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Conserved domains on  [gi|149041008|gb|EDL94965|]
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protein tyrosine phosphatase, non-receptor type 14 (predicted), isoform CRA_a [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 559-845 0e+00

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: 625.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 559 RLRALKKKLEDGMVFTEYEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGS 638
Cdd:cd14599    1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 639 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 718
Cdd:cd14599   81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 719 LKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGVKTRHPPIVVHCSAGVGRTGVVILSE 798
Cdd:cd14599  161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 149041008 799 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 845
Cdd:cd14599  241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
 
Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 559-845 0e+00

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: 625.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 559 RLRALKKKLEDGMVFTEYEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGS 638
Cdd:cd14599    1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 639 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 718
Cdd:cd14599   81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 719 LKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGVKTRHPPIVVHCSAGVGRTGVVILSE 798
Cdd:cd14599  161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 149041008 799 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 845
Cdd:cd14599  241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
572-842 1.29e-94

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 297.26  E-value: 1.29e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008   572 VFTEYEQIPNKKANGI-FSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVvgGSEWHYIATQGPLP 650
Cdd:smart00194   2 LEEEFEKLDRLKPDDEsCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGP--NGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008   651 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQER 730
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008   731 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSVLEGvktrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKV 810
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG------PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                          250       260       270
                   ....*....|....*....|....*....|..
gi 149041008   811 EVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:smart00194 228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
596-842 1.52e-94

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 296.08  E-value: 1.52e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008  596 NAERSRIREVVPYEENRVELIPTKENNtGYINASHIKVVVGgsEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 675
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGYKK--PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008  676 EGGRTKSHRYWPKlgSKHSSATYGKFKVTTK-FRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLS 754
Cdd:pfam00102  78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008  755 YLEEIQSVRRHTnsvlegvktRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYK 834
Cdd:pfam00102 156 LLRKVRKSSLDG---------RSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                  ....*...
gi 149041008  835 FVYQVLVQ 842
Cdd:pfam00102 227 FLYDAILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 575-845 8.30e-47

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 170.11  E-value: 8.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 575 EYEQIPNKKANGIFSTATlpENAERSRIREVVPYEENRVELiPTKENNTGYINASHikvvVGGSEW--HYIATQGPLPHT 652
Cdd:PHA02738  30 EHQKVISEKVDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYkkKFICGQAPTRQT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 653 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLlSGQERTV 732
Cdd:PHA02738 103 CYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQTV 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 733 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRR--HTNSVLEGVKTRHPP-IVVHCSAGVGRTGVVILSELMIYCLEHNEK 809
Cdd:PHA02738 180 THFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESLQIGHNRLQPPpIVVHCNAGLGRTPCYCVVDISISRFDACAT 259

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 149041008 810 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 845
Cdd:PHA02738 260 VSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVN 295
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
594-846 6.34e-30

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 120.20  E-value: 6.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 594 PENAERSRIREVVPYEENRVEliptkeNNTGYINASHIKVvvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTA 673
Cdd:COG5599   40 INGSPLNRFRDIQPYKETALR------ANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 674 EEEGG--RTKSHRYWpklgskHSSATYGKFKVTTK------FRTDSGCYAttgLKVKHLLSGQE-RTVWHLQYTDWPHHG 744
Cdd:COG5599  111 DDEISkpKVKMPVYF------RQDGEYGKYEVSSEltesiqLRDGIEART---YVLTIKGTGQKkIEIPVLHVKNWPDHG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 745 CPEDVQgflsyLEEIqsvrrhTNSVLEGVKTRHP---PIVVHCSAGVGRTGVVILselmIYCLE------HNEKVEVPTM 815
Cdd:COG5599  182 AISAEA-----LKNL------ADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIA----CLALSksinalVQITLSVEEI 246

                        250       260       270
                 ....*....|....*....|....*....|..
gi 149041008 816 LRFLREQR-MFMIQTIAQykfvYQVLVQFLQN 846
Cdd:COG5599  247 VIDMRTSRnGGMVQTSEQ----LDVLVKLAEQ 274
 
Name Accession Description Interval E-value
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 559-845 0e+00

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: 625.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 559 RLRALKKKLEDGMVFTEYEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGS 638
Cdd:cd14599    1 RCKTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 639 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 718
Cdd:cd14599   81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 719 LKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGVKTRHPPIVVHCSAGVGRTGVVILSE 798
Cdd:cd14599  161 LKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 149041008 799 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 845
Cdd:cd14599  241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 625-845 2.79e-146

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: 429.78  E-value: 2.79e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVT 704
Cdd:cd14598    1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEgVKTRHPPIVVHC 784
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTID-PKSPNPPVLVHC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149041008 785 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 845
Cdd:cd14598  160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 625-844 1.34e-140

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: 414.93  E-value: 1.34e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVT 704
Cdd:cd14540    1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLeGVKTRHPPIVVHC 784
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDV-AGHNRNPPTLVHC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 785 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 844
Cdd:cd14540  160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
572-842 1.29e-94

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 297.26  E-value: 1.29e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008   572 VFTEYEQIPNKKANGI-FSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVvgGSEWHYIATQGPLP 650
Cdd:smart00194   2 LEEEFEKLDRLKPDDEsCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGP--NGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008   651 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQER 730
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGE--PLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008   731 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSVLEGvktrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKV 810
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAV----RKSQSTSTG------PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                          250       260       270
                   ....*....|....*....|....*....|..
gi 149041008   811 EVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:smart00194 228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
596-842 1.52e-94

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 296.08  E-value: 1.52e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008  596 NAERSRIREVVPYEENRVELIPTKENNtGYINASHIKVVVGgsEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 675
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGYKK--PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008  676 EGGRTKSHRYWPKlgSKHSSATYGKFKVTTK-FRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLS 754
Cdd:pfam00102  78 EKGREKCAQYWPE--EEGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008  755 YLEEIQSVRRHTnsvlegvktRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYK 834
Cdd:pfam00102 156 LLRKVRKSSLDG---------RSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                  ....*...
gi 149041008  835 FVYQVLVQ 842
Cdd:pfam00102 227 FLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 625-838 1.35e-79

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: 255.29  E-value: 1.35e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVvvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHssATYGKFKVT 704
Cdd:cd00047    1 YINASYIDG--YRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKP--LEYGDITVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegvktrhpPIVVHC 784
Cdd:cd00047   77 LVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG----------PIVVHC 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 149041008 785 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd00047  147 SAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 557-836 2.87e-73

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: 241.29  E-value: 2.87e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 557 DERLRALKKKLEDGMVFTEYEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVELiptkENNTGYINASHIKVVVG 636
Cdd:cd14600    1 EESMAQLKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNMEIP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 637 GSEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgskHSSATYGKFKVTTKFRTDSGCY 714
Cdd:cd14600   77 SANIvnKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDP---PDVMEYGGFRVQCHSEDCTIAY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 715 ATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRrhtnsvlegvkTRHPPIVVHCSAGVGRTGVV 794
Cdd:cd14600  154 VFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKR-----------VENEPVLVHCSAGIGRTGVL 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 149041008 795 ILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFV 836
Cdd:cd14600  223 VTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV 264
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 625-844 2.01e-70

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: 230.72  E-value: 2.01e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlGSKHSSATYGKFKVT 704
Cdd:cd14538    1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPD-SLNKPLICGGRLEVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeIQSVRRHTNSVlegvktrhpPIVVHC 784
Cdd:cd14538   80 LEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRF---IRYMRRIHNSG---------PIVVHC 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 785 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 844
Cdd:cd14538  148 SAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 572-837 1.84e-65

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: 219.93  E-value: 1.84e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 572 VFTEYEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHikvvVGGSEWH--YIATQGP 648
Cdd:cd14543    5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLpKRNGDERTDYINANF----MDGYKQKnaYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 649 LPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ 728
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPL--EEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 729 ERTVWHLQYTDWPHHGCPEDVQGFLSYLEEiqsVRRHTNSVLEGVKTR---H---PPIVVHCSAGVGRTGVVILSELMIY 802
Cdd:cd14543  159 SRQVTHFQFTSWPDFGVPSSAAALLDFLGE---VRQQQALAVKAMGDRwkgHppgPPIVVHCSAGIGRTGTFCTLDICLS 235

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 149041008 803 CLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 837
Cdd:cd14543  236 QLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 625-836 2.58e-64

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: 214.50  E-value: 2.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhSSATYGKFK 702
Cdd:cd14541    2 YINANYVNMEIPGSGIvnRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLG---ETMQFGNLQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 703 VTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeIQSVRRHTNSVLEgvktrhpPIVV 782
Cdd:cd14541   79 ITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDF---VKRVRQNRVGMVE-------PTVV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 149041008 783 HCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFV 836
Cdd:cd14541  149 HCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV 202
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 625-838 4.94e-61

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: 205.56  E-value: 4.94e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEwHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVT 704
Cdd:cd18533    1 YINASYITLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP---SGEYEGEYGDLTVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 ----TKFrtDSGCYATTGLKVKHlLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegvktrHPPI 780
Cdd:cd18533   77 lvseEEN--DDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASL--------DPPI 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149041008 781 VVHCSAGVGRTGVVILSELMIYCLE--HNEKVE-------VPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd18533  146 IVHCSAGVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 595-844 1.26e-58

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: 200.06  E-value: 1.26e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 595 ENAERSRIREVVPYEENRVELiptkENNTGYINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAE 674
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 675 EEGGRTKSHRYWPKLGSKhSSATYGKFKVT-TKFRTDSGcYATTGLKVKHLLSGQERTVWHLQYTDWPHHGC---PEDVQ 750
Cdd:cd14597   78 VEGGKIKCQRYWPEILGK-TTMVDNRLQLTlVRMQQLKN-FVIRVLELEDIQTREVRHITHLNFTAWPDHDTpsqPEQLL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 751 GFLSYLEEIQsvrrhtnsvlegvktRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTI 830
Cdd:cd14597  156 TFISYMRHIH---------------KSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTE 220

                        250
                 ....*....|....
gi 149041008 831 AQYKFVYQVLVQFL 844
Cdd:cd14597  221 DQYIFCYQVILYVL 234
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 596-846 2.88e-58

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: 199.61  E-value: 2.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 596 NAERSRIREVVPYEENRVELIPTKENNTG--YINASHIKVVVGGS-----EWHYIATQGPLPHTCHDFWQMVWEQGVNVI 668
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPGsdYINANYIRNENEGPttdenAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 669 AMVTAEEEGGRTKSHRYWPKLGSKHSsatYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ-ERTVWHLQYTDWPHHGCPE 747
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQKQ---YGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 748 DVQGFLSYLEEIQSVRRHTNSvlEGvktrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNE---KVEVPTMLRFLREQRM 824
Cdd:cd14544  158 DPGGVLNFLEDVNQRQESLPH--AG------PIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRS 229

                        250       260
                 ....*....|....*....|..
gi 149041008 825 FMIQTIAQYKFVYQVLVQFLQN 846
Cdd:cd14544  230 GMVQTEAQYKFIYVAVAQYIET 251
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 625-842 3.80e-57

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: 195.16  E-value: 3.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEW--HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhSSATYGKFK 702
Cdd:cd14601    2 YINANYINMEIPSSSIinRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPS---GSSSYGGFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 703 VTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHtnsvlegvktRHPPIVV 782
Cdd:cd14601   79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAG----------KDEPVVV 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 783 HCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14601  149 HCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 625-837 1.02e-54

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: 187.94  E-value: 1.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIkvvvggSEWH----YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGK 700
Cdd:cd14549    1 YINANYV------DGYNkaraYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE----TYGN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 701 FKVTTKFRTDSGCYATTGLKVKHL------LSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsVRRHTNSVLEGVK 774
Cdd:cd14549   71 IQVTLLSTEVLATYTVRTFSLKNLklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF------VRKSSAANPPGAG 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149041008 775 trhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 837
Cdd:cd14549  145 ----PIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 625-845 1.38e-53

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: 184.95  E-value: 1.38e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVT 704
Cdd:cd14596    1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPE--TLQEPMELENYQLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRhtnsvlEGvktrhpPIVVHC 784
Cdd:cd14596   79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN------TG------PIVVHC 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149041008 785 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 845
Cdd:cd14596  147 SAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 601-838 3.30e-53

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: 184.48  E-value: 3.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 601 RIREVVPYEENRVELIP-TKENNTGYINASHIKvvvgG--SEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 677
Cdd:cd14548    1 RYTNILPYDHSRVKLIPiNEEEGSDYINANYIP----GynSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 678 GRTKSHRYWPKlgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLE 757
Cdd:cd14548   77 GRVKCDHYWPF---DQDPVYYGDITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 758 EIQSVRRHTNSvlegvktrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 837
Cdd:cd14548  152 LVRDYIKQEKG----------PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221


                 .
gi 149041008 838 Q 838
Cdd:cd14548  222 Q 222
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 574-842 8.98e-53

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: 185.03  E-value: 8.98e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 574 TEYEQIPNK----KANGIFST--ATLPENAERSRIREVVPYEENRVELIP-TKENNTGYINASHIKVVVGgsEWHYIATQ 646
Cdd:cd14603    2 GEFSEIRACsaafKADYVCSTvaGGRKENVKKNRYKDILPYDQTRVILSLlQEEGHSDYINANFIKGVDG--SRAYIATQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 647 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTT--KFRTDSGCYATTgLKVKHl 724
Cdd:cd14603   80 GPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWA---QEQEPLQTGPFTITLvkEKRLNEEVILRT-LKVTF- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 725 lSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEiqsVRRHTNSVLEgvktrhpPIVVHCSAGVGRTGVVILSElMIYCL 804
Cdd:cd14603  155 -QKESRSVSHFQYMAWPDHGIPDSPDCMLAMIEL---ARRLQGSGPE-------PLCVHCSAGCGRTGVICTVD-YVRQL 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 149041008 805 EHNEKVEvPTMLRF-----LREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14603  223 LLTQRIP-PDFSIFdvvleMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 596-842 1.37e-52

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: 183.37  E-value: 1.37e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 596 NAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKvvvgGSEWH--YIATQGPLPHTCHDFWQMVWEQGVNVIAMVT 672
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEgVPGSDYINANYCD----GYRKQnaYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 673 AEEEGGRTKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGF 752
Cdd:cd14553   79 KLEERSRVKCDQYWPTRG----TETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPF 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 753 LSYLeeiqsvRRhtnsvlegVKTRHP----PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQ 828
Cdd:cd14553  155 LAFL------RR--------VKACNPpdagPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQ 220

                        250
                 ....*....|....
gi 149041008 829 TIAQYKFVYQVLVQ 842
Cdd:cd14553  221 TEDQYIFIHDALLE 234
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 591-838 5.47e-52

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: 181.57  E-value: 5.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 591 ATLPENAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKvvvgGSEWH--YIATQGPLPHTCHDFWQMVWEQGVNV 667
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRgVEGSDYINASFID----GYRQRgaYIATQGPLAETTEDFWRMLWEHNSTI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 668 IAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPE 747
Cdd:cd14554   77 IVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 748 DVQGFLSYLEEIQSVRRHTNSvlEGvktrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMI 827
Cdd:cd14554  153 SGEGFIDFIGQVHKTKEQFGQ--EG------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMV 224

                        250
                 ....*....|.
gi 149041008 828 QTIAQYKFVYQ 838
Cdd:cd14554  225 QTEDQYQFCYR 235
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 594-845 1.60e-51

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: 181.23  E-value: 1.60e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 594 PENAERSRIREVVPYEENRVELIPTKENNTG--YINASHIK---VVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVI 668
Cdd:cd14606   16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGsdYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 669 AMVTAEEEGGRTKSHRYWPKLGSKHSsatYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQE-RTVWHLQYTDWPHHGCPE 747
Cdd:cd14606   96 VMTTREVEKGRNKCVPYWPEVGMQRA---YGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 748 DVQGFLSYLEEIqsvrrhtNSVLEGVKtRHPPIVVHCSAGVGRTGVVILSELMIYCLEH---NEKVEVPTMLRFLREQRM 824
Cdd:cd14606  173 EPGGVLSFLDQI-------NQRQESLP-HAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRS 244

                        250       260
                 ....*....|....*....|.
gi 149041008 825 FMIQTIAQYKFVYQVLVQFLQ 845
Cdd:cd14606  245 GMVQTEAQYKFIYVAIAQFIE 265
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 625-838 1.83e-51

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: 179.12  E-value: 1.83e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEwHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgSKHSSATYGKFKVT 704
Cdd:cd14539    1 YINASLIEDLTPYCP-RFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPT--ERGQALVYGAITVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVlegvktrHPPIVVHC 784
Cdd:cd14539   78 LQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSL-------QTPIVVHC 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149041008 785 SAGVGRTGV-VILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14539  151 SSGVGRTGAfCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 601-838 3.18e-50

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: 176.05  E-value: 3.18e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 601 RIREVVPYEENRVeLIPTKENN--TGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGg 678
Cdd:cd14547    2 RYKTILPNEHSRV-CLPSVDDDplSSYINANYIRGY-DGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 679 RTKSHRYWPKLgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEE 758
Cdd:cd14547   79 KEKCAQYWPEE----ENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 759 IQSVRRHTNSvlegvktrHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14547  153 VEEARQTEPH--------RGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 599-842 9.80e-50

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: 175.03  E-value: 9.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 599 RSRIREVVPYEENRVEL-IPTKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 677
Cdd:cd14602    1 KNRYKDILPYDHSRVELsLITSDEDSDYINANFIKGVYGPRA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 678 GRTKSHRYWPKLGSkhSSATYGKFKVTTKFRTDSGCYATTGLKVKhlLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLE 757
Cdd:cd14602   79 GKKKCERYWAEPGE--MQLEFGPFSVTCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 758 EIQSVRRHTNsvlegvktrhPPIVVHCSAGVGRTGVVILSELMIYCLEHN---EKVEVPTMLRFLREQRMFMIQTIAQYK 834
Cdd:cd14602  155 DVRCYQEDDS----------VPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYE 224


                 ....*...
gi 149041008 835 FVYQVLVQ 842
Cdd:cd14602  225 LVYNAVIE 232
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 575-844 1.38e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 176.85  E-value: 1.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 575 EYEQIPNKKAN-GIFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 652
Cdd:cd14627   31 EFKRLANSKAHtSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGSDYINASFIDGY--RQQKAYIATQGPLAET 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 653 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 732
Cdd:cd14627  109 TEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTV 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 733 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegvktRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 812
Cdd:cd14627  185 RQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFG--------QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDI 256

                        250       260       270
                 ....*....|....*....|....*....|..
gi 149041008 813 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 844
Cdd:cd14627  257 FQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 600-844 3.23e-49

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: 173.54  E-value: 3.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 600 SRIREVVPYEENRVELIPTKENNTG-YINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 678
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSdYINANYMPGY--WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 679 RTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEe 758
Cdd:cd14619   79 RVKCEHYWP---LDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRR- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 759 iqSVRRHTNSVLEGvktrhPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14619  155 --LLRQWLDQTMSG-----GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQ 227


                 ....*.
gi 149041008 839 VLVQFL 844
Cdd:cd14619  228 CILDFL 233
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 595-845 9.07e-49

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: 173.28  E-value: 9.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 595 ENAERSRIREVVPYEENRVELIPTKENNTG--YINASHI------KVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVN 666
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVsdYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 667 VIAMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ-ERTVWHLQYTDWPHHGC 745
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWP---DEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 746 PEDVQGFLSYLEEIqsvrrhtNSVLEGVkTRHPPIVVHCSAGVGRTGVVILSELMIYCLEhnEK-----VEVPTMLRFLR 820
Cdd:cd14605  158 PSDPGGVLDFLEEV-------HHKQESI-MDAGPVVVHCSAGIGRTGTFIVIDILIDIIR--EKgvdcdIDVPKTIQMVR 227

                        250       260
                 ....*....|....*....|....*
gi 149041008 821 EQRMFMIQTIAQYKFVYQVLVQFLQ 845
Cdd:cd14605  228 SQRSGMVQTEAQYRFIYMAVQHYIE 252
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 575-844 1.63e-48

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: 173.76  E-value: 1.63e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 575 EYEQIPNKKAN-GIFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 652
Cdd:cd14628   30 EFKRLASSKAHtSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGSDYINASFIDGY--RQQKAYIATQGPLAET 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 653 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 732
Cdd:cd14628  108 TEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTV 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 733 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegvktRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 812
Cdd:cd14628  184 RQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFG--------QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDI 255

                        250       260       270
                 ....*....|....*....|....*....|..
gi 149041008 813 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 844
Cdd:cd14628  256 FQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 576-842 2.26e-47

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: 170.21  E-value: 2.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 576 YEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVELipTKENNTgYINASHIKVvvGGSEWHYIATQGPLPHTCHD 655
Cdd:cd14608    5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL--HQEDND-YINASLIKM--EEAQRSYILTQGPLPNTCGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 656 FWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHL 735
Cdd:cd14608   80 FWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 736 QYTDWPHHGCPEDVQGFLSYLEEIqsvrRHTNSvlegVKTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNE---KVEV 812
Cdd:cd14608  160 HYTTWPDFGVPESPASFLNFLFKV----RESGS----LSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDI 231

                        250       260       270
                 ....*....|....*....|....*....|
gi 149041008 813 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14608  232 KKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 600-838 3.27e-47

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: 167.78  E-value: 3.27e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 600 SRIREVVPYEENRVELIPTKEN-NTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 678
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVpGSDYINASYISGYLCPNE--FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 679 RTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKV-KHllsGQERTVWHLQYTDWPHHGCPEDVQGFLSYLE 757
Cdd:cd14616   79 RIRCHQYWPE--DNKPVTVFGDIVITKLMEDVQIDWTIRDLKIeRH---GDYMMVRQCNFTSWPEHGVPESSAPLIHFVK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 758 EIQSVRRHTNSvlegvktrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVY 837
Cdd:cd14616  154 LVRASRAHDNT----------PMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223


                 .
gi 149041008 838 Q 838
Cdd:cd14616  224 Q 224
PHA02738 PHA02738
hypothetical protein; Provisional
 575-845 8.30e-47

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 170.11  E-value: 8.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 575 EYEQIPNKKANGIFSTATlpENAERSRIREVVPYEENRVELiPTKENNTGYINASHikvvVGGSEW--HYIATQGPLPHT 652
Cdd:PHA02738  30 EHQKVISEKVDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANY----VDGFEYkkKFICGQAPTRQT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 653 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLlSGQERTV 732
Cdd:PHA02738 103 CYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDV--EQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQTV 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 733 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRR--HTNSVLEGVKTRHPP-IVVHCSAGVGRTGVVILSELMIYCLEHNEK 809
Cdd:PHA02738 180 THFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelAQESLQIGHNRLQPPpIVVHCNAGLGRTPCYCVVDISISRFDACAT 259

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 149041008 810 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 845
Cdd:PHA02738 260 VSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVN 295
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 558-842 1.02e-46

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: 168.29  E-value: 1.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 558 ERLRAlkkklEDGMVFT-EYEQI-PNKKANgiFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKvv 634
Cdd:cd14626    8 ERLKA-----NDGLKFSqEYESIdPGQQFT--WENSNLEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYID-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 635 vGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGC 713
Cdd:cd14626   79 -GYRKQNaYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE----TYGMIQVTLLDTVELAT 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 714 YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGvktrhpPIVVHCSAGVGRTGV 793
Cdd:cd14626  154 YSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKAC----NPPDAG------PMVVHCSAGVGRTGC 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 149041008 794 VILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14626  224 FIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 599-838 1.44e-46

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: 166.03  E-value: 1.44e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 599 RSRIREVVPYEENRVELiptKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 678
Cdd:cd14545    3 RYRDRDPYDHDRSRVKL---KQGDNDYINASLVEVEEAKRS--YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 679 RTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLee 758
Cdd:cd14545   78 QIKCAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL-- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 759 iQSVRRHtnSVLEgvkTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNE--KVEVPTMLRFLREQRMFMIQTIAQYKFV 836
Cdd:cd14545  156 -QKVRES--GSLS---SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFS 229


                 ..
gi 149041008 837 YQ 838
Cdd:cd14545  230 YL 231
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 601-838 7.46e-46

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: 164.22  E-value: 7.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 601 RIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT 680
Cdd:cd14615    2 RYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKE--FIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 681 KSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiq 760
Cdd:cd14615   80 KCEEYWPSKQKK----DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINF----- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 761 svrRHTnsVLEGVK--TRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14615  151 ---RHL--VREYMKqnPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 593-843 1.28e-45

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: 164.24  E-value: 1.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 593 LPENAERSRIREVVPYEENRVEL--IPTKENNTGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAM 670
Cdd:cd14612   12 IPGHASKDRYKTILPNPQSRVCLrrAGSQEEEGSYINANYIRGY-DGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 671 VTAEEEGgRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQ 750
Cdd:cd14612   91 ITKLKEK-KEKCVHYWPE-----KEGTYGRFEIRVQDMKECDGYTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 751 GFLSYLEEIQSVRRhtnsvlegVKTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTI 830
Cdd:cd14612  163 PLLRLVAEVEESRQ--------TAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTS 234

                        250
                 ....*....|...
gi 149041008 831 AQYKFVYQVLVQF 843
Cdd:cd14612  235 EQYQFLHHTLALY 247
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 600-838 1.30e-45

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: 163.55  E-value: 1.30e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 600 SRIREVVPYEENRVELIPTKENN-TGYINASHIKvvvGGS-EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 677
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIP---GNNfRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 678 GRTKSHRYWPklgSKHSSATYGKFKVttKFRTDSGCYATTGLKVKhlLSGQE-----RTVWHLQYTDWPHHGCPEDVQGF 752
Cdd:cd14617   78 GRVKCDHYWP---ADQDSLYYGDLIV--QMLSESVLPEWTIREFK--ICSEEqldapRLVRHFHYTVWPDHGVPETTQSL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 753 LSYleeIQSVRRHTNsvlegvktRHP---PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQT 829
Cdd:cd14617  151 IQF---VRTVRDYIN--------RTPgsgPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQT 219


                 ....*....
gi 149041008 830 IAQYKFVYQ 838
Cdd:cd14617  220 ECQYVYLHQ 228
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 576-837 1.67e-45

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: 163.98  E-value: 1.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 576 YEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVELIPTkENNtgYINAShiKVVVGGSEWHYIATQGPLPHTCHD 655
Cdd:cd14607    4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNT-END--YINAS--LVVIEEAQRSYILTQGPLPNTCCH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 656 FWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHL 735
Cdd:cd14607   79 FWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 736 QYTDWPHHGCPEDVQGFLSYLEEIQSVRrhtnsvleGVKTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNE--KVEVP 813
Cdd:cd14607  159 HYTTWPDFGVPESPASFLNFLFKVRESG--------SLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIK 230

                        250       260
                 ....*....|....*....|....
gi 149041008 814 TMLRFLREQRMFMIQTIAQYKFVY 837
Cdd:cd14607  231 QVLLDMRKYRMGLIQTPDQLRFSY 254
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 575-844 2.61e-45

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: 164.90  E-value: 2.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 575 EYEQIPNKKAN-GIFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 652
Cdd:cd14629   31 EFKLLANSKAHtSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGSDYINASFIDGY--RQQKAYIATQGPLAET 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 653 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 732
Cdd:cd14629  109 TEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWP----AERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTI 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 733 WHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegvktRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEV 812
Cdd:cd14629  185 RQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFG--------QDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDM 256

                        250       260       270
                 ....*....|....*....|....*....|..
gi 149041008 813 PTMLRFLREQRMFMIQTIAQYKFVYQVLVQFL 844
Cdd:cd14629  257 FQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 625-838 1.27e-44

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: 159.51  E-value: 1.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVT 704
Cdd:cd14542    1 YINANFIKGVSGSKA--YIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEE--QLQFGPFKIS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 ---TKFRTDSgcYATTGLKVKhlLSGQERTVWHLQYTDWPHHGCPEDVQgflSYLEEIQSVRRHTNSvlegvktRHPPIV 781
Cdd:cd14542   77 lekEKRVGPD--FLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVD---PILDLVRLVRDYQGS-------EDVPIC 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149041008 782 VHCSAGVGRTGVV--------ILSELMIyclehNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14542  143 VHCSAGCGRTGTIcaidyvwnLLKTGKI-----PEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 558-845 3.84e-44

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: 161.64  E-value: 3.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 558 ERLRALKKKLEDG-----MVFTEYEQIPNK-KANGIFSTAT--LPENAERSRIREVVPYEENRVEL-IPTKENNTGYINA 628
Cdd:cd14604   11 ERVQAMKSTDHNGednfaSDFMRLRRLSTKyRTEKIYPTATgeKEENVKKNRYKDILPFDHSRVKLtLKTSSQDSDYINA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 629 SHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhsSATYGKFKVT---T 705
Cdd:cd14604   91 NFIKGVYGPKA--YIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEE--PMTFGPFRISceaE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 706 KFRTDsgcYATTGLKVKhlLSGQERTVWHLQYTDWPHHGCPedvQGFLSYLEEIQSVRRHTNSvlEGVktrhpPIVVHCS 785
Cdd:cd14604  167 QARTD---YFIRTLLLE--FQNETRRLYQFHYVNWPDHDVP---SSFDSILDMISLMRKYQEH--EDV-----PICIHCS 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149041008 786 AGVGRTGVVILSELMIYCLEHN---EKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 845
Cdd:cd14604  232 AGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFE 294
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 625-838 5.35e-44

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: 157.68  E-value: 5.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKvvvGGSE-WHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLgsKHSSATYGkfKV 703
Cdd:cd14557    1 YINASYID---GFKEpRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSM--EEGSRAFG--DV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 704 TTKFRTDSGC--YATTGLKVKHLL-SGQERTVWHLQYTDWPHHGCPEDVQGFLsyleeiqSVRRHTNSVLEGVKTrhpPI 780
Cdd:cd14557   74 VVKINEEKICpdYIIRKLNINNKKeKGSGREVTHIQFTSWPDHGVPEDPHLLL-------KLRRRVNAFNNFFSG---PI 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149041008 781 VVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14557  144 VVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 575-842 1.28e-43

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: 159.49  E-value: 1.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 575 EYEQI-PNKKANgiFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASHIKVVvgGSEWHYIATQGPLPHT 652
Cdd:cd14625   27 EYESIdPGQQFT--WEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGY--RKQNAYIATQGPLPET 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 653 CHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 732
Cdd:cd14625  103 FGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTE----TYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREV 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 733 WHLQYTDWPHHGCPEDVQGFLSYLeeiqsvRRhtnsvlegVKTRHP----PIVVHCSAGVGRTGVVILSELMIYCLEHNE 808
Cdd:cd14625  179 RQFQFTAWPDHGVPEYPTPFLAFL------RR--------VKTCNPpdagPIVVHCSAGVGRTGCFIVIDAMLERIKHEK 244

                        250       260       270
                 ....*....|....*....|....*....|....
gi 149041008 809 KVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14625  245 TVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 594-842 1.26e-42

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: 156.35  E-value: 1.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 594 PENAERSRIREVVPYEENRVEL--IPTKEN-NTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 670
Cdd:cd17667   25 PDNKHKNRYINILAYDHSRVKLrpLPGKDSkHSDYINANYVDGYNKAKA--YIATQGPLKSTFEDFWRMIWEQNTGIIVM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 671 VTAEEEGGRTKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGL-----KVKHLLSGQ------ERTVWHLQYTD 739
Cdd:cd17667  103 ITNLVEKGRRKCDQYWP----TENSEEYGNIIVTLKSTKIHACYTVRRFsirntKVKKGQKGNpkgrqnERTVIQYHYTQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 740 WPHHGCPEDVQGFLSYleeiqsVRRHTNSvlegvktRHP---PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTML 816
Cdd:cd17667  179 WPDMGVPEYALPVLTF------VRRSSAA-------RTPemgPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFL 245

                        250       260
                 ....*....|....*....|....*.
gi 149041008 817 RFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd17667  246 KHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 600-841 2.06e-42

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: 154.33  E-value: 2.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 600 SRIREVVPYEENRVELIP-TKENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 678
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQlGGEPHSDYINANFIPGYTSPQE--FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 679 RTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEE 758
Cdd:cd14618   79 RVLCDHYWP---SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFREL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 759 IQSVRRHTNSvlegvktrHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14618  156 VREHVQATKG--------KGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                 ...
gi 149041008 839 VLV 841
Cdd:cd14618  228 CIL 230
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 590-844 2.36e-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: 154.66  E-value: 2.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 590 TATLPENAERSRIREVVPYEENRVELIPT-KENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 668
Cdd:cd14614    6 AADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQE--YIATQGPLPETRNDFWKMVLQQKSQII 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 669 AMVTAEEEGGRTKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQErtVWHLQYTDWPHHGCPeD 748
Cdd:cd14614   84 VMLTQCNEKRRVKCDHYWP---FTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD--VMHFNYTAWPDHGVP-T 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 749 VQGFLSYLEEIQSVRRHTNSvlegvktRHPPIVVHCSAGVGRTGVVI-LSELMIYCLEHnEKVEVPTMLRFLREQRMFMI 827
Cdd:cd14614  158 ANAAESILQFVQMVRQQAVK-------SKGPMIIHCSAGVGRTGTFIaLDRLLQHIRDH-EFVDILGLVSEMRSYRMSMV 229

                        250
                 ....*....|....*..
gi 149041008 828 QTIAQYKFVYQVlVQFL 844
Cdd:cd14614  230 QTEEQYIFIHQC-VQLM 245
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 625-837 2.76e-42

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: 153.37  E-value: 2.76e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVvvggsewH------YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTY 698
Cdd:cd14546    1 YINASTIYD-------HdprnpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE----VY 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 699 GKFKVTTkFRTDSGC--YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsvRRHTNSVLEGvktR 776
Cdd:cd14546   70 HIYEVHL-VSEHIWCddYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEF-------RRKVNKSYRG---R 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149041008 777 HPPIVVHCSAGVGRTGVVILSELMIYCLEHNEK-VEVPTMLRFLREQRMFMIQTIAQYKFVY 837
Cdd:cd14546  139 SCPIVVHCSDGAGRTGTYILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 625-841 5.40e-42

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 152.44  E-value: 5.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHssatYGKFKVT 704
Cdd:cd17668    1 YINANYVDGY--NKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE----YGNFLVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGCYATTGLKVKH--LLSG------QERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegvktr 776
Cdd:cd17668   75 QKSVQVLAYYTVRNFTLRNtkIKKGsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG-------- 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149041008 777 hpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 841
Cdd:cd17668  147 --PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 605-842 2.03e-41

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: 151.63  E-value: 2.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 605 VVPYEENRVELIPTKEN-NTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSH 683
Cdd:cd14620    4 ILPYDHSRVILSQLDGIpCSDYINASYIDGYKEKNK--FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 684 RYWPKLGSkhssATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ---ERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQ 760
Cdd:cd14620   82 QYWPDQGC----WTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 761 SVrrhtNSVLEGvktrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 840
Cdd:cd14620  158 SV----NPVHAG------PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227


                 ..
gi 149041008 841 VQ 842
Cdd:cd14620  228 LE 229
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 595-843 4.54e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 152.85  E-value: 4.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 595 ENAERSRIREVVPYEENRVeLIPTKENNTGYINASHikvvVGG--SEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVT 672
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRV-ILKIEDGGDDFINASY----VDGhnAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMIT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 673 AEEEGGRTKSHRYW-PKlgsKHSSATYGKFKVTTK----FRTdsgcYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPE 747
Cdd:PHA02742 126 KIMEDGKEACYPYWmPH---ERGKATHGEFKIKTKkiksFRN----YAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 748 DVQGFLSYLEEIQSVRRHTNSVLEG-VKTRHPPIVVHCSAGVGRTGVVILSELMIYclEHNEKVEVP--TMLRFLREQRM 824
Cdd:PHA02742 199 DPNKFLDFVLAVREADLKADVDIKGeNIVKEPPILVHCSAGLDRAGAFCAIDICIS--KYNERAIIPllSIVRDLRKQRH 276

                        250
                 ....*....|....*....
gi 149041008 825 FMIQTIAQYKFVYQVLVQF 843
Cdd:PHA02742 277 NCLSLPQQYIFCYFIVLIF 295
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 558-842 5.56e-41

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: 152.19  E-value: 5.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 558 ERLRAlkkklEDGMVFT-EYEQI-PNKKANgiFSTATLPENAERSRIREVVPYEENRVeLIPTKENNTG--YINASHIKV 633
Cdd:cd14624   14 ERLKA-----NDNLKFSqEYESIdPGQQFT--WEHSNLEVNKPKNRYANVIAYDHSRV-LLSAIEGIPGsdYINANYIDG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 634 VvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKVTTKFRTDSGC 713
Cdd:cd14624   86 Y--RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE----TYGLIQVTLLDTVELAT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 714 YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLeeiqsvRRhtnsvlegVKTRHP----PIVVHCSAGVG 789
Cdd:cd14624  160 YCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL------RR--------VKTCNPpdagPMVVHCSAGVG 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 149041008 790 RTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14624  226 RTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 625-838 5.72e-41

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: 149.29  E-value: 5.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKvvvGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKhssaTYGKFKV 703
Cdd:cd14551    1 YINASYID---GYQEKNkFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW----TYGNLRV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 704 TTKFRTDSGCYATTGLKVKHLLSG----QERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGvktrhpP 779
Cdd:cd14551   74 RVEDTVVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSA----NPPRAG------P 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149041008 780 IVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14551  144 IVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 625-837 1.03e-40

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: 148.69  E-value: 1.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKvvvggSEWH---YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKF 701
Cdd:cd14558    1 YINASFID-----GYWGpksLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGD-----EKKTYGDI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 702 KVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSvRRHTNSVLEGvktRHPPIV 781
Cdd:cd14558   71 EVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQ-KLPYKNSKHG---RSVPIV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149041008 782 VHCSAGVGRTGvvilselmIYC-----LE--HNEK-VEVPTMLRFLREQRMFMIQTIAQYKFVY 837
Cdd:cd14558  147 VHCSDGSSRTG--------IFCalwnlLEsaETEKvVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 625-841 1.69e-40

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: 147.80  E-value: 1.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKVT 704
Cdd:cd14552    1 YINASFIDGY--RQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG----SVSSGDITVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNsvlegvktrHPPIVVHC 784
Cdd:cd14552   75 LKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSG---------NHPITVHC 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149041008 785 SAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 841
Cdd:cd14552  146 SAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 625-837 2.21e-40

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: 147.61  E-value: 2.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT-KSHRYWPKlgSKHSSATYGKFKV 703
Cdd:cd17658    1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPA--EENESREFGRISV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 704 TTK-FRTDSGCYATTGLKVKHL-LSGQERTVWHLQYTDWPHHGCPEDVQgflsYLEEIqsVRRhtnsvLEGVKTRHPPIV 781
Cdd:cd17658   79 TNKkLKHSQHSITLRVLEVQYIeSEEPPLSVLHIQYPEWPDHGVPKDTR----SVREL--LKR-----LYGIPPSAGPIV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149041008 782 VHCSAGVGRTGVvilselmiYCLEHN----------EKVEVPTMLRFLREQRMFMIQTIAQYKFVY 837
Cdd:cd17658  148 VHCSAGIGRTGA--------YCTIHNtirrilegdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 601-840 5.19e-40

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: 147.50  E-value: 5.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 601 RIREVVPYEENRVeLIPTK--ENNTGYINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGG 678
Cdd:cd14623    1 RVLQIIPYEFNRV-IIPVKrgEENTDYVNASFIDGYRQKDS--YIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 679 RTKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEE 758
Cdd:cd14623   78 QEKCAQYWPSDG----SVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 759 IQSVRRHTNSvlegvktrHpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14623  154 VQKQQQQSGN--------H-PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYK 224


                 ..
gi 149041008 839 VL 840
Cdd:cd14623  225 VV 226
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 556-835 2.11e-39

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: 147.49  E-value: 2.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 556 MDERLRALKKKLEDGMVFTEYEQIPNKkangiFSTATLPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHIkVV 634
Cdd:cd14609    7 MEDHLRNRDRLAKEWQALCAYQAEPNT-----CSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPI-IE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 635 VGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKVTTkFRTDSGC- 713
Cdd:cd14609   81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEG----SSLYHIYEVNL-VSEHIWCe 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 714 -YATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsvRRHTNSVLEGvktRHPPIVVHCSAGVGRTG 792
Cdd:cd14609  156 dFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDF-------RRKVNKCYRG---RSCPIIVHCSDGAGRTG 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 149041008 793 VVILSELMIYCLEHNEK-VEVPTMLRFLREQRMFMIQTIAQYKF 835
Cdd:cd14609  226 TYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGMVRTKDQFEF 269
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 570-844 7.85e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 146.69  E-value: 7.85e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 570 GMVFTEYEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKvvvgGSE--WHYIATQG 647
Cdd:PHA02747  25 GIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWID----GFEddKKFIATQG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 648 PLPHTCHDFWQMVWEQGVNVIAMVT-AEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLS 726
Cdd:PHA02747 101 PFAETCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCL--NEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKIL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 727 GQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGVKTRHPPIVVHCSAGVGRTGVVILSELMIYCLEH 806
Cdd:PHA02747 179 KDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVK 258

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 149041008 807 NEKVEVPTMLRFLREQRMFMIQTIAQYKFV---YQVLVQFL 844
Cdd:PHA02747 259 RKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFL 299
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 554-842 1.23e-38

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: 145.94  E-value: 1.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 554 VPMDERLRALKKKL-EDGMVF-TEYEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVELIPTKE-NNTGYINASH 630
Cdd:cd14621    8 LPVDKLEEEINRRMaDDNKLFrEEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 631 IKvvvGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSkhssATYGKFKVTTKFRT 709
Cdd:cd14621   88 IN---GYQEKNkFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGC----WTYGNIRVSVEDVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 710 DSGCYATTGLKVKHL--LSGQ--ERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVrrhtNSVLEGvktrhpPIVVHCS 785
Cdd:cd14621  161 VLVDYTVRKFCIQQVgdVTNKkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNC----NPQYAG------AIVVHCS 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149041008 786 AGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14621  231 AGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 599-838 1.24e-38

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: 143.52  E-value: 1.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 599 RSRIREVVPYEENRVELIPTKENN--TGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEE 676
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDslSTYINANYIRGY-GGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 677 GGRtKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQGFLSYL 756
Cdd:cd14611   81 KNE-KCVLYWPE-----KRGIYGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 757 EEIQSVRRhtNSVLEGvktrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFV 836
Cdd:cd14611  153 LDVEEDRL--ASPGRG------PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                 ..
gi 149041008 837 YQ 838
Cdd:cd14611  225 HH 226
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 556-835 1.36e-38

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: 145.20  E-value: 1.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 556 MDERLRAlKKKLE-DGMVFTEYEQIPNKKAngifsTATLPENAERSRIREVVPYEENRVEL-IPTKENNTGYINASHIkV 633
Cdd:cd14610    9 MEDHLKN-KNRLEkEWEALCAYQAEPNATN-----VAQREENVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASPI-M 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 634 VVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSK--HssaTYGKFKVTTKFRTDS 711
Cdd:cd14610   82 DHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNlyH---IYEVNLVSEHIWCED 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 712 gcYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsvRRHTNSVLEGvktRHPPIVVHCSAGVGRT 791
Cdd:cd14610  159 --FLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDF-------RRKVNKCYRG---RSCPIIVHCSDGAGRS 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 149041008 792 GVVILSELMIYCLEHNEK-VEVPTMLRFLREQRMFMIQTIAQYKF 835
Cdd:cd14610  227 GTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 625-842 2.26e-38

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: 141.98  E-value: 2.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFKVT 704
Cdd:cd14555    1 YINANYIDGYHRPN--HYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPD-----DTEVYGDIKVT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsVRRhtnsvlegVKTRHP----PI 780
Cdd:cd14555   74 LVETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGF------IRR--------VKASNPpsagPI 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149041008 781 VVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14555  140 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 593-840 3.67e-38

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: 143.08  E-value: 3.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 593 LPENAERSRIREVVPYEENRVELIPTKENN--TGYINASHIKVVvGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAM 670
Cdd:cd14613   22 IPGLVRKNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGY-GGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 671 VTAEEEGGRtKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHllSGQERTVWHLQYTDWPHHGCPEDVQ 750
Cdd:cd14613  101 ITNIEEMNE-KCTEYWPE-----EQVTYEGIEITVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAP 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 751 GFLSYLEEIQSVRRHTnsvlegvKTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTI 830
Cdd:cd14613  173 PLLQLVQEVEEARQQA-------EPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTC 245

                        250
                 ....*....|
gi 149041008 831 AQYKFVYQVL 840
Cdd:cd14613  246 EQYQFVHHVL 255
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 595-842 1.62e-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: 140.55  E-value: 1.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 595 ENAERSRIREVVPYEENRVELIPTKEN-NTGYINASHIKVVvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTA 673
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGY--HRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 674 EEEGGRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFL 753
Cdd:cd14630   80 LVEVGRVKCVRYWPD-----DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 754 SYLEEIqsvrRHTNSVLEGvktrhpPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQY 833
Cdd:cd14630  155 GFVRQV----KFLNPPDAG------PIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQY 224


                 ....*....
gi 149041008 834 KFVYQVLVQ 842
Cdd:cd14630  225 VFVHDAILE 233
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 612-842 5.67e-37

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: 138.61  E-value: 5.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 612 RVELIPTKENNTG-YINASHIKVVVGGSewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlg 690
Cdd:cd14631    1 RVILQPVEDDPSSdYINANYIDGYQRPS--HYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 691 skhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsVRRhtnsvl 770
Cdd:cd14631   77 ---DTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSF------IRR------ 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149041008 771 egVKTRHP----PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14631  142 --VKLSNPpsagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 625-843 2.77e-36

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: 135.90  E-value: 2.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKvvvGGSEWHY-IATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGskhsSATYGKFKV 703
Cdd:cd14622    2 YINASFID---GYRQKDYfIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG----SVTHGEITI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 704 TTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegvktrhPPIVVH 783
Cdd:cd14622   75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGN---------HPIVVH 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 784 CSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQF 843
Cdd:cd14622  146 CSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 625-842 2.87e-36

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: 135.95  E-value: 2.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFKVT 704
Cdd:cd14632    1 YINANYIDGYHRSN--HFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPD-----DSDTYGDIKIT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsVRRhtnsvlegVKTRHP----PI 780
Cdd:cd14632   74 LLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAF------IRR--------VKASTPpdagPV 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149041008 781 VVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14632  140 VVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 566-842 1.52e-35

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: 136.33  E-value: 1.52e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 566 KLEDGMVFTEYEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVELIPTK-ENNTGYINASHIKVVVGGSewHYIA 644
Cdd:cd14633   10 KCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEgETSSDYINGNYIDGYHRPN--HYIA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 645 TQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHL 724
Cdd:cd14633   88 TQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-----DTEIYKDIKVTLIETELLAEYVIRTFAVEKR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 725 LSGQERTVWHLQYTDWPHHGCPEDVQGFLSYleeiqsVRRhtnsvlegVKTRHP----PIVVHCSAGVGRTGVVILSELM 800
Cdd:cd14633  163 GVHEIREIRQFHFTGWPDHGVPYHATGLLGF------VRQ--------VKSKSPpnagPLVVHCSAGAGRTGCFIVIDIM 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 149041008 801 IYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14633  229 LDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
731-840 1.58e-30

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 115.92  E-value: 1.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008   731 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegvktrHPPIVVHCSAGVGRTGVVILSELMIYCLEH-NEK 809
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSES--------SGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGE 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 149041008   810 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 840
Cdd:smart00404  73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 731-840 1.58e-30

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: 115.92  E-value: 1.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008   731 TVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSvlegvktrHPPIVVHCSAGVGRTGVVILSELMIYCLEH-NEK 809
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSES--------SGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGE 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 149041008   810 VEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 840
Cdd:smart00012  73 VDIFDTVKELRSQRPGMVQTEEQYLFLYRAL 103
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 571-840 2.11e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 122.83  E-value: 2.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 571 MVFTEYEQIPNKKANGIFSTATLPENAERSRIREVVPYEENRVEL--------------------IPTKENNTGYINASH 630
Cdd:PHA02746  26 FVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkieVTSEDNAENYIHANF 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 631 IKvvvGGSEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaEEEGGRTKSHRYWPKlgSKHSSATYGKFKVTTKFRT 709
Cdd:PHA02746 106 VD---GFKEANkFICAQGPKEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFELWTK--EEDSELAFGRFVAKILDII 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 710 DSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGVKTRHPPIVVHCSAGVG 789
Cdd:PHA02746 180 EELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADNDPQTLGPIVVHCSAGIG 259

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 149041008 790 RTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVL 840
Cdd:PHA02746 260 RAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
594-846 6.34e-30

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 120.20  E-value: 6.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 594 PENAERSRIREVVPYEENRVEliptkeNNTGYINASHIKVvvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTA 673
Cdd:COG5599   40 INGSPLNRFRDIQPYKETALR------ANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 674 EEEGG--RTKSHRYWpklgskHSSATYGKFKVTTK------FRTDSGCYAttgLKVKHLLSGQE-RTVWHLQYTDWPHHG 744
Cdd:COG5599  111 DDEISkpKVKMPVYF------RQDGEYGKYEVSSEltesiqLRDGIEART---YVLTIKGTGQKkIEIPVLHVKNWPDHG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 745 CPEDVQgflsyLEEIqsvrrhTNSVLEGVKTRHP---PIVVHCSAGVGRTGVVILselmIYCLE------HNEKVEVPTM 815
Cdd:COG5599  182 AISAEA-----LKNL------ADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIA----CLALSksinalVQITLSVEEI 246

                        250       260       270
                 ....*....|....*....|....*....|..
gi 149041008 816 LRFLREQR-MFMIQTIAQykfvYQVLVQFLQN 846
Cdd:COG5599  247 VIDMRTSRnGGMVQTSEQ----LDVLVKLAEQ 274
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 642-838 2.63e-26

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: 107.11  E-value: 2.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 642 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTkSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCYATTGLKV 721
Cdd:cd14556   16 FIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWP----DEGSGTYGPIQVEFVSTTIDEDVISRIFRL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 722 KHLLSGQE--RTVWHLQYTDWPHHG-CPEDVQGFLSYLEEIQSVRRHTNsvlEGvktrhpPIVVHCSAGVGRTGVVILSE 798
Cdd:cd14556   91 QNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSG---EG------PIVVHCLNGVGRSGVFCAIS 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 149041008 799 LMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14556  162 SVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 625-838 5.69e-19

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: 85.84  E-value: 5.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKShrYWPKLGSKHSSATYGKFKVT 704
Cdd:cd14550    1 YINASYLQGYRRSNE--FIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVTLSG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDSGcyaTTGLKVKHLL--SGQER---TVWHLQYTDWPHHGCPedvqgFLSYLEEIQSVRRHTnsvlegvKTRHPP 779
Cdd:cd14550   77 EDHSCLSN---EIRLIVRDFIleSTQDDyvlEVRQFQCPSWPNPCSP-----IHTVFELINTVQEWA-------QQRDGP 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149041008 780 IVVH-----CSAGVgrtgVVILSELMIYcLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14550  142 IVVHdryggVQAAT----FCALTTLHQQ-LEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 625-841 2.97e-18

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: 83.96  E-value: 2.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVtAEEEGGRTKSHRYWPklgSKHSSATYGKFKVT 704
Cdd:cd17670    1 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQGLAEDEFVYWP---SREESMNCEAFTVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TkFRTDSGCYATTGLKVKH---LLSGQERTVW---HLQYTDWPHHGCPedvqgflsyleeIQSVRRHTNSVLEGVKTRHP 778
Cdd:cd17670   75 L-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNPDAP------------ISSTFELINVIKEEALTRDG 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149041008 779 PIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 841
Cdd:cd17670  142 PTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 625-842 1.27e-15

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 76.60  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINA----SHIKVVVggsewhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaeEEGGRTKSHRYWPklgsKHSSATYGK 700
Cdd:cd14634    1 YINAalmdSHKQPAA------FIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWP----EKTSCCYGP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 701 FKVTTKFRTDSGCYATTGLKVKHLLSGQE--RTVWHLQYTDWP-HHGCPEDVQGFLsyleeiQSVRRhTNSVLEGVKTRH 777
Cdd:cd14634   69 IQVEFVSADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPaYRDTPPSKRSIL------KVVRR-LEKWQEQYDGRE 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149041008 778 PPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14634  142 GRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 625-841 9.54e-15

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: 73.87  E-value: 9.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVT-----AEEEggrtksHRYWPklgSKHSSATYG 699
Cdd:cd17669    1 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPdgqnmAEDE------FVYWP---NKDEPINCE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 700 KFKVTTkFRTDSGCYAT-TGLKVKHLL--SGQERTVW---HLQYTDWPHHGCPedvqgflsyleeIQSVRRHTNSVLEGV 773
Cdd:cd17669   70 TFKVTL-IAEEHKCLSNeEKLIIQDFIleATQDDYVLevrHFQCPKWPNPDSP------------ISKTFELISIIKEEA 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149041008 774 KTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLV 841
Cdd:cd17669  137 ANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 625-842 9.97e-15

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: 73.79  E-value: 9.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRT-KSHRYWPKLGSKHssatYGKFKV 703
Cdd:cd14637    1 YINAALTDSYTRSAA--FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQ----YGPMEV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 704 TTKFRTDSGCYATTGLKVKHLLSGQER--TVWHLQYTDW-PHHGCPEDVQGFLSYLEEIQSVRRhtnsvlegvKTRHPPI 780
Cdd:cd14637   75 EFVSGSADEDIVTRLFRVQNITRLQEGhlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQR---------ESGEGRT 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149041008 781 VVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14637  146 VVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 639-845 9.07e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 73.08  E-value: 9.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 639 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEggRTKSHRYWpklgskhsSATYGKFKVTTKFRTDSGCYATTG 718
Cdd:PHA02740  90 EQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD--KKCFNQFW--------SLKEGCVITSDKFQIETLEIIIKP 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 719 LKVKHLLS-----GQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQS----VRRHTNSVLEGvktrhpPIVVHCSAGVG 789
Cdd:PHA02740 160 HFNLTLLSltdkfGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadLEKHKADGKIA------PIIIDCIDGIS 233

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 149041008 790 RTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQ 845
Cdd:PHA02740 234 SSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 625-842 7.75e-13

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: 68.18  E-value: 7.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 625 YINASHIKVVVGGSEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKshRYWPKLGSKHSSATYGKFkVT 704
Cdd:cd14635    1 YINAALMDSYKQPSA--FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCP--QYWPENGVHRHGPIQVEF-VS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 705 TKFRTDsgcYATTGLKVKHLLSGQE--RTVWHLQYTDWP-HHGCPEDVQGFLSYLEEIQSVRRHtnsvLEGVKTRhppIV 781
Cdd:cd14635   76 ADLEED---IISRIFRIYNAARPQDgyRMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEE----YNGGEGR---TV 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149041008 782 VHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14635  146 VHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 642-842 2.09e-12

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: 66.97  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 642 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTaeEEGGRTKSHRYWPKLGskhsSATYGKFKVTTkFRTDSGCYATTGL-K 720
Cdd:cd14636   16 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN--EVDLAQGCPQYWPEEG----MLRYGPIQVEC-MSCSMDCDVISRIfR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 721 VKHLLSGQE--RTVWHLQYTDWP-HHGCPEDVQGFLSYLEEIQSVRRHTNsvlEGvktrHPPIVVHCSAGVGRTGVVILS 797
Cdd:cd14636   89 ICNLTRPQEgyLMVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEECD---EG----EGRTIIHCLNGGGRSGMFCAI 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 149041008 798 ELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQ 842
Cdd:cd14636  162 SIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 626-834 8.21e-11

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: 62.80  E-value: 8.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 626 INASHIKVvvgGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWpklgskHSSATYGKFKVTT 705
Cdd:cd14559   18 LNANRVQI---GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF------RQSGTYGSVTVKS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 706 KfRTDSGcYATTGLKVKHL---LSGQERT----VWHLqyTDWPHHGcPEDVQGfLSYLEEIQSVRRHT--------NSVL 770
Cdd:cd14559   89 K-KTGKD-ELVDGLKADMYnlkITDGNKTitipVVHV--TNWPDHT-AISSEG-LKELADLVNKSAEEkrnfykskGSSA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149041008 771 EGVKTRHPPiVVHCSAGVGRTGVVILSELMIyclEHNEKVEVPTMLRFLREQR-MFMIQTIAQYK 834
Cdd:cd14559  163 INDKNKLLP-VIHCRAGVGRTGQLAAAMELN---KSPNNLSVEDIVSDMRTSRnGKMVQKDEQLD 223
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 768-838 2.82e-08

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: 52.74  E-value: 2.82e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149041008 768 SVLEGVKTRHPPIVVHCSAGVGRTGVVILSELMIYcleHNEKVEVptMLRFLREQRMFMI-QTIAQYKFVYQ 838
Cdd:cd14494   47 EVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLL---GGMSAEE--AVRIVRLIRPGGIpQTIEQLDFLIK 113
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 768-836 1.57e-05

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: 46.57  E-value: 1.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149041008 768 SVLEGVKtrhppIVVHCSAGVGRTGVVILSELMIYClehneKVEVPTMLRFLREQRMFMIQTIAQYKFV 836
Cdd:cd14506  105 ALQEGGK-----VAVHCHAGLGRTGVLIACYLVYAL-----RMSADQAIRLVRSKRPNSIQTRGQVLCV 163
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 740-838 1.85e-05

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: 45.72  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 740 WPHH-----GCPEDVQGFLSYLEEIQSVrrhtnsvLEGVKTrhppIVVHCSAGVGRTGVVILSELmiycLEHNEKVEVPT 814
Cdd:cd14505   75 WHHLpipdgGVPSDIAQWQELLEELLSA-------LENGKK----VLIHCKGGLGRTGLIAACLL----LELGDTLDPEQ 139

                         90       100
                 ....*....|....*....|....
gi 149041008 815 MLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:cd14505  140 AIAAVRALRPGAIQTPKQENFLHQ 163
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 749-823 2.54e-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: 41.48  E-value: 2.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149041008  749 VQGFLSYLEEIQSVRRHTNSVLEGVKTRHPPIVVHCSAGVGRTGVVILSELMIYclehnEKVEVPTMLRFLREQR 823
Cdd:pfam00782  41 IPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKT-----RNLSLNEAYSFVKERR 110
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
724-838 3.26e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 41.49  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 724 LLSGQERTVWHLQYTDWPHH------GCPEDVQGFLSYLEEIQSVRRhtnsvlegvktRHPPIVVHCSAGVGRTGVVILS 797
Cdd:COG2453   32 LTEEEELLLGLLEEAGLEYLhlpipdFGAPDDEQLQEAVDFIDEALR-----------EGKKVLVHCRGGIGRTGTVAAA 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 149041008 798 eLMIYclehnEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQ 838
Cdd:COG2453  101 -YLVL-----LGLSAEEALARVRAARPGAVETPAQRAFLER 135
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
716-823 8.80e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 40.34  E-value: 8.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008   716 TTGLKVKHLLSGQERTVW----HLQYTDWPHHGcpEDVQGFLSYLEEiqsvrrhTNSVLEGVKTRHPPIVVHCSAGVGRT 791
Cdd:smart00195  22 LKKLGITHVINVTNEVPNyngsDFTYLGVPIDD--NTETKISPYFPE-------AVEFIEDAESKGGKVLVHCQAGVSRS 92

                           90       100       110
                   ....*....|....*....|....*....|..
gi 149041008   792 GVVILSELMIYclehnEKVEVPTMLRFLREQR 823
Cdd:smart00195  93 ATLIIAYLMKT-----RNMSLNDAYDFVKDRR 119
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 756-838 3.30e-03

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: 38.80  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149041008 756 LEEIQSVRRhtnsVLEGVKTRHPPIVVHCSAGVGRTGvVILSELMIYClehnEKVEVPTMLRFLREQRMFMIQTIAQYKF 835
Cdd:cd14504   65 LEQIDEFLD----IVEEANAKNEAVLVHCLAGKGRTG-TMLACYLVKT----GKISAVDAINEIRRIRPGSIETSEQEKF 135


                 ...
gi 149041008 836 VYQ 838
Cdd:cd14504  136 VIQ 138
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 780-824 8.79e-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: 8.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 149041008 780 IVVHCSAGVGRTGVVILSeLMIYCLEHNEKVEVptmLRFLREQRM 824
Cdd:cd14497   98 AVVHCKAGKGRTGTVICA-YLLYYGQYSTADEA---LEYFAKKRF 138
 
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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