- 219
Cdd:PHA02747  123 MLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKY-ILTLIEitdKILKDSRKISHFQCSEWFEDETPSDh 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 220 --FDSILDMISLMRK-------YQEHEDVPICIHCSAGCGRTGAICAIDYTWN-LLKAGKIPEEFNVFNLiqemRTQRHS 289
Cdd:PHA02747  202 pdFIKFIKIIDINRKksgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNqLVKRKAICLAKTAEKI----REQRHA 277

                         250
                  ....*....|..
gi 1907161252 290 AVQTKEQYELVH 301
Cdd:PHA02747  278 GIMNFDDYLFIQ 289
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 75-301 1.79e-46

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: 165.09  E-value: 1.79e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  75 KNRYKDILPFDHSRVKLTLKTPSQD-SDYINANFIKGVYG-PKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEM 152
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 153 GrKKCERYWP----LYGEDPITFAPFKiSCENeqartdYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILdmiS 228
Cdd:cd14611    82 N-EKCVLYWPekrgIYGKVEVLVNSVK-ECDN------YTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLL---Q 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907161252 229 LMRKYQEHEDV-----PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 301
Cdd:cd14611   151 LMLDVEEDRLAspgrgPVVVHCSAGIGRTGCFIATTIGCQQLKEEGV---VDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 101-304 2.32e-46

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: 164.02  E-value: 2.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 101 DYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPlyGEDPITFAPFKISCEN 180
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWP--SEGSVTHGEITIEIKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 181 EQARTDYFIRTLLLEFQNE--SRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHE-DVPICIHCSAGCGRTGAICA 257
Cdd:cd14622    79 DTLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTgNHPIVVHCSAGAGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907161252 258 IDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14622   159 LS---NILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 70-306 2.88e-46

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: 166.42  E-value: 2.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  70 EENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACRE 149
Cdd:cd14625    45 EVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 150 FEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLLEFQ--NESRRLYQFHYVNWPDHDVPSSFDSILDMI 227
Cdd:cd14625   125 EEKSRIKCDQYWPSRGTE--TYGMIQVTLLDTIELATFCVRTFSLHKNgsSEKREVRQFQFTAWPDHGVPEYPTPFLAFL 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907161252 228 SLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14625   203 RRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID---AMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 102-306 5.57e-46

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: 162.91  E-value: 5.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPlygEDPITFAPFKISCENE 181
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP---DDSDTYGDIKITLLKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLLEFQNESRR--LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAID 259
Cdd:cd14632    78 ETLAEYSVRTFALERRGYSARheVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907161252 260 YTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14632   158 VMLDMAECEGV---VDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 78-304 2.10e-45

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: 162.42  E-value: 2.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  78 YKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKC 157
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 158 ERYWPLYGedPITFAPFKISCENEQARTDYFIRTLLLEFQ-----NESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRK 232
Cdd:cd14620    81 YQYWPDQG--CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907161252 233 YQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:cd14620   159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 70-306 3.22e-44

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: 160.67  E-value: 3.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  70 EENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACRE 149
Cdd:cd14624    45 EVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 150 FEMGRKKCERYWPLYGEDpiTFAPFKISCENEQARTDYFIRTLLLeFQN---ESRRLYQFHYVNWPDHDVPSSFDSILDM 226
Cdd:cd14624   125 EERSRVKCDQYWPSRGTE--TYGLIQVTLLDTVELATYCVRTFAL-YKNgssEKREVRQFQFTAWPDHGVPEHPTPFLAF 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 227 ISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:cd14624   202 LRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 102-302 2.34e-43

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: 155.37  E-value: 2.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENE 181
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLLEFQNE---SRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAI 258
Cdd:cd14557    81 KICPDYIIRKLNINNKKEkgsGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907161252 259 DYTWNLLKA-GKIpeefNVFNLIQEMRTQRHSAVQTKEQYELVHR 302
Cdd:cd14557   161 DAMLEGLEAeGRV----DVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PHA02738 PHA02738
hypothetical protein; Provisional
 55-304 5.08e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 158.55  E-value: 5.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  55 KYRTEKIYPTATGEKEeNVKKNRYKDILPFDHSRVklTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRM 134
Cdd:PHA02738   33 KVISEKVDGTFNAEKK-NRKLNRYLDAVCFDHSRV--ILPAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRM 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 135 IWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNES-RRLYQFHYVNWPD 213
Cdd:PHA02738  110 LWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPD 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 214 HDVPSSFDSILDMISLMRKYQE--HEDV-----------PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLI 280
Cdd:PHA02738  190 HDVPKNTSEFLNFVLEVRQCQKelAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACAT---VSIPSIV 266

                         250       260
                  ....*....|....*....|....
gi 1907161252 281 QEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:PHA02738  267 SSIRNQRYYSLFIPFQYFFCYRAV 290
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 55-309 8.21e-43

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 157.08  E-value: 8.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  55 KYRTEKIYPTATgeKEENVKKNRYKDILPFDHSRVKLtLKTPSQDSDYINANFIKGVYGPKA--YVATQGPLANTVIDFW 132
Cdd:cd14599    23 KKKADGVFTTAT--LPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFW 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 133 RMIWEYNVVIIVMACREFEMGRKKCERYWPLYG--EDPITFAPFKISCENEQ-----ARTDYFIRTLLlefQNESRRLYQ 205
Cdd:cd14599   100 QMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGskHSSATYGKFKVTTKFRTdsgcyATTGLKVKHLL---SGQERTVWH 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 206 FHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDV----------PICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFN 275
Cdd:cd14599   177 LQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHN---EKVE 253

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907161252 276 VFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 309
Cdd:cd14599   254 VPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
58-306 8.46e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 156.79  E-value: 8.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  58 TEKIYPTATGEKEE----NVKKNRYKDILPFDHSRVkltlktpSQDSDYINANFIKgVYGPKAYVATQGPLANTVIDFWR 133
Cdd:COG5599    24 TNELAPSHNDPQYLqninGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQ-VIGNHRYIATQYPLEEQLEDFFQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 134 MIWEYNVVIIVM--ACREFEMGRKKCERYWPLYGEdpitFAPFKISCE---NEQARTDYFIRTLLLEFQN---ESRRLYQ 205
Cdd:COG5599    96 MLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGE----YGKYEVSSElteSIQLRDGIEARTYVLTIKGtgqKKIEIPV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 206 FHYVNWPDHDVPSSfDSILDMISLMRKYQEHEDV---PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpEEFNVFNLIQE 282
Cdd:COG5599   172 LHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVID 249

                         250       260
                  ....*....|....*....|....*.
gi 1907161252 283 MRTQR-HSAVQTKEQY-ELVHRAIAQ 306
Cdd:COG5599   250 MRTSRnGGMVQTSEQLdVLVKLAEQQ 275
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 102-302 1.53e-42

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: 153.14  E-value: 1.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDpiTFAPFKISCENE 181
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLLEFQNES------RRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAI 255
Cdd:cd14551    79 VVLVDYTTRKFCIQKVNRGigekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907161252 256 CAIDYTWNLLKA-GKIpeefNVFNLIQEMRTQRHSAVQTKEQYELVHR 302
Cdd:cd14551   159 IVIDAMLDMMHAeGKV----DVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 102-301 9.42e-40

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: 145.60  E-value: 9.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGV--YGPKaYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCE 179
Cdd:cd14539     1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 180 NEQARTDYFIRTLLLEF--QNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHED---VPICIHCSAGCGRTGA 254
Cdd:cd14539    80 SVRTTPTHVERIISIQHkdTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRslqTPIVVHCSSGVGRTGA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907161252 255 ICAIDYTWNLLKAGK-IPeefNVFNLIQEMRTQRHSAVQTKEQYELVH 301
Cdd:cd14539   160 FCLLYAAVQEIEAGNgIP---DLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 102-301 1.03e-39

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: 145.24  E-value: 1.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMaCREFEMGRKKCERYWPLYGEDpiTFAPFKISCENE 181
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVM-LNQLDPKDQSCPQYWPDEGSG--TYGPIQVEFVST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLL----EFQNESRRLYQFHYVNWPDH-DVPSSFDSILDMISLMRKYQEH-EDVPICIHCSAGCGRTGAI 255
Cdd:cd14556    78 TIDEDVISRIFRLqnttRPQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRSGVF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907161252 256 CAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 301
Cdd:cd14556   158 CAISSVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 69-297 1.11e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 148.61  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  69 KEENVKKNRYKDILPFDHSRVklTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACR 148
Cdd:PHA02742   49 ELKNMKKCRYPDAPCFDRNRV--ILKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 149 EFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRL--YQFHYVNWPDHDVPSSFDSILDM 226
Cdd:PHA02742  127 IMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLdiKHFAYEDWPHGGLPRDPNKFLDF 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 227 ISLMRKYQEHEDV-----------PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKE 295
Cdd:PHA02742  207 VLAVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIVRDLRKQRHNCLSLPQ 283


                  ..
gi 1907161252 296 QY 297
Cdd:PHA02742  284 QY 285
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 102-309 1.37e-37

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: 140.11  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKA--YVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYG--EDPITFAPFKIS 177
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGsrHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 178 CENEQ-----ARTDYFIRTLLlefQNESRRLYQFHYVNWPDHDVPSS---FDSILDMISLMRKYQ------EHEDVPICI 243
Cdd:cd14598    81 TRFRTdsgcyATTGLKIKHLL---TGQERTVWHLQYTDWPEHGCPEDlkgFLSYLEEIQSVRRHTnstidpKSPNPPVLV 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907161252 244 HCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLiqeMRTQRHSAVQTKEQYELVHRAIAQLFE 309
Cdd:cd14598   158 HCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDM---LRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
203-306 1.93e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 132.48  E-value: 1.93e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  203 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLI 280
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 1907161252  281 QEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 203-306 1.93e-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: 1.93e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  203 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAGKipEEFNVFNLI 280
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 1907161252  281 QEMRTQRHSAVQTKEQYELVHRAIAQ 306
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 69-304 8.71e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 137.85  E-value: 8.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  69 KEENVKKNRYKDILPFDHSRVKLT-----------------LKTPSQDSD--YINANFIKGVYGPKAYVATQGPLANTVI 129
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkIEVTSEDNAenYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 130 DFWRMIWEYNVVIIVmACREFEMGRKKCERYWPLYGEDPITFAPF--KISCENEQARtdyFIRTLLL---EFQNESRRLY 204
Cdd:PHA02746  128 DFFKLISEHESQVIV-SLTDIDDDDEKCFELWTKEEDSELAFGRFvaKILDIIEELS---FTKTRLMitdKISDTSREIH 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 205 QFHYVNWPDHDVPSSFDSILDMISL-------MRKYQEHEDV---PICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEF 274
Cdd:PHA02746  204 HFWFPDWPDNGIPTGMAEFLELINKvneeqaeLIKQADNDPQtlgPIVVHCSAGIGRAGTFCAID---NALEQLEKEKEV 280

                         250       260       270
                  ....*....|....*....|....*....|
gi 1907161252 275 NVFNLIQEMRTQRHSAVQTKEQYELVHRAI 304
Cdd:PHA02746  281 CLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 102-297 1.22e-32

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: 125.27  E-value: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKG---VYGPKaYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRK-KCERYWPLYGEDPITFApfKIS 177
Cdd:cd17658     1 YINASLVETpasESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFG--RIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 178 CENEQARTDYFIRTL-LLEFQ-NES----RRLYQFHYVNWPDHDVPSSFDSILDMISlmRKYQEHEDV-PICIHCSAGCG 250
Cdd:cd17658    78 VTNKKLKHSQHSITLrVLEVQyIESeeppLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGIPPSAgPIVVHCSAGIG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907161252 251 RTGAICAIDYTWNLLKAGKIpEEFNVFNLIQEMRTQRHSAVQTKEQY 297
Cdd:cd17658   156 RTGAYCTIHNTIRRILEGDM-SAVDLSKTVRKFRSQRIGMVQTQDQY 201
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 102-301 5.29e-28

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: 112.04  E-value: 5.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACrefEMGRKK-CERYWP-----LYGEDPITFapfk 175
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWPektscCYGPIQVEF---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 176 ISCENEQARTDYFIRTLLLEFQNESRRLYQ-FHYVNWPDH-DVPSSFDSILDMISLMRKYQEHED---VPICIHCSAGCG 250
Cdd:cd14634    74 VSADIDEDIISRIFRICNMARPQDGYRIVQhLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDgreGRTVVHCLNGGG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907161252 251 RTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 301
Cdd:cd14634   154 RSGTFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 102-301 1.63e-27

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: 110.50  E-value: 1.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMaCREFEMGrKKCERYWPlyGEDPITFAPFKISCENE 181
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-LNEVDLA-QGCPQYWP--EEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTL----LLEFQNESRRLYQFHYVNWPDH-DVPSSFDSILDMISLMRKYQEHEDV---PICIHCSAGCGRTG 253
Cdd:cd14636    77 SMDCDVISRIFricnLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgegRTIIHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907161252 254 AICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 301
Cdd:cd14636   157 MFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 102-304 5.67e-24

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 100.45  E-value: 5.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCErYWPlYGEDPITFAPFKISCENE 181
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWP-NKDEPINCETFKVTLIAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QAR-----TDYFIRTLLLEFQNESRRLYQFHYV--NWPDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGA 254
Cdd:cd17669    79 EHKclsneEKLIIQDFILEATQDDYVLEVRHFQcpKWPNPDSPIS--KTFELISIIKEEAANRDGPMIVHDEHGGVTAGT 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907161252 255 ICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVqtkEQYELVHRAI 304
Cdd:cd17669   157 FCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDI---EQYQFLYKAI 203
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 102-258 5.34e-21

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 91.61  E-value: 5.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVM--ACREFEmgrkKCERYWPLyGEDPITFAPFKISCE 179
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMltDNELNE----DEPIYWPT-KEKPLECETFKVTLS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 180 NE-----QARTDYFIRTLLLE-----FQNESRrlyQFHYVNWPDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGC 249
Cdd:cd14550    76 GEdhsclSNEIRLIVRDFILEstqddYVLEVR---QFQCPSWPNPCSPIH--TVFELINTVQEWAQQRDGPIVVHDRYGG 150


                  ....*....
gi 1907161252 250 GRTGAICAI 258
Cdd:cd14550   151 VQAATFCAL 159
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 102-301 9.29e-21

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: 91.29  E-value: 9.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMaCREFEMGrKKCERYWPLYGEDpiTFAPFKISCENE 181
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVM-LNDVDPA-QLCPQYWPENGVH--RHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 182 QARTDYFIRTLLL----EFQNESRRLYQFHYVNWPDH-DVPSSFDSILDMISLMRKYQEHED---VPICIHCSAGCGRTG 253
Cdd:cd14635    77 DLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNggeGRTVVHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907161252 254 AICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 301
Cdd:cd14635   157 TFCAISIVCEMLRH---QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 102-304 2.08e-20

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 90.12  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCErYWPlYGEDPITFAPFKIS---- 177
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWP-SREESMNCEAFTVTlisk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 178 ---C-ENEQartDYFIRTLLLEFQNESRRLYQFHYV--NWPDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGR 251
Cdd:cd17670    79 drlClSNEE---QIIIHDFILEATQDDYVLEVRHFQcpKWPNPDAPIS--STFELINVIKEEALTRDGPTIVHDEFGAVS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907161252 252 TGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVqtkEQYELVHRAI 304
Cdd:cd17670   154 AGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDI---EQYQFLYKAM 203
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 102-297 1.36e-19

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: 87.66  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 102 YINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRK-KCERYWPLYGEDpiTFAPFKISCEN 180
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQ--QYGPMEVEFVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 181 EQARTDyfIRTLLLEFQNESRR------LYQFHYVNW-PDHDVPSSFDSILDMISLMRKYQ-EHEDVPICIHCSAGCGRT 252
Cdd:cd14637    79 GSADED--IVTRLFRVQNITRLqeghlmVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQrESGEGRTVVHCLNGGGRS 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907161252 253 GAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 297
Cdd:cd14637   157 GTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQY 198
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 67-305 4.00e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 70.77  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  67 GEKEENVKKNRYKD------ILPFDHSRVKLtlktpSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNV 140
Cdd:PHA02740   42 ANKACAQAENKAKDenlalhITRLLHRRIKL-----FNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 141 VIIVMACREFEmgrKKC-ERYWPLYGEDPITFAPFKISCEnEQARTDYFIRTLLL--EFQNESRRLYQFHYVNWP----D 213
Cdd:PHA02740  117 QIIVLISRHAD---KKCfNQFWSLKEGCVITSDKFQIETL-EIIIKPHFNLTLLSltDKFGQAQKISHFQYTAWPadgfS 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 214 HDVPSSFD---SILDMISLMRKYQEHEDV-PICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHS 289
Cdd:PHA02740  193 HDPDAFIDffcNIDDLCADLEKHKADGKIaPIIIDCIDGISSSAVFCVFDICATEFDKTGM---LSIANALKKVRQKKYG 269

                         250
                  ....*....|....*.
gi 1907161252 290 AVQTKEQYELVHRAIA 305
Cdd:PHA02740  270 CMNCLDDYVFCYHLIA 285
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 76-299 5.38e-10

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: 60.11  E-value: 5.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252  76 NRYKDIlpfdHSRVKLTLKTPsqdsdyINANFIKgVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRK 155
Cdd:cd14559     1 NRFTNI----QTRVSTPVGKN------LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 156 KCERYW-PLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSIL--DMISLMRK 232
Cdd:cd14559    70 GLPPYFrQSGTYGSVTVKSKKTGKDELVDGLKADMYNLKITDGNKTITIPVVHVTNWPDHTAISSEGLKElaDLVNKSAE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 233 --------------YQEHEDVPIcIHCSAGCGRTGAICAIdytwnlLKAGKIPEEFNVFNLIQEMRTQR-HSAVQTKEQY 297
Cdd:cd14559   150 ekrnfykskgssaiNDKNKLLPV-IHCRAGVGRTGQLAAA------MELNKSPNNLSVEDIVSDMRTSRnGKMVQKDEQL 222


                  ..
gi 1907161252 298 EL 299
Cdd:cd14559   223 DT 224
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
205-302 7.20e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 57.67  E-value: 7.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 205 QFHYVNWPDHDVPS--SFDSILDMIslMRKYQEHEdvPICIHCSAGCGRTGAICAidyTWnLLKAGKIPEEfnvfnLIQE 282
Cdd:COG2453    49 EYLHLPIPDFGAPDdeQLQEAVDFI--DEALREGK--KVLVHCRGGIGRTGTVAA---AY-LVLLGLSAEE-----ALAR 115

                          90       100
                  ....*....|....*....|
gi 1907161252 283 MRTQRHSAVQTKEQYELVHR 302
Cdd:COG2453   116 VRAARPGAVETPAQRAFLER 135
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 196-301 3.68e-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: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 196 FQNESRRLYQFhyvNWPDHDVPSsFDSILDMISLMRKYQEhEDVPICIHCSAGCGRTG-AICAIdytwnLLKAGKIPEEf 274
Cdd:cd14506    72 FMRAGIYFYNF---GWKDYGVPS-LTTILDIVKVMAFALQ-EGGKVAVHCHAGLGRTGvLIACY-----LVYALRMSAD- 140

                          90       100
                  ....*....|....*....|....*..
gi 1907161252 275 nvfNLIQEMRTQRHSAVQTKEQYELVH 301
Cdd:cd14506   141 ---QAIRLVRSKRPNSIQTRGQVLCVR 164
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 221-302 1.92e-07

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 50.04  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 221 DSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwnLLKAGKIPeefnVFNLIQEMRTQR-HSAVQTKEQYEL 299
Cdd:cd14494    39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACY----LVLLGGMS----AEEAVRIVRLIRpGGIPQTIEQLDF 110


                  ...
gi 1907161252 300 VHR 302
Cdd:cd14494   111 LIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 203-300 6.24e-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: 49.20  E-value: 6.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 203 LYQFHYVNW-----PDHDVPSsFDSILDMISLMrKYQEHEDVPICIHCSAGCGRTGAICAIdYtwnLLKAGKIPEEfnvf 277
Cdd:cd14504    44 SDTCPGLRYhhipiEDYTPPT-LEQIDEFLDIV-EEANAKNEAVLVHCLAGKGRTGTMLAC-Y---LVKTGKISAV---- 113

                          90       100
                  ....*....|....*....|...
gi 1907161252 278 NLIQEMRTQRHSAVQTKEQYELV 300
Cdd:cd14504   114 DAINEIRRIRPGSIETSEQEKFV 136
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 205-257 3.85e-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: 3.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907161252 205 QFHYVNWPDHDVPSsFDSILDMISLMRKY-QEHEDVPICIHCSAGCGRTGAICA 257
Cdd:cd14497    62 RVLHYGFPDHHPPP-LGLLLEIVDDIDSWlSEDPNNVAVVHCKAGKGRTGTVIC 114
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 200-301 1.47e-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: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 200 SRRLYQ---FHY----VNWPDHDVPSsfdsILDMISLMRKYQEH----EDVPICIHCSAGCGRTG-AICAidytWnLLKA 267
Cdd:cd14510    63 SERGYDpkyFHNrverVPIDDHNVPT----LDEMLSFTAEVREWmaadPKNVVAIHCKGGKGRTGtMVCA----W-LIYS 133

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907161252 268 GKIPEEFNVFNLIQEMRT-----QRHSAVQTKEQYELVH 301
Cdd:cd14510   134 GQFESAKEALEYFGERRTdksvsSKFQGVETPSQSRYVG 172
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 187-302 2.34e-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: 42.25  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 187 YFIRTLLLEFQneSRRLYQFHYVnWPDHDVPSSFDSIL----DMISLMRKYQEhedvpICIHCSAGCGRTGAICAIdytw 262
Cdd:cd14505    59 LGVPDLLEQYQ--QAGITWHHLP-IPDGGVPSDIAQWQelleELLSALENGKK-----VLIHCKGGLGRTGLIAAC---- 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907161252 263 NLLKAG-KIPEEfnvfNLIQEMRTQRHSAVQTKEQYELVHR 302
Cdd:cd14505   127 LLLELGdTLDPE----QAIAAVRALRPGAIQTPKQENFLHQ 163
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 186-258 2.26e-03

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: 39.28  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 186 DYFIRTLL-LEFQNESRRLY-------QFHYVN------WPDHDVPSSFDSILDMISlmrkyqehEDVPICIHCSAGCGR 251
Cdd:cd14529    31 KLGIKTVIdLRGADERAASEeaaakidGVKYVNlplsatRPTESDVQSFLLIMDLKL--------APGPVLIHCKHGKDR 102


                  ....*..
gi 1907161252 252 TGAICAI 258
Cdd:cd14529   103 TGLVSAL 109
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 207-295 3.02e-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: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161252 207 HYVNWP-DHDVPSSFDSILDMISLMR-KYQEHEDVPICIHCSAGCGRTGAICAIdytwNLLKAGKIPEEfnvfnLIQEMR 284
Cdd:cd18537    64 QVLDWPfDDGAPPSNQIVDDWLNLLKvKFREEPGCCIAVHCVAGLGRAPVLVAL----ALIECGMKYED-----AVQFIR 134

                          90
                  ....*....|.
gi 1907161252 285 TQRHSAVQTKE 295
Cdd:cd18537   135 QKRRGAFNSKQ 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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