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Conserved domains on  [gi|1955810723|ref|XP_038857582|]
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tyrosine-protein phosphatase non-receptor type 9-like [Salvelinus namaycush]

Protein Classification

SEC14 family lipid-binding protein( domain architecture ID 13931872)

SEC14 family lipid-binding protein contains a lipid-binding domain that is found in secretory proteins and in lipid regulated proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 285-553 0e+00

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: 543.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 285 QRSGIHLEYVEIRKEQPPGTFHCALAAYNQERNRYGDVLCLDQTRVCLKTR-QNERSDYINASFMDGYKQKNAYIGTQGP 363
Cdd:cd14543     1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRnGDERTDYINANFMDGYKQKNAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 364 LEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQK 443
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 444 QVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAVKGMGPQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDM 523
Cdd:cd14543   161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 1955810723 524 GTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14543   241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 80-230 2.47e-29

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


:

Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 113.55  E-value: 2.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723   80 ELLSGKFTVLSVR--DPAGASIALYTAKLHHPNKTGNHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSNYTNFEL 155
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955810723  156 DLSKKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVKM---SDLCQHLPRDCLPEHLGGLLP 230
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGGTLD 158
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
10-58 3.91e-07

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 46.77  E-value: 3.91e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1955810723   10 EQATKQFLEEINKWTTQHgVSQLSWEVAVKFLMARKFDVLRAIELFHSY 58
Cdd:smart01100   1 EEALEELRELLEKHPDLL-PPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 285-553 0e+00

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: 543.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 285 QRSGIHLEYVEIRKEQPPGTFHCALAAYNQERNRYGDVLCLDQTRVCLKTR-QNERSDYINASFMDGYKQKNAYIGTQGP 363
Cdd:cd14543     1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRnGDERTDYINANFMDGYKQKNAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 364 LEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQK 443
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 444 QVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAVKGMGPQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDM 523
Cdd:cd14543   161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 1955810723 524 GTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14543   241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
292-558 3.76e-110

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 329.62  E-value: 3.76e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  292 EYVEIRKEQPP-GTFHCALAAYNQERNRYGDVLCLDQTRVCLKTRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGD 370
Cdd:smart00194   5 EFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPSTVED 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  371 FWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQY 450
Cdd:smart00194  85 FWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHY 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  451 LSWPDYGVPTSALTLIDFLGAVKRQQRQavkgmgpqwrghpLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQ 530
Cdd:smart00194 165 TNWPDHGVPESPESILDLIRAVRKSQST-------------STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 1955810723  531 TVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
313-558 4.64e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 320.73  E-value: 4.64e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQnERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEG 392
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDP-GPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 393 GRKKCGQYWPLEEGGQEVYSHMAVVNQR-VDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGA 471
Cdd:pfam00102  80 GREKCAQYWPEEEGESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 472 VKrqqrqavkgmgpQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:pfam00102 160 VR------------KSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIF 227


                  ....*..
gi 1955810723 552 CHNAILE 558
Cdd:pfam00102 228 LYDAILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 292-556 1.53e-67

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 221.72  E-value: 1.53e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 292 EYVEIRKEQPPGTFHCALAayNQERNRYGDVLCLDQTRVCLKTRQNeRSDYINASFMDGYKQKNAYIGTQGPLEKTYGDF 371
Cdd:PHA02738   30 EHQKVISEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERN-RGDYINANYVDGFEYKKKFICGQAPTRQTCYDF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 372 WRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQkQVTHFQYL 451
Cdd:PHA02738  107 YRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSATQ-TVTHFNFT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 452 SWPDYGVPTSALTLIDFLGAVKRQQRQAVKG---MGPQwRGHPlgPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNV 528
Cdd:PHA02738  186 AWPDHDVPKNTSEFLNFVLEVRQCQKELAQEslqIGHN-RLQP--PPIVVHCNAGLGRTPCYCVVDISISRFDACATVSI 262

                         250       260
                  ....*....|....*....|....*...
gi 1955810723 529 CQTVRWMRTQRAFTIQTPDQYYFCHNAI 556
Cdd:PHA02738  263 PSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
311-564 2.52e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 131.37  E-value: 2.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 311 AYNQERNRYGDVLCLDQTRVclktRQNERsdYINASFMDGyKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTN 390
Cdd:COG5599    40 INGSPLNRFRDIQPYKETAL----RANLG--YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 391 EGG--RKKCGQYWPLeeggQEVYSHMAVVNQRVDnhSHYSQTTLELHN----MEKCEQKQ--VTHFQYLSWPDYGVPTSA 462
Cdd:COG5599   113 EISkpKVKMPVYFRQ----DGEYGKYEVSSELTE--SIQLRDGIEARTyvltIKGTGQKKieIPVLHVKNWPDHGAISAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 463 lTLIDFLGAVKRQQRQAVKgmgpqwrghPLGPPmVVHCSAGIGRTGTFcaldICLSQLQDMG------TLNVCQTVRWMR 536
Cdd:COG5599   187 -ALKNLADLIDKKEKIKDP---------DKLLP-VVHCRAGVGRTGTL----IACLALSKSInalvqiTLSVEEIVIDMR 251

                         250       260
                  ....*....|....*....|....*....
gi 1955810723 537 TQRAFTI-QTPDQYyfchNAILEHAQRQG 564
Cdd:COG5599   252 TSRNGGMvQTSEQL----DVLVKLAEQQI 276
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 80-230 2.47e-29

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 113.55  E-value: 2.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723   80 ELLSGKFTVLSVR--DPAGASIALYTAKLHHPNKTGNHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSNYTNFEL 155
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955810723  156 DLSKKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVKM---SDLCQHLPRDCLPEHLGGLLP 230
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGGTLD 158
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 82-228 1.96e-26

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 105.11  E-value: 1.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  82 LSGKFTVLSVRDPAGASIALYTAKLHHPNKTGNHVVLQALFYLLDRAVESFETQRNGLVFIYDMAGSNYTNF-ELDLSKK 160
Cdd:cd00170     7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLsDLSLLKK 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 161 ILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVK--MSDLCQHLPRDCLPEHLGGL 228
Cdd:cd00170    87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
83-227 6.84e-24

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 97.71  E-value: 6.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  83 SGKFTVLSvRDPAGASIALYTAKLHHPNKTGNHVVLQALFYLLDRAV-ESFETQRNGLVFIYDMAGSNYTNFE---LDLS 158
Cdd:pfam00650   1 GGKVYLHG-RDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALlLMPEGQVEGLTVIIDLKGLSLSNMDwwsISLL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955810723 159 KKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVKMSD---LCQHLPRDCLPEHLGG 227
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNeeeLEKYIPPEQLPKEYGG 151
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
10-58 3.91e-07

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 46.77  E-value: 3.91e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1955810723   10 EQATKQFLEEINKWTTQHgVSQLSWEVAVKFLMARKFDVLRAIELFHSY 58
Cdd:smart01100   1 EEALEELRELLEKHPDLL-PPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 285-553 0e+00

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: 543.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 285 QRSGIHLEYVEIRKEQPPGTFHCALAAYNQERNRYGDVLCLDQTRVCLKTR-QNERSDYINASFMDGYKQKNAYIGTQGP 363
Cdd:cd14543     1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRnGDERTDYINANFMDGYKQKNAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 364 LEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQK 443
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 444 QVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAVKGMGPQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDM 523
Cdd:cd14543   161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 1955810723 524 GTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14543   241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
292-558 3.76e-110

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 329.62  E-value: 3.76e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  292 EYVEIRKEQPP-GTFHCALAAYNQERNRYGDVLCLDQTRVCLKTRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGD 370
Cdd:smart00194   5 EFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPSTVED 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  371 FWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQY 450
Cdd:smart00194  85 FWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHY 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  451 LSWPDYGVPTSALTLIDFLGAVKRQQRQavkgmgpqwrghpLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQ 530
Cdd:smart00194 165 TNWPDHGVPESPESILDLIRAVRKSQST-------------STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 1955810723  531 TVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
313-558 4.64e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 320.73  E-value: 4.64e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQnERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEG 392
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDP-GPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 393 GRKKCGQYWPLEEGGQEVYSHMAVVNQR-VDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGA 471
Cdd:pfam00102  80 GREKCAQYWPEEEGESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 472 VKrqqrqavkgmgpQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:pfam00102 160 VR------------KSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIF 227


                  ....*..
gi 1955810723 552 CHNAILE 558
Cdd:pfam00102 228 LYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 342-553 2.02e-90

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: 276.86  E-value: 2.02e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRV 421
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQavkgmgpqwrghpLGPPMVVHCS 501
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK-------------PNGPIVVHCS 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1955810723 502 AGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd00047   148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 313-558 1.07e-79

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: 250.39  E-value: 1.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQN-ERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNE 391
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 392 GGRKKCGQYWPLEegGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLga 471
Cdd:cd14553    83 RSRVKCDQYWPTR--GTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 472 vKRqqrqaVKGMGPqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:cd14553   159 -RR-----VKACNP-----PDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIF 227


                  ....*..
gi 1955810723 552 CHNAILE 558
Cdd:cd14553   228 IHDALLE 234
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 342-554 1.98e-76

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: 240.72  E-value: 1.98e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEegGQEVYSHMAVVNQRV 421
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKE--GTETYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKC------EQKQVTHFQYLSWPDYGVPTSALTLIDFlgaVKRQQRQAVKGMGpqwrghplgpP 495
Cdd:cd14549    79 EVLATYTVRTFSLKNLKLKkvkgrsSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPPGAG----------P 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1955810723 496 MVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHN 554
Cdd:cd14549   146 IVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 313-557 1.40e-73

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: 234.73  E-value: 1.40e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLK-TRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNE 391
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQpIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 392 GGRKKCGQYWPLEEGGQEVYshmAVVNQRVD-NHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLG 470
Cdd:cd14554    86 MGREKCHQYWPAERSARYQY---FVVDPMAEyNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 471 AVKRQQRQ-AVKGmgpqwrghplgpPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQY 549
Cdd:cd14554   163 QVHKTKEQfGQEG------------PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQY 230


                  ....*...
gi 1955810723 550 YFCHNAIL 557
Cdd:cd14554   231 QFCYRAAL 238
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 318-553 6.28e-72

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: 229.55  E-value: 6.28e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 318 RYGDVLCLDQTRVCLK-TRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKK 396
Cdd:cd14548     1 RYTNILPYDHSRVKLIpINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 397 CGQYWPLEEgGQEVYSHMAV--VNQRVDNHSHYSQTTLELHNmekcEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKr 474
Cdd:cd14548    81 CDHYWPFDQ-DPVYYGDITVtmLSESVLPDWTIREFKLERGD----EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVR- 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955810723 475 qqrqavkgmgpQWRGHPLGpPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14548   155 -----------DYIKQEKG-PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 342-553 2.00e-70

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: 225.21  E-value: 2.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMD-GYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPlEEGGQEVYSHMAV--VN 418
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVelVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 419 QRVDNHSHYSQTTLELHnMEKCEQKQVTHFQYLSWPDYGVPTSA---LTLIDFLGAVKRQqrqavkgmgpqwrgHPLGPP 495
Cdd:cd18533    80 EEENDDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPedlLTLIKLKRELNDS--------------ASLDPP 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955810723 496 MVVHCSAGIGRTGTFCALDICLSQLQDMGTLN---------VCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd18533   145 IIVHCSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 316-553 6.38e-69

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: 222.27  E-value: 6.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 316 RNRYGDVLCLDQTRVCLKTrQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRK 395
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKL-KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 396 KCGQYWPLEEGGQEVYSH--MAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLgavk 473
Cdd:cd14545    80 KCAQYWPQGEGNAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL---- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 474 rqqrQAVKGMGPQWRGHplGPPmVVHCSAGIGRTGTFCALDICLSQL--QDMGTLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:cd14545   156 ----QKVRESGSLSSDV--GPP-VVHCSAGIGRSGTFCLVDTCLVLIekGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228


                  ..
gi 1955810723 552 CH 553
Cdd:cd14545   229 SY 230
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 313-558 3.60e-68

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: 221.83  E-value: 3.60e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKT---RQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRT 389
Cdd:cd17667    27 NKHKNRYINILAYDHSRVKLRPlpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 390 NEGGRKKCGQYWPLEEggQEVYSHMAVVNQRVDNHSHYSQTTLELHNME-----------KCEQKQVTHFQYLSWPDYGV 458
Cdd:cd17667   107 VEKGRRKCDQYWPTEN--SEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkgqkgnpkgRQNERTVIQYHYTQWPDMGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 459 PTSALTLIDFlgaVKRQQRQAVKGMGpqwrghplgpPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQ 538
Cdd:cd17667   185 PEYALPVLTF---VRRSSAARTPEMG----------PVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQ 251

                         250       260
                  ....*....|....*....|
gi 1955810723 539 RAFTIQTPDQYYFCHNAILE 558
Cdd:cd17667   252 RNYLVQTEEQYIFIHDALLE 271
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 313-560 4.16e-68

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: 221.83  E-value: 4.16e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQN-ERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNE 391
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 392 GGRKKCGQYWPLEegGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLga 471
Cdd:cd14626   121 KSRVKCDQYWPIR--GTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFL-- 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 472 vkrqqrQAVKGMGPqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:cd14626   197 ------RRVKACNP-----PDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIF 265


                  ....*....
gi 1955810723 552 CHNAILEHA 560
Cdd:cd14626   266 IHEALLEAA 274
PHA02738 PHA02738
hypothetical protein; Provisional
 292-556 1.53e-67

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 221.72  E-value: 1.53e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 292 EYVEIRKEQPPGTFHCALAayNQERNRYGDVLCLDQTRVCLKTRQNeRSDYINASFMDGYKQKNAYIGTQGPLEKTYGDF 371
Cdd:PHA02738   30 EHQKVISEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERN-RGDYINANYVDGFEYKKKFICGQAPTRQTCYDF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 372 WRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQkQVTHFQYL 451
Cdd:PHA02738  107 YRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSATQ-TVTHFNFT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 452 SWPDYGVPTSALTLIDFLGAVKRQQRQAVKG---MGPQwRGHPlgPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNV 528
Cdd:PHA02738  186 AWPDHDVPKNTSEFLNFVLEVRQCQKELAQEslqIGHN-RLQP--PPIVVHCNAGLGRTPCYCVVDISISRFDACATVSI 262

                         250       260
                  ....*....|....*....|....*...
gi 1955810723 529 CQTVRWMRTQRAFTIQTPDQYYFCHNAI 556
Cdd:PHA02738  263 PSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 289-551 8.09e-66

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 216.79  E-value: 8.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 289 IHLEYVEIRKEQPPGTFHCALAAYNQERNRYGDVLCLDQTRVCLKTRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTY 368
Cdd:PHA02747   27 IRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETC 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 369 GDFWRMVWEQNVLVIVMTTRTNE-GGRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTH 447
Cdd:PHA02747  107 ADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISH 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 448 FQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAVKGMGPQwrgHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLN 527
Cdd:PHA02747  187 FQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPK---DALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAIC 263

                         250       260
                  ....*....|....*....|....
gi 1955810723 528 VCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:PHA02747  264 LAKTAEKIREQRHAGIMNFDDYLF 287
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 287-559 6.70e-65

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: 213.83  E-value: 6.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 287 SGIHLEYVEIRKEQPPGT-FHCALAAYNQERNRYGDVLCLDQTRVCLK-TRQNERSDYINASFMDGYKQKNAYIGTQGPL 364
Cdd:cd14627    26 TGMELEFKRLANSKAHTSrFISANLPCNKFKNRLVNIMPYETTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 365 EKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQevYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQ 444
Cdd:cd14627   106 AETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRT 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 445 VTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAVKgmgpqwrghplGPPMVVHCSAGIGRTGTFCALDICLSQLQDMG 524
Cdd:cd14627   184 VRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQ-----------DGPISVHCSAGVGRTGVFITLSIVLERMRYEG 252

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1955810723 525 TLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILEH 559
Cdd:cd14627   253 VVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 287-559 6.67e-64

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: 211.13  E-value: 6.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 287 SGIHLEYVEIRKEQPPGT-FHCALAAYNQERNRYGDVLCLDQTRVCLK-TRQNERSDYINASFMDGYKQKNAYIGTQGPL 364
Cdd:cd14628    25 TGMELEFKRLASSKAHTSrFISANLPCNKFKNRLVNIMPYESTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 365 EKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQevYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQ 444
Cdd:cd14628   105 AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRT 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 445 VTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAVKgmgpqwrghplGPPMVVHCSAGIGRTGTFCALDICLSQLQDMG 524
Cdd:cd14628   183 VRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQ-----------DGPISVHCSAGVGRTGVFITLSIVLERMRYEG 251

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1955810723 525 TLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILEH 559
Cdd:cd14628   252 VVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 292-561 7.70e-64

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 211.40  E-value: 7.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 292 EYVEIRKEQPPGTFHCALAAYNQERNRYGDVLCLDQTRVCLKTRQNeRSDYINASFMDGYKQKNAYIGTQGPLEKTYGDF 371
Cdd:PHA02742   31 EHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 372 WRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYL 451
Cdd:PHA02742  110 WQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 452 SWPDYGVPTSALTLIDFLGAVKRQQRQAVKGMGPQWRGHPlgPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQT 531
Cdd:PHA02742  190 DWPHGGLPRDPNKFLDFVLAVREADLKADVDIKGENIVKE--PPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSI 267

                         250       260       270
                  ....*....|....*....|....*....|
gi 1955810723 532 VRWMRTQRAFTIQTPDQYYFCHNAILEHAQ 561
Cdd:PHA02742  268 VRDLRKQRHNCLSLPQQYIFCYFIVLIFAK 297
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 293-561 9.88e-64

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: 210.27  E-value: 9.88e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 293 YVEIRKEQppGTFHCALAAY--NQERNRYGDVLCLDQTRVCLKTRQNersDYINASFMDGYKQKNAYIGTQGPLEKTYGD 370
Cdd:cd14608     5 YQDIRHEA--SDFPCRVAKLpkNKNRNRYRDVSPFDHSRIKLHQEDN---DYINASLIKMEEAQRSYILTQGPLPNTCGH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 371 FWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVY--SHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHF 448
Cdd:cd14608    80 FWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 449 QYLSWPDYGVPTSALTLIDFLGAVKRQqrqavKGMGPQWrghplgPPMVVHCSAGIGRTGTFCALDICL---SQLQDMGT 525
Cdd:cd14608   160 HYTTWPDFGVPESPASFLNFLFKVRES-----GSLSPEH------GPVVVHCSAGIGRSGTFCLADTCLllmDKRKDPSS 228

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1955810723 526 LNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILEHAQ 561
Cdd:cd14608   229 VDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAK 264
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 317-553 1.21e-63

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: 208.02  E-value: 1.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 317 NRYGDVLCLDQTRVCLKTRQN-ERSDYINASFMDGYKQKN-AYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGgR 394
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDdPLSSYINANYIRGYDGEEkAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 395 KKCGQYWPLEEGgqEVYSHMAVVNQRVDNHSHYSQTTLELHNMEkcEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKr 474
Cdd:cd14547    80 EKCAQYWPEEEN--ETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE- 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955810723 475 QQRQAVKGMGPqwrghplgppMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14547   155 EARQTEPHRGP----------IVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 257-558 2.37e-63

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: 209.56  E-value: 2.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 257 IPLADSSVHTPGLEAMclpefmahlgrlQRSGIHLEYVEIRKEQPPGTFHCALAAyNQERNRYGDVLCLDQTRVCLKTRQ 336
Cdd:cd14625     4 IPISELAEHTERLKAN------------DNLKLSQEYESIDPGQQFTWEHSNLEV-NKPKNRYANVIAYDHSRVILQPIE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 337 N-ERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPleEGGQEVYSHMA 415
Cdd:cd14625    71 GiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP--SRGTETYGMIQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 416 VVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLgavkrqqrQAVKGMGPqwrghPLGPP 495
Cdd:cd14625   149 VTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFL--------RRVKTCNP-----PDAGP 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955810723 496 MVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14625   216 IVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 317-558 2.61e-63

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 207.36  E-value: 2.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 317 NRYGDVLCLDQTRVCLKTRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKK 396
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 397 CGQYWPLEegGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQ 476
Cdd:cd14615    81 CEEYWPSK--QKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 477 RQavkgmgpqwrgHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAI 556
Cdd:cd14615   159 KQ-----------NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCA 227


                  ..
gi 1955810723 557 LE 558
Cdd:cd14615   228 LD 229
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 342-556 1.91e-62

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: 204.04  E-value: 1.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPleEGGQEVYSHMAVVNQRV 421
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAVKGmgpqwrghplgpPMVVHCS 501
Cdd:cd14552    79 TDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH------------PITVHCS 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1955810723 502 AGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAI 556
Cdd:cd14552   147 AGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 313-561 2.58e-62

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: 205.77  E-value: 2.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQNER--SDYINASFM-------DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVI 383
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVpgSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 384 VMTTRTNEGGRKKCGQYWPlEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNM-EKCEQKQVTHFQYLSWPDYGVPTSA 462
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWP-DEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 463 LTLIDFLGAVKRQQRQAvkgmgpqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMG---TLNVCQTVRWMRTQR 539
Cdd:cd14544   160 GGVLNFLEDVNQRQESL-----------PHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQR 228

                         250       260
                  ....*....|....*....|..
gi 1955810723 540 AFTIQTPDQYYFCHNAILEHAQ 561
Cdd:cd14544   229 SGMVQTEAQYKFIYVAVAQYIE 250
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 313-559 2.68e-62

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: 206.89  E-value: 2.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLK-TRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNE 391
Cdd:cd14629    53 NKFKNRLVNIMPYELTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 392 GGRKKCGQYWPLEEGGQevYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGA 471
Cdd:cd14629   133 MGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQ 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 472 VKRQQRQAVKgmgpqwrghplGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:cd14629   211 VHKTKEQFGQ-----------DGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQL 279


                  ....*...
gi 1955810723 552 CHNAILEH 559
Cdd:cd14629   280 CYRAALEY 287
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 342-557 5.61e-62

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: 203.29  E-value: 5.61e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEegGQEVYSHMAVVNQRV 421
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAD--GSEEYGNFLVTQKSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHN--MEKCEQK------QVTHFQYLSWPDYGVPTSALTLIDFLgavkRQQRQAvkgmgpqwRGHPLG 493
Cdd:cd17668    79 QVLAYYTVRNFTLRNtkIKKGSQKgrpsgrVVTQYHYTQWPDMGVPEYTLPVLTFV----RKASYA--------KRHAVG 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955810723 494 pPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAIL 557
Cdd:cd17668   147 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 317-558 3.26e-61

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: 202.04  E-value: 3.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 317 NRYGDVLCLDQTRVCLK-TRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRK 395
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKpIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 396 KCGQYWPLEEgGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQ 475
Cdd:cd14619    81 KCEHYWPLDY-TPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 476 QRQAVKGmgpqwrghplGPPmVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNA 555
Cdd:cd14619   160 LDQTMSG----------GPT-VVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQC 228


                  ...
gi 1955810723 556 ILE 558
Cdd:cd14619   229 ILD 231
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 276-558 6.57e-61

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: 203.04  E-value: 6.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 276 EFMAHLGRLqRSGIHLEYVEIRKEQPPG---TFHCALAAYNQERNRYGDVLCLDQTRVCLKTRQN-ERSDYINASFMDGY 351
Cdd:cd14624     8 ELADHIERL-KANDNLKFSQEYESIDPGqqfTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 352 KQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPleEGGQEVYSHMAVVNQRVDNHSHYSQTT 431
Cdd:cd14624    87 RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP--SRGTETYGLIQVTLLDTVELATYCVRT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 432 LELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLgavkrqqrQAVKGMGPqwrghPLGPPMVVHCSAGIGRTGTFC 511
Cdd:cd14624   165 FALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL--------RRVKTCNP-----PDAGPMVVHCSAGVGRTGCFI 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1955810723 512 ALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14624   232 VIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 289-556 2.08e-60

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 202.95  E-value: 2.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 289 IHLEYVEIRKEQPPGTFHCALAAYNQERNRYGDVLCLDQTRVCLKTR--------------------QNERSDYINASFM 348
Cdd:PHA02746   27 VLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAHeslkmfdvgdsdgkkievtsEDNAENYIHANFV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 349 DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGgRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYS 428
Cdd:PHA02746  107 DGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDD-DEKCFELWTKEEDSELAFGRFVAKILDIIEELSFT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 429 QTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAVKGM--GPQWRGhplgpPMVVHCSAGIGR 506
Cdd:PHA02746  186 KTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQAdnDPQTLG-----PIVVHCSAGIGR 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1955810723 507 TGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAI 556
Cdd:PHA02746  261 AGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 293-556 5.10e-60

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: 199.81  E-value: 5.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 293 YVEIRKEQPPGTFHCALAAYNQERNRYGDVLCLDQTRVCLktrQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFW 372
Cdd:cd14607     4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKL---QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 373 RMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRV--DNHSHYSQTTLELHNMEKCEQKQVTHFQY 450
Cdd:cd14607    81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLseDVKSYYTVHLLQLENINSGETRTISHFHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 451 LSWPDYGVPTSALTLIDFLGAVKRQqrqavKGMGPQwrghplGPPMVVHCSAGIGRTGTFCALDICLSQLQ--DMGTLNV 528
Cdd:cd14607   161 TTWPDFGVPESPASFLNFLFKVRES-----GSLSPE------HGPAVVHCSAGIGRSGTFSLVDTCLVLMEkkDPDSVDI 229

                         250       260
                  ....*....|....*....|....*...
gi 1955810723 529 CQTVRWMRTQRAFTIQTPDQYYFCHNAI 556
Cdd:cd14607   230 KQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 335-558 7.68e-60

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: 198.35  E-value: 7.68e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 335 RQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEegGQEVYSHM 414
Cdd:cd14623    19 RGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSD--GSVSYGDI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 415 AVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAvkgmgpqwRGHplgp 494
Cdd:cd14623    97 TIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQS--------GNH---- 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955810723 495 PMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14623   165 PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 317-557 2.88e-59

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: 196.70  E-value: 2.88e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 317 NRYGDVLCLDQTRVCL-KTRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRK 395
Cdd:cd14618     1 NRYPHVLPYDHSRVRLsQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 396 KCGQYWPlEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVkRQ 475
Cdd:cd14618    81 LCDHYWP-SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELV-RE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 476 QRQAVKGMGpqwrghplgpPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNA 555
Cdd:cd14618   159 HVQATKGKG----------PTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                  ..
gi 1955810723 556 IL 557
Cdd:cd14618   229 IL 230
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 313-558 8.10e-59

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: 196.97  E-value: 8.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQNE-RSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNE 391
Cdd:cd14603    30 NVKKNRYKDILPYDQTRVILSLLQEEgHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 392 GGRKKCGQYWPLEEGGQEV--YSHMAVVNQRVDNHSHYSQTTLELHNmekcEQKQVTHFQYLSWPDYGVPTSALTLIDFL 469
Cdd:cd14603   110 MGKKKCERYWAQEQEPLQTgpFTITLVKEKRLNEEVILRTLKVTFQK----ESRSVSHFQYMAWPDHGIPDSPDCMLAMI 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 470 GAVKRQQrqavkGMGPQwrghplgpPMVVHCSAGIGRTGTFCALD-----ICLSQLQDmgTLNVCQTVRWMRTQRAFTIQ 544
Cdd:cd14603   186 ELARRLQ-----GSGPE--------PLCVHCSAGCGRTGVICTVDyvrqlLLTQRIPP--DFSIFDVVLEMRKQRPAAVQ 250

                         250
                  ....*....|....
gi 1955810723 545 TPDQYYFCHNAILE 558
Cdd:cd14603   251 TEEQYEFLYHTVAQ 264
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 313-558 1.11e-58

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: 195.63  E-value: 1.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQNE-RSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNE 391
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 392 GGRKKCGQYWPLEeggQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLga 471
Cdd:cd14630    83 VGRVKCVRYWPDD---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFV-- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 472 vkRQqrqaVKGMGPqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:cd14630   158 --RQ----VKFLNP-----PDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVF 226


                  ....*..
gi 1955810723 552 CHNAILE 558
Cdd:cd14630   227 VHDAILE 233
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 341-557 1.68e-58

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: 194.08  E-value: 1.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 341 DYINASFMD----GYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPlEEGGQEVYSHMAV 416
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWP-DLGETMQFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 417 VNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVkRQQRQavkGMgpqwrghplGPPM 496
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRV-RQNRV---GM---------VEPT 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955810723 497 VVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAIL 557
Cdd:cd14541   147 VVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 342-558 2.82e-58

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: 193.36  E-value: 2.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFM--DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWP-------LEEGGQEVys 412
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslnkplICGGRLEV-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 413 hmAVVNQRvdNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAvkgmgpqwrghpl 492
Cdd:cd14538    79 --SLEKYQ--SLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSG------------- 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955810723 493 gpPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14538   142 --PIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 313-563 7.39e-58

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: 195.54  E-value: 7.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRV--CLKTrQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTN 390
Cdd:cd14604    57 NVKKNRYKDILPFDHSRVklTLKT-SSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 391 EGGRKKCGQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTL--ELHNmekcEQKQVTHFQYLSWPDYGVPTSALTLIDF 468
Cdd:cd14604   136 EMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLllEFQN----ETRRLYQFHYVNWPDHDVPSSFDSILDM 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 469 LGAVKR-QQRQAVkgmgpqwrghplgpPMVVHCSAGIGRTGTFCALDICLSQLQdMGTL----NVCQTVRWMRTQRAFTI 543
Cdd:cd14604   212 ISLMRKyQEHEDV--------------PICIHCSAGCGRTGAICAIDYTWNLLK-AGKIpeefNVFNLIQEMRTQRHSAV 276

                         250       260
                  ....*....|....*....|
gi 1955810723 544 QTPDQYYFCHNAILEHAQRQ 563
Cdd:cd14604   277 QTKEQYELVHRAIAQLFEKQ 296
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 276-557 2.58e-57

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: 193.14  E-value: 2.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 276 EFMAHLGRLQRSG-IHLEYVEIRKEQPPGTFHCALAAYNQERNRYGDVLCLDQTRVCLktrqNERSDYINASFMD----G 350
Cdd:cd14600     2 ESMAQLKKGLESGtVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNmeipS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 351 YKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPleeGGQEV--YSHMAVVNQRVDNHSHYS 428
Cdd:cd14600    78 ANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWP---DPPDVmeYGGFRVQCHSEDCTIAYV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 429 QTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVkRQQRQAvkgmgpqwrghplGPPMVVHCSAGIGRTG 508
Cdd:cd14600   155 FREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYV-RSKRVE-------------NEPVLVHCSAGIGRTG 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1955810723 509 TFCALD--ICLSQL-QDMGTLNVcqtVRWMRTQRAFTIQTPDQYYFCHNAIL 557
Cdd:cd14600   221 VLVTMEtaMCLTERnQPVYPLDI---VRKMRDQRAMMVQTSSQYKFVCEAIL 269
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 313-558 3.27e-56

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: 190.09  E-value: 3.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQNER--SDYINASFM------DGYKQKNaYIGTQGPLEKTYGDFWRMVWEQNVLVIV 384
Cdd:cd14606    18 NKSKNRYKNILPFDHSRVILQGRDSNIpgSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRVIV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 385 MTTRTNEGGRKKCGQYWPlEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQ-KQVTHFQYLSWPDYGVPTSAL 463
Cdd:cd14606    97 MTTREVEKGRNKCVPYWP-EVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 464 TLIDFLGAVKRQQRQAvkgmgpqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGT---LNVCQTVRWMRTQRA 540
Cdd:cd14606   176 GVLSFLDQINQRQESL-----------PHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRS 244

                         250
                  ....*....|....*...
gi 1955810723 541 FTIQTPDQYYFCHNAILE 558
Cdd:cd14606   245 GMVQTEAQYKFIYVAIAQ 262
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 342-553 8.69e-56

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: 186.57  E-value: 8.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVvnqRV 421
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVV---KI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYS----QTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFlgavkRQQRQAVKGMGpqwrghplGPPMV 497
Cdd:cd14557    78 NEEKICPdyiiRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKL-----RRRVNAFNNFF--------SGPIV 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1955810723 498 VHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14557   145 VHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 313-558 3.85e-55

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: 187.56  E-value: 3.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQNER-SDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNE 391
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 392 GGRKKCGQYWPLEeggQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGA 471
Cdd:cd14633   120 VGRVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQ 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 472 VKRqqrqavkgmgpqwRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:cd14633   197 VKS-------------KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVF 263


                  ....*..
gi 1955810723 552 CHNAILE 558
Cdd:cd14633   264 IHDAILE 270
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 316-556 8.63e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 185.81  E-value: 8.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 316 RNRYGDVLCLDQTRVCLKTR--QNERSDYINASFMDGYKQK-NAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEG 392
Cdd:cd14612    18 KDRYKTILPNPQSRVCLRRAgsQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 393 gRKKCGQYWPLEEGgqeVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCeqKQVTHFQYLSWPDYGVPTSALTLIDFLGAV 472
Cdd:cd14612    98 -KEKCVHYWPEKEG---TYGRFEIRVQDMKECDGYTIRDLTIQLEEES--RSVKHYWFSSWPDHQTPESAGPLLRLVAEV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 473 KrQQRQAVKGMGPqwrghplgppMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFC 552
Cdd:cd14612   172 E-ESRQTAASPGP----------IVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                  ....
gi 1955810723 553 HNAI 556
Cdd:cd14612   241 HHTL 244
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 313-557 2.75e-54

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: 184.32  E-value: 2.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQNER-SDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNE 391
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEEEgSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 392 GGRKKCGQYWPLEEgGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEkcEQKQVTHFQYLSWPDYGVPT--SALTLIDFL 469
Cdd:cd14614    92 KRRVKCDHYWPFTE-EPVAYGDITVEMLSEEEQPDWAIREFRVSYAD--EVQDVMHFNYTAWPDHGVPTanAAESILQFV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 470 GAVkRQQRQAVKGmgpqwrghplgpPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQY 549
Cdd:cd14614   169 QMV-RQQAVKSKG------------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 235


                  ....*...
gi 1955810723 550 YFCHNAIL 557
Cdd:cd14614   236 IFIHQCVQ 243
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 313-557 2.96e-54

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: 183.88  E-value: 2.96e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLktrqNERSDYINASF--MDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTN 390
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 391 EGGRKKCGQYWPLEEGGQEVYS---HMAVVN-QRVDNhshYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLI 466
Cdd:cd14597    79 EGGKIKCQRYWPEILGKTTMVDnrlQLTLVRmQQLKN---FVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 467 DFLGAVKRQqrqavkgmgpqwrgHPLGpPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTP 546
Cdd:cd14597   156 TFISYMRHI--------------HKSG-PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTE 220

                         250
                  ....*....|.
gi 1955810723 547 DQYYFCHNAIL 557
Cdd:cd14597   221 DQYIFCYQVIL 231
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 317-553 3.11e-54

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: 183.58  E-value: 3.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 317 NRYGDVLCLDQTRVCLKTRQNER-SDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRK 395
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 396 KCGQYWPLEeggQEVYSHMAVVNQRVdnhshySQTTL---ELHNMEKCEQKQ------VTHFQYLSWPDYGVPTSALTLI 466
Cdd:cd14617    81 KCDHYWPAD---QDSLYYGDLIVQML------SESVLpewTIREFKICSEEQldaprlVRHFHYTVWPDHGVPETTQSLI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 467 DFLGAVKRQQRQAvkgmgpqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTP 546
Cdd:cd14617   152 QFVRTVRDYINRT-----------PGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTE 220


                  ....*..
gi 1955810723 547 DQYYFCH 553
Cdd:cd14617   221 CQYVYLH 227
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 313-556 3.47e-54

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: 184.45  E-value: 3.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQ-NER-SDYINASFM--------DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLV 382
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDGDpNEPvSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 383 IVMTTRTNEGGRKKCGQYWPLEEGGQEvYSHMAVVNQRVDNHSHYSQTTLELHNM-EKCEQKQVTHFQYLSWPDYGVPTS 461
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPDEYALKE-YGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 462 ALTLIDFLGAVKRQQrQAVKGMGpqwrghplgpPMVVHCSAGIGRTGTFCALDICLSQLQDMGT---LNVCQTVRWMRTQ 538
Cdd:cd14605   161 PGGVLDFLEEVHHKQ-ESIMDAG----------PVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQ 229

                         250
                  ....*....|....*...
gi 1955810723 539 RAFTIQTPDQYYFCHNAI 556
Cdd:cd14605   230 RSGMVQTEAQYRFIYMAV 247
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 302-558 3.86e-54

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: 185.26  E-value: 3.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 302 PGTFHCALAAYNQERNRYGDVLCLDQTRVCLKTRQNE-RSDYINAS-FMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQN 379
Cdd:cd14610    33 PNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHsHSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 380 VLVIVMTTRTNEGGRKKCGQYWPLEegGQEVYsHMAVVNQrVDNH---SHYSQTTLELHNMEKCEQKQVTHFQYLSWPDY 456
Cdd:cd14610   113 CVVIVMLTPLAENGVKQCYHYWPDE--GSNLY-HIYEVNL-VSEHiwcEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQ 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 457 GVPTSALTLIDFlgavKRQQRQAVKGMgpqwrghplGPPMVVHCSAGIGRTGTFCALDICLSQL-QDMGTLNVCQTVRWM 535
Cdd:cd14610   189 GVPASTRSLLDF----RRKVNKCYRGR---------SCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHL 255

                         250       260
                  ....*....|....*....|...
gi 1955810723 536 RTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14610   256 RDQRPGMVQTKEQFEFALTAVAE 278
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 316-558 8.46e-54

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: 182.73  E-value: 8.46e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 316 RNRYGDVLCLDQTRVCLK-TRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGR 394
Cdd:cd14602     1 KNRYKDILPYDHSRVELSlITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 395 KKCGQYWPleEGGQEV--YSHMAVVNQRVDNHSHYSQTTLELHNMEKCeqKQVTHFQYLSWPDYGVPTSALTLIDFLGAV 472
Cdd:cd14602    81 KKCERYWA--EPGEMQleFGPFSVTCEAEKRKSDYIIRTLKVKFNSET--RTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 473 KRQQrqavkgmgpqwrgHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDmGTLNVCQTV----RWMRTQRAFTIQTPDQ 548
Cdd:cd14602   157 RCYQ-------------EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKD-GIIPENFSVfsliQEMRTQRPSLVQTKEQ 222

                         250
                  ....*....|
gi 1955810723 549 YYFCHNAILE 558
Cdd:cd14602   223 YELVYNAVIE 232
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 313-559 1.63e-53

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: 184.07  E-value: 1.63e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 313 NQERNRYGDVLCLDQTRVCLKTRQN-ERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNE 391
Cdd:cd14621    52 NKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 392 GGRKKCGQYWPleEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNM----EKCEQKQVTHFQYLSWPDYGVPTSALTLID 467
Cdd:cd14621   132 RKECKCAQYWP--DQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLK 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 468 FLgavkrqqrQAVKGMGPQWRGhplgpPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPD 547
Cdd:cd14621   210 FL--------KKVKNCNPQYAG-----AIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDM 276

                         250
                  ....*....|..
gi 1955810723 548 QYYFCHNAILEH 559
Cdd:cd14621   277 QYVFIYQALLEH 288
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 342-551 2.29e-53

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: 180.11  E-value: 2.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPleEGGQEVYSHMAVVNQRV 421
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP--DQGCWTYGNLRVRVEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKC----EQKQVTHFQYLSWPDYGVPTSALTLIDFLgavkrqqrQAVKGMGPQWRGhplgpPMV 497
Cdd:cd14551    79 VVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFL--------KKVKSANPPRAG-----PIV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1955810723 498 VHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:cd14551   146 VHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVF 199
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 342-560 2.77e-53

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: 180.73  E-value: 2.77e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINAS---FMDGYKQKNaYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQ--EVYSHMAV 416
Cdd:cd14540     1 YINAShitATVGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaLTFGEYKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 417 VNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFL---GAVKRQQRQAVkgmgpqwRGHPLG 493
Cdd:cd14540    80 STKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLeeiNSVRRHTNQDV-------AGHNRN 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955810723 494 PPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILEHA 560
Cdd:cd14540   153 PPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 342-553 7.09e-53

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: 179.13  E-value: 7.09e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEeggQEVYSHMAVVNQRV 421
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDE---KKTYGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQavkgmgpQWRGHPLGPPMVVHCS 501
Cdd:cd14558    78 EKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPY-------KNSKHGRSVPIVVHCS 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1955810723 502 AGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14558   151 DGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 342-554 2.59e-52

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: 177.62  E-value: 2.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQRV 421
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSH-YSQTTLELHnmEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQrqavkGMGPqwrghplgPPMVVHC 500
Cdd:cd14542    81 KRVGPdFLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQ-----GSED--------VPICVHC 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1955810723 501 SAGIGRTGTFCALDICLSQLQDMG---TLNVCQTVRWMRTQRAFTIQTPDQYYFCHN 554
Cdd:cd14542   146 SAGCGRTGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 319-558 4.45e-52

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: 177.83  E-value: 4.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 319 YGDVLCLDQTRVCL-KTRQNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKC 397
Cdd:cd14620     1 YPNILPYDHSRVILsQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 398 GQYWPleEGGQEVYSHMAVVNQRVdnhshysqTTLELHNMEK-CEQKQ----------VTHFQYLSWPDYGVPTSALTLI 466
Cdd:cd14620    81 YQYWP--DQGCWTYGNIRVAVEDC--------VVLVDYTIRKfCIQPQlpdgckaprlVTQLHFTSWPDFGVPFTPIGML 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 467 DFLgavkrqqrQAVKGMGPQWRGhplgpPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTP 546
Cdd:cd14620   151 KFL--------KKVKSVNPVHAG-----PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTD 217

                         250
                  ....*....|..
gi 1955810723 547 DQYYFCHNAILE 558
Cdd:cd14620   218 MQYSFIYQALLE 229
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 342-558 6.80e-52

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: 176.26  E-value: 6.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEeggQEVYSHMAVVNQRV 421
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD---TEVYGDIKVTLVET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLgavkRQqrqaVKGMGPqwrghPLGPPMVVHCS 501
Cdd:cd14555    78 EPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFI----RR----VKASNP-----PSAGPIVVHCS 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1955810723 502 AGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14555   145 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 341-556 1.89e-51

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: 175.19  E-value: 1.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 341 DYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEegGQEVYSHMAVVNQR 420
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE--GSVTHGEITIEIKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 421 VDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAVKGmgpqwrghplgpPMVVHC 500
Cdd:cd14622    79 DTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH------------PIVVHC 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1955810723 501 SAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAI 556
Cdd:cd14622   147 SAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 342-553 2.86e-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: 174.88  E-value: 2.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNA-YIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQR 420
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 421 VDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVK---RQQRqavkgmgpqwrghPLGPPMV 497
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshyLQQR-------------SLQTPIV 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 498 VHCSAGIGRTGTFCALdicLSQLQDM----GTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14539   148 VHCSSGVGRTGAFCLL---YAAVQEIeagnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 342-558 4.71e-51

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: 174.17  E-value: 4.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKN-AYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPleEGGQEVYsHMAVVNQr 420
Cdd:cd14546     1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP--EEGSEVY-HIYEVHL- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 421 VDNHS---HYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQavkgmgpqwrghpLGPPMV 497
Cdd:cd14546    77 VSEHIwcdDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRG-------------RSCPIV 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955810723 498 VHCSAGIGRTGTFCALDICLSQL-QDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14546   144 VHCSDGAGRTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 341-558 6.92e-51

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: 173.98  E-value: 6.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 341 DYINASFMD----GYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPlEEGGQEVYSHMAV 416
Cdd:cd14601     1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 417 VNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVkRQQRQavkgmgpqwrGHPlgPPM 496
Cdd:cd14601    80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLV-RNKRA----------GKD--EPV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955810723 497 VVHCSAGIGRTGTFCALD--ICLSQL-QDMGTLNVcqtVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14601   147 VVHCSAGIGRTGVLITMEtaMCLIECnQPVYPLDI---VRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 283-561 1.07e-50

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: 175.96  E-value: 1.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 283 RLQRSGIHLEYVEIRKEQPPGTFHCALAAYNQERNRYGDVLCLDQTRVCLKTRQNERSDYINASFMDGY--KQKNAYIGT 360
Cdd:cd14599     8 KLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTvgGEEWHYIAT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 361 QGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPL--EEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNME 438
Cdd:cd14599    88 QGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 439 KCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQAVKGMGPQWRGHplgPPMVVHCSAGIGRTGTFCALDICLS 518
Cdd:cd14599   168 SGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCN---PPIVVHCSAGVGRTGVVILTELMIG 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1955810723 519 QLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILEHAQ 561
Cdd:cd14599   245 CLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 342-558 1.37e-50

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: 172.93  E-value: 1.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEeggQEVYSHMAVVNQRV 421
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD---SDTYGDIKITLLKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLgavkrqqrQAVKGMGPqwrghPLGPPMVVHCS 501
Cdd:cd14632    78 ETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFI--------RRVKASTP-----PDAGPVVVHCS 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1955810723 502 AGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14632   145 AGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 316-556 1.59e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 174.67  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 316 RNRYGDVLCLDQTRVCLKTRQNER--SDYINASFMDGY-KQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEG 392
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 393 GrKKCGQYWPLEeggQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEkcEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAV 472
Cdd:cd14613   108 N-EKCTEYWPEE---QVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 473 KRQQRQAVKGMGPqwrghplgppMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFC 552
Cdd:cd14613   182 EEARQQAEPNCGP----------VIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFV 251


                  ....
gi 1955810723 553 HNAI 556
Cdd:cd14613   252 HHVL 255
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 342-554 5.84e-50

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: 171.49  E-value: 5.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKN--AYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRK-KCGQYWPLEEGGQEVYSHMAVVN 418
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 419 QRVdNHSHYSQT--TLELHNMEKCEQ-KQVTHFQYLSWPDYGVPTSALTLidflgavkRQQRQAVKGMGPQwrghpLGpP 495
Cdd:cd17658    81 KKL-KHSQHSITlrVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSV--------RELLKRLYGIPPS-----AG-P 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955810723 496 MVVHCSAGIGRTGTFCALDICLSQ--LQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHN 554
Cdd:cd17658   146 IVVHCSAGIGRTGAYCTIHNTIRRilEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 329-558 1.09e-49

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 170.97  E-value: 1.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 329 RVCLKTRQNE-RSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEegg 407
Cdd:cd14631     1 RVILQPVEDDpSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 408 QEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRqavkgmgpqw 487
Cdd:cd14631    78 TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNP---------- 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955810723 488 rghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14631   148 ---PSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 316-554 1.89e-49

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: 170.87  E-value: 1.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 316 RNRYGDVLCLDQTRVCLKTRQNER--SDYINASFMDGYK-QKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEG 392
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDslSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 393 GrKKCGQYWPLEEGgqeVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCeqKQVTHFQYLSWPDYGVPTSALTLIDFLGAV 472
Cdd:cd14611    82 N-EKCVLYWPEKRG---IYGKVEVLVNSVKECDNYTIRNLTLKQGSQS--RSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 473 KrQQRQAVKGMGPqwrghplgppMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFC 552
Cdd:cd14611   156 E-EDRLASPGRGP----------VVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                  ..
gi 1955810723 553 HN 554
Cdd:cd14611   225 HH 226
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 302-558 3.04e-49

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: 172.14  E-value: 3.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 302 PGTFHCALAAYNQERNRYGDVLCLDQTRVCLKTRQN-ERSDYINAS-FMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQN 379
Cdd:cd14609    31 PNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNpSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 380 VLVIVMTTRTNEGGRKKCGQYWPLEegGQEVYsHMAVVNqRVDNH---SHYSQTTLELHNMEKCEQKQVTHFQYLSWPDY 456
Cdd:cd14609   111 CTVIVMLTPLVEDGVKQCDRYWPDE--GSSLY-HIYEVN-LVSEHiwcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 457 GVPTSALTLIDFLGAVKRqqrqavkgmgpQWRGHPLgpPMVVHCSAGIGRTGTFCALDICLSQL-QDMGTLNVCQTVRWM 535
Cdd:cd14609   187 GIPSSTRPLLDFRRKVNK-----------CYRGRSC--PIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHV 253

                         250       260
                  ....*....|....*....|...
gi 1955810723 536 RTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14609   254 RDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 342-558 5.75e-47

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: 163.38  E-value: 5.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASF--MDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVvnq 419
Cdd:cd14596     1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQL--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 420 RVDNHS---HYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQqrqavkgmgpqwrgHPLGPpM 496
Cdd:cd14596    78 RLENYQalqYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKV--------------HNTGP-I 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955810723 497 VVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14596   143 VVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 340-553 1.25e-45

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: 160.46  E-value: 1.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 340 SDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWPLEEGGQEVYSHMAVVNQ 419
Cdd:cd14616    25 SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCHQYWPEDNKPVTVFGDIVITKL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 420 RVDNHSHYSQTTLELHNMEKCeqKQVTHFQYLSWPDYGVPTSALTLIDFLGAVkRQQRqavkgmgpqwrgHPLGPPMVVH 499
Cdd:cd14616   105 MEDVQIDWTIRDLKIERHGDY--MMVRQCNFTSWPEHGVPESSAPLIHFVKLV-RASR------------AHDNTPMIVH 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1955810723 500 CSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14616   170 CSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 342-553 3.74e-44

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: 155.64  E-value: 3.74e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGrKKCGQYWPLEEGGQEVYSHMAVVNQRV 421
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKD-QSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DnhSHYSQTTLELHNMEKCEQKQ--VTHFQYLSWPDYG-VPTSALTLIDFLGAVKRQQRQAVKGmgpqwrghplgpPMVV 498
Cdd:cd14556    80 D--EDVISRIFRLQNTTRPQEGYrmVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEG------------PIVV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1955810723 499 HCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14556   146 HCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 342-558 5.87e-40

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: 145.12  E-value: 5.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMD---GYKQKNaYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWP-LEEGGQEV-YSHMAV 416
Cdd:cd14598     1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrLGSRHNTVtYGRFKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 417 VNQRVDNHSHYSQTTLELHNMEKCEQKQVTHFQYLSWPDYGVPTSA---LTLIDFLGAVKRQQRQAVKGMGPQwrghplg 493
Cdd:cd14598    80 TTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLkgfLSYLEEIQSVRRHTNSTIDPKSPN------- 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955810723 494 PPMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14598   153 PPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
444-558 8.36e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 129.40  E-value: 8.36e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  444 QVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQavkgmgpqwrgHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQD- 522
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ-----------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAe 69

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1955810723  523 MGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:smart00404  70 AGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 444-558 8.36e-36

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 129.40  E-value: 8.36e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  444 QVTHFQYLSWPDYGVPTSALTLIDFLGAVKRQQRQavkgmgpqwrgHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQD- 522
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ-----------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAe 69

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1955810723  523 MGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:smart00012  70 AGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
311-564 2.52e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 131.37  E-value: 2.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 311 AYNQERNRYGDVLCLDQTRVclktRQNERsdYINASFMDGyKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTN 390
Cdd:COG5599    40 INGSPLNRFRDIQPYKETAL----RANLG--YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 391 EGG--RKKCGQYWPLeeggQEVYSHMAVVNQRVDnhSHYSQTTLELHN----MEKCEQKQ--VTHFQYLSWPDYGVPTSA 462
Cdd:COG5599   113 EISkpKVKMPVYFRQ----DGEYGKYEVSSELTE--SIQLRDGIEARTyvltIKGTGQKKieIPVLHVKNWPDHGAISAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 463 lTLIDFLGAVKRQQRQAVKgmgpqwrghPLGPPmVVHCSAGIGRTGTFcaldICLSQLQDMG------TLNVCQTVRWMR 536
Cdd:COG5599   187 -ALKNLADLIDKKEKIKDP---------DKLLP-VVHCRAGVGRTGTL----IACLALSKSInalvqiTLSVEEIVIDMR 251

                         250       260
                  ....*....|....*....|....*....
gi 1955810723 537 TQRAFTI-QTPDQYyfchNAILEHAQRQG 564
Cdd:COG5599   252 TSRNGGMvQTSEQL----DVLVKLAEQQI 276
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 342-558 6.98e-33

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: 125.13  E-value: 6.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGgrKKCGQYWPleEGGQEVYSHMAVVNQRV 421
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA--QLCMQYWP--EKTSCCYGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKCEQ--KQVTHFQYLSWPDY-GVPTSALTLIDFLGAVKRQQRQAVKGMGpqwrghplgpPMVV 498
Cdd:cd14634    77 DIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGREG----------RTVV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 499 HCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14634   147 HCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 292-556 5.06e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 125.46  E-value: 5.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 292 EYVEIRKEQPPGtfhcALAAYNQERNRYGD-VLCLDQTRVcLKTRQNERSD--YINASFMDGYKQKNAYIGTQGPLEKTY 368
Cdd:PHA02740   30 EYRAIVPEHEDE----ANKACAQAENKAKDeNLALHITRL-LHRRIKLFNDekVLDARFVDGYDFEQKFICIINLCEDAC 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 369 GDFWRMVWEQNVLVIVMTTRTNEggrKKC-GQYWPLEEGGQEVYSHMAVVNQRVDNHSHYSQTTLELHNMEKCEQKqVTH 447
Cdd:PHA02740  105 DKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQAQK-ISH 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 448 FQYLSWPDYGVPTSALTLIDFLGAVKR-----QQRQAVKGMGPqwrghplgppMVVHCSAGIGRTGTFCALDICLSQLQD 522
Cdd:PHA02740  181 FQYTAWPADGFSHDPDAFIDFFCNIDDlcadlEKHKADGKIAP----------IIIDCIDGISSSAVFCVFDICATEFDK 250

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1955810723 523 MGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAI 556
Cdd:PHA02740  251 TGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 342-558 7.18e-30

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: 116.55  E-value: 7.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRK-KCGQYWPleEGGQEVYSHMAVVNQR 420
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP--EPGLQQYGPMEVEFVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 421 VDNHSHYSQTTLELHNMEKCEQKQ--VTHFQYLSWPDY-GVPTSALTLIDFLGAVKRQQRQAVKGMgpqwrghplgppMV 497
Cdd:cd14637    79 GSADEDIVTRLFRVQNITRLQEGHlmVRHFQFLRWSAYrDTPDSKKAFLHLLASVEKWQRESGEGR------------TV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955810723 498 VHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14637   147 VHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 342-558 1.64e-29

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: 115.56  E-value: 1.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGgrKKCGQYWPleEGGQEVYSHMAVVNQRV 421
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWP--ENGVHRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKCEQ--KQVTHFQYLSWPDY-GVPTSALTLIDFLGAVKRQQRQAVKGMGPQwrghplgppmVV 498
Cdd:cd14635    77 DLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGEGRT----------VV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 499 HCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14635   147 HCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 80-230 2.47e-29

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 113.55  E-value: 2.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723   80 ELLSGKFTVLSVR--DPAGASIALYTAKLHHPNKTGNHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSNYTNFEL 155
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955810723  156 DLSKKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVKM---SDLCQHLPRDCLPEHLGGLLP 230
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGGTLD 158
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 342-551 1.93e-28

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: 112.41  E-value: 1.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGrkKCGQYWPLEEggQEVYSHMAVVNQRV 421
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKE--KPLECETFKVTLSG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKCEQKQ------VTHFQYLSWPDygvPTSAL-TLIDFLGAVKRQQRQAVKgmgpqwrghplgp 494
Cdd:cd14550    77 EDHSCLSNEIRLIVRDFILESTQddyvleVRQFQCPSWPN---PCSPIhTVFELINTVQEWAQQRDG------------- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1955810723 495 PMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:cd14550   141 PIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 342-558 4.82e-28

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: 111.66  E-value: 4.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGgrKKCGQYWPleEGGQEVYSHMAVVNQRV 421
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWP--EEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNHSHYSQTTLELHNMEKCEQK--QVTHFQYLSWPDY-GVPTSALTLIDFLGAVKRQQRQAVKGMGPqwrghplgppMVV 498
Cdd:cd14636    77 SMDCDVISRIFRICNLTRPQEGylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGEGR----------TII 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 499 HCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAILE 558
Cdd:cd14636   147 HCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 82-228 1.96e-26

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 105.11  E-value: 1.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  82 LSGKFTVLSVRDPAGASIALYTAKLHHPNKTGNHVVLQALFYLLDRAVESFETQRNGLVFIYDMAGSNYTNF-ELDLSKK 160
Cdd:cd00170     7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLsDLSLLKK 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 161 ILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVK--MSDLCQHLPRDCLPEHLGGL 228
Cdd:cd00170    87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGGT 156
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 342-557 4.21e-24

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 100.07  E-value: 4.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCgQYWPLEEggQEVYSHMAVVNQRV 421
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKD--EPINCETFKVTLIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 422 DNH---SHYSQTTLELHNMEKCEQK---QVTHFQYLSWPDYGVPTS-ALTLIDFLgavkrqQRQAVKGMGpqwrghplgp 494
Cdd:cd17669    78 EEHkclSNEEKLIIQDFILEATQDDyvlEVRHFQCPKWPNPDSPISkTFELISII------KEEAANRDG---------- 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955810723 495 PMVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAIL 557
Cdd:cd17669   142 PMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
CRAL_TRIO pfam00650
CRAL/TRIO domain;
83-227 6.84e-24

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 97.71  E-value: 6.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  83 SGKFTVLSvRDPAGASIALYTAKLHHPNKTGNHVVLQALFYLLDRAV-ESFETQRNGLVFIYDMAGSNYTNFE---LDLS 158
Cdd:pfam00650   1 GGKVYLHG-RDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALlLMPEGQVEGLTVIIDLKGLSLSNMDwwsISLL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955810723 159 KKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVKMSD---LCQHLPRDCLPEHLGG 227
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNeeeLEKYIPPEQLPKEYGG 151
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 342-557 3.24e-23

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: 97.83  E-value: 3.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 342 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTrTNEGGRKKCGQYWPLEEGGQ--EVYSHMAVVNQ 419
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQGLAEDEFVYWPSREESMncEAFTVTLISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 420 RVdNHSHYSQTTLELHNMEKCEQK---QVTHFQYLSWPDYGVP-TSALTLIDFLgavkrqQRQAVKGMGpqwrghplgpP 495
Cdd:cd17670    80 RL-CLSNEEQIIIHDFILEATQDDyvlEVRHFQCPKWPNPDAPiSSTFELINVI------KEEALTRDG----------P 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955810723 496 MVVHCSAGIGRTGTFCALDICLSQLQDMGTLNVCQTVRWMRTQRAFTIQTPDQYYFCHNAIL 557
Cdd:cd17670   143 TIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 354-549 3.33e-12

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: 66.27  E-value: 3.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 354 KNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTNEGGRKKCGQYWpleeGGQEVYSHMAVVNQRVDNHSHYSQTTLE 433
Cdd:cd14559    28 KNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF----RQSGTYGSVTVKSKKTGKDELVDGLKAD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 434 LHNME-KCEQKQVT----HFQylSWPDYG-VPTSAL-TLIDFLGAVKRQQRQAVKGMGPQWRGHPLGPPMVVHCSAGIGR 506
Cdd:cd14559   104 MYNLKiTDGNKTITipvvHVT--NWPDHTaISSEGLkELADLVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGR 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1955810723 507 TGTFCAlDICLSQLQDmgTLNVCQTVRWMRTQR-AFTIQTPDQY 549
Cdd:cd14559   182 TGQLAA-AMELNKSPN--NLSVEDIVSDMRTSRnGKMVQKDEQL 222
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 492-554 6.51e-11

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: 59.67  E-value: 6.51e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955810723 492 LGPPMVVHCSAGIGRTGTFCALDICLSQLQDMGtlnvcQTVRWMRTQRAFTI-QTPDQYYFCHN 554
Cdd:cd14494    55 PGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAE-----EAVRIVRLIRPGGIpQTIEQLDFLIK 113
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 96-234 2.79e-08

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 52.71  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723  96 GASIALYTAKLHHPNKTGNHVVLQALFYLLDRAVESFETQrnGLVFIYDMAGSNYTNFE-LDLSKKILNLLKGAFPARLK 174
Cdd:pfam13716   1 GRPVLVFISKLLPSRPASLDDLDRLLFYLLKTLSEKLKGK--PFVVVVDHTGVTSENFPsLSFLKKAYDLLPRAFKKNLK 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955810723 175 KVLIVGAPVWFRVpYNLLSLLLKEKLRERVQMVKMS---DLCQHLPRDCLPEHLGGLLPLDAH 234
Cdd:pfam13716  79 AVYVVHPSTFLRT-FLKTLGSLLGSKKLRKKVHYVSslsELWEGIDREQLPTELPGVLSYDEE 140
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
10-58 3.91e-07

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 46.77  E-value: 3.91e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1955810723   10 EQATKQFLEEINKWTTQHgVSQLSWEVAVKFLMARKFDVLRAIELFHSY 58
Cdd:smart01100   1 EEALEELRELLEKHPDLL-PPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 437-553 3.24e-06

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: 47.26  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 437 MEKCEQKQVTHFQYlSWPDYGVPT---SALTLIDFLGAVKRQQRQAVkgmgpqwrghplgppmvVHCSAGIGRTGTFCAL 513
Cdd:cd14505    65 LEQYQQAGITWHHL-PIPDGGVPSdiaQWQELLEELLSALENGKKVL-----------------IHCKGGLGRTGLIAAC 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1955810723 514 diCLSQLQDmgTLNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14505   127 --LLLELGD--TLDPEQAIAAVRALRPGAIQTPKQENFLH 162
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
430-551 1.22e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 45.35  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 430 TTLELHNMEKCEQKQVTHFqYLSWPDYGVPTSAlTLIDFLGAVKRQQRQavkgmgpqwrGHPLgppmVVHCSAGIGRTGT 509
Cdd:COG2453    33 TEEEELLLGLLEEAGLEYL-HLPIPDFGAPDDE-QLQEAVDFIDEALRE----------GKKV----LVHCRGGIGRTGT 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1955810723 510 FCALDICLSQlqdmgtLNVCQTVRWMRTQRAFTIQTPDQYYF 551
Cdd:COG2453    97 VAAAYLVLLG------LSAEEALARVRAARPGAVETPAQRAF 132
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 454-548 1.47e-04

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: 42.26  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 454 PDYGVPTsaLTLID-FLGAVKrqqrQAVKgmgpqwrghpLGPPMVVHCSAGIGRTGTFCAldiCLsqLQDMGTLNVCQTV 532
Cdd:cd14504    58 EDYTPPT--LEQIDeFLDIVE----EANA----------KNEAVLVHCLAGKGRTGTMLA---CY--LVKTGKISAVDAI 116

                          90
                  ....*....|....*.
gi 1955810723 533 RWMRTQRAFTIQTPDQ 548
Cdd:cd14504   117 NEIRRIRPGSIETSEQ 132
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 442-553 2.83e-04

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: 42.34  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810723 442 QKQVTHFQYlSWPDYGVPTSAlTLIDFLGAVKRQQRQAVKgmgpqwrghplgppMVVHCSAGIGRTGTFCAldiC-LSQL 520
Cdd:cd14506    74 RAGIYFYNF-GWKDYGVPSLT-TILDIVKVMAFALQEGGK--------------VAVHCHAGLGRTGVLIA---CyLVYA 134

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1955810723 521 QDMgtlNVCQTVRWMRTQRAFTIQTPDQYYFCH 553
Cdd:cd14506   135 LRM---SADQAIRLVRSKRPNSIQTRGQVLCVR 164
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 495-513 9.11e-03

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


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 37.35  E-value: 9.11e-03
                          10
                  ....*....|....*....
gi 1955810723 495 PMVVHCSAGIGRTGTFCAL 513
Cdd:cd14529    91 PVLIHCKHGKDRTGLVSAL 109
 
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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