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Conserved domains on  [gi|808356106|ref|NP_501293|]
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Protein-tyrosine phosphatase [Caenorhabditis elegans]

Protein Classification

tyrosine-protein phosphatase( domain architecture ID 11987518)

tyrosine-protein phosphatase catalyzes the dephosphorylation of phosphotyrosine groups in phosphoproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
76-313 3.34e-93

Protein-tyrosine phosphatase;


:

Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.20  E-value: 3.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106   76 HHKNRYKDVGCLDNNRVKLAHPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGA 155
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  156 KKCSEYYATKEKPELVFHekdqKITVKyeasgTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLS 235
Cdd:pfam00102  82 EKCAQYWPEEEGESLEYG----DFTVT-----LKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  236 IIELLIKAR-----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIeETDKILQKIREQRNNSIQTDHQYLFVHQV 310
Cdd:pfam00102 153 LLDLLRKVRkssldGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEV-DIFQIVKELRSQRPGMVQTLEQYIFLYDA 231


                  ...
gi 808356106  311 MMN 313
Cdd:pfam00102 232 ILE 234
 
Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
76-313 3.34e-93

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.20  E-value: 3.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106   76 HHKNRYKDVGCLDNNRVKLAHPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGA 155
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  156 KKCSEYYATKEKPELVFHekdqKITVKyeasgTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLS 235
Cdd:pfam00102  82 EKCAQYWPEEEGESLEYG----DFTVT-----LKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  236 IIELLIKAR-----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIeETDKILQKIREQRNNSIQTDHQYLFVHQV 310
Cdd:pfam00102 153 LLDLLRKVRkssldGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEV-DIFQIVKELRSQRPGMVQTLEQYIFLYDA 231


                  ...
gi 808356106  311 MMN 313
Cdd:pfam00102 232 ILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
50-313 2.77e-88

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 265.68  E-value: 2.77e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106    50 GLRNEFNAMKR-FNDFDKMQSFKKAQDHHKNRYKDVGCLDNNRVKLAHPP-WPHDYIHANFVSTPANAKRFICAQAPLDN 127
Cdd:smart00194   1 GLEEEFEKLDRlKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106   128 TCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFHekdqKITVkyeasgTVKFVKPTKAVVKETVLIIE 207
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYG----DITV------TLKSVEKVDDYTIRTLEVTN 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106   208 GPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKAR----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIeET 283
Cdd:smart00194 151 TGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRksqsTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV-DI 229

                          250       260       270
                   ....*....|....*....|....*....|
gi 808356106   284 DKILQKIREQRNNSIQTDHQYLFVHQVMMN 313
Cdd:smart00194 230 FEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 103-309 1.25e-59

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: 190.19  E-value: 1.25e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFHEkdqkITVk 182
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGD----ITV- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 yeasgTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKAR----PLKGPIAVHCSAGI 258
Cdd:cd00047   76 -----TLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRkearKPNGPIVVHCSAGV 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808356106 259 GRTGSVVMIEYMCEQLLNGNQIeETDKILQKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd00047  151 GRTGTFIAIDILLERLEAEGEV-DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 72-314 4.05e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 140.52  E-value: 4.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  72 KAQDHHKNRYKDVGCLDNNRVKLAHPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLM 151
Cdd:PHA02742  49 ELKNMKKCRYPDAPCFDRNRVILKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 152 EKGAKKCSEYYATKEKPELVFhekdQKITVKYEASGTVKFVKPTkavvkeTVLIIEGPGGQVLKTTHYHWIDWPDRGVPP 231
Cdd:PHA02742 129 EDGKEACYPYWMPHERGKATH----GEFKIKTKKIKSFRNYAVT------NLCLTDTNTGASLDIKHFAYEDWPHGGLPR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 232 ADLSIIELLIKAR--------PLKG-------PIAVHCSAGIGRTGSVVMIEyMCEQLLNGNQIEETDKILQKIREQRNN 296
Cdd:PHA02742 199 DPNKFLDFVLAVReadlkadvDIKGenivkepPILVHCSAGLDRAGAFCAID-ICISKYNERAIIPLLSIVRDLRKQRHN 277

                        250
                 ....*....|....*...
gi 808356106 297 SIQTDHQYLFVHQVMMNF 314
Cdd:PHA02742 278 CLSLPQQYIFCYFIVLIF 295
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
68-315 2.89e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 113.65  E-value: 2.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  68 QSFKKAQDHHKNRYKDVGCLDNNRVKLAHPpwphdYIHANFVSTPANaKRFICAQAPLDNTCADFWYMCLQERVEAIFML 147
Cdd:COG5599   35 QYLQNINGSPLNRFRDIQPYKETALRANLG-----YLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVLVVL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 148 --CNLMEKGAKKCSEYyatkekpelvFHEKDQKITVKYEASGTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWP 225
Cdd:COG5599  109 asDDEISKPKVKMPVY----------FRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGQKKIEIPVLHVKNWP 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 226 DRGVPPAD------LSIIELLIKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEET-DKILQKIREQRNNSI 298
Cdd:COG5599  179 DHGAISAEalknlaDLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLSvEEIVIDMRTSRNGGM 258

                        250
                 ....*....|....*...
gi 808356106 299 -QTDHQYlfvhQVMMNFF 315
Cdd:COG5599  259 vQTSEQL----DVLVKLA 272
 
Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
76-313 3.34e-93

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.20  E-value: 3.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106   76 HHKNRYKDVGCLDNNRVKLAHPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGA 155
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  156 KKCSEYYATKEKPELVFHekdqKITVKyeasgTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLS 235
Cdd:pfam00102  82 EKCAQYWPEEEGESLEYG----DFTVT-----LKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  236 IIELLIKAR-----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIeETDKILQKIREQRNNSIQTDHQYLFVHQV 310
Cdd:pfam00102 153 LLDLLRKVRkssldGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEV-DIFQIVKELRSQRPGMVQTLEQYIFLYDA 231


                  ...
gi 808356106  311 MMN 313
Cdd:pfam00102 232 ILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
50-313 2.77e-88

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 265.68  E-value: 2.77e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106    50 GLRNEFNAMKR-FNDFDKMQSFKKAQDHHKNRYKDVGCLDNNRVKLAHPP-WPHDYIHANFVSTPANAKRFICAQAPLDN 127
Cdd:smart00194   1 GLEEEFEKLDRlKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106   128 TCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFHekdqKITVkyeasgTVKFVKPTKAVVKETVLIIE 207
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYG----DITV------TLKSVEKVDDYTIRTLEVTN 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106   208 GPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKAR----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIeET 283
Cdd:smart00194 151 TGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRksqsTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV-DI 229

                          250       260       270
                   ....*....|....*....|....*....|
gi 808356106   284 DKILQKIREQRNNSIQTDHQYLFVHQVMMN 313
Cdd:smart00194 230 FEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 103-309 1.25e-59

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: 190.19  E-value: 1.25e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFHEkdqkITVk 182
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGD----ITV- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 yeasgTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKAR----PLKGPIAVHCSAGI 258
Cdd:cd00047   76 -----TLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRkearKPNGPIVVHCSAGV 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808356106 259 GRTGSVVMIEYMCEQLLNGNQIeETDKILQKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd00047  151 GRTGTFIAIDILLERLEAEGEV-DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 50-308 6.70e-51

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: 170.24  E-value: 6.70e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  50 GLRNEFNAMKRFNDFDKMQSFKKAQDHHKNRYKDVGCLDNNRVKLAHP--PWPHDYIHANFVSTPANAKRFICAQAPLDN 127
Cdd:cd14543    4 GIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRngDERTDYINANFMDGYKQKNAYIATQGPLPK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 128 TCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFhekdQKITVKYEAsgtvkfVKPTKAVVKETVLIIE 207
Cdd:cd14543   84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRY----GDLTVTNLS------VENKEHYKKTTLEIHN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 208 GPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKAR-----------------PLKGPIAVHCSAGIGRTGSVVMIEYM 270
Cdd:cd14543  154 TETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRqqqalavkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDIC 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 808356106 271 CEQL-----LNgnqIEETdkiLQKIREQRNNSIQTDHQYLFVH 308
Cdd:cd14543  234 LSQLedvgtLN---VMQT---VRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 75-316 3.34e-45

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: 155.58  E-value: 3.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  75 DHHKNRYKDVGCLDNNRVKLAhpPWP------HDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLC 148
Cdd:cd17667   27 NKHKNRYINILAYDHSRVKLR--PLPgkdskhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 149 NLMEKGAKKCSEYYATKEKPE---LVFHEKDQKI----TVKYEASGTVKFVKPTKAVVKetvliiegpGGQVLKTT-HYH 220
Cdd:cd17667  105 NLVEKGRRKCDQYWPTENSEEygnIIVTLKSTKIhacyTVRRFSIRNTKVKKGQKGNPK---------GRQNERTViQYH 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 221 WIDWPDRGVPPADLSIIELLIKAR----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDkILQKIREQRNN 296
Cdd:cd17667  176 YTQWPDMGVPEYALPVLTFVRRSSaartPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLG-FLKHIRTQRNY 254

                        250       260
                 ....*....|....*....|
gi 808356106 297 SIQTDHQYLFVHQVMMNFFL 316
Cdd:cd17667  255 LVQTEEQYIFIHDALLEAIL 274
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 78-306 9.78e-45

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: 152.93  E-value: 9.78e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLAHPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKK 157
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 158 CSEYYATKEKPELVFHEKDQKITVKYEASG---TVKFVKPTKAVVKETVLIIegpggqvlkttHYHWIDWPDRGVPPADL 234
Cdd:cd14545   81 CAQYWPQGEGNAMIFEDTGLKVTLLSEEDKsyyTVRTLELENLKTQETREVL-----------HFHYTTWPDFGVPESPA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 235 SIIELLIKAR------PLKGPIAVHCSAGIGRTGSVVMIEyMCEQLLNGNQIEETD--KILQKIREQRNNSIQTDHQYLF 306
Cdd:cd14545  150 AFLNFLQKVResgslsSDVGPPVVHCSAGIGRSGTFCLVD-TCLVLIEKGNPSSVDvkKVLLEMRKYRMGLIQTPDQLRF 228
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 103-308 1.12e-44

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: 151.73  E-value: 1.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFhekdqkITVK 182
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGN------IQVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 YE-----ASGTVK-F-VKPTKAVVKETvliiEGPGGQVlktTHYHWIDWPDRGVPPADLSIIELLIKA----RPLKGPIA 251
Cdd:cd14549   75 LLstevlATYTVRtFsLKNLKLKKVKG----RSSERVV---YQYHYTQWPDHGVPDYTLPVLSFVRKSsaanPPGAGPIV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808356106 252 VHCSAGIGRTGSVVMIEYMCEqllngnQIEETDKI-----LQKIREQRNNSIQTDHQYLFVH 308
Cdd:cd14549  148 VHCSAGVGRTGTYIVIDSMLQ------QIQDKGTVnvfgfLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 71-306 2.83e-44

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: 153.26  E-value: 2.83e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  71 KKAQDHHKNRYKDVGCLDNNRVKLAHPPwpHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNL 150
Cdd:cd14608   21 KLPKNKNRNRYRDVSPFDHSRIKLHQED--NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 151 MEKGAKKCSEYYATKEKPELVFHEKDQKITVKYE---ASGTVKFVKPTKAVVKETVLIIegpggqvlkttHYHWIDWPDR 227
Cdd:cd14608   99 MEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEdikSYYTVRQLELENLTTQETREIL-----------HFHYTTWPDF 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 228 GVPPADLSIIELLIKAR------PLKGPIAVHCSAGIGRTGSVVMIEyMCEQLLNGNQIE---ETDKILQKIREQRNNSI 298
Cdd:cd14608  168 GVPESPASFLNFLFKVResgslsPEHGPVVVHCSAGIGRSGTFCLAD-TCLLLMDKRKDPssvDIKKVLLEMRKFRMGLI 246


                 ....*...
gi 808356106 299 QTDHQYLF 306
Cdd:cd14608  247 QTADQLRF 254
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 80-309 1.24e-43

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: 149.81  E-value: 1.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  80 RYKDVGCLDNNRVKL-AHPPWPH-DYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKK 157
Cdd:cd14548    1 RYTNILPYDHSRVKLiPINEEEGsDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 158 CSEYYATKEKPelVFHeKDQKITVKYEASgtvkfvkPTKAVVKEtvLIIEGpGGQVLKTTHYHWIDWPDRGVPPADLSII 237
Cdd:cd14548   81 CDHYWPFDQDP--VYY-GDITVTMLSESV-------LPDWTIRE--FKLER-GDEVRSVRQFHFTAWPDHGVPEAPDSLL 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356106 238 ELLIKAR----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIeETDKILQKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd14548  148 RFVRLVRdyikQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYV-DIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 103-309 1.54e-43

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


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 149.32  E-value: 1.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANA-KRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYatkekPELVFHEKDQKITV 181
Cdd:cd18533    1 YINASYITLPGTSsKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYW-----PSGEYEGEYGDLTV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 182 KYEASgtvKFVKPTKAVVkeTVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIEL------LIKARPLKGPIAVHCS 255
Cdd:cd18533   76 ELVSE---EENDDGGFIV--REFELSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLiklkreLNDSASLDPPIIVHCS 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808356106 256 AGIGRTGSVVMIEYMCEQLLNG-----NQIEETD---KILQKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd18533  151 AGVGRTGTFIALDSLLDELKRGlsdsqDLEDSEDpvyEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 79-309 7.11e-43

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: 147.93  E-value: 7.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  79 NRYKDVGCLDNNRVKLahPPWPHD----YIHANFVSTPANA-KRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEK 153
Cdd:cd14547    1 NRYKTILPNEHSRVCL--PSVDDDplssYINANYIRGYDGEeKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 154 GAkKCSEYYATKEKpelvfhEKDQKITVkyeasgTVKFVKPTKA-VVKETVLIiegPGGQVLKTTHYHWIDWPDRGVPPA 232
Cdd:cd14547   79 KE-KCAQYWPEEEN------ETYGDFEV------TVQSVKETDGyTVRKLTLK---YGGEKRYLKHYWYTSWPDHKTPEA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 233 DLSIIEL------LIKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETdKILQKIREQRNNSIQTDHQYLF 306
Cdd:cd14547  143 AQPLLSLvqeveeARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVL-GIVCQLRLDRGGMVQTAEQYEF 221


                 ...
gi 808356106 307 VHQ 309
Cdd:cd14547  222 VHR 224
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 35-320 1.62e-42

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: 149.31  E-value: 1.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  35 QIVQFVQTTLEKGPIGLRNEFNAMKRFNDFDKMQSF------KKAQDHHKNRYKDVGCLDNNRVKLA--HPPWPHDYIHA 106
Cdd:cd14604   11 ERVQAMKSTDHNGEDNFASDFMRLRRLSTKYRTEKIyptatgEKEENVKKNRYKDILPFDHSRVKLTlkTSSQDSDYINA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 107 NFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFHEKdqKITVKYEAS 186
Cdd:cd14604   91 NFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPF--RISCEAEQA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 187 GTVKFVKptkavvketVLIIEGPgGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKARPLKG----PIAVHCSAGIGRTG 262
Cdd:cd14604  169 RTDYFIR---------TLLLEFQ-NETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEhedvPICIHCSAGCGRTG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 263 SVVMIEYMCEQLLNGNQIEETD--KILQKIREQRNNSIQTDHQYLFVHQVMMNFFlEKKL 320
Cdd:cd14604  239 AICAIDYTWNLLKAGKIPEEFNvfNLIQEMRTQRHSAVQTKEQYELVHRAIAQLF-EKQL 297
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 71-306 2.29e-42

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: 147.81  E-value: 2.29e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  71 KKAQDHHKNRYKDVGCLDNNRVKLAHPPwpHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNL 150
Cdd:cd14607   20 KYPENRNRNRYRDVSPYDHSRVKLQNTE--NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 151 MEKGAKKCSEYYATKEKPELVFHEKDQKITVKYE---ASGTVKFVKPTKAVVKETVLIiegpggqvlktTHYHWIDWPDR 227
Cdd:cd14607   98 VEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEdvkSYYTVHLLQLENINSGETRTI-----------SHFHYTTWPDF 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 228 GVPPADLSIIELLIKAR------PLKGPIAVHCSAGIGRTGSVVMIEyMCEQLLNGNQIEETD--KILQKIREQRNNSIQ 299
Cdd:cd14607  167 GVPESPASFLNFLFKVResgslsPEHGPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSVDikQVLLDMRKYRMGLIQ 245


                 ....*..
gi 808356106 300 TDHQYLF 306
Cdd:cd14607  246 TPDQLRF 252
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 103-312 2.32e-42

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: 146.28  E-value: 2.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPE---LVFHEKDQKI 179
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEygnFLVTQKSVQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 180 TVKYEASG-TVKFVKPTKAVVKETvliiegPGGQVLktTHYHWIDWPDRGVPPADLSIIELLIKARPLK----GPIAVHC 254
Cdd:cd17668   81 LAYYTVRNfTLRNTKIKKGSQKGR------PSGRVV--TQYHYTQWPDMGVPEYTLPVLTFVRKASYAKrhavGPVVVHC 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356106 255 SAGIGRTGSVVMIEYMCEQLlngnQIEETDKI---LQKIREQRNNSIQTDHQYLFVHQVMM 312
Cdd:cd17668  153 SAGVGRTGTYIVLDSMLQQI----QHEGTVNIfgfLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 78-315 3.10e-42

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: 147.66  E-value: 3.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLA--HPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGA 155
Cdd:cd14603   33 KNRYKDILPYDQTRVILSllQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIEMGK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 156 KKCSEYYATKEKPeLVFhekdQKITVKyeasgTVKFVKPTKAVVKETVLIIEGPGGQVLktTHYHWIDWPDRGVPPADLS 235
Cdd:cd14603  113 KKCERYWAQEQEP-LQT----GPFTIT-----LVKEKRLNEEVILRTLKVTFQKESRSV--SHFQYMAWPDHGIPDSPDC 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 236 IIELLIKARPLKG----PIAVHCSAGIGRTGSVVMIEYMcEQLLNGNQIEETDKILQ---KIREQRNNSIQTDHQYLFVH 308
Cdd:cd14603  181 MLAMIELARRLQGsgpePLCVHCSAGCGRTGVICTVDYV-RQLLLTQRIPPDFSIFDvvlEMRKQRPAAVQTEEQYEFLY 259


                 ....*..
gi 808356106 309 QVMMNFF 315
Cdd:cd14603  260 HTVAQMF 266
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 79-314 5.59e-41

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: 143.11  E-value: 5.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  79 NRYKDVGCLDNNRVKLA--HPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAK 156
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKpiHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 157 KCSEYYATKEKPELvfHEkDQKITVKYEAsgtvkfVKPTKAVVKETVLIIEGPGGQVLKttHYHWIDWPDRGVPPADLSI 236
Cdd:cd14619   81 KCEHYWPLDYTPCT--YG-HLRVTVVSEE------VMENWTVREFLLKQVEEQKTLSVR--HFHFTAWPDHGVPSSTDTL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 237 IEL------LIKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQlLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQV 310
Cdd:cd14619  150 LAFrrllrqWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQ-LQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQC 228


                 ....
gi 808356106 311 MMNF 314
Cdd:cd14619  229 ILDF 232
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 79-313 4.22e-40

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: 140.72  E-value: 4.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  79 NRYKDVGCLDNNRVKLAHPPWPH-DYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKK 157
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTdDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 158 CSEYYATKEKPELvfhekdQKITVkyeaSGTVKFVKPTKAVVKETVLIIEGpgGQVLKTTHYHWIDWPDRGVPpadlSII 237
Cdd:cd14615   81 CEEYWPSKQKKDY------GDITV----TMTSEIVLPEWTIRDFTVKNAQT--NESRTVRHFHFTSWPDHGVP----ETT 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 238 ELLIKAR----------PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIeETDKILQKIREQRNNSIQTDHQYLFV 307
Cdd:cd14615  145 DLLINFRhlvreymkqnPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVV-DVYGIVYDLRMHRPLMVQTEDQYVFL 223


                 ....*.
gi 808356106 308 HQVMMN 313
Cdd:cd14615  224 NQCALD 229
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 103-309 2.51e-39

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: 137.94  E-value: 2.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFheKDQKIT-V 181
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQF--GPFKISlE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 182 KYEASGTVKFVKPTKAVVKETVLIIegpggqvlktTHYHWIDWPDRGVPPADLSIIELLIKARPLKG----PIAVHCSAG 257
Cdd:cd14542   79 KEKRVGPDFLIRTLKVTFQKESRTV----------YQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGsedvPICVHCSAG 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 808356106 258 IGRTGSVVMIEYMCEQLLNGNQIEETD--KILQKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd14542  149 CGRTGTICAIDYVWNLLKTGKIPEEFSlfDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 71-317 2.53e-39

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: 139.99  E-value: 2.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  71 KKAQDHHKNRYKDVGCLDNNRVKLAHPpwpHDYIHANFVST-PANAK---RFICAQAPLDNTCADFWYMCLQERVEAIFM 146
Cdd:cd14600   36 KLPQNMDKNRYKDVLPYDATRVVLQGN---EDYINASYVNMeIPSANivnKYIATQGPLPHTCAQFWQVVWEQKLSLIVM 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 147 LCNLMEKGAKKCSEYYAtkEKPELVFHEKDQkITVKYEASgtvkfvkpTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPD 226
Cdd:cd14600  113 LTTLTERGRTKCHQYWP--DPPDVMEYGGFR-VQCHSEDC--------TIAYVFREMLLTNTQTGEERTVTHLQYVAWPD 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 227 RGVPPADLSIIELLIKARPLK---GPIAVHCSAGIGRTGSVVMIEY-MCeqLLNGNQIEETDKILQKIREQRNNSIQTDH 302
Cdd:cd14600  182 HGVPDDSSDFLEFVNYVRSKRvenEPVLVHCSAGIGRTGVLVTMETaMC--LTERNQPVYPLDIVRKMRDQRAMMVQTSS 259

                        250
                 ....*....|....*
gi 808356106 303 QYLFVHQVMMNFFLE 317
Cdd:cd14600  260 QYKFVCEAILRVYEE 274
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 72-314 4.05e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 140.52  E-value: 4.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  72 KAQDHHKNRYKDVGCLDNNRVKLAHPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLM 151
Cdd:PHA02742  49 ELKNMKKCRYPDAPCFDRNRVILKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 152 EKGAKKCSEYYATKEKPELVFhekdQKITVKYEASGTVKFVKPTkavvkeTVLIIEGPGGQVLKTTHYHWIDWPDRGVPP 231
Cdd:PHA02742 129 EDGKEACYPYWMPHERGKATH----GEFKIKTKKIKSFRNYAVT------NLCLTDTNTGASLDIKHFAYEDWPHGGLPR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 232 ADLSIIELLIKAR--------PLKG-------PIAVHCSAGIGRTGSVVMIEyMCEQLLNGNQIEETDKILQKIREQRNN 296
Cdd:PHA02742 199 DPNKFLDFVLAVReadlkadvDIKGenivkepPILVHCSAGLDRAGAFCAID-ICISKYNERAIIPLLSIVRDLRKQRHN 277

                        250
                 ....*....|....*...
gi 808356106 297 SIQTDHQYLFVHQVMMNF 314
Cdd:PHA02742 278 CLSLPQQYIFCYFIVLIF 295
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 78-317 5.33e-39

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: 138.75  E-value: 5.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLA---HPPWPHDYIHANFVSTP-------ANAKRFICAQAPLDNTCADFWYMCLQERVEAIFML 147
Cdd:cd14544    4 KNRYKNILPFDHTRVILKdrdPNVPGSDYINANYIRNEnegpttdENAKTYIATQGCLENTVSDFWSMVWQENSRVIVMT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 148 CNLMEKGAKKCSEYYatkekPELVFHEKDQKITVKyeasgTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDR 227
Cdd:cd14544   84 TKEVERGKNKCVRYW-----PDEGMQKQYGPYRVQ-----NVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDH 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 228 GVPPADLSIIELL------IKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETD--KILQKIREQRNNSIQ 299
Cdd:cd14544  154 GVPSDPGGVLNFLedvnqrQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDiqKTIQMVRSQRSGMVQ 233

                        250
                 ....*....|....*...
gi 808356106 300 TDHQYLFVHqVMMNFFLE 317
Cdd:cd14544  234 TEAQYKFIY-VAVAQYIE 250
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 102-307 3.81e-38

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: 135.15  E-value: 3.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 102 DYIHANFVST--PANA--KRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYatkekPELvfHEKDQ 177
Cdd:cd14541    1 DYINANYVNMeiPGSGivNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYW-----PDL--GETMQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 178 ----KITVKYEasgtvkfvKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKARPLKG----P 249
Cdd:cd14541   74 fgnlQITCVSE--------EVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVgmveP 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 808356106 250 IAVHCSAGIGRTGSVVMIEY-MCeqLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFV 307
Cdd:cd14541  146 TVVHCSAGIGRTGVLITMETaMC--LIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV 202
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 77-308 8.24e-38

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: 135.22  E-value: 8.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  77 HKNRYKDVGCLDNNRVKLAHPPW--PHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKG 154
Cdd:cd14553    5 PKNRYANVIAYDHSRVILQPIEGvpGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 155 AKKCSEYYATKEKpelvfhEKDQKITVkyeasgTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADL 234
Cdd:cd14553   85 RVKCDQYWPTRGT------ETYGLIQV------TLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPT 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808356106 235 SIIELLIKAR----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKIlQKIREQRNNSIQTDHQYLFVH 308
Cdd:cd14553  153 PFLAFLRRVKacnpPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHV-TCLRAQRNYMVQTEDQYIFIH 229
PHA02738 PHA02738
hypothetical protein; Provisional
 79-311 2.38e-36

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 133.51  E-value: 2.38e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  79 NRYKDVGCLDNNRVKLAHPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKC 158
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKC 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 159 SEYYATKEKPELVFHekdqkitvKYEASGTVkfVKPTKAVVKETVLIIEGPGGqVLKTTHYHWIDWPDRGVPPADLSIIE 238
Cdd:PHA02738 133 FPYWSDVEQGSIRFG--------KFKITTTQ--VETHPHYVKSTLLLTDGTSA-TQTVTHFNFTAWPDHDVPKNTSEFLN 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 239 LLIKARPLKG-----------------PIAVHCSAGIGRTGSVVMIEYMCEQlLNGNQIEETDKILQKIREQRNNSIQTD 301
Cdd:PHA02738 202 FVLEVRQCQKelaqeslqighnrlqppPIVVHCNAGLGRTPCYCVVDISISR-FDACATVSIPSIVSSIRNQRYYSLFIP 280

                        250
                 ....*....|
gi 808356106 302 HQYLFVHQVM 311
Cdd:PHA02738 281 FQYFFCYRAV 290
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 78-315 5.56e-36

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: 130.35  E-value: 5.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLA--HPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGA 155
Cdd:cd14602    1 KNRYKDILPYDHSRVELSliTSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 156 KKCSEYYAtkEKPELVFHEKDQKITVKYEASGTVKFVKPTKAVVKETVLIIEgpggqvlkttHYHWIDWPDRGVPPADLS 235
Cdd:cd14602   81 KKCERYWA--EPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIY----------QFHYKNWPDHDVPSSIDP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 236 IIELLIKARPLKG----PIAVHCSAGIGRTGSVVMIEYMCeQLLNGNQIEETDKI---LQKIREQRNNSIQTDHQYLFVH 308
Cdd:cd14602  149 ILELIWDVRCYQEddsvPICIHCSAGCGRTGVICAIDYTW-MLLKDGIIPENFSVfslIQEMRTQRPSLVQTKEQYELVY 227


                 ....*..
gi 808356106 309 QVMMNFF 315
Cdd:cd14602  228 NAVIELF 234
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 103-312 5.81e-36

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: 129.42  E-value: 5.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAK--RFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFHEKDQKIT 180
Cdd:cd14538    1 YINASHIRIPVGGDtyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 181 VKYEAsgtvkfvkpTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKARPL--KGPIAVHCSAGI 258
Cdd:cd14538   81 EKYQS---------LQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIhnSGPIVVHCSAGI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356106 259 GRTGSVV-------MIEYMCEQLLNgnqieetdKILQKIREQRNNSIQTDHQYLFVHQVMM 312
Cdd:cd14538  152 GRTGVLItidvalgLIERDLPFDIQ--------DIVKDLREQRQGMIQTKDQYIFCYKACL 204
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 74-314 6.67e-36

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: 130.52  E-value: 6.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  74 QDHHKNRYKDVGCLDNNRVKL--AHPPWP-HDYIHANFV--------STPANAKRFICAQAPLDNTCADFWYMCLQERVE 142
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLhdGDPNEPvSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 143 AIFMLCNLMEKGAKKCSEYYatkekPElvfhekdqKITVKYEASGTVKFVKPTKA---VVKETVLIIEGPGGQVLKTTHY 219
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYW-----PD--------EYALKEYGVMRVRNVKESAAhdyILRELKLSKVGQGNTERTVWQY 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 220 HWIDWPDRGVPPADLSIIELLIKARPLK------GPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETD--KILQKIR 291
Cdd:cd14605  148 HFRTWPDHGVPSDPGGVLDFLEEVHHKQesimdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDvpKTIQMVR 227

                        250       260
                 ....*....|....*....|...
gi 808356106 292 EQRNNSIQTDHQYLFVHQVMMNF 314
Cdd:cd14605  228 SQRSGMVQTEAQYRFIYMAVQHY 250
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 103-306 1.63e-35

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: 127.97  E-value: 1.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPA--NAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAK-KCSEYYATKEKPELVFhekdQKI 179
Cdd:cd17658    1 YINASLVETPAseSLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREF----GRI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 180 TVkyeasgTVKFVKPTKAVVKETVL---IIEGPGgQVLKTTHYHWIDWPDRGVPPADLSIIELLIKAR---PLKGPIAVH 253
Cdd:cd17658   77 SV------TNKKLKHSQHSITLRVLevqYIESEE-PPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYgipPSAGPIVVH 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808356106 254 CSAGIGRTGSVVMIEYMCEQLLNGNqIEETD--KILQKIREQRNNSIQTDHQYLF 306
Cdd:cd17658  150 CSAGIGRTGAYCTIHNTIRRILEGD-MSAVDlsKTVRKFRSQRIGMVQTQDQYIF 203
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 103-309 6.73e-35

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: 126.57  E-value: 6.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYY---ATKEKPELVFHEKDQKI 179
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWpdqGCWTYGNLRVRVEDTVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 180 TVKYeasgtvkfvkptkaVVKETVLIIEGPGG---QVLKTTHYHWIDWPDRGVPPADLSIIELLIKAR----PLKGPIAV 252
Cdd:cd14551   81 LVDY--------------TTRKFCIQKVNRGIgekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKsanpPRAGPIVV 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 808356106 253 HCSAGIGRTGSVVMIEYMCEqLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd14551  147 HCSAGVGRTGTFIVIDAMLD-MMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 74-312 1.52e-34

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: 126.48  E-value: 1.52e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  74 QDHHKNRYKDVGCLDNNRVKLAHPpwpHDYIHANFVSTPANAKRF--ICAQAPLDNTCADFWYMCLQERVEAIFMLCNLM 151
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLGDE---GGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 152 EKGAKKCSEYYATKEKPELVFHEKDQKITVKYEAsgtvkfvkpTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVP- 230
Cdd:cd14597   79 EGGKIKCQRYWPEILGKTTMVDNRLQLTLVRMQQ---------LKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPs 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 231 -PADLSIIELLIKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEqLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd14597  150 qPEQLLTFISYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLG-LISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                 ...
gi 808356106 310 VMM 312
Cdd:cd14597  229 VIL 231
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
217-313 1.17e-33

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 119.77  E-value: 1.17e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106   217 THYHWIDWPDRGVPPADLSIIELL------IKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKILQKI 290
Cdd:smart00404   3 KHYHYTGWPDHGVPESPDSILELLravkknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVKEL 82

                           90       100
                   ....*....|....*....|...
gi 808356106   291 REQRNNSIQTDHQYLFVHQVMMN 313
Cdd:smart00404  83 RSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 217-313 1.17e-33

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: 119.77  E-value: 1.17e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106   217 THYHWIDWPDRGVPPADLSIIELL------IKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKILQKI 290
Cdd:smart00012   3 KHYHYTGWPDHGVPESPDSILELLravkknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVKEL 82

                           90       100
                   ....*....|....*....|...
gi 808356106   291 REQRNNSIQTDHQYLFVHQVMMN 313
Cdd:smart00012  83 RSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 74-312 1.20e-33

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: 124.37  E-value: 1.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  74 QDHHKNRYKDVGCLDNNRVKLAHPPW-PH-DYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLM 151
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGdPHsDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 152 EKGAKKCSEYYatkekPELVFHEKDQKITVKYeasgtvkfVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPP 231
Cdd:cd14630   82 EVGRVKCVRYW-----PDDTEVYGDIKVTLIE--------TEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPC 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 232 ADLSIIELLIKAR----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKIlQKIREQRNNSIQTDHQYLFV 307
Cdd:cd14630  149 YATGLLGFVRQVKflnpPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCV-RELRAQRVNMVQTEEQYVFV 227


                 ....*
gi 808356106 308 HQVMM 312
Cdd:cd14630  228 HDAIL 232
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 79-312 1.22e-33

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: 123.90  E-value: 1.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  79 NRYKDVGCLDNNRVKLAH-PPWPH-DYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAK 156
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQlGGEPHsDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 157 KCSEYYATKEKPELVFHEKDQKITVKYEASGTVKFVKPTKAVVKETvliiegpggqvLKTTHYHWIDWPDRGVPPADLSI 236
Cdd:cd14618   81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE-----------RRVKHLHYTAWPDHGIPESTSSL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 237 I---ELL---IKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQlLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQV 310
Cdd:cd14618  150 MafrELVrehVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQ-LKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                 ..
gi 808356106 311 MM 312
Cdd:cd14618  229 IL 230
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 51-316 3.08e-33

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: 124.75  E-value: 3.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  51 LRNEFNAMKRFNDFDKMQSFKKAQDHHKNRYKDVGCLDNNRVKLAHPPW--PHDYIHANFVSTPANAKRFICAQAPLDNT 128
Cdd:cd14621   28 FREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvpDSDYINASFINGYQEKNKFIAAQGPKEET 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 129 CADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATK---EKPELVFHEKDQKITVKY-------EASGTVKFVKPTKAV 198
Cdd:cd14621  108 VNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQgcwTYGNIRVSVEDVTVLVDYtvrkfciQQVGDVTNKKPQRLI 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 199 vketvliiegpggqvlktTHYHWIDWPDRGVPPADLSIIELLIKAR----PLKGPIAVHCSAGIGRTGSVVMIEYMCEqL 274
Cdd:cd14621  188 ------------------TQFHFTSWPDFGVPFTPIGMLKFLKKVKncnpQYAGAIVVHCSAGVGRTGTFIVIDAMLD-M 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 808356106 275 LNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMMNFFL 316
Cdd:cd14621  249 MHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYL 290
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 70-321 4.30e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 125.14  E-value: 4.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  70 FKKAQDHHKNRYKDVGCLDNNRVKL-AHPPWP--------------------HDYIHANFVSTPANAKRFICAQAPLDNT 128
Cdd:PHA02746  46 FLKKENLKKNRFHDIPCWDHSRVVInAHESLKmfdvgdsdgkkievtsednaENYIHANFVDGFKEANKFICAQGPKEDT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 129 CADFWYMCLQERVEAIFMLCNLmEKGAKKCSEYYATKEKPELVFHEKDQKI-TVKYEASGTVKFVKPTKaVVKETVLIIe 207
Cdd:PHA02746 126 SEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEDSELAFGRFVAKIlDIIEELSFTKTRLMITD-KISDTSREI- 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 208 gpggqvlktTHYHWIDWPDRGVPPADLSIIELLIK-----ARPLK---------GPIAVHCSAGIGRTGSVVMIEYMCEQ 273
Cdd:PHA02746 203 ---------HHFWFPDWPDNGIPTGMAEFLELINKvneeqAELIKqadndpqtlGPIVVHCSAGIGRAGTFCAIDNALEQ 273

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 808356106 274 LLNGNQIEETDKILqKIREQRNNSIQTDHQYLFVHQVMMNFFLE--KKLF 321
Cdd:PHA02746 274 LEKEKEVCLGEIVL-KIRKQRHSSVFLPEQYAFCYKALKYAIIEeaKKKF 322
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 71-314 5.68e-33

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: 123.07  E-value: 5.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  71 KKAQDHHKNRYKDVGCLDNNRVKL--AHPPWP-HDYIHANFV-----STPANAKRFICAQAPLDNTCADFWYMCLQERVE 142
Cdd:cd14606   14 QRPENKSKNRYKNILPFDHSRVILqgRDSNIPgSDYINANYVknqllGPDENAKTYIASQGCLEATVNDFWQMAWQENSR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 143 AIFMLCNLMEKGAKKCSEYYatkekPELVFHEKDQKITVKYEASGTVKFVKptkavVKETVLIIEGPGGQVLKTTHYHWI 222
Cdd:cd14606   94 VIVMTTREVEKGRNKCVPYW-----PEVGMQRAYGPYSVTNCGEHDTTEYK-----LRTLQVSPLDNGELIREIWHYQYL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 223 DWPDRGVPPADLSIIELLIKAR------PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETD--KILQKIREQR 294
Cdd:cd14606  164 SWPDHGVPSEPGGVLSFLDQINqrqeslPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDiqKTIQMVRAQR 243

                        250       260
                 ....*....|....*....|
gi 808356106 295 NNSIQTDHQYLFVHQVMMNF 314
Cdd:cd14606  244 SGMVQTEAQYKFIYVAIAQF 263
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 78-312 7.43e-33

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: 123.22  E-value: 7.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLAH----PPwpHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEK 153
Cdd:cd14626   44 KNRYANVIAYDHSRVILTSvdgvPG--SDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEK 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 154 GAKKCSEYYATKEKPELVFHEKDQKITVKYeASGTVKfvkptkavvkeTVLIIEGPGGQVLKTTHYHWIDWPDRGVPPAD 233
Cdd:cd14626  122 SRVKCDQYWPIRGTETYGMIQVTLLDTVEL-ATYSVR-----------TFALYKNGSSEKREVRQFQFMAWPDHGVPEYP 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 234 LSIIELLIKAR----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLlngnQIEETDKILQKI---REQRNNSIQTDHQYLF 306
Cdd:cd14626  190 TPILAFLRRVKacnpPDAGPMVVHCSAGVGRTGCFIVIDAMLERM----KHEKTVDIYGHVtcmRSQRNYMVQTEDQYIF 265


                 ....*.
gi 808356106 307 VHQVMM 312
Cdd:cd14626  266 IHEALL 271
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 78-311 9.29e-33

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: 122.28  E-value: 9.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLAHPPwPHD----YIHANFV-STPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLME 152
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPD-QDDplssYINANYIrGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 153 KGaKKCSEYYATKEkpelvfhekdqkitVKYEA-SGTVKFVKPTKAVVKEtvLIIEGPGGQVLKTTHYHWIDWPDRGVP- 230
Cdd:cd14613  107 MN-EKCTEYWPEEQ--------------VTYEGiEITVKQVIHADDYRLR--LITLKSGGEERGLKHYWYTSWPDQKTPd 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 231 --PADLSII----ELLIKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEetdkILQ---KIREQRNNSIQTD 301
Cdd:cd14613  170 naPPLLQLVqeveEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVD----ILRttcQLRLDRGGMIQTC 245

                        250
                 ....*....|
gi 808356106 302 HQYLFVHQVM 311
Cdd:cd14613  246 EQYQFVHHVL 255
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 78-309 9.43e-33

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: 121.92  E-value: 9.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLA--HPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGA 155
Cdd:cd14614   15 KNRYTNILPYDFSRVKLVsmHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 156 KKCSEYYATKEKP--------ELVFHEKDQKITVKyeaSGTVKFVKPTKAVvketvliiegpggqvlktTHYHWIDWPDR 227
Cdd:cd14614   95 VKCDHYWPFTEEPvaygditvEMLSEEEQPDWAIR---EFRVSYADEVQDV------------------MHFNYTAWPDH 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 228 GVPPADL--SIIEL--LIKARPLK--GPIAVHCSAGIGRTGSVVMIEYMCeQLLNGNQIEETDKILQKIREQRNNSIQTD 301
Cdd:cd14614  154 GVPTANAaeSILQFvqMVRQQAVKskGPMIIHCSAGVGRTGTFIALDRLL-QHIRDHEFVDILGLVSEMRSYRMSMVQTE 232


                 ....*...
gi 808356106 302 HQYLFVHQ 309
Cdd:cd14614  233 EQYIFIHQ 240
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 79-309 1.37e-32

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: 121.17  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  79 NRYKDVGCLDNNRVKLAHPPWP--HDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAK 156
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVpgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 157 KCSEYYATKEKPELVFHE-KDQKITVKYEASGTVKFVKPTKAvvketvliiegpgGQVLKTTHYHWIDWPDRGVPPADLS 235
Cdd:cd14616   81 RCHQYWPEDNKPVTVFGDiVITKLMEDVQIDWTIRDLKIERH-------------GDYMMVRQCNFTSWPEHGVPESSAP 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808356106 236 IIEL--LIKA-RPLKG-PIAVHCSAGIGRTGSVVMIEYMCeQLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd14616  148 LIHFvkLVRAsRAHDNtPMIVHCSAGVGRTGVFIALDHLT-QHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 52-320 1.72e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 123.19  E-value: 1.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  52 RNEFNAMKRFND---------FDKM-QSFKKAQDHHKNRYKDVGCLDNNRVKL-AHPPWPHDYIHANFVSTPANAKRFIC 120
Cdd:PHA02747  18 RNQLNCFGIIRDehhqiilkpFDGLiANFEKPENQPKNRYWDIPCWDHNRVILdSGGGSTSDYIHANWIDGFEDDKKFIA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 121 AQAPLDNTCADFWYMCLQERVEAIFMLC-NLMEKGAKKCSEYYATKEKPELV---FHEKDQKITvkyeasgtvkfVKPTk 196
Cdd:PHA02747  98 TQGPFAETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDmedFRIETLKTS-----------VRAK- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 197 aVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVP---PADLSIIELLIKARPLKG-----------PIAVHCSAGIGRTG 262
Cdd:PHA02747 166 -YILTLIEITDKILKDSRKISHFQCSEWFEDETPsdhPDFIKFIKIIDINRKKSGklfnpkdallcPIVVHCSDGVGKTG 244

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 263 SVVMIEYMCEQLLNGNQIeETDKILQKIREQRNNSIQTDHQYLFVHQV--MMNFFLEKKL 320
Cdd:PHA02747 245 IFCAVDICLNQLVKRKAI-CLAKTAEKIREQRHAGIMNFDDYLFIQPGyeVLHYFLSKIK 303
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 81-312 4.66e-32

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: 119.66  E-value: 4.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  81 YKDVGCLDNNRVKLAH----PPwpHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAK 156
Cdd:cd14620    1 YPNILPYDHSRVILSQldgiPC--SDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 157 KCSEYYATK------------EKPELVFHEKDQKITVKYEASGTVKfvkPTKAVvketvliiegpggqvlktTHYHWIDW 224
Cdd:cd14620   79 KCYQYWPDQgcwtygnirvavEDCVVLVDYTIRKFCIQPQLPDGCK---APRLV------------------TQLHFTSW 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 225 PDRGVPPADLSIIELLIKARPLK----GPIAVHCSAGIGRTGSVVMIEYMCEqLLNGNQIEETDKILQKIREQRNNSIQT 300
Cdd:cd14620  138 PDFGVPFTPIGMLKFLKKVKSVNpvhaGPIVVHCSAGVGRTGTFIVIDAMID-MMHAEQKVDVFEFVSRIRNQRPQMVQT 216

                        250
                 ....*....|..
gi 808356106 301 DHQYLFVHQVMM 312
Cdd:cd14620  217 DMQYSFIYQALL 228
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 69-312 7.56e-32

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: 120.53  E-value: 7.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  69 SFKKAQDHHKNRYKDVGCLDNNRVKLA--HPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFM 146
Cdd:cd14633   34 SAKKDENRMKNRYGNIIAYDHSRVRLQpiEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIM 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 147 LCNLMEKGAKKCSEYYatkekPELVFHEKDQKITVkYEASGTVKFVKPTKAVVKETVliiegpgGQVLKTTHYHWIDWPD 226
Cdd:cd14633  114 VTNLVEVGRVKCCKYW-----PDDTEIYKDIKVTL-IETELLAEYVIRTFAVEKRGV-------HEIREIRQFHFTGWPD 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 227 RGVPPADLSIIELL--IKAR--PLKGPIAVHCSAGIGRTGSVVMIEYMCEqLLNGNQIEETDKILQKIREQRNNSIQTDH 302
Cdd:cd14633  181 HGVPYHATGLLGFVrqVKSKspPNAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSRRVNMVQTEE 259

                        250
                 ....*....|
gi 808356106 303 QYLFVHQVMM 312
Cdd:cd14633  260 QYVFIHDAIL 269
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 103-309 1.38e-31

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: 117.62  E-value: 1.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFHEkdqkITVK 182
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGD----VVVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 YEASgtvkfvKPTKAVVKETVLIIEGP-GGQVLKTTHYHWIDWPDRGVPPADlsiiELLIKARP--------LKGPIAVH 253
Cdd:cd14557   77 INEE------KICPDYIIRKLNINNKKeKGSGREVTHIQFTSWPDHGVPEDP----HLLLKLRRrvnafnnfFSGPIVVH 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 808356106 254 CSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKILqKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd14557  147 CSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVV-KLRRQRCLMVQVEAQYILIHQ 201
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 78-311 5.76e-31

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: 117.24  E-value: 5.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKL---AHPPWPHDYIHANFVSTPANAKR-FICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEK 153
Cdd:cd14612   18 KDRYKTILPNPQSRVCLrraGSQEEEGSYINANYIRGYDGKEKaYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 154 gAKKCSEYYATKEKPELVFHEKDQKITvkyEASGTVkfvkptkavVKETVLIIEGPGGQVlktTHYHWIDWPDRGVPPAD 233
Cdd:cd14612   98 -KEKCVHYWPEKEGTYGRFEIRVQDMK---ECDGYT---------IRDLTIQLEEESRSV---KHYWFSSWPDHQTPESA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 234 LSIIELLI------KARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLlngnqiEETDK-----ILQKIREQRNNSIQTDH 302
Cdd:cd14612  162 GPLLRLVAeveesrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQL------KDTGKvdilgIVCQLRLDRGGMIQTSE 235


                 ....*....
gi 808356106 303 QYLFVHQVM 311
Cdd:cd14612  236 QYQFLHHTL 244
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 79-309 8.61e-31

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: 116.17  E-value: 8.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  79 NRYKDVGCLDNNRVKLAHPPWP--HDYIHANFVstPANAKR--FICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKG 154
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDpcSDYINASYI--PGNNFRreYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 155 AKKCSEYYATKEKP----ELVFHEKDQKITVKYeasgTVKFVKPTKAVVKETVLIIEgpggqvlkttHYHWIDWPDRGVP 230
Cdd:cd14617   79 RVKCDHYWPADQDSlyygDLIVQMLSESVLPEW----TIREFKICSEEQLDAPRLVR----------HFHYTVWPDHGVP 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 231 PADLSIIELLIKAR------PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIeETDKILQKIREQRNNSIQTDHQY 304
Cdd:cd14617  145 ETTQSLIQFVRTVRdyinrtPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSV-DIYGAVHDLRLHRVHMVQTECQY 223


                 ....*
gi 808356106 305 LFVHQ 309
Cdd:cd14617  224 VYLHQ 228
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 103-314 1.49e-30

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: 115.25  E-value: 1.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVS-TPANAKRF-ICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYY--ATKEKPELVFHEkdQK 178
Cdd:cd14540    1 YINASHITaTVGGKQRFyIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptLGGEHDALTFGE--YK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 179 ITVKYEASgTVKFVKpTKAVVKETvliiegPGGQVLKTTHYHWIDWPDRGVPPAD---LSIIE-------LLIKARPLKG 248
Cdd:cd14540   79 VSTKFSVS-SGCYTT-TGLRVKHT------LSGQSRTVWHLQYTDWPDHGCPEDVsgfLDFLEeinsvrrHTNQDVAGHN 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356106 249 ---PIAVHCSAGIGRTGSVVMIEYMCEQLLNgNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMMNF 314
Cdd:cd14540  151 rnpPTLVHCSAGVGRTGVVILADLMLYCLDH-NEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 103-312 5.83e-30

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: 113.47  E-value: 5.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYatkekPELVFHEKDQKITVk 182
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYW-----PDDTEVYGDIKVTL- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 YEASGTVKFVKPTKAVVKETVliiegpgGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKAR----PLKGPIAVHCSAGI 258
Cdd:cd14555   75 VETEPLAEYVVRTFALERRGY-------HEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKasnpPSAGPIVVHCSAGA 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 808356106 259 GRTGSVVMIEYMCEqLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMM 312
Cdd:cd14555  148 GRTGCYIVIDIMLD-MAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 103-312 1.12e-29

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: 112.92  E-value: 1.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAK--RFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYA-TKEKPELVfhEKDQKI 179
Cdd:cd14596    1 YINASYITMPVGEEelFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPeTLQEPMEL--ENYQLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 180 TVKYEASGTVkFVKPTKAVVKETvliiegpgGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKARP--LKGPIAVHCSAG 257
Cdd:cd14596   79 LENYQALQYF-IIRIIKLVEKET--------GENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKvhNTGPIVVHCSAG 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808356106 258 IGRTGSVVMIEYMCEQLLNGNQIEETDkILQKIREQRNNSIQTDHQYLFVHQVMM 312
Cdd:cd14596  150 IGRAGVLICVDVLLSLIEKDLSFNIKD-IVREMRQQRYGMIQTKDQYLFCYKVVL 203
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 77-309 1.36e-29

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: 113.39  E-value: 1.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  77 HKNRYKDVGCLDNNRVKLAhpPWP----HDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLME 152
Cdd:cd14554    8 FKNRLVNILPYESTRVCLQ--PIRgvegSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 153 KGAKKCSEYYATkekpelvfhekDQKITVKYEASGTVKFVKPTKAVVKEtVLIIEGPGGQVLKTTHYHWIDWPDRGVPPA 232
Cdd:cd14554   86 MGREKCHQYWPA-----------ERSARYQYFVVDPMAEYNMPQYILRE-FKVTDARDGQSRTVRQFQFTDWPEQGVPKS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 233 DLSIIELLIKARPLK------GPIAVHCSAGIGRTG-----SVVMIEYMCEQLLNgnqIEETDKILqkiREQRNNSIQTD 301
Cdd:cd14554  154 GEGFIDFIGQVHKTKeqfgqeGPITVHCSAGVGRTGvfitlSIVLERMRYEGVVD---VFQTVKLL---RTQRPAMVQTE 227


                 ....*...
gi 808356106 302 HQYLFVHQ 309
Cdd:cd14554  228 DQYQFCYR 235
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
68-315 2.89e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 113.65  E-value: 2.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  68 QSFKKAQDHHKNRYKDVGCLDNNRVKLAHPpwphdYIHANFVSTPANaKRFICAQAPLDNTCADFWYMCLQERVEAIFML 147
Cdd:COG5599   35 QYLQNINGSPLNRFRDIQPYKETALRANLG-----YLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVLVVL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 148 --CNLMEKGAKKCSEYyatkekpelvFHEKDQKITVKYEASGTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWP 225
Cdd:COG5599  109 asDDEISKPKVKMPVY----------FRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGQKKIEIPVLHVKNWP 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 226 DRGVPPAD------LSIIELLIKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEET-DKILQKIREQRNNSI 298
Cdd:COG5599  179 DHGAISAEalknlaDLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLSvEEIVIDMRTSRNGGM 258

                        250
                 ....*....|....*...
gi 808356106 299 -QTDHQYlfvhQVMMNFF 315
Cdd:COG5599  259 vQTSEQL----DVLVKLA 272
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 103-309 2.98e-29

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: 111.71  E-value: 2.98e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVS--TPAnAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFhekdQKIT 180
Cdd:cd14539    1 YINASLIEdlTPY-CPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVY----GAIT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 181 VkyeasgTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPAD---LSIIELLI----KARPLKGPIAVH 253
Cdd:cd14539   76 V------SLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPnplLRFIEEVHshylQQRSLQTPIVVH 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 808356106 254 CSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd14539  150 CSSGVGRTGAFCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 102-317 5.08e-29

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: 111.19  E-value: 5.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 102 DYIHANFVS--TPANA--KRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYatkekPElvfhEKDQ 177
Cdd:cd14601    1 DYINANYINmeIPSSSiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYW-----PE----PSGS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 178 KITVKYEASGTVKFVKPTKAVVKETVLIIEGpgGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKARPLKG----PIAVH 253
Cdd:cd14601   72 SSYGGFQVTCHSEEGNPAYVFREMTLTNLEK--NESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAgkdePVVVH 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356106 254 CSAGIGRTGSVVMIEY-MCeqLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMMNFFLE 317
Cdd:cd14601  150 CSAGIGRTGVLITMETaMC--LIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 78-309 6.71e-29

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: 111.16  E-value: 6.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLaHPPWPHD----YIHANFVSTPANAKR-FICAQAPLDNTCADFWYMCLQERVEAIFMLCNLME 152
Cdd:cd14611    2 KNRYKTILPNPHSRVCL-KPKNSNDslstYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 153 KGaKKCSEYYATKekpelvfhekdQKITVKYEASgtVKFVKPTKAVVKETVLIIEGpgGQVLKTTHYHWIDWPDRGVPPA 232
Cdd:cd14611   81 KN-EKCVLYWPEK-----------RGIYGKVEVL--VNSVKECDNYTIRNLTLKQG--SQSRSVKHYWYTSWPDHKTPDS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 233 DLSIIELLI------KARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKILQkIREQRNNSIQTDHQYLF 306
Cdd:cd14611  145 AQPLLQLMLdveedrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQ-LRVDRGGMVQTSEQYEF 223


                 ...
gi 808356106 307 VHQ 309
Cdd:cd14611  224 VHH 226
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 102-312 6.88e-29

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: 110.88  E-value: 6.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 102 DYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYatkekPELVFHEKDQKITV 181
Cdd:cd14631   14 DYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW-----PDDTEVYGDFKVTC 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 182 KYeasgtvkfVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKAR----PLKGPIAVHCSAG 257
Cdd:cd14631   89 VE--------MEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKlsnpPSAGPIVVHCSAG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808356106 258 IGRTGSVVMIEYMCEqLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMM 312
Cdd:cd14631  161 AGRTGCYIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 78-315 3.25e-28

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: 110.86  E-value: 3.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLA-HPPWPHDYIHANFVSTPANAK--RFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKG 154
Cdd:cd14599   41 RNRIREVVPYEENRVELVpTKENNTGYINASHIKVTVGGEewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 155 AKKCSEYYAtkekpelvfhekdqKITVKYEASGTVKFVKPTKAVVKETVLIIEGP------GGQVLKTTHYHWIDWPDRG 228
Cdd:cd14599  121 RSKSHRYWP--------------KLGSKHSSATYGKFKVTTKFRTDSGCYATTGLkvkhllSGQERTVWHLQYTDWPDHG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 229 VP---PADLSIIE-----------LLIKARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIeETDKILQKIREQR 294
Cdd:cd14599  187 CPeevQGFLSYLEeiqsvrrhtnsMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKV-EVPVMLRHLREQR 265

                        250       260
                 ....*....|....*....|.
gi 808356106 295 NNSIQTDHQYLFVHQVMMNFF 315
Cdd:cd14599  266 MFMIQTIAQYKFVYQVLIQFL 286
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 78-312 3.28e-28

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: 110.95  E-value: 3.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLA--HPPWPHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGA 155
Cdd:cd14625   50 KNRYANVIAYDHSRVILQpiEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 156 KKCSEYYATKEKPELVFHEKDQKITVKYeASGTVKfvkptkavvkeTVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLS 235
Cdd:cd14625  130 IKCDQYWPSRGTETYGMIQVTLLDTIEL-ATFCVR-----------TFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTP 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 236 IIELLIKAR----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKIlQKIREQRNNSIQTDHQYLFVHQVM 311
Cdd:cd14625  198 FLAFLRRVKtcnpPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHV-TLMRSQRNYMVQTEDQYSFIHDAL 276


                 .
gi 808356106 312 M 312
Cdd:cd14625  277 L 277
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 78-312 1.98e-27

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: 108.67  E-value: 1.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKL-AHPPWP-HDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGA 155
Cdd:cd14624   50 KNRYANVIAYDHSRVLLsAIEGIPgSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 156 KKCSEYYATK--EKPELVfhekdqKITVkyeasgtVKFVKPTKAVVKETVLIIEGpGGQVLKTTHYHWIDWPDRGVPPAD 233
Cdd:cd14624  130 VKCDQYWPSRgtETYGLI------QVTL-------LDTVELATYCVRTFALYKNG-SSEKREVRQFQFTAWPDHGVPEHP 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 234 LSIIELLIKAR----PLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKIlQKIREQRNNSIQTDHQYLFVHQ 309
Cdd:cd14624  196 TPFLAFLRRVKtcnpPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHV-TLMRAQRNYMVQTEDQYIFIHD 274


                 ...
gi 808356106 310 VMM 312
Cdd:cd14624  275 ALL 277
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 103-312 4.21e-27

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: 105.90  E-value: 4.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYatkekPELVFHEKDQKIT-V 181
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYW-----PDDSDTYGDIKITlL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 182 KYEasgtvkfvkpTKAVVKETVLIIEGPGGQVL-KTTHYHWIDWPDRGVPPADLSIIELLIKAR----PLKGPIAVHCSA 256
Cdd:cd14632   76 KTE----------TLAEYSVRTFALERRGYSARhEVKQFHFTSWPEHGVPYHATGLLAFIRRVKastpPDAGPVVVHCSA 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 808356106 257 GIGRTGSVVMIEYMCEqLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMM 312
Cdd:cd14632  146 GAGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 103-311 7.67e-27

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: 105.04  E-value: 7.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKekpELVFHekdQKITVK 182
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED---GSVSS---GDITVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 yeasgtVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKARPLK-----GPIAVHCSAG 257
Cdd:cd14552   75 ------LKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQqqsgnHPITVHCSAG 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 808356106 258 IGRTGSVVMIEYMCEQlLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVM 311
Cdd:cd14552  149 AGRTGTFCALSTVLER-VKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 102-315 5.32e-25

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: 102.50  E-value: 5.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 102 DYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFHEKDQkitv 181
Cdd:cd14627   82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDP---- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 182 kyeasgTVKFVKPtKAVVKEtVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKARPLK------GPIAVHCS 255
Cdd:cd14627  158 ------MAEYNMP-QYILRE-FKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKeqfgqdGPISVHCS 229

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 256 AGIGRTGSVVMIEYMCEQlLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMMNFF 315
Cdd:cd14627  230 AGVGRTGVFITLSIVLER-MRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 78-306 6.94e-25

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 101.65  E-value: 6.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  78 KNRYKDVGCLDNNRVKLAHP--PWPHDYIHAN-FVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKG 154
Cdd:cd14609   45 KNRNPDFVPYDHARIKLKAEsnPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDG 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 155 AKKCSEYYAtkEKPELVFHekdqkitvKYEASGTVKFVKPTKAVVKETVLiiEGPGGQVLKT-THYHWIDWPDRGVPPAD 233
Cdd:cd14609  125 VKQCDRYWP--DEGSSLYH--------IYEVNLVSEHIWCEDFLVRSFYL--KNVQTQETRTlTQFHFLSWPAEGIPSST 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356106 234 LSIIELLIKA----RPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGnqIEETD--KILQKIREQRNNSIQTDHQYLF 306
Cdd:cd14609  193 RPLLDFRRKVnkcyRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG--VKEIDiaATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 103-315 8.86e-25

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: 100.05  E-value: 8.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKR--FICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYatkekPELvfheKDQKIT 180
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYW-----PRL----GSRHNT 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 181 VKY-EASGTVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVP---PADLSIIELLIKAR----------PL 246
Cdd:cd14598   72 VTYgRFKITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPedlKGFLSYLEEIQSVRrhtnstidpkSP 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356106 247 KGPIAVHCSAGIGRTGSVVMIEYMCeQLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMMNFF 315
Cdd:cd14598  152 NPPVLVHCSAGVGRTGVVILSEIMI-ACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 102-315 9.64e-25

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: 101.73  E-value: 9.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 102 DYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFHEKDQkitv 181
Cdd:cd14628   81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDP---- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 182 kyeasgTVKFVKPtKAVVKEtVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKARPLK------GPIAVHCS 255
Cdd:cd14628  157 ------MAEYNMP-QYILRE-FKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKeqfgqdGPISVHCS 228

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 256 AGIGRTGSVVMIEYMCEQlLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMMNFF 315
Cdd:cd14628  229 AGVGRTGVFITLSIVLER-MRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 103-307 1.31e-24

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: 99.06  E-value: 1.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVS--TPANAKrFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYAtkEKPELVFHekDQKIT 180
Cdd:cd14546    1 YINASTIYdhDPRNPA-YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP--EEGSEVYH--IYEVH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 181 VKYEASGTVKFV------KPTKAVVKETVliiegpggqvlktTHYHWIDWPDRGVPPADLSIIELLIKA----RPLKGPI 250
Cdd:cd14546   76 LVSEHIWCDDYLvrsfylKNLQTSETRTV-------------TQFHFLSWPDEGIPASAKPLLEFRRKVnksyRGRSCPI 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 808356106 251 AVHCSAGIGRTGSVVMIEYMCEQLLNGnqIEETD--KILQKIREQRNNSIQTDHQYLFV 307
Cdd:cd14546  143 VVHCSDGAGRTGTYILIDMVLNRMAKG--AKEIDiaATLEHLRDQRPGMVKTKDQFEFV 199
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 71-306 2.91e-24

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: 100.13  E-value: 2.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  71 KKAQDHHKNRYKDVGCLDNNRV--KLAHPPWPHDYIHANFV--STPANAKrFICAQAPLDNTCADFWYMCLQERVEAIFM 146
Cdd:cd14610   40 QREENVQKNRSLAVLPYDHSRIilKAENSHSHSDYINASPImdHDPRNPA-YIATQGPLPATVADFWQMVWESGCVVIVM 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 147 LCNLMEKGAKKCSEYYAtkEKPELVFHekdqkitvKYEASGTVKFVKPTKAVVKeTVLIIEGPGGQVLKTTHYHWIDWPD 226
Cdd:cd14610  119 LTPLAENGVKQCYHYWP--DEGSNLYH--------IYEVNLVSEHIWCEDFLVR-SFYLKNLQTNETRTVTQFHFLSWND 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 227 RGVPPADLSIIELLIKA----RPLKGPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKILQKIREQRNNSIQTDH 302
Cdd:cd14610  188 QGVPASTRSLLDFRRKVnkcyRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKE 267


                 ....
gi 808356106 303 QYLF 306
Cdd:cd14610  268 QFEF 271
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 102-314 9.52e-24

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: 97.00  E-value: 9.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 102 DYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKpelVFHekdQKITV 181
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS---VTH---GEITI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 182 KyeasgtVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLI---KARPLKG--PIAVHCSA 256
Cdd:cd14622   75 E------IKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAavqKQQQQTGnhPIVVHCSA 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 808356106 257 GIGRTGSVVMIEYMCEQlLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMMNF 314
Cdd:cd14622  149 GAGRTGTFIALSNILER-VKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 102-315 3.93e-23

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 97.10  E-value: 3.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 102 DYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPELVFHEKDQkitv 181
Cdd:cd14629   82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDP---- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 182 kyeasgTVKFVKPtKAVVKEtVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKARPLK------GPIAVHCS 255
Cdd:cd14629  158 ------MAEYNMP-QYILRE-FKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKeqfgqdGPITVHCS 229

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 256 AGIGRTGSVVMIEYMCEQlLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVMMNFF 315
Cdd:cd14629  230 AGVGRTGVFITLSIVLER-MRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 102-311 6.20e-23

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: 95.11  E-value: 6.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 102 DYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATkekpELVFHEKDQKITV 181
Cdd:cd14623   25 DYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPS----DGSVSYGDITIEL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 182 KYEasgtvkfvKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPP---ADLSIIELLIKARPLKG--PIAVHCSA 256
Cdd:cd14623  101 KKE--------EECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSdgkGMINIIAAVQKQQQQSGnhPITVHCSA 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808356106 257 GIGRTGSVVMIEYMCEQlLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQVM 311
Cdd:cd14623  173 GAGRTGTFCALSTVLER-VKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 103-306 4.21e-20

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: 86.68  E-value: 4.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKpelvfhekdqkitvK 182
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK--------------T 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 YEASG-TVKFVKPTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGVPPADLSIIELLIKAR----------PLKGPIA 251
Cdd:cd14558   67 YGDIEvELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpyknskhGRSVPIV 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 808356106 252 VHCSAGIGRTGsvvmIEYMCEQLLNGNQIEETDKILQ---KIREQRNNSIQTDHQYLF 306
Cdd:cd14558  147 VHCSDGSSRTG----IFCALWNLLESAETEKVVDVFQvvkALRKQRPGMVSTLEQYQF 200
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 103-309 5.92e-18

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: 80.91  E-value: 5.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLcNLMEKGAKKCSEYYatkekPElvfhekdqkitvk 182
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYW-----PD------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 yEASGT-----VKFVKPTKA--VVKETVLI--IEGPGGQVLKTTHYHWIDWP-DRGVPPADLSIIELLI-----KARPLK 247
Cdd:cd14556   62 -EGSGTygpiqVEFVSTTIDedVISRIFRLqnTTRPQEGYRMVQQFQFLGWPrDRDTPPSKRALLKLLSevekwQEQSGE 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356106 248 GPIAVHCSAGIGRTGSVVMIEYMCEQLlngnQIEETDKILQKIREQRN---NSIQTDHQYLFVHQ 309
Cdd:cd14556  141 GPIVVHCLNGVGRSGVFCAISSVCERI----KVENVVDVFQAVKTLRNhrpNMVETEEQYKFCYD 201
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 103-313 2.84e-15

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: 73.52  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLcNLMEkGAKKCSEYYATKE-------KPELVFHEK 175
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMD-AAQLCMQYWPEKTsccygpiQVEFVSADI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 176 DQKITVKYeasgtvkFVKPTKAVVKETVLIIEgpggqvlkttHYHWIDWPD-RGVPPADLSIIELLIKARPLK------- 247
Cdd:cd14634   79 DEDIISRI-------FRICNMARPQDGYRIVQ----------HLQYIGWPAyRDTPPSKRSILKVVRRLEKWQeqydgre 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808356106 248 GPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIeETDKILQKIREQRNNSIQTDHQYLFVHQVMMN 313
Cdd:cd14634  142 GRTVVHCLNGGGRSGTFCAICSVCEMIQQQNII-DVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
219-309 8.79e-14

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 67.69  E-value: 8.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 219 YHWIDWPDRGVPPAD--LSIIELLIKARPLKGPIAVHCSAGIGRTGsVVMIEYMCEQLLngnqieETDKILQKIREQRNN 296
Cdd:COG2453   50 YLHLPIPDFGAPDDEqlQEAVDFIDEALREGKKVLVHCRGGIGRTG-TVAAAYLVLLGL------SAEEALARVRAARPG 122

                         90
                 ....*....|...
gi 808356106 297 SIQTDHQYLFVHQ 309
Cdd:COG2453  123 AVETPAQRAFLER 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 236-309 7.62e-10

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 55.82  E-value: 7.62e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808356106 236 IIELLIKARPLKGPIAVHCSAGIGRTGsVVMIEYMCEQLLNGnqIEEtdkILQKIREQRNNSI-QTDHQYLFVHQ 309
Cdd:cd14494   45 FLEVLDQAEKPGEPVLVHCKAGVGRTG-TLVACYLVLLGGMS--AEE---AVRIVRLIRPGGIpQTIEQLDFLIK 113
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 224-308 1.27e-09

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: 57.36  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 224 WPDRGVPPAD--LSIIELLIKARPLKGPIAVHCSAGIGRTGsvVMIEymCeQLLNGNQIEETDKILQkIREQRNNSIQTD 301
Cdd:cd14506   84 WKDYGVPSLTtiLDIVKVMAFALQEGGKVAVHCHAGLGRTG--VLIA--C-YLVYALRMSADQAIRL-VRSKRPNSIQTR 157


                 ....*..
gi 808356106 302 HQYLFVH 308
Cdd:cd14506  158 GQVLCVR 164
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 219-309 4.04e-09

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: 54.96  E-value: 4.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 219 YHWIDWPDRGVPPAD---LSIIELLIKARPLKGPIAVHCSAGIGRTGSVVmieyMCeQLLNGNQIEETDKILQKIREQRN 295
Cdd:cd14505   75 WHHLPIPDGGVPSDIaqwQELLEELLSALENGKKVLIHCKGGLGRTGLIA----AC-LLLELGDTLDPEQAIAAVRALRP 149

                         90
                 ....*....|....
gi 808356106 296 NSIQTDHQYLFVHQ 309
Cdd:cd14505  150 GAIQTPKQENFLHQ 163
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 103-312 6.97e-09

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: 55.00  E-value: 6.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSeYYATKEKPELVfhekdQKITVK 182
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINC-----ETFKVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 YEASGTVKFVKPTKAVVKEtvLIIEGPGGQ-VLKTTHYHWIDWPDRGVPPADLSIIELLIK--ARPLKGPIAVHCSAGIG 259
Cdd:cd17669   75 LIAEEHKCLSNEEKLIIQD--FILEATQDDyVLEVRHFQCPKWPNPDSPISKTFELISIIKeeAANRDGPMIVHDEHGGV 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 808356106 260 RTGSVVMIEYMCEQLLNGNQIE--ETDKILQKIREqrnnSIQTD-HQYLFVHQVMM 312
Cdd:cd17669  153 TAGTFCALTTLMHQLEKENSVDvyQVAKMINLMRP----GVFTDiEQYQFLYKAIL 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 103-312 7.81e-09

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 55.08  E-value: 7.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLmeKGAKKCSEYYatkekPELVFHeKDQKITVK 182
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYW-----PENGVH-RHGPIQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 YEASGTvkfvkpTKAVVKETVLIIEG--PGGQVLKTTHYHWIDWP-DRGVPPADLSIIELLIKARPLK-------GPIAV 252
Cdd:cd14635   73 FVSADL------EEDIISRIFRIYNAarPQDGYRMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQeeynggeGRTVV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 253 HCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKIlQKIREQRNNSIQTDHQYLFVHQVMM 312
Cdd:cd14635  147 HCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAV-KTLRNNKPNMVDLLDQYKFCYEVAL 205
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 219-309 1.57e-08

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: 52.66  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 219 YHWIDWPDrGVPPADLSI---IELLIKARPLKGPIAVHCSAGIGRTGSVVmieyMCEQLLNGNQieETDKILQKIREQRN 295
Cdd:cd14504   52 YHHIPIED-YTPPTLEQIdefLDIVEEANAKNEAVLVHCLAGKGRTGTML----ACYLVKTGKI--SAVDAINEIRRIRP 124

                         90
                 ....*....|....
gi 808356106 296 NSIQTDHQYLFVHQ 309
Cdd:cd14504  125 GSIETSEQEKFVIQ 138
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 103-312 5.13e-08

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: 52.72  E-value: 5.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLmeKGAKKCSEYYatkekPElvfhekdqkitvk 182
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYW-----PE------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 yeaSGTVKFvKPTKA----------VVKETVLI--IEGPGGQVLKTTHYHWIDWPD-RGVPPADLSIIELLIKARPLK-- 247
Cdd:cd14636   61 ---EGMLRY-GPIQVecmscsmdcdVISRIFRIcnLTRPQEGYLMVQQFQYLGWAShREVPGSKRSFLKLILQVEKWQee 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 248 -----GPIAVHCSAGIGRTGSVVMIEYMCEQLLNGNQIEETDKIlQKIREQRNNSIQTDHQYLFVHQVMM 312
Cdd:cd14636  137 cdegeGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAV-KTLRNSKPNMVETPEQYRFCYDVAL 205
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 104-304 8.59e-08

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 52.02  E-value: 8.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 104 IHANFVSTpANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGAKKCSEYYATKEKPElvfhekdqKITVKY 183
Cdd:cd14559   18 LNANRVQI-GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGTYG--------SVTVKS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 184 EASGTVKFVKPTKavVKETVLIIEGPGgqvlKTTH---YHWIDWPDRGVPPADLSI---------IELLIKARPLKGPIA 251
Cdd:cd14559   89 KKTGKDELVDGLK--ADMYNLKITDGN----KTITipvVHVTNWPDHTAISSEGLKeladlvnksAEEKRNFYKSKGSSA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808356106 252 V----------HCSAGIGRTGsvVMIEYMCeqLLNGNQIEETDKILQKIREQRNNSI-QTDHQY 304
Cdd:cd14559  163 IndknkllpviHCRAGVGRTG--QLAAAME--LNKSPNNLSVEDIVSDMRTSRNGKMvQKDEQL 222
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 103-257 1.32e-07

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: 51.17  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 103 YIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKGakKCSEYYATKEKPeLVFhekdQKITVK 182
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKP-LEC----ETFKVT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 183 YEASGTVKFVKPTKAVVKEtvLIIEGPggQ---VLKTTHYHWIDWPDRGVPPAD-LSIIELLIK-ARPLKGPIAVH---- 253
Cdd:cd14550   74 LSGEDHSCLSNEIRLIVRD--FILEST--QddyVLEVRQFQCPSWPNPCSPIHTvFELINTVQEwAQQRDGPIVVHdryg 149


                 ....*
gi 808356106 254 -CSAG 257
Cdd:cd14550  150 gVQAA 154
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 89-321 2.96e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 48.04  E-value: 2.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106  89 NNRVKLAHPpwpHDYIHANFVSTPANAKRFICAQAPLDNTCADFWYMCLQERVEAIFMLCNLMEKgaKKCSEYYATKEKP 168
Cdd:PHA02740  67 HRRIKLFND---EKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK--KCFNQFWSLKEGC 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 169 ELVFhekdQKITVKyeasgTVKFVkpTKAVVKETVLIIEGPGGQVLKTTHYHWIDWPDRGV---PPADL----SIIELLI 241
Cdd:PHA02740 142 VITS----DKFQIE-----TLEII--IKPHFNLTLLSLTDKFGQAQKISHFQYTAWPADGFshdPDAFIdffcNIDDLCA 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 242 KARPLK-----GPIAVHCSAGIGrTGSVVMIEYMCEQLLNGNQIEETDKILQKIREQRNNSIQTDHQYLFVHQvMMNFFL 316
Cdd:PHA02740 211 DLEKHKadgkiAPIIIDCIDGIS-SSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYH-LIAAYL 288


                 ....*
gi 808356106 317 EKKLF 321
Cdd:PHA02740 289 KEKFD 293
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 223-305 1.00e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 45.01  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 223 DWP--DRGVPPADL--SIIELL----IKARPLKGPIAVHCSAGIGRTGSVV---MIEYmceqllnGNqIEETDKIlQKIR 291
Cdd:PTZ00242  66 DWPfdDGAPPPKAVidNWLRLLdqefAKQSTPPETIAVHCVAGLGRAPILValaLVEY-------GG-MEPLDAV-GFVR 136

                         90
                 ....*....|....*
gi 808356106 292 EQRNNSI-QTDHQYL 305
Cdd:PTZ00242 137 EKRKGAInQTQLQFL 151
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 225-263 1.33e-04

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 42.05  E-value: 1.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 808356106 225 PDRGVPPAD-----LSIIElliKArplKGPIAVHCSAGIGRTGS 263
Cdd:cd14499   88 PDGSTPSDDivkkfLDICE---NE---KGAIAVHCKAGLGRTGT 125
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 223-305 1.37e-04

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


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 41.82  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 223 DWP--DRGVPPAD-----LSIIE-LLIKARPLKGPIAVHCSAGIGRTGSVV---MIEYmceqllnGNQIEETdkiLQKIR 291
Cdd:cd14500   63 DWPfdDGSPPPDDvvddwLDLLKtRFKEEGKPGACIAVHCVAGLGRAPVLVaiaLIEL-------GMKPEDA---VEFIR 132

                         90
                 ....*....|....*
gi 808356106 292 EQRNNSI-QTDHQYL 305
Cdd:cd14500  133 KKRRGAInSKQLQFL 147
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 218-266 8.23e-04

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 39.07  E-value: 8.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 808356106 218 HYHWIDWPDrgVPPADLS-----IIELLIKARPLKGPIAVHCSAGIGRTGSVVM 266
Cdd:cd14498   47 KYLRIPIED--SPDEDILshfeeAIEFIEEALKKGGKVLVHCQAGVSRSATIVI 98
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 222-300 1.05e-03

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 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: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 39.24  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 222 IDWP-DRGVPPADLSIIELL--IKARPLKGP---IAVHCSAGIGRTGSVVMIEYmceqLLNGNQIEETdkiLQKIREQRN 295
Cdd:cd18535   62 VDWPfDDGAPPPGKVVEDWLslLKTKFCEDPgccVAVHCVAGLGRAPVLVALAL----IESGMKYEDA---IQFIRQKRR 134


                 ....*
gi 808356106 296 NSIQT 300
Cdd:cd18535  135 GAINS 139
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 220-296 1.56e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 38.72  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 220 HWIDWPDRGVPPADL------SIIELLIKarplkGP---IAVHCSAGIGRTGSVVmieymCEQLLNGNQIEETDKILQKI 290
Cdd:cd14497   64 LHYGFPDHHPPPLGLlleivdDIDSWLSE-----DPnnvAVVHCKAGKGRTGTVI-----CAYLLYYGQYSTADEALEYF 133


                 ....*.
gi 808356106 291 REQRNN 296
Cdd:cd14497  134 AKKRFK 139
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 220-309 1.56e-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: 38.90  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 220 HWIDWP-DRGVPPAD------LSIIELLIKARPlKGPIAVHCSAGIGRTGSVVMIeymceQLLNGNQieETDKILQKIRE 292
Cdd:cd18537   64 QVLDWPfDDGAPPSNqivddwLNLLKVKFREEP-GCCIAVHCVAGLGRAPVLVAL-----ALIECGM--KYEDAVQFIRQ 135

                         90
                 ....*....|....*..
gi 808356106 293 QRNNSIQTDhQYLFVHQ 309
Cdd:cd18537  136 KRRGAFNSK-QLLYLEK 151
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 250-308 1.80e-03

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: 38.88  E-value: 1.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808356106 250 IAVHCSAGIGRTGSVVmieymCEQLLNGNQIEETDKILQKIREQRNN--------SIQTDHQYLFVH 308
Cdd:cd14510  111 VAIHCKGGKGRTGTMV-----CAWLIYSGQFESAKEALEYFGERRTDksvsskfqGVETPSQSRYVG 172
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 218-265 2.70e-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: 38.12  E-value: 2.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 808356106 218 HYHWIDWPDRGVPPADLSIIELL--IKARPlkGPIAVHCSAGIGRTGSVV 265
Cdd:cd14529   60 KYVNLPLSATRPTESDVQSFLLImdLKLAP--GPVLIHCKHGKDRTGLVS 107
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 220-298 2.95e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 38.76  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356106 220 HWIDWPDRGVPPAD-----LSIIELLIKARplkGPIAVHCSAGIGRT---GSVVMIEYmceqllngnQIEETDKILqKIR 291
Cdd:PTZ00393 141 HELIFPDGDAPTVDivsnwLTIVNNVIKNN---RAVAVHCVAGLGRApvlASIVLIEF---------GMDPIDAIV-FIR 207


                 ....*..
gi 808356106 292 EQRNNSI 298
Cdd:PTZ00393 208 DRRKGAI 214
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
242-273 2.99e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 37.65  E-value: 2.99e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 808356106   242 KARPLKGPIAVHCSAGIGRTGSVVMIEYMCEQ 273
Cdd:smart00195  73 DAESKGGKVLVHCQAGVSRSATLIIAYLMKTR 104
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 236-271 3.56e-03

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 36.86  E-value: 3.56e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 808356106  236 IIELLIKARPLKGPIAVHCSAGIGRTGSVVMIEYMC 271
Cdd:pfam00782  58 AVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMK 93
 
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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