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Conserved domains on  [gi|17541250|ref|NP_501766|]
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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;
19-256 7.86e-91

Protein-tyrosine phosphatase;


:

Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 269.11  E-value: 7.86e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250    19 HGKNRYKDVGCLDNNRVKLGG-AWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLTGdPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250    98 KKCHEYLPTEDNkDTMSFKekgqKVTVKFESSKAIKfrdnsaAKVTKTVLTVEGAGCD-KLKVNHYHWIDWPDRGVPTAD 176
Cdd:pfam00102  82 EKCAQYWPEEEG-ESLEYG----DFTVTLKKEKEDE------KDYTVRTLEVSNGGSEeTRTVKHFHYTGWPDHGVPESP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   177 NAILELLEKARVSK-----GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVH 251
Cdd:pfam00102 151 NSLLDLLRKVRKSSldgrsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEV-DIFQIVKELRSQRPGMVQTLEQYIFLY 229


                  ....*
gi 17541250   252 QVMMN 256
Cdd:pfam00102 230 DAILE 234
 
Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
19-256 7.86e-91

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 269.11  E-value: 7.86e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250    19 HGKNRYKDVGCLDNNRVKLGG-AWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLTGdPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250    98 KKCHEYLPTEDNkDTMSFKekgqKVTVKFESSKAIKfrdnsaAKVTKTVLTVEGAGCD-KLKVNHYHWIDWPDRGVPTAD 176
Cdd:pfam00102  82 EKCAQYWPEEEG-ESLEYG----DFTVTLKKEKEDE------KDYTVRTLEVSNGGSEeTRTVKHFHYTGWPDHGVPESP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   177 NAILELLEKARVSK-----GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVH 251
Cdd:pfam00102 151 NSLLDLLRKVRKSSldgrsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEV-DIFQIVKELRSQRPGMVQTLEQYIFLY 229


                  ....*
gi 17541250   252 QVMMN 256
Cdd:pfam00102 230 DAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
5-256 8.77e-86

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 257.20  E-value: 8.77e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250      5 NDFSKMKAFKDAQeHGKNRYKDVGCLDNNRVKL--GGAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDR 82
Cdd:smart00194  15 DDESCTVAAFPEN-RDKNRYKDVLPYDHTRVKLkpPPGEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250     83 VETIFMLCNYKEKGAKKCHEYLPtEDNKDTMSFKekgqKVTVKFESskaikfrDNSAAKVTKTVLTVEGAGCDK-LKVNH 161
Cdd:smart00194  94 VTVIVMLTELVEKGREKCAQYWP-DEEGEPLTYG----DITVTLKS-------VEKVDDYTIRTLEVTNTGCSEtRTVTH 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250    162 YHWIDWPDRGVPTADNAILELLEKAR----VSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQR 237
Cdd:smart00194 162 YHYTNWPDHGVPESPESILDLIRAVRksqsTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV-DIFEIVKELRSQR 240

                          250
                   ....*....|....*....
gi 17541250    238 NNSVQTDHQYLFVHQVMMN 256
Cdd:smart00194 241 PGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 45-252 7.41e-65

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: 201.75  E-value: 7.41e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEDNKdTMSFKEkgqkVTV 124
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGK-PLEYGD----ITV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KFESSKaikfrdnSAAKVTKTVLTVEGAGCDK-LKVNHYHWIDWPDRGVPTADNAILELLEKAR----VSKGPIAVHCSA 199
Cdd:cd00047  76 TLVSEE-------ELSDYTIRTLELSPKGCSEsREVTHLHYTGWPDHGVPSSPEDLLALVRRVRkearKPNGPIVVHCSA 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17541250 200 GIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd00047 149 GVGRTGTFIAIDILLERLEAEGEV-DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 21-257 1.10e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 140.14  E-value: 1.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   21 KNRYKDVGCLDNNRVKL----GGAwphEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKG 96
Cdd:PHA02742  55 KCRYPDAPCFDRNRVILkiedGGD---DFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   97 AKKCHEYLPTednkdtmsfKEKGQKVTVKFeSSKAIKFRDNSAAKVTKTVLTVEGAGCdKLKVNHYHWIDWPDRGVPTAD 176
Cdd:PHA02742 132 KEACYPYWMP---------HERGKATHGEF-KIKTKKIKSFRNYAVTNLCLTDTNTGA-SLDIKHFAYEDWPHGGLPRDP 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  177 NAILELL---------------EKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEdTDKIIQKIREQRNNSV 241
Cdd:PHA02742 201 NKFLDFVlavreadlkadvdikGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIP-LLSIVRDLRKQRHNCL 279

                        250
                 ....*....|....*.
gi 17541250  242 QTDHQYLFVHQVMMNF 257
Cdd:PHA02742 280 SLPQQYIFCYFIVLIF 295
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
13-262 1.26e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 139.46  E-value: 1.26e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  13 FKDAQEHGKNRYKDVGCLDNNRVKLGGAwpheYIHANYVSTPtNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNY 92
Cdd:COG5599  37 LQNINGSPLNRFRDIQPYKETALRANLG----YLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  93 KE--KGAKKCHEYlptednkdtmsFKEKGQ--KVTVKFESSKAIKFRDNSAAKVTKtvLTVEGAGCDKLKVNHYHWIDWP 168
Cdd:COG5599 112 DEisKPKVKMPVY-----------FRQDGEygKYEVSSELTESIQLRDGIEARTYV--LTIKGTGQKKIEIPVLHVKNWP 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 169 DRGVPTAD------NAILELLEKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAG-QIIEDTDKIIQKIREQRNNS- 240
Cdd:COG5599 179 DHGAISAEalknlaDLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALvQITLSVEEIVIDMRTSRNGGm 258

                       250       260
                ....*....|....*....|..
gi 17541250 241 VQTDHQYlfvhQVMMNFFEKRG 262
Cdd:COG5599 259 VQTSEQL----DVLVKLAEQQI 276
 
Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
19-256 7.86e-91

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 269.11  E-value: 7.86e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250    19 HGKNRYKDVGCLDNNRVKLGG-AWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLTGdPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250    98 KKCHEYLPTEDNkDTMSFKekgqKVTVKFESSKAIKfrdnsaAKVTKTVLTVEGAGCD-KLKVNHYHWIDWPDRGVPTAD 176
Cdd:pfam00102  82 EKCAQYWPEEEG-ESLEYG----DFTVTLKKEKEDE------KDYTVRTLEVSNGGSEeTRTVKHFHYTGWPDHGVPESP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   177 NAILELLEKARVSK-----GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVH 251
Cdd:pfam00102 151 NSLLDLLRKVRKSSldgrsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEV-DIFQIVKELRSQRPGMVQTLEQYIFLY 229


                  ....*
gi 17541250   252 QVMMN 256
Cdd:pfam00102 230 DAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
5-256 8.77e-86

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 257.20  E-value: 8.77e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250      5 NDFSKMKAFKDAQeHGKNRYKDVGCLDNNRVKL--GGAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDR 82
Cdd:smart00194  15 DDESCTVAAFPEN-RDKNRYKDVLPYDHTRVKLkpPPGEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250     83 VETIFMLCNYKEKGAKKCHEYLPtEDNKDTMSFKekgqKVTVKFESskaikfrDNSAAKVTKTVLTVEGAGCDK-LKVNH 161
Cdd:smart00194  94 VTVIVMLTELVEKGREKCAQYWP-DEEGEPLTYG----DITVTLKS-------VEKVDDYTIRTLEVTNTGCSEtRTVTH 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250    162 YHWIDWPDRGVPTADNAILELLEKAR----VSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQR 237
Cdd:smart00194 162 YHYTNWPDHGVPESPESILDLIRAVRksqsTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV-DIFEIVKELRSQR 240

                          250
                   ....*....|....*....
gi 17541250    238 NNSVQTDHQYLFVHQVMMN 256
Cdd:smart00194 241 PGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 45-252 7.41e-65

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: 201.75  E-value: 7.41e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEDNKdTMSFKEkgqkVTV 124
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGK-PLEYGD----ITV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KFESSKaikfrdnSAAKVTKTVLTVEGAGCDK-LKVNHYHWIDWPDRGVPTADNAILELLEKAR----VSKGPIAVHCSA 199
Cdd:cd00047  76 TLVSEE-------ELSDYTIRTLELSPKGCSEsREVTHLHYTGWPDHGVPSSPEDLLALVRRVRkearKPNGPIVVHCSA 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17541250 200 GIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd00047 149 GVGRTGTFIAIDILLERLEAEGEV-DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 21-258 8.75e-50

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: 165.38  E-value: 8.75e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKL------GGAwphEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKE 94
Cdd:cd14603  33 KNRYKDILPYDQTRVILsllqeeGHS---DYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  95 KGAKKCHEYLPTEDnkDTMSFKekgqkvtvKFESSKAIKFRDNSAAKVTKTVLTVegagCDK-LKVNHYHWIDWPDRGVP 173
Cdd:cd14603 110 MGKKKCERYWAQEQ--EPLQTG--------PFTITLVKEKRLNEEVILRTLKVTF----QKEsRSVSHFQYMAWPDHGIP 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 174 TADNAILELLEKARVSKG----PIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTD--KIIQKIREQRNNSVQTDHQY 247
Cdd:cd14603 176 DSPDCMLAMIELARRLQGsgpePLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSifDVVLEMRKQRPAAVQTEEQY 255

                       250
                ....*....|.
gi 17541250 248 LFVHQVMMNFF 258
Cdd:cd14603 256 EFLYHTVAQMF 266
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 23-252 1.33e-48

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: 160.98  E-value: 1.33e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  23 RYKDVGCLDNNRVKLGGAWPHE---YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKK 99
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEEEgsdYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 100 CHEYLPtednKDTMSFKEKGQKVTVKFESSKaikfrdnsaAKVTKTVLTVEGAGcDKLKVNHYHWIDWPDRGVPTADNAI 179
Cdd:cd14548  81 CDHYWP----FDQDPVYYGDITVTMLSESVL---------PDWTIREFKLERGD-EVRSVRQFHFTAWPDHGVPEAPDSL 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17541250 180 LELLEKARV----SKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14548 147 LRFVRLVRDyikqEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYV-DIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 45-251 4.54e-48

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: 159.05  E-value: 4.54e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEdnkDTMSFKEkgqkVTV 124
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKE---GTETYGN----IQV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KFESSKAIkfrdnsaAKVTKTVLTVEGAGCDKLK-------VNHYHWIDWPDRGVPTADNAILELLEKARVSK----GPI 193
Cdd:cd14549  74 TLLSTEVL-------ATYTVRTFSLKNLKLKKVKgrsservVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANppgaGPI 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17541250 194 AVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVH 251
Cdd:cd14549 147 VVHCSAGVGRTGTYIVIDSMLQQIQDKGTV-NVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 20-259 4.75e-48

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: 160.32  E-value: 4.75e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  20 GKNRYKDVGCLDNNRVKLGGAWPH----EYIHANYVSTPT-------NPKRFICTQAPLEKTCADFWFMCLQDRVETIFM 88
Cdd:cd14544   3 GKNRYKNILPFDHTRVILKDRDPNvpgsDYINANYIRNENegpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRVIVM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  89 LCNYKEKGAKKCHEYLPTEDNKDtmsfKEKGQKVtvkfessKAIKFRDNSAAKVTKTVLTVEGAGCDKLKVNHYHWIDWP 168
Cdd:cd14544  83 TTKEVERGKNKCVRYWPDEGMQK----QYGPYRV-------QNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWP 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 169 DRGVPTADNAILELLE------KARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQL----LAGQIieDTDKIIQKIREQRN 238
Cdd:cd14544 152 DHGVPSDPGGVLNFLEdvnqrqESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIkrkgLDCDI--DIQKTIQMVRSQRS 229

                       250       260
                ....*....|....*....|.
gi 17541250 239 NSVQTDHQYLFVHQVMMNFFE 259
Cdd:cd14544 230 GMVQTEAQYKFIYVAVAQYIE 250
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 45-252 2.53e-47

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: 157.03  E-value: 2.53e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTP-TNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEdnkdtmSFKEKGQKVT 123
Cdd:cd18533   1 YINASYITLPgTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSG------EYEGEYGDLT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 124 VKFESSKAIkfrDNSAAKVTKTVLTVEGAGcdKLKVNHYHWIDWPDRGVPTADNAILELLEKAR------VSKGPIAVHC 197
Cdd:cd18533  75 VELVSEEEN---DDGGFIVREFELSKEDGK--VKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRelndsaSLDPPIIVHC 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17541250 198 SAGIGRTGSVVMLEYVMDQLLAG----QIIEDTD----KIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd18533 150 SAGVGRTGTFIALDSLLDELKRGlsdsQDLEDSEdpvyEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 21-261 3.05e-47

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: 159.71  E-value: 3.05e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLGGAWPH---EYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14604  60 KNRYKDILPFDHSRVKLTLKTSSqdsDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGR 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEdNKDTMSFKEKgqKVTVKFESSKAIKFrdnsaakvTKTvLTVEGAGcDKLKVNHYHWIDWPDRGVPTADN 177
Cdd:cd14604 140 KKCERYWPLY-GEEPMTFGPF--RISCEAEQARTDYF--------IRT-LLLEFQN-ETRRLYQFHYVNWPDHDVPSSFD 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 178 AILELLEKARV----SKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTD--KIIQKIREQRNNSVQTDHQYLFVH 251
Cdd:cd14604 207 SILDMISLMRKyqehEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNvfNLIQEMRTQRHSAVQTKEQYELVH 286

                       250
                ....*....|
gi 17541250 252 QVMMNFFEKR 261
Cdd:cd14604 287 RAIAQLFEKQ 296
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 21-251 1.98e-46

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: 156.76  E-value: 1.98e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLG---GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14543  32 KNRYGDVLCLDQSRVKLPkrnGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGR 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEDNkdtmsFKEKGQKVTVKFESSKaiKFRDnsaakVTKTVLTVEGAGCD-KLKVNHYHWIDWPDRGVPTAD 176
Cdd:cd14543 112 VKCGQYWPLEEG-----SSLRYGDLTVTNLSVE--NKEH-----YKKTTLEIHNTETDeSRQVTHFQFTSWPDFGVPSSA 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 177 NAILELLEKAR------------VSKG-----PIAVHCSAGIGRTGSVVMLEYVMDQLlagqiiEDTDKI-----IQKIR 234
Cdd:cd14543 180 AALLDFLGEVRqqqalavkamgdRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQL------EDVGTLnvmqtVRRMR 253

                       250
                ....*....|....*..
gi 17541250 235 EQRNNSVQTDHQYLFVH 251
Cdd:cd14543 254 TQRAFSIQTPDQYYFCY 270
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 22-252 7.75e-46

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: 153.71  E-value: 7.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  22 NRYKDVGCLDNNRVKLGGAWPHE---YIHANYVSTPTN-PKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDPlssYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 kKCHEYLPTEDNkdtmsfkEKGQKVTVKFESskaIKFRDNSAakVTKTVLTVEGagcDKLKVNHYHWIDWPDRGVPTADN 177
Cdd:cd14547  81 -KCAQYWPEEEN-------ETYGDFEVTVQS---VKETDGYT--VRKLTLKYGG---EKRYLKHYWYTSWPDHKTPEAAQ 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 178 AILEL------LEKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAgQIIEDTDKIIQKIREQRNNSVQTDHQYLFVH 251
Cdd:cd14547 145 PLLSLvqeveeARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLRE-EGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223


                .
gi 17541250 252 Q 252
Cdd:cd14547 224 R 224
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 21-259 5.85e-45

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: 152.48  E-value: 5.85e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLGGAWPHE----YIHANYV-------STPTNPKR-FICTQAPLEKTCADFWFMCLQDRVETIFM 88
Cdd:cd14605   5 KNRYKNILPFDHTRVVLHDGDPNEpvsdYINANIImpefetkCNNSKPKKsYIATQGCLQNTVNDFWRMVFQENSRVIVM 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  89 LCNYKEKGAKKCHEYLPtednkDTMSFKEKG-QKV-TVKFESSKAIKFRDNSAAKVtktvltveGAGCDKLKVNHYHWID 166
Cdd:cd14605  85 TTKEVERGKSKCVKYWP-----DEYALKEYGvMRVrNVKESAAHDYILRELKLSKV--------GQGNTERTVWQYHFRT 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 167 WPDRGVPTADNAILELLEKARVSK------GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTD--KIIQKIREQRN 238
Cdd:cd14605 152 WPDHGVPSDPGGVLDFLEEVHHKQesimdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDvpKTIQMVRSQRS 231

                       250       260
                ....*....|....*....|.
gi 17541250 239 NSVQTDHQYLFVHQVMMNFFE 259
Cdd:cd14605 232 GMVQTEAQYRFIYMAVQHYIE 252
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 45-252 9.11e-45

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: 150.27  E-value: 9.11e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPtEDNKDTMSFKEkgqkVTV 124
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWP-EEGEEQLQFGP----FKI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KFESSKAIkfrdnSAAKVTKTvLTVEgAGCDKLKVNHYHWIDWPDRGVPTADNAILELLEKARVSKG----PIAVHCSAG 200
Cdd:cd14542  76 SLEKEKRV-----GPDFLIRT-LKVT-FQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGsedvPICVHCSAG 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17541250 201 IGRTGSVVMLEYVMDQLLAGQIIEDTD--KIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14542 149 CGRTGTICAIDYVWNLLKTGKIPEEFSlfDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 22-257 6.18e-44

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: 149.27  E-value: 6.18e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  22 NRYKDVGCLDNNRVKLG---GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAK 98
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKpihEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  99 KCHEYLPTednkDTMSFKEKGQKVTVKFES-SKAIKFRDnsaakvtKTVLTVEGAGcdKLKVNHYHWIDWPDRGVPTADN 177
Cdd:cd14619  81 KCEHYWPL----DYTPCTYGHLRVTVVSEEvMENWTVRE-------FLLKQVEEQK--TLSVRHFHFTAWPDHGVPSSTD 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 178 AILELLEKAR------VSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVH 251
Cdd:cd14619 148 TLLAFRRLLRqwldqtMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLL-GPFSFVQKMRENRPLMVQTESQYVFLH 226


                ....*.
gi 17541250 252 QVMMNF 257
Cdd:cd14619 227 QCILDF 232
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 21-255 1.09e-43

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: 149.80  E-value: 1.09e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKL----GGAWPH-EYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEK 95
Cdd:cd17667  30 KNRYINILAYDHSRVKLrplpGKDSKHsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEK 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  96 GAKKCHEYLPTEDNkdtmsfkEKGQKVTVKFESSKA--------IKFRDNSAAKVTKTvlTVEGAGCDKLkVNHYHWIDW 167
Cdd:cd17667 110 GRRKCDQYWPTENS-------EEYGNIIVTLKSTKIhacytvrrFSIRNTKVKKGQKG--NPKGRQNERT-VIQYHYTQW 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 168 PDRGVPTADNAILELLEKARVSK----GPIAVHCSAGIGRTGSVVmleyVMDQLLagQIIEDTDKI-----IQKIREQRN 238
Cdd:cd17667 180 PDMGVPEYALPVLTFVRRSSAARtpemGPVLVHCSAGVGRTGTYI----VIDSML--QQIKDKSTVnvlgfLKHIRTQRN 253

                       250
                ....*....|....*..
gi 17541250 239 NSVQTDHQYLFVHQVMM 255
Cdd:cd17667 254 YLVQTEEQYIFIHDALL 270
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 20-259 1.68e-43

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: 149.26  E-value: 1.68e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  20 GKNRYKDVGCLDNNRVKLGGAWPH----EYIHANYV-----STPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLC 90
Cdd:cd14606  20 SKNRYKNILPFDHSRVILQGRDSNipgsDYINANYVknqllGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIVMTT 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  91 NYKEKGAKKCHEYLPtednkDTMSFKEKGQKVTvkfessKAIKFRDNSAAKVTKTVLTVEGAGCDKLKVNHYHWIDWPDR 170
Cdd:cd14606 100 REVEKGRNKCVPYWP-----EVGMQRAYGPYSV------TNCGEHDTTEYKLRTLQVSPLDNGELIREIWHYQYLSWPDH 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 171 GVPTADNAILELLEKARV------SKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTD--KIIQKIREQRNNSVQ 242
Cdd:cd14606 169 GVPSEPGGVLSFLDQINQrqeslpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDiqKTIQMVRAQRSGMVQ 248

                       250
                ....*....|....*..
gi 17541250 243 TDHQYLFVHQVMMNFFE 259
Cdd:cd14606 249 TEAQYKFIYVAIAQFIE 265
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 45-255 2.15e-43

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: 147.05  E-value: 2.15e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEDNKDTMSF--KEKGQKV 122
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFlvTQKSVQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 123 tVKFESSKAIKFRDNSAAKVTKTVLTVEGAgcdklkVNHYHWIDWPDRGVPTADNAILELLEKARVSK----GPIAVHCS 198
Cdd:cd17668  81 -LAYYTVRNFTLRNTKIKKGSQKGRPSGRV------VTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKrhavGPVVVHCS 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 199 AGIGRTGSVVMLEYVMDQLLAgqiiEDTDKI---IQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd17668 154 AGVGRTGTYIVLDSMLQQIQH----EGTVNIfgfLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 14-260 1.32e-42

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: 146.92  E-value: 1.32e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  14 KDAQEHGKNRYKDVGCLDNNRVKLGGAwpHEYIHANYVSTPTNP----KRFICTQAPLEKTCADFWFMCLQDRVETIFML 89
Cdd:cd14600  36 KLPQNMDKNRYKDVLPYDATRVVLQGN--EDYINASYVNMEIPSanivNKYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  90 CNYKEKGAKKCHEYLPteDNKDTMSFkeKGQKVTVKFEsskaikfrDNSAAKVTKTVLTVEGAGCDKLKVNHYHWIDWPD 169
Cdd:cd14600 114 TTLTERGRTKCHQYWP--DPPDVMEY--GGFRVQCHSE--------DCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPD 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 170 RGVPTADNAILEL---LEKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTDkIIQKIREQRNNSVQTDHQ 246
Cdd:cd14600 182 HGVPDDSSDFLEFvnyVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLD-IVRKMRDQRAMMVQTSSQ 260

                       250
                ....*....|....
gi 17541250 247 YLFVHQVMMNFFEK 260
Cdd:cd14600 261 YKFVCEAILRVYEE 274
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 20-252 3.61e-42

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: 145.03  E-value: 3.61e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  20 GKNRYKDVGCLDNNRVKLGGAWPHE---YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKG 96
Cdd:cd14614  14 CKNRYTNILPYDFSRVKLVSMHEEEgsdYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  97 AKKCHEYLPTedNKDTMSFKEKGQKVTVKFESSKAI--KFRDNSAAKVTktvltvegagcdklKVNHYHWIDWPDRGVPT 174
Cdd:cd14614  94 RVKCDHYWPF--TEEPVAYGDITVEMLSEEEQPDWAirEFRVSYADEVQ--------------DVMHFNYTAWPDHGVPT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 175 ADNA--ILELL----EKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYL 248
Cdd:cd14614 158 ANAAesILQFVqmvrQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFV-DILGLVSEMRSYRMSMVQTEEQYI 236


                ....
gi 17541250 249 FVHQ 252
Cdd:cd14614 237 FIHQ 240
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 21-251 1.29e-41

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: 143.31  E-value: 1.29e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLG---GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14553   6 KNRYANVIAYDHSRVILQpieGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEDNkDTMSFKEKGQKVTVKFesskaikfrdnsaAKVTKTVLTVEGAGC-DKLKVNHYHWIDWPDRGVPTAD 176
Cdd:cd14553  86 VKCDQYWPTRGT-ETYGLIQVTLLDTVEL-------------ATYTVRTFALHKNGSsEKREVRQFQFTAWPDHGVPEHP 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17541250 177 NAILELLEKARVSK----GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVH 251
Cdd:cd14553 152 TPFLAFLRRVKACNppdaGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTV-DIYGHVTCLRAQRNYMVQTEDQYIFIH 229
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 11-249 1.35e-40

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: 141.26  E-value: 1.35e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  11 KAFKDAQEHGKNRYKDVGCLDNNRVKLGGAwPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLC 90
Cdd:cd14607  17 RVAKYPENRNRNRYRDVSPYDHSRVKLQNT-ENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  91 NYKEKGAKKCHEYLPTEDnKDTMSFKEKGQKVTVKFESSKAIkfrdnsaakVTKTVLTVEGAGCDKLK-VNHYHWIDWPD 169
Cdd:cd14607  96 RIVEKDSVKCAQYWPTDE-EEVLSFKETGFSVKLLSEDVKSY---------YTVHLLQLENINSGETRtISHFHYTTWPD 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 170 RGVPTADNAILELLEKARVS------KGPIAVHCSAGIGRTGSVVMLE---YVMDQLLAGQIieDTDKIIQKIREQRNNS 240
Cdd:cd14607 166 FGVPESPASFLNFLFKVRESgslspeHGPAVVHCSAGIGRSGTFSLVDtclVLMEKKDPDSV--DIKQVLLDMRKYRMGL 243


                ....*....
gi 17541250 241 VQTDHQYLF 249
Cdd:cd14607 244 IQTPDQLRF 252
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 22-252 2.28e-40

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: 139.66  E-value: 2.28e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  22 NRYKDVGCLDNNRVKL---GGAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAK 98
Cdd:cd14616   1 NRFPNIKPYNNNRVKLiadAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  99 KCHEYLPtEDNKDTMSFkekGQKVTVKFESSKAIKFrdnsaakvTKTVLTVEGAGcDKLKVNHYHWIDWPDRGVPTADNA 178
Cdd:cd14616  81 RCHQYWP-EDNKPVTVF---GDIVITKLMEDVQIDW--------TIRDLKIERHG-DYMMVRQCNFTSWPEHGVPESSAP 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541250 179 ILELLEKARVSKG----PIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14616 148 LIHFVKLVRASRAhdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFV-DIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 21-249 4.59e-40

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: 139.06  E-value: 4.59e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKL----GGAwphEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKG 96
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVklkqGDN---DYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  97 AKKCHEYLPTEDNKDtMSFKEKGQKVTVKFESSKA-IKFRD----NSAAKVTKTVLtvegagcdklkvnHYHWIDWPDRG 171
Cdd:cd14545  78 QIKCAQYWPQGEGNA-MIFEDTGLKVTLLSEEDKSyYTVRTleleNLKTQETREVL-------------HFHYTTWPDFG 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 172 VPTADNAILELLEKARVS------KGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIE-DTDKIIQKIREQRNNSVQTD 244
Cdd:cd14545 144 VPESPAAFLNFLQKVRESgslssdVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSSvDVKKVLLEMRKYRMGLIQTP 223


                ....*
gi 17541250 245 HQYLF 249
Cdd:cd14545 224 DQLRF 228
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 21-257 1.10e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 140.14  E-value: 1.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   21 KNRYKDVGCLDNNRVKL----GGAwphEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKG 96
Cdd:PHA02742  55 KCRYPDAPCFDRNRVILkiedGGD---DFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   97 AKKCHEYLPTednkdtmsfKEKGQKVTVKFeSSKAIKFRDNSAAKVTKTVLTVEGAGCdKLKVNHYHWIDWPDRGVPTAD 176
Cdd:PHA02742 132 KEACYPYWMP---------HERGKATHGEF-KIKTKKIKSFRNYAVTNLCLTDTNTGA-SLDIKHFAYEDWPHGGLPRDP 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  177 NAILELL---------------EKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEdTDKIIQKIREQRNNSV 241
Cdd:PHA02742 201 NKFLDFVlavreadlkadvdikGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIP-LLSIVRDLRKQRHNCL 279

                        250
                 ....*....|....*.
gi 17541250  242 QTDHQYLFVHQVMMNF 257
Cdd:PHA02742 280 SLPQQYIFCYFIVLIF 295
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 44-250 1.15e-39

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: 137.46  E-value: 1.15e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  44 EYIHANYV------STPTNpkRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPteDNKDTMSFKE 117
Cdd:cd14541   1 DYINANYVnmeipgSGIVN--RYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWP--DLGETMQFGN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 118 KgQKVTVKFESSKAIKFRDnsaAKVTKTVLTVEgagcdkLKVNHYHWIDWPDRGVPTADNAILELLEKARVSKG----PI 193
Cdd:cd14541  77 L-QITCVSEEVTPSFAFRE---FILTNTNTGEE------RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVgmvePT 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17541250 194 AVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTDkIIQKIREQRNNSVQTDHQYLFV 250
Cdd:cd14541 147 VVHCSAGIGRTGVLITMETAMCLIEANEPVYPLD-IVRTMRDQRAMLIQTPSQYRFV 202
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
13-262 1.26e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 139.46  E-value: 1.26e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  13 FKDAQEHGKNRYKDVGCLDNNRVKLGGAwpheYIHANYVSTPtNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNY 92
Cdd:COG5599  37 LQNINGSPLNRFRDIQPYKETALRANLG----YLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  93 KE--KGAKKCHEYlptednkdtmsFKEKGQ--KVTVKFESSKAIKFRDNSAAKVTKtvLTVEGAGCDKLKVNHYHWIDWP 168
Cdd:COG5599 112 DEisKPKVKMPVY-----------FRQDGEygKYEVSSELTESIQLRDGIEARTYV--LTIKGTGQKKIEIPVLHVKNWP 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 169 DRGVPTAD------NAILELLEKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAG-QIIEDTDKIIQKIREQRNNS- 240
Cdd:COG5599 179 DHGAISAEalknlaDLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALvQITLSVEEIVIDMRTSRNGGm 258

                       250       260
                ....*....|....*....|..
gi 17541250 241 VQTDHQYlfvhQVMMNFFEKRG 262
Cdd:COG5599 259 VQTSEQL----DVLVKLAEQQI 276
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 21-255 1.50e-39

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: 138.04  E-value: 1.50e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLGGAwpHEYIHANYVSTPTNPKRF--ICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAK 98
Cdd:cd14597   6 KNRYKNILPYDTTRVPLGDE--GGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGGKI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  99 KCHEYLPTEDNKDTMsFKEKGQKVTVKFESSKAIKFRdnsaakvtktVLTVEGAGCDKLK-VNHYHWIDWPDRGVPTADN 177
Cdd:cd14597  84 KCQRYWPEILGKTTM-VDNRLQLTLVRMQQLKNFVIR----------VLELEDIQTREVRhITHLNFTAWPDHDTPSQPE 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 178 AILELLEKAR--VSKGPIAVHCSAGIGRTGSVVMLEYVMDqLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd14597 153 QLLTFISYMRhiHKSGPIITHCSAGIGRSGTLICIDVVLG-LISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 45-252 5.18e-39

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: 135.59  E-value: 5.18e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVS--TPTNPkRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTednkdtmsfkEKGQKV 122
Cdd:cd14539   1 YINASLIEdlTPYCP-RFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPT----------ERGQAL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 123 -----TVKFESSKA----------IKFRDNSAAKVtktvltvegagcdklkVNHYHWIDWPDRGVPTADNAILELLE--- 184
Cdd:cd14539  70 vygaiTVSLQSVRTtpthveriisIQHKDTRLSRS----------------VVHLQFTTWPELGLPDSPNPLLRFIEevh 133

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17541250 185 ----KARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14539 134 shylQQRSLQTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 45-249 1.57e-38

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: 134.51  E-value: 1.57e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPT--NPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAK-KCHEYLPTEDNKDtmsfKEKGqK 121
Cdd:cd17658   1 YINASLVETPAseSLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENES----REFG-R 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 122 VTVKfesSKAIKFRDNSaakVTKTVLTVEGAGCDK--LKVNHYHWIDWPDRGVPTADNAILELLEKARV---SKGPIAVH 196
Cdd:cd17658  76 ISVT---NKKLKHSQHS---ITLRVLEVQYIESEEppLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGippSAGPIVVH 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17541250 197 CSAGIGRTGSVVMLEYVMDQLLAGQIIE-DTDKIIQKIREQRNNSVQTDHQYLF 249
Cdd:cd17658 150 CSAGIGRTGAYCTIHNTIRRILEGDMSAvDLSKTVRKFRSQRIGMVQTQDQYIF 203
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 24-255 2.75e-38

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: 134.30  E-value: 2.75e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  24 YKDVGCLDNNRV---KLGGAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKC 100
Cdd:cd14620   1 YPNILPYDHSRVilsQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 101 HEYLPtednkDTMSFKEKGQKVTVKfessKAIKFRDNSAAKvtktvLTVEGAGCDKLK----VNHYHWIDWPDRGVPTAD 176
Cdd:cd14620  81 YQYWP-----DQGCWTYGNIRVAVE----DCVVLVDYTIRK-----FCIQPQLPDGCKaprlVTQLHFTSWPDFGVPFTP 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 177 NAILELLEKAR----VSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14620 147 IGMLKFLKKVKsvnpVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKV-DVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225


                ...
gi 17541250 253 VMM 255
Cdd:cd14620 226 ALL 228
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 22-256 2.87e-38

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: 134.56  E-value: 2.87e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  22 NRYKDVGCLDNNRVKLG--GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKK 99
Cdd:cd14615   1 NRYNNVLPYDISRVKLSvqSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 100 CHEYLPTEDNKDtmsfkekgqkvtvkfesskaikFRDNSAAKVTKTVL--------TVEGAGC-DKLKVNHYHWIDWPDR 170
Cdd:cd14615  81 CEEYWPSKQKKD----------------------YGDITVTMTSEIVLpewtirdfTVKNAQTnESRTVRHFHFTSWPDH 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 171 GVPTADNAILELLEKAR------VSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTD 244
Cdd:cd14615 139 GVPETTDLLINFRHLVReymkqnPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVV-DVYGIVYDLRMHRPLMVQTE 217

                       250
                ....*....|..
gi 17541250 245 HQYLFVHQVMMN 256
Cdd:cd14615 218 DQYVFLNQCALD 229
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 22-255 3.80e-38

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: 134.30  E-value: 3.80e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  22 NRYKDVGCLDNNRVKLG--GAWPH-EYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAK 98
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSqlGGEPHsDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  99 KCHEYLPTEDNKDTMSfkekgqKVTVKFESskaikfRDNSAAKVTKTVLTVEGAGCDKLKVNHYHWIDWPDRGVPTADNA 178
Cdd:cd14618  81 LCDHYWPSESTPVSYG------HITVHLLA------QSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSS 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 179 ILELLE------KARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14618 149 LMAFRElvrehvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVV-DVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                ...
gi 17541250 253 VMM 255
Cdd:cd14618 228 CIL 230
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 45-255 6.05e-38

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: 132.88  E-value: 6.05e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPT--NPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEDNKDTMsfkeKGQKV 122
Cdd:cd14538   1 YINASHIRIPVggDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLI----CGGRL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 123 TVKFESSKA--------IKFRDNSAAKVTktvltvegagcdklKVNHYHWIDWPDRGVPTADNAILELLEKARVS--KGP 192
Cdd:cd14538  77 EVSLEKYQSlqdfvirrISLRDKETGEVH--------------HITHLNFTTWPDHGTPQSADPLLRFIRYMRRIhnSGP 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541250 193 IAVHCSAGIGRTGSVVMLEYV---MDQLLAGQIIEdtdkIIQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd14538 143 IVVHCSAGIGRTGVLITIDVAlglIERDLPFDIQD----IVKDLREQRQGMIQTKDQYIFCYKACL 204
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 21-255 1.97e-37

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: 133.62  E-value: 1.97e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKL---GGAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14626  44 KNRYANVIAYDHSRVILtsvDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSR 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEdNKDTMSFKEKGQKVTVKFesskaikfrdnsAAKVTKTVLTVEGAGCDKLKVNHYHWIDWPDRGVPTADN 177
Cdd:cd14626 124 VKCDQYWPIR-GTETYGMIQVTLLDTVEL------------ATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPT 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 178 AILELLEKARV----SKGPIAVHCSAGIGRTGSVVmleyVMDQLLAGQIIEDTDKI---IQKIREQRNNSVQTDHQYLFV 250
Cdd:cd14626 191 PILAFLRRVKAcnppDAGPMVVHCSAGVGRTGCFI----VIDAMLERMKHEKTVDIyghVTCMRSQRNYMVQTEDQYIFI 266


                ....*
gi 17541250 251 HQVMM 255
Cdd:cd14626 267 HEALL 271
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 45-252 2.16e-37

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: 131.19  E-value: 2.16e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEDNKDTMSFKEKGQKVTV 124
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KFEsskaikfrdnsaaKVTKTVL---TVEGAGCDKL-KVNHYHWIDWPDRGVPTADNAILELLEKAR----VSKGPIAVH 196
Cdd:cd14551  81 LVD-------------YTTRKFCiqkVNRGIGEKRVrLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKsanpPRAGPIVVH 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17541250 197 CSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14551 148 CSAGVGRTGTFIVIDAMLDMMHAEGKV-DVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 17-255 4.54e-37

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: 131.69  E-value: 4.54e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  17 QEHGKNRYKDVGCLDNNRVKLG--GAWPH-EYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYK 93
Cdd:cd14630   2 ENRNKNRYGNIISYDHSRVRLQllDGDPHsDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  94 EKGAKKCHEYLPTEdnkdtmsfkekgqkvTVKFESSKAIKFRDNSAAKVTKTVLTVEGAGCDKLK-VNHYHWIDWPDRGV 172
Cdd:cd14630  82 EVGRVKCVRYWPDD---------------TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIReIRQFHFTSWPDHGV 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 173 PTADNAILELLEKARV----SKGPIAVHCSAGIGRTGSVVMLEYVMDqLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYL 248
Cdd:cd14630 147 PCYATGLLGFVRQVKFlnppDAGPIVVHCSAGAGRTGCFIAIDIMLD-MAENEGVVDIFNCVRELRAQRVNMVQTEEQYV 225


                ....*..
gi 17541250 249 FVHQVMM 255
Cdd:cd14630 226 FVHDAIL 232
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 13-260 5.14e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 133.59  E-value: 5.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   13 FKDAQEHGKNRYKDVGCLDNNRVKL--GGAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLC 90
Cdd:PHA02747  46 FEKPENQPKNRYWDIPCWDHNRVILdsGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   91 NYKE-KGAKKCHEYL-PTED-NKDTMSFKEKGQKVTVKfesskaikfrdnsAAKVTKTVLTVEGAGCDKLKVNHYHWIDW 167
Cdd:PHA02747 126 PTKGtNGEEKCYQYWcLNEDgNIDMEDFRIETLKTSVR-------------AKYILTLIEITDKILKDSRKISHFQCSEW 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  168 PDRGVPTADN---AILELLEKARVSKG-----------PIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEdTDKIIQKI 233
Cdd:PHA02747 193 FEDETPSDHPdfiKFIKIIDINRKKSGklfnpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAIC-LAKTAEKI 271

                        250       260       270
                 ....*....|....*....|....*....|
gi 17541250  234 REQRNNSVQTDHQYLFV---HQVMMNFFEK 260
Cdd:PHA02747 272 REQRHAGIMNFDDYLFIqpgYEVLHYFLSK 301
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
158-256 5.17e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 127.09  E-value: 5.17e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250    158 KVNHYHWIDWPDRGVPTADNAILELLEKARVS------KGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTDKIIQ 231
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNlnqsesSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 17541250    232 KIREQRNNSVQTDHQYLFVHQVMMN 256
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 158-256 5.17e-37

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: 127.09  E-value: 5.17e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250    158 KVNHYHWIDWPDRGVPTADNAILELLEKARVS------KGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTDKIIQ 231
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNlnqsesSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 17541250    232 KIREQRNNSVQTDHQYLFVHQVMMN 256
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 45-257 5.90e-37

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: 130.65  E-value: 5.90e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPK--RFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTE-DNKDTMSFKEkgqk 121
Cdd:cd14540   1 YINASHITATVGGKqrFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLgGEHDALTFGE---- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 122 vtvkFESSKaiKFRDNSAAKVTKTVLTVEGAGCDKLKVNHYHWIDWPDRGVPTADNAILELLEKAR--------VSKG-- 191
Cdd:cd14540  77 ----YKVST--KFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINsvrrhtnqDVAGhn 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17541250 192 ---PIAVHCSAGIGRTGsVVMLEYVMDQLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQVMMNF 257
Cdd:cd14540 151 rnpPTLVHCSAGVGRTG-VVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 21-258 2.03e-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: 129.57  E-value: 2.03e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLGGAWPHE---YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEdsdYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPtedNKDTMSFKEKGQKVTVKFESSKaikfrdnsaakvTKTVLTVEGAGCDKL--KVNHYHWIDWPDRGVPTA 175
Cdd:cd14602  81 KKCERYWA---EPGEMQLEFGPFSVTCEAEKRK------------SDYIIRTLKVKFNSEtrTIYQFHYKNWPDHDVPSS 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 176 DNAILELLEKARVSKG----PIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTD--KIIQKIREQRNNSVQTDHQYLF 249
Cdd:cd14602 146 IDPILELIWDVRCYQEddsvPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSvfSLIQEMRTQRPSLVQTKEQYEL 225


                ....*....
gi 17541250 250 VHQVMMNFF 258
Cdd:cd14602 226 VYNAVIELF 234
PHA02738 PHA02738
hypothetical protein; Provisional
 22-259 4.76e-36

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 131.20  E-value: 4.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   22 NRYKDVGCLDNNRVKLggawPHE-----YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKG 96
Cdd:PHA02738  53 NRYLDAVCFDHSRVIL----PAErnrgdYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   97 AKKCHEYLPTEDNKDtMSFKeKGQKVTVKFESSKAIkfrdnsaakVTKTVLTVEGAGCDKlKVNHYHWIDWPDRGVPTAD 176
Cdd:PHA02738 129 REKCFPYWSDVEQGS-IRFG-KFKITTTQVETHPHY---------VKSTLLLTDGTSATQ-TVTHFNFTAWPDHDVPKNT 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  177 ----NAILEL------LEKARVSKG-------PIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEdTDKIIQKIREQRNN 239
Cdd:PHA02738 197 seflNFVLEVrqcqkeLAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVS-IPSIVSSIRNQRYY 275

                        250       260
                 ....*....|....*....|
gi 17541250  240 SVQTDHQYLFVHQVMMNFFE 259
Cdd:PHA02738 276 SLFIPFQYFFCYRAVKRYVN 295
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 11-249 6.27e-36

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: 129.76  E-value: 6.27e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  11 KAFKDAQEHGKNRYKDVGCLDNNRVKLGGAwPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLC 90
Cdd:cd14608  18 RVAKLPKNKNRNRYRDVSPFDHSRIKLHQE-DNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLN 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  91 NYKEKGAKKCHEYLPTEDNKDtMSFKEKGQKVTVKFESSKA-IKFR----DNSAAKVTKTVLtvegagcdklkvnHYHWI 165
Cdd:cd14608  97 RVMEKGSLKCAQYWPQKEEKE-MIFEDTNLKLTLISEDIKSyYTVRqlelENLTTQETREIL-------------HFHYT 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 166 DWPDRGVPTADNAILELLEKARVS------KGPIAVHCSAGIGRTGSVVMLE---YVMDQLLAGQIIeDTDKIIQKIREQ 236
Cdd:cd14608 163 TWPDFGVPESPASFLNFLFKVRESgslspeHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSV-DIKKVLLEMRKF 241

                       250
                ....*....|...
gi 17541250 237 RNNSVQTDHQYLF 249
Cdd:cd14608 242 RMGLIQTADQLRF 254
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 21-252 2.32e-35

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: 127.26  E-value: 2.32e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLG---GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14554   9 KNRLVNILPYESTRVCLQpirGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGR 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEDNK-------DTMSFKEKGQKVTVKFESSKAikfRDNSAAKVTKtvltvegagcdklkvnhYHWIDWPDR 170
Cdd:cd14554  89 EKCHQYWPAERSAryqyfvvDPMAEYNMPQYILREFKVTDA---RDGQSRTVRQ-----------------FQFTDWPEQ 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 171 GVPTADNAILELLEKARVSK------GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTD 244
Cdd:cd14554 149 GVPKSGEGFIDFIGQVHKTKeqfgqeGPITVHCSAGVGRTGVFITLSIVLERMRYEGVV-DVFQTVKLLRTQRPAMVQTE 227


                ....*...
gi 17541250 245 HQYLFVHQ 252
Cdd:cd14554 228 DQYQFCYR 235
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 44-255 4.99e-35

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: 125.52  E-value: 4.99e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  44 EYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPtEDNKDTMSFKekgqkvt 123
Cdd:cd14631  14 DYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFK------- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 124 VKFESSKAIkfrdnsAAKVTKTvLTVEGAGCDKLK-VNHYHWIDWPDRGVPTADNAILELLEKARVSK----GPIAVHCS 198
Cdd:cd14631  86 VTCVEMEPL------AEYVVRT-FTLERRGYNEIReVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNppsaGPIVVHCS 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17541250 199 AGIGRTGSVVMLEYVMDqLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd14631 159 AGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 21-255 5.38e-35

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: 127.52  E-value: 5.38e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKL---GGAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14625  50 KNRYANVIAYDHSRVILqpiEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSR 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEdNKDTMSFKEKGQKVTVKFesskaikfrdnsAAKVTKTVLTVEGAGCDKLKVNHYHWIDWPDRGVPTADN 177
Cdd:cd14625 130 IKCDQYWPSR-GTETYGMIQVTLLDTIEL------------ATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPT 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 178 AILELLEKARV----SKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQV 253
Cdd:cd14625 197 PFLAFLRRVKTcnppDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTV-DIYGHVTLMRSQRNYMVQTEDQYSFIHDA 275


                ..
gi 17541250 254 MM 255
Cdd:cd14625 276 LL 277
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 45-255 2.01e-34

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: 123.49  E-value: 2.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPtednKDTMSFKEKgqKVT- 123
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP----DDTEVYGDI--KVTl 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 124 VKFESskaikfrdnSAAKVTKTvLTVEGAGCDKLK-VNHYHWIDWPDRGVPTADNAILELLEKARVSK----GPIAVHCS 198
Cdd:cd14555  75 VETEP---------LAEYVVRT-FALERRGYHEIReVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNppsaGPIVVHCS 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17541250 199 AGIGRTGSVVMLEYVMDqLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd14555 145 AGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 14-255 3.33e-34

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: 125.16  E-value: 3.33e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  14 KDAQEHGKNRYKDVGCLDNNRVKLG---GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLC 90
Cdd:cd14633  36 KKDENRMKNRYGNIIAYDHSRVRLQpieGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVT 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  91 NYKEKGAKKCHEYLPtednKDTMSFKEkgQKVTVkfesskaikFRDNSAAKVTKTVLTVEGAGCDKLK-VNHYHWIDWPD 169
Cdd:cd14633 116 NLVEVGRVKCCKYWP----DDTEIYKD--IKVTL---------IETELLAEYVIRTFAVEKRGVHEIReIRQFHFTGWPD 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 170 RGVPTADNAILELLEKARV----SKGPIAVHCSAGIGRTGSVVMLEYVMDqLLAGQIIEDTDKIIQKIREQRNNSVQTDH 245
Cdd:cd14633 181 HGVPYHATGLLGFVRQVKSksppNAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSRRVNMVQTEE 259

                       250
                ....*....|
gi 17541250 246 QYLFVHQVMM 255
Cdd:cd14633 260 QYVFIHDAIL 269
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 21-258 6.34e-34

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: 6.34e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLG---GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14621  55 KNRYVNILPYDHSRVHLTpveGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKE 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEDNKDTMSFKEKGQKVTVKFESSkAIKFrdnsaakVTKTVLTVEGAGCDKLkVNHYHWIDWPDRGVPTADN 177
Cdd:cd14621 135 CKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYT-VRKF-------CIQQVGDVTNKKPQRL-ITQFHFTSWPDFGVPFTPI 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 178 AILELLEKARVSK----GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQV 253
Cdd:cd14621 206 GMLKFLKKVKNCNpqyaGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKV-DVYGFVSRIRAQRCQMVQTDMQYVFIYQA 284


                ....*
gi 17541250 254 MMNFF 258
Cdd:cd14621 285 LLEHY 289
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 21-259 2.15e-33

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: 123.18  E-value: 2.15e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKL--GGAWPHEYIHANYVSTPTNPK--RFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKG 96
Cdd:cd14599  41 RNRIREVVPYEENRVELvpTKENNTGYINASHIKVTVGGEewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  97 AKKCHEYLPTEDNKDTMSFKEKGqKVTVkfesskaiKFRDNSAAKVTKTVLTVEGAGCDKLKVNHYHWIDWPDRGVPTAD 176
Cdd:cd14599 121 RSKSHRYWPKLGSKHSSATYGKF-KVTT--------KFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEV 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 177 NAILELLEK--------------ARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEdTDKIIQKIREQRNNSVQ 242
Cdd:cd14599 192 QGFLSYLEEiqsvrrhtnsmldsTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVE-VPVMLRHLREQRMFMIQ 270

                       250
                ....*....|....*..
gi 17541250 243 TDHQYLFVHQVMMNFFE 259
Cdd:cd14599 271 TIAQYKFVYQVLIQFLK 287
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 45-252 4.45e-33

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: 119.93  E-value: 4.45e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEDNkDTMSFKEkgqkVTV 124
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEE-GSRAFGD----VVV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KFESSKaiKFRDNSAAKVTKTVLTVEGAGCDklkVNHYHWIDWPDRGVPTADNAILELleKARVSK------GPIAVHCS 198
Cdd:cd14557  76 KINEEK--ICPDYIIRKLNINNKKEKGSGRE---VTHIQFTSWPDHGVPEDPHLLLKL--RRRVNAfnnffsGPIVVHCS 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17541250 199 AGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14557 149 AGVGRTGTYIGIDAMLEGLEAEGRV-DVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 21-255 8.22e-33

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: 121.76  E-value: 8.22e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLG---GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14624  50 KNRYANVIAYDHSRVLLSaieGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSR 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEdNKDTMSFKEKGQKVTVKFesskaikfrdnsAAKVTKTVLTVEGAGCDKLKVNHYHWIDWPDRGVPTADN 177
Cdd:cd14624 130 VKCDQYWPSR-GTETYGLIQVTLLDTVEL------------ATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPT 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 178 AILELLEKARV----SKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQV 253
Cdd:cd14624 197 PFLAFLRRVKTcnppDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTV-DIYGHVTLMRAQRNYMVQTEDQYIFIHDA 275


                ..
gi 17541250 254 MM 255
Cdd:cd14624 276 LL 277
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 21-254 8.91e-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: 120.74  E-value: 8.91e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLGGAWPHE----YIHANYVSTPTNPKR-FICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEK 95
Cdd:cd14613  28 KNRYKTILPNPHSRVCLTSPDQDDplssYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  96 GaKKCHEYLPTEdnkdtmSFKEKGQKVTVKfessKAIKFRDNSAakvtkTVLTVEgAGCDKLKVNHYHWIDWPDRGVPTA 175
Cdd:cd14613 108 N-EKCTEYWPEE------QVTYEGIEITVK----QVIHADDYRL-----RLITLK-SGGEERGLKHYWYTSWPDQKTPDN 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 176 DNAILELL-------EKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYL 248
Cdd:cd14613 171 APPLLQLVqeveearQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVV-DILRTTCQLRLDRGGMIQTCEQYQ 249


                ....*.
gi 17541250 249 FVHQVM 254
Cdd:cd14613 250 FVHHVL 255
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 21-267 9.64e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 122.44  E-value: 9.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   21 KNRYKDVGCLDNNRVKLG----------GAW------------PHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMC 78
Cdd:PHA02746  54 KNRFHDIPCWDHSRVVINaheslkmfdvGDSdgkkievtsednAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   79 LQDRVETIFMLCNYkEKGAKKCHEYLptednkdtmsFKEKGQKVTVKFESSKAIKFRDNSAAKVTKTVLTVEGAGCDKlK 158
Cdd:PHA02746 134 SEHESQVIVSLTDI-DDDDEKCFELW----------TKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR-E 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  159 VNHYHWIDWPDRGVPTADNAILELL-----EKARVSK---------GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIE 224
Cdd:PHA02746 202 IHHFWFPDWPDNGIPTGMAEFLELInkvneEQAELIKqadndpqtlGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVC 281

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 17541250  225 dTDKIIQKIREQRNNSVQTDHQYLFVHQVMmnffeKRGLLDEA 267
Cdd:PHA02746 282 -LGEIVLKIRKQRHSSVFLPEQYAFCYKAL-----KYAIIEEA 318
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 45-255 1.12e-32

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: 119.08  E-value: 1.12e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPK--RFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPtEDNKDTMsfkeKGQKV 122
Cdd:cd14596   1 YINASYITMPVGEEelFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWP-ETLQEPM----ELENY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 123 TVKFESSKAIKFRDNSAAKVtktvltVEGAGCDKLKVNHYHWIDWPDRGVPTADNAILELLEKARV--SKGPIAVHCSAG 200
Cdd:cd14596  76 QLRLENYQALQYFIIRIIKL------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKvhNTGPIVVHCSAG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17541250 201 IGRTGSVVMLEYVMDQLLAGQIIEDTDkIIQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd14596 150 IGRAGVLICVDVLLSLIEKDLSFNIKD-IVREMRQQRYGMIQTKDQYLFCYKVVL 203
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 21-258 1.27e-32

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: 121.38  E-value: 1.27e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLG---GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14627  56 KNRLVNIMPYETTRVCLQpirGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGR 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEDNK-------DTMSFKEKGQKVTVKFESSKAikfRDNSAAKVTKtvltvegagcdklkvnhYHWIDWPDR 170
Cdd:cd14627 136 EKCHQYWPAERSAryqyfvvDPMAEYNMPQYILREFKVTDA---RDGQSRTVRQ-----------------FQFTDWPEQ 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 171 GVPTADNAILELLEKARVSK------GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTD 244
Cdd:cd14627 196 GVPKSGEGFIDFIGQVHKTKeqfgqdGPISVHCSAGVGRTGVFITLSIVLERMRYEGVV-DIFQTVKMLRTQRPAMVQTE 274

                       250
                ....*....|....
gi 17541250 245 HQYLFVHQVMMNFF 258
Cdd:cd14627 275 DEYQFCYQAALEYL 288
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 45-255 1.63e-32

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: 118.62  E-value: 1.63e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPteDNKDTmsfkekgqkvtv 124
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP--DDSDT------------ 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 kFESSKAIKFRDNSAAKVTKTVLTVEGAGCD-KLKVNHYHWIDWPDRGVPTADNAILELLEKARVSK----GPIAVHCSA 199
Cdd:cd14632  67 -YGDIKITLLKTETLAEYSVRTFALERRGYSaRHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTppdaGPVVVHCSA 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17541250 200 GIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd14632 146 GAGRTGCYIVLDVMLDMAECEGVV-DIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 22-252 1.78e-32

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: 119.25  E-value: 1.78e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  22 NRYKDVGCLDNNRVKLGGAWPH---EYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAK 98
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDDpcsDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  99 KCHEYLPTEdnKDTMSFKEkgqkVTVKFESSKAIKFRDNSAAKVTKTvltvEGAGCDKLkVNHYHWIDWPDRGVPTADNA 178
Cdd:cd14617  81 KCDHYWPAD--QDSLYYGD----LIVQMLSESVLPEWTIREFKICSE----EQLDAPRL-VRHFHYTVWPDHGVPETTQS 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 179 ILELLEKAR------VSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14617 150 LIQFVRTVRdyinrtPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSV-DIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 21-258 5.99e-32

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: 119.45  E-value: 5.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLG---GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14628  55 KNRLVNIMPYESTRVCLQpirGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGR 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEDNK-------DTMSFKEKGQKVTVKFESSKAikfRDNSAAKVTKtvltvegagcdklkvnhYHWIDWPDR 170
Cdd:cd14628 135 EKCHQYWPAERSAryqyfvvDPMAEYNMPQYILREFKVTDA---RDGQSRTVRQ-----------------FQFTDWPEQ 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 171 GVPTADNAILELLEKARVSK------GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTD 244
Cdd:cd14628 195 GVPKSGEGFIDFIGQVHKTKeqfgqdGPISVHCSAGVGRTGVFITLSIVLERMRYEGVV-DIFQTVKMLRTQRPAMVQTE 273

                       250
                ....*....|....
gi 17541250 245 HQYLFVHQVMMNFF 258
Cdd:cd14628 274 DQYQFCYRAALEYL 287
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 44-260 1.15e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 116.58  E-value: 1.15e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  44 EYIHANYVS--TPTNP--KRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEDNKDTMSfkeKG 119
Cdd:cd14601   1 DYINANYINmeIPSSSiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYG---GF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 120 QKVTVKFESSKAIKFRDNSAAKVTKTvltvegagcDKLKVNHYHWIDWPDRGVPTADNAILE---LLEKARVSKG-PIAV 195
Cdd:cd14601  78 QVTCHSEEGNPAYVFREMTLTNLEKN---------ESRPLTQIQYIAWPDHGVPDDSSDFLDfvcLVRNKRAGKDePVVV 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541250 196 HCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTDkIIQKIREQRNNSVQTDHQYLFVHQVMMNFFEK 260
Cdd:cd14601 149 HCSAGIGRTGVLITMETAMCLIECNQPVYPLD-IVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 45-254 1.67e-31

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 115.83  E-value: 1.67e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEdnkDTMSFKEkgqkVTV 124
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED---GSVSSGD----ITV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KfesskaIKFRDNSAAKVTKTVLTVEGAGCDKLKVNHYHWIDWPDRGVPTADNAILELL-----EKARVSKGPIAVHCSA 199
Cdd:cd14552  74 E------LKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIaavqkQQQQSGNHPITVHCSA 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17541250 200 GIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQVM 254
Cdd:cd14552 148 GAGRTGTFCALSTVLERVKAEGVL-DVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 21-254 5.86e-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: 115.70  E-value: 5.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLGGAWPHE----YIHANYVST-PTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEK 95
Cdd:cd14612  18 KDRYKTILPNPQSRVCLRRAGSQEeegsYINANYIRGyDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  96 gAKKCHEYLPTEDNkdtmSFKEKGQKVTvKFESSKAIKFRDnsaakvtktvLTVEGAGcDKLKVNHYHWIDWPDRGVPTA 175
Cdd:cd14612  98 -KEKCVHYWPEKEG----TYGRFEIRVQ-DMKECDGYTIRD----------LTIQLEE-ESRSVKHYWFSSWPDHQTPES 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 176 DNAILELL------EKARVSKGPIAVHCSAGIGRTGSVVMLEyvmdqlLAGQIIEDTDK-----IIQKIREQRNNSVQTD 244
Cdd:cd14612 161 AGPLLRLVaeveesRQTAASPGPIVVHCSAGIGRTGCFIATS------IGCQQLKDTGKvdilgIVCQLRLDRGGMIQTS 234

                       250
                ....*....|
gi 17541250 245 HQYLFVHQVM 254
Cdd:cd14612 235 EQYQFLHHTL 244
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 44-257 9.45e-31

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: 113.95  E-value: 9.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  44 EYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEdnkDTMSFKEkgqkVT 123
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE---GSVTHGE----IT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 124 VKFES---SKAIKFRDnsaakvtkTVLTVEGAGCDKLkVNHYHWIDWPDRGVPTADNAILELL-----EKARVSKGPIAV 195
Cdd:cd14622  74 IEIKNdtlLETISIRD--------FLVTYNQEKQTRL-VRQFHFHGWPEIGIPAEGKGMIDLIaavqkQQQQTGNHPIVV 144

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17541250 196 HCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQVMMNF 257
Cdd:cd14622 145 HCSAGAGRTGTFIALSNILERVKAEGLL-DVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 21-258 1.98e-29

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: 112.90  E-value: 1.98e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLG---GAWPHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGA 97
Cdd:cd14629  56 KNRLVNIMPYELTRVCLQpirGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGR 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  98 KKCHEYLPTEDNK-------DTMSFKEKGQKVTVKFESSKAikfRDNSAAKVTKtvltvegagcdklkvnhYHWIDWPDR 170
Cdd:cd14629 136 EKCHQYWPAERSAryqyfvvDPMAEYNMPQYILREFKVTDA---RDGQSRTIRQ-----------------FQFTDWPEQ 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 171 GVPTADNAILELLEKARVSK------GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTD 244
Cdd:cd14629 196 GVPKTGEGFIDFIGQVHKTKeqfgqdGPITVHCSAGVGRTGVFITLSIVLERMRYEGVV-DMFQTVKTLRTQRPAMVQTE 274

                       250
                ....*....|....
gi 17541250 245 HQYLFVHQVMMNFF 258
Cdd:cd14629 275 DQYQLCYRAALEYL 288
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 45-250 4.70e-29

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 109.84  E-value: 4.70e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVS--TPTNPKrFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPtednkdtmsfkEKGQKV 122
Cdd:cd14546   1 YINASTIYdhDPRNPA-YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-----------EEGSEV 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 123 TVKFE---SSKAIKFRD---------NSAAKVTKTVltvegagcdklkvNHYHWIDWPDRGVPTADNAILELLEKA-RVS 189
Cdd:cd14546  69 YHIYEvhlVSEHIWCDDylvrsfylkNLQTSETRTV-------------TQFHFLSWPDEGIPASAKPLLEFRRKVnKSY 135

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541250 190 KG---PIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFV 250
Cdd:cd14546 136 RGrscPIVVHCSDGAGRTGTYILIDMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFV 199
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 21-249 7.12e-29

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: 111.30  E-value: 7.12e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLGGAWPH---EYIHANYV--STPTNPKrFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEK 95
Cdd:cd14610  47 KNRSLAVLPYDHSRIILKAENSHshsDYINASPImdHDPRNPA-YIATQGPLPATVADFWQMVWESGCVVIVMLTPLAEN 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  96 GAKKCHEYLPTEdNKDTMSFKEkgqkVTVKFESSKAIKFRDNSAakVTKTVLTVEgagcdKLKVNHYHWIDWPDRGVPTA 175
Cdd:cd14610 126 GVKQCYHYWPDE-GSNLYHIYE----VNLVSEHIWCEDFLVRSF--YLKNLQTNE-----TRTVTQFHFLSWNDQGVPAS 193

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541250 176 DNAILELLEKA----RVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLF 249
Cdd:cd14610 194 TRSLLDFRRKVnkcyRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 45-259 9.24e-29

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: 109.29  E-value: 9.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKR--FICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEDNKDTmsfkekgqkv 122
Cdd:cd14598   1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHN---------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 123 TVKFESSK-AIKFRDNSAAKVT-----KTVLTVEgagcdKLKVNHYHWIDWPDRGVPTADNAILELLEK----------- 185
Cdd:cd14598  71 TVTYGRFKiTTRFRTDSGCYATtglkiKHLLTGQ-----ERTVWHLQYTDWPEHGCPEDLKGFLSYLEEiqsvrrhtnst 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541250 186 --ARVSKGPIAVHCSAGIGRTGsVVMLEYVMDQLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQVMMNFFE 259
Cdd:cd14598 146 idPKSPNPPVLVHCSAGVGRTG-VVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 21-252 1.50e-27

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: 106.16  E-value: 1.50e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLGGAWPHE----YIHANYVSTPTNPKR-FICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEK 95
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNSNDslstYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  96 GaKKCHEYLPtednkdtmsfKEKG--QKVTVKFESSKAIKFRdnsaakVTKTVLTVEGAGCDKLKvnHYHWIDWPDRGVP 173
Cdd:cd14611  82 N-EKCVLYWP----------EKRGiyGKVEVLVNSVKECDNY------TIRNLTLKQGSQSRSVK--HYWYTSWPDHKTP 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 174 TADNAILELL------EKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQY 247
Cdd:cd14611 143 DSAQPLLQLMldveedRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVV-DVLSIVCQLRVDRGGMVQTSEQY 221


                ....*
gi 17541250 248 LFVHQ 252
Cdd:cd14611 222 EFVHH 226
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 44-254 2.67e-27

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 105.51  E-value: 2.67e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  44 EYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPTEdnkDTMSFKEkgqkVT 123
Cdd:cd14623  25 DYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSD---GSVSYGD----IT 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 124 VKfesskaIKFRDNSAAKVTKTVLTVEGAGCDKLKVNHYHWIDWPDRGVPTADNAILELL---EKARVSKG--PIAVHCS 198
Cdd:cd14623  98 IE------LKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIaavQKQQQQSGnhPITVHCS 171

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17541250 199 AGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQVM 254
Cdd:cd14623 172 AGAGRTGTFCALSTVLERVKAEGIL-DVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 21-249 8.00e-26

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: 103.19  E-value: 8.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  21 KNRYKDVGCLDNNRVKLG---GAWPHEYIHANYV--STPTNPKrFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEK 95
Cdd:cd14609  45 KNRNPDFVPYDHARIKLKaesNPSRSDYINASPIieHDPRMPA-YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVED 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  96 GAKKCHEYLPTEdnkdtmsfkekGQKVTVKFES---SKAIKFRD---------NSAAKVTKTVltvegagcdklkvNHYH 163
Cdd:cd14609 124 GVKQCDRYWPDE-----------GSSLYHIYEVnlvSEHIWCEDflvrsfylkNVQTQETRTL-------------TQFH 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 164 WIDWPDRGVPTADNAILELLEKA----RVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEDTDKIIQKIREQRNN 239
Cdd:cd14609 180 FLSWPAEGIPSSTRPLLDFRRKVnkcyRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLEHVRDQRPG 259

                       250
                ....*....|
gi 17541250 240 SVQTDHQYLF 249
Cdd:cd14609 260 MVRTKDQFEF 269
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 45-249 1.43e-22

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: 92.46  E-value: 1.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCHEYLPteDNKDTMSFKEkgqkVTV 124
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG--DEKKTYGDIE----VEL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KFESSKAIKFRDNSAAKVTKTVltvegagcDKLKVNHYHWIDWPDRGVPTADNAILELLEKARVSKG----------PIA 194
Cdd:cd14558  75 KDTEKSPTYTVRVFEITHLKRK--------DSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPyknskhgrsvPIV 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17541250 195 VHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLF 249
Cdd:cd14558 147 VHCSDGSSRTGIFCALWNLLESAETEKVV-DVFQVVKALRKQRPGMVSTLEQYQF 200
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 45-252 1.09e-20

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: 87.46  E-value: 1.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLcNYKEKGAKKCHEYLPtednkdtmsfkEKGQKVTV 124
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWP-----------DEGSGTYG 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KFEsskaIKFRDNSAAK-VTKTVLTVEGAGCD---KLKVNHYHWIDWP-DRGVPTADNAILELLekARVSK-------GP 192
Cdd:cd14556  69 PIQ----VEFVSTTIDEdVISRIFRLQNTTRPqegYRMVQQFQFLGWPrDRDTPPSKRALLKLL--SEVEKwqeqsgeGP 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 193 IAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14556 143 IVVHCLNGVGRSGVFCAISSVCERIKVENVV-DVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 45-256 8.08e-16

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: 74.29  E-value: 8.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLcnYKEKGAKKCHEYLPtedNKDTMSFKekgqKVTV 124
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML--NEMDAAQLCMQYWP---EKTSCCYG----PIQV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KFESSKAIKFRDNSAAKVTKTVLTVEGAGCdklkVNHYHWIDWPD-RGVPTADNAILELL-------EKARVSKGPIAVH 196
Cdd:cd14634  72 EFVSADIDEDIISRIFRICNMARPQDGYRI----VQHLQYIGWPAyRDTPPSKRSILKVVrrlekwqEQYDGREGRTVVH 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 197 CSAGIGRTGSVVMLEYVmDQLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQVMMN 256
Cdd:cd14634 148 CLNGGGRSGTFCAICSV-CEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
162-252 2.34e-15

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 71.16  E-value: 2.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 162 YHWIDWPDRGVPTADN--AILELLEKARVSKGPIAVHCSAGIGRTGSVV---MLEYVMdqllagqiieDTDKIIQKIREQ 236
Cdd:COG2453  50 YLHLPIPDFGAPDDEQlqEAVDFIDEALREGKKVLVHCRGGIGRTGTVAaayLVLLGL----------SAEEALARVRAA 119

                        90
                ....*....|....*.
gi 17541250 237 RNNSVQTDHQYLFVHQ 252
Cdd:COG2453 120 RPGAVETPAQRAFLER 135
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 146-252 4.51e-12

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: 62.29  E-value: 4.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 146 VLTV-EGAGCDKLKVNH---YHWIDWPDRGVPTAD--NAILELLEKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLA 219
Cdd:cd14504  32 VVTLtEEPPPEHSDTCPglrYHHIPIEDYTPPTLEqiDEFLDIVEEANAKNEAVLVHCLAGKGRTGTMLACYLVKTGKIS 111

                        90       100       110
                ....*....|....*....|....*....|...
gi 17541250 220 GqiiedtDKIIQKIREQRNNSVQTDHQYLFVHQ 252
Cdd:cd14504 112 A------VDAINEIRRIRPGSIETSEQEKFVIQ 138
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 162-252 3.96e-11

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: 60.35  E-value: 3.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 162 YHWIDWPDRGVPTADNAILELLE--KARVSKGP-IAVHCSAGIGRTGSV-----VMLEYVMDQllagqiiedtDKIIQKI 233
Cdd:cd14505  75 WHHLPIPDGGVPSDIAQWQELLEelLSALENGKkVLIHCKGGLGRTGLIaacllLELGDTLDP----------EQAIAAV 144

                        90
                ....*....|....*....
gi 17541250 234 REQRNNSVQTDHQYLFVHQ 252
Cdd:cd14505 145 RALRPGAIQTPKQENFLHQ 163
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 45-200 7.07e-11

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: 60.41  E-value: 7.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGakKCHEYLPTEDNK-DTMSFKekgqkvt 123
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPlECETFK------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 124 VKFESSKAIKfrDNSAAKVTKTVLTVEGAGCD-KLKVNHYHWIDWPDRGVP--TADNAILELLEKARVSKGPIAVH---- 196
Cdd:cd14550  72 VTLSGEDHSC--LSNEIRLIVRDFILESTQDDyVLEVRQFQCPSWPNPCSPihTVFELINTVQEWAQQRDGPIVVHdryg 149


                ....*
gi 17541250 197 -CSAG 200
Cdd:cd14550 150 gVQAA 154
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 45-255 1.32e-10

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 59.54  E-value: 1.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKE-KGAKKCHEYLPtednkdtmsfkEKGQK-- 121
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQsNSAWPCLQYWP-----------EPGLQqy 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 122 --VTVKFESSKAIKFRDNSAAKVTKTVLTVEGagcdKLKVNHYHWIDW-PDRGVPTADNAILELLE-----KARVSKGPI 193
Cdd:cd14637  70 gpMEVEFVSGSADEDIVTRLFRVQNITRLQEG----HLMVRHFQFLRWsAYRDTPDSKKAFLHLLAsvekwQRESGEGRT 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17541250 194 AVHCSAGIGRTGSVVMLEYVMDqLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd14637 146 VVHCLNGGGRSGTYCASAMILE-MIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 178-252 2.32e-10

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 56.97  E-value: 2.32e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541250 178 AILELLEKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAGqiiedtDKIIQKIREQRNNS-VQTDHQYLFVHQ 252
Cdd:cd14494  44 RFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSA------EEAVRIVRLIRPGGiPQTIEQLDFLIK 113
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 22-247 3.23e-10

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 58.95  E-value: 3.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  22 NRYKDVGCldnnRVKLGGAWPheyIHANYVSTPTNPkRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKCH 101
Cdd:cd14559   1 NRFTNIQT----RVSTPVGKN---LNANRVQIGNKN-VAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 102 EYlptednkdtmsFKEKGQKVTVKFESSKAIKFRDNSAAKVTKTVLTVEGAGCD-KLKVnhYHWIDWPDRG-VPT----- 174
Cdd:cd14559  73 PY-----------FRQSGTYGSVTVKSKKTGKDELVDGLKADMYNLKITDGNKTiTIPV--VHVTNWPDHTaISSeglke 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 175 --------ADNAILELLEKARVS-----KGPIAVHCSAGIGRTGSVVMLEYVMDQllagQIIEDTDKIIQKIREQRNNS- 240
Cdd:cd14559 140 ladlvnksAEEKRNFYKSKGSSAindknKLLPVIHCRAGVGRTGQLAAAMELNKS----PNNLSVEDIVSDMRTSRNGKm 215


                ....*..
gi 17541250 241 VQTDHQY 247
Cdd:cd14559 216 VQKDEQL 222
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 45-255 4.01e-10

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: 58.08  E-value: 4.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEKGAKKChEYLPTED---NKDTMsfkekgqK 121
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDepiNCETF-------K 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 122 VTVKFESSKAIKFRDNsaakVTKTVLTVEGAGCDK-LKVNHYHWIDWPDRGVPTADNaiLELL----EKARVSKGPIAVH 196
Cdd:cd17669  73 VTLIAEEHKCLSNEEK----LIIQDFILEATQDDYvLEVRHFQCPKWPNPDSPISKT--FELIsiikEEAANRDGPMIVH 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17541250 197 CSAGIGRTGSVVMLEYVMDQLLAGQIIeDTDKIIQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd17669 147 DEHGGVTAGTFCALTTLMHQLEKENSV-DVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 45-255 4.56e-10

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: 58.16  E-value: 4.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEkgAKKCHEYLPTEDnkdtmsfKEKGQKVTV 124
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDP--AQLCPQYWPENG-------VHRHGPIQV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 125 KFESSKAIK------FRDNSAAKVTKTVLTVEgagcdklkvnHYHWIDWP-DRGVPTADNAILELL-------EKARVSK 190
Cdd:cd14635  72 EFVSADLEEdiisriFRIYNAARPQDGYRMVQ----------QFQFLGWPmYRDTPVSKRSFLKLIrqvdkwqEEYNGGE 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541250 191 GPIAVHCSAGIGRTGSVVMLEYVMdQLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd14635 142 GRTVVHCLNGGGRSGTFCAISIVC-EMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 45-255 4.23e-09

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: 55.42  E-value: 4.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEkgAKKCHEYLPTED-------NKDTMSFKE 117
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDL--AQGCPQYWPEEGmlrygpiQVECMSCSM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 118 KGQKVTVKFesskaikfrdnsaaKVTKTVLTVEGAgcdkLKVNHYHWIDWPD-RGVPTADNAILELL-------EKARVS 189
Cdd:cd14636  79 DCDVISRIF--------------RICNLTRPQEGY----LMVQQFQYLGWAShREVPGSKRSFLKLIlqvekwqEECDEG 140

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541250 190 KGPIAVHCSAGIGRTGSVVMLEYVMdQLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQVMM 255
Cdd:cd14636 141 EGRTIIHCLNGGGRSGMFCAISIVC-EMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 167-278 6.68e-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: 54.66  E-value: 6.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 167 WPDRGVPTADNA--ILELLEKARVSKGPIAVHCSAGIGRTGSVVMLEYVMDQLLAgqiiedTDKIIQKIREQRNNSVQTD 244
Cdd:cd14506  84 WKDYGVPSLTTIldIVKVMAFALQEGGKVAVHCHAGLGRTGVLIACYLVYALRMS------ADQAIRLVRSKRPNSIQTR 157

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17541250 245 HQYLFVH-------QVMMNFfekRGLLDEATSAIHKDFTDQ 278
Cdd:cd14506 158 GQVLCVRefaqfllPLRNVF---ACPDPKAAVTLRQYLIRQ 195
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 45-256 1.31e-08

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 53.91  E-value: 1.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  45 YIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNyKEKGAKKCHEYLPT-EDNKDTMSFkekgqkvT 123
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSrEESMNCEAF-------T 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 124 VKFESSKAIKFRDNSAAKVTKTVLtvEGAGCDK-LKVNHYHWIDWPDRGVPTAdnAILELL----EKARVSKGPIAVHCS 198
Cdd:cd17670  73 VTLISKDRLCLSNEEQIIIHDFIL--EATQDDYvLEVRHFQCPKWPNPDAPIS--STFELInvikEEALTRDGPTIVHDE 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17541250 199 AGIGRTGSVVMLEyVMDQLLAGQIIEDTDKIIQKIREQRNNSVQTDHQYLFVHQVMMN 256
Cdd:cd17670 149 FGAVSAGTLCALT-TLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 144-214 1.21e-06

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: 46.77  E-value: 1.21e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17541250 144 KTVLTVeGAGCDKLKVNH---YHWIDWPDrgVPTAD-----NAILELLEKARVSKGPIAVHCSAGIGRTGSVVMLeYVM 214
Cdd:cd14498  28 THILNV-AGEPPPNKFPDgikYLRIPIED--SPDEDilshfEEAIEFIEEALKKGGKVLVHCQAGVSRSATIVIA-YLM 102
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 166-248 4.61e-06

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: 45.67  E-value: 4.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 166 DWP--DRGVPTAD--NAILELLEK----ARVSKGPIAVHCSAGIGRTGSVVML---EYVMDQLLAgqiiedtdkiIQKIR 234
Cdd:cd14500  63 DWPfdDGSPPPDDvvDDWLDLLKTrfkeEGKPGACIAVHCVAGLGRAPVLVAIaliELGMKPEDA----------VEFIR 132

                        90
                ....*....|....*..
gi 17541250 235 EQRN---NSVQTdhQYL 248
Cdd:cd14500 133 KKRRgaiNSKQL--QFL 147
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 168-214 6.56e-06

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: 45.52  E-value: 6.56e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 17541250 168 PDRGVPTaDNAILELLEKARVSKGPIAVHCSAGIGRTGSVVMLeYVM 214
Cdd:cd14499  88 PDGSTPS-DDIVKKFLDICENEKGAIAVHCKAGLGRTGTLIAC-YLM 132
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 32-254 9.40e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 43.03  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250   32 NNRVKLGGAwpHEYIHANYVSTPTNPKRFICTQAPLEKTCADFWFMCLQDRVETIFMLCNYKEkgaKKCHEYLptednkd 111
Cdd:PHA02740  67 HRRIKLFND--EKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD---KKCFNQF------- 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  112 tMSFKEKGQKVTVKFEsSKAIKFRDNSAAKVTKTVLTVEGAgcDKLKVNHYHWIDWPDRGVPTADNAILEL--------- 182
Cdd:PHA02740 135 -WSLKEGCVITSDKFQ-IETLEIIIKPHFNLTLLSLTDKFG--QAQKISHFQYTAWPADGFSHDPDAFIDFfcniddlca 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541250  183 -LEKARVSK--GPIAVHCSAGIGRTGSVVMLEYVMDQLLAGQIIEdTDKIIQKIREQRNNSVQTDHQYLFVHQVM 254
Cdd:PHA02740 211 dLEKHKADGkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLS-IANALKKVRQKKYGCMNCLDDYVFCYHLI 284
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 166-248 1.68e-04

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 41.16  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250  166 DWP--DRGVPTAD--NAILELL--EKARVSKGP--IAVHCSAGIGRTGSVVML---EY-VMDQLLAgqiiedtdkiIQKI 233
Cdd:PTZ00242  66 DWPfdDGAPPPKAviDNWLRLLdqEFAKQSTPPetIAVHCVAGLGRAPILVALalvEYgGMEPLDA----------VGFV 135

                         90
                 ....*....|....*.
gi 17541250  234 REQRNNSV-QTDHQYL 248
Cdd:PTZ00242 136 REKRKGAInQTQLQFL 151
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
177-215 1.81e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 40.73  E-value: 1.81e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 17541250    177 NAILELLEKARVSKGPIAVHCSAGIGRTGSVVMlEYVMD 215
Cdd:smart00195  65 PEAVEFIEDAESKGGKVLVHCQAGVSRSATLII-AYLMK 102
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 165-243 2.81e-04

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: 40.39  E-value: 2.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 165 IDWP-DRGVPTADNAILELLE--KARVSKGP---IAVHCSAGIGRTGSVVMLEYVMdqllAGQIIEDTdkiIQKIREQRN 238
Cdd:cd18535  62 VDWPfDDGAPPPGKVVEDWLSllKTKFCEDPgccVAVHCVAGLGRAPVLVALALIE----SGMKYEDA---IQFIRQKRR 134


                ....*
gi 17541250 239 NSVQT 243
Cdd:cd18535 135 GAINS 139
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 177-215 4.36e-04

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: 39.55  E-value: 4.36e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 17541250   177 NAILELLEKARVSKGPIAVHCSAGIGRTGSVVMlEYVMD 215
Cdd:pfam00782  56 EEAVEFIDDARQKGGKVLVHCQAGISRSATLII-AYLMK 93
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 163-262 7.57e-04

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


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 39.29  E-value: 7.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 163 HWIDWP-DRGVPTADNAILELLE--KARVSKGP---IAVHCSAGIGRTGSVVMLEYVMdqllAGQIIEDTDKIIQKIREQ 236
Cdd:cd18537  64 QVLDWPfDDGAPPSNQIVDDWLNllKVKFREEPgccIAVHCVAGLGRAPVLVALALIE----CGMKYEDAVQFIRQKRRG 139

                        90       100
                ....*....|....*....|....*.
gi 17541250 237 RNNSVQTDHQYLFVHQVMMNFFEKRG 262
Cdd:cd18537 140 AFNSKQLLYLEKYRPKMRLRFKDSNG 165
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 179-217 7.65e-04

dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. 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.


Pssm-ID: 350416 [Multi-domain]  Cd Length: 140  Bit Score: 38.94  E-value: 7.65e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 17541250 179 ILELLEKARVSKGPIAVHCSAGIGRTGSVVmLEYVMDQL 217
Cdd:cd14568  68 AVEFIEKARASNKRVLVHCLAGISRSATIA-IAYIMKHM 105
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 163-228 9.03e-04

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 39.92  E-value: 9.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17541250  163 HWIDWPDRGVPTAD--NAILELLEKARVSKGPIAVHCSAGIGRT---GSVVMLEYVMDQLLAGQIIEDTDK 228
Cdd:PTZ00393 141 HELIFPDGDAPTVDivSNWLTIVNNVIKNNRAVAVHCVAGLGRApvlASIVLIEFGMDPIDAIVFIRDRRK 211
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 144-210 1.31e-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: 38.51  E-value: 1.31e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541250 144 KTVLT---------VEGAGCDKLKVNHYHwIDWPDRGVPTADNAILELLEKARVSKGPIAVHCSAGIGRTGSVVML 210
Cdd:cd14529  35 KTVIDlrgaderaaSEEAAAKIDGVKYVN-LPLSATRPTESDVQSFLLIMDLKLAPGPVLIHCKHGKDRTGLVSAL 109
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 147-208 2.15e-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: 37.94  E-value: 2.15e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17541250 147 LTVEGAGCDKLKVNHYHWIDWPDRGVPTADNaILELLEKAR--VSKGP---IAVHCSAGIGRTGSVV 208
Cdd:cd14497  48 LSEEEYDDDSKFEGRVLHYGFPDHHPPPLGL-LLEIVDDIDswLSEDPnnvAVVHCKAGKGRTGTVI 113
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
178-279 3.59e-03

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 38.02  E-value: 3.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 178 AILELLEKARvsKGPIAVHCSAGIGRTGSVVMLeyVmdQLLAG----QIIED-------TDKIIQKIREQRNNSVQTDhq 246
Cdd:COG2365 123 AAFRALADAE--NGPVLFHCTAGKDRTGVAAAL--L--LLALGvpreTIMADylltneyLAPLRARLLAALRAALGDE-- 194

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17541250 247 ylfVHQVMMNFFE-KRGLLDEATSAIHKDF--TDQY 279
Cdd:COG2365 195 ---DPELLAPLLGvRPEYLEAALDAIDERYgsVDAY 227
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 181-234 7.53e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual specificity protein phosphatase 19 (DUSP19), also called low molecular weight dual specificity phosphatase 3 (LMW-DSP3) or stress-activated protein kinase (SAPK) pathway-regulating phosphatase 1 (SKRP1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It 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. DUSP19 interacts with the MAPK kinase MKK7, a JNK activator, and inactivates the JNK MAPK pathway.


Pssm-ID: 350373 [Multi-domain]  Cd Length: 137  Bit Score: 36.18  E-value: 7.53e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 17541250 181 ELLEKARVSKGPIAVHCSAGIGRTGSVVmLEYVMDQllAGQIIEDTDKIIQKIR 234
Cdd:cd14523  70 EFIDEAKSQDGVVLVHCNAGVSRSASIV-IGYLMAT--ENLSFEDAFSLVKNAR 120
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 131-214 8.36e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar proteins; Dual specificity protein phosphatase 12 (DUSP12), also called YVH1, 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. DUSP12 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 targets p38 MAPK to regulate macrophage response to bacterial infection. It also ameliorates cardiac hypertrophy in response to pressure overload through c-Jun N-terminal kinase (JNK) inhibition. DUSP12 has been identified as a modulator of cell cycle progression, a function independent of phosphatase activity and mediated by its C-terminal zinc-binding domain.


Pssm-ID: 350370 [Multi-domain]  Cd Length: 144  Bit Score: 36.07  E-value: 8.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541250 131 AIKFRDNSAAKVTKtVLTVE------GAGCDKLKVNHYHWIDwpdrgvpTADNAILELLE-------KARvSKGPIAVHC 197
Cdd:cd14520  16 AADYLSLREAGITH-VLTVDseepidAPPVGKLVRKFVPALD-------EESTDLLSRLDecldfidEGR-AEGAVLVHC 86

                        90
                ....*....|....*..
gi 17541250 198 SAGIGRTGSVVMlEYVM 214
Cdd:cd14520  87 HAGVSRSAAVVT-AYLM 102
 
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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