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Conserved domains on  [gi|678205613|gb|KFV72594|]
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Tyrosine-protein phosphatase non-receptor type 9, partial [Dryobates pubescens]

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 ...
 279-549 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: 584.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 279 QKRGIYEEYEEIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPYSrPELTDYINASFMDGYKQRNAYIGTQG 358
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNG-DERTDYINANFMDGYKQKNAYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 359 PLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRER 438
Cdd:cd14543   80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 439 RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD 518
Cdd:cd14543  160 RQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLED 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 678205613 519 VGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14543  240 VGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 70-220 6.26e-35

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: 128.96  E-value: 6.26e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613    70 ELLSGKFTILSVR--DPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSQYTNFEL 145
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678205613   146 DLSKKILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVKM---SELKEHLPRECLPEYLGGSLK 220
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGGTLD 158
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
1-48 1.48e-06

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 45.23  E-value: 1.48e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 678205613     1 QATKQFLEEINKWTGqYNVSPLSWNVAVKFLMARKFDVLRAIELFHSY 48
Cdd:smart01100   2 EALEELRELLEKHPD-LLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 279-549 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: 584.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 279 QKRGIYEEYEEIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPYSrPELTDYINASFMDGYKQRNAYIGTQG 358
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNG-DERTDYINANFMDGYKQKNAYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 359 PLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRER 438
Cdd:cd14543   80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 439 RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD 518
Cdd:cd14543  160 RQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLED 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 678205613 519 VGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14543  240 VGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
282-554 1.93e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 353.12  E-value: 1.93e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   282 GIYEEYEEIRR-RSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPysRPELTDYINASFMDGYKQRNAYIGTQGPL 360
Cdd:smart00194   1 GLEEEFEKLDRlKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPP--PGEGSDYINASYIDGPNGPKAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   361 ENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRL 440
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   441 VSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAvsalgprfkghpgGPPIVVHCSAGIGRTGTFCALDICLSQLQDVG 520
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTS-------------TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                          250       260       270
                   ....*....|....*....|....*....|....
gi 678205613   521 TLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:smart00194 226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
307-554 4.74e-115

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 341.14  E-value: 4.74e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613  307 NQEKNRYGDVPCLDQTRVKLAkpySRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 386
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT---GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613  387 EGGRRKCGQYWPLEKDFQVRYGALTITNLGVE-NLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFL 465
Cdd:pfam00102  78 EKGREKCAQYWPEEEGESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613  466 GAVKQQQRvavsalgprfkgHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQY 545
Cdd:pfam00102 158 RKVRKSSL------------DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQY 225


                  ....*....
gi 678205613  546 HFCYAAILE 554
Cdd:pfam00102 226 IFLYDAILE 234
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 264-552 7.52e-68

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 222.60  E-value: 7.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 264 KSVTLQELLDHVSH-KQKRGIYEEYEEIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLA-----KPY------- 330
Cdd:PHA02746   7 EIFNAFDFFDKTNHaKFCEFVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINaheslKMFdvgdsdg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 331 SRPELT------DYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGgRRKCGQYWPLEKDFQ 404
Cdd:PHA02746  87 KKIEVTsednaeNYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDD-DEKCFELWTKEEDSE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 405 VRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQR--VAVSALGPR 482
Cdd:PHA02746 166 LAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAelIKQADNDPQ 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 483 FKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAI 552
Cdd:PHA02746 246 TLG-----PIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 70-220 6.26e-35

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: 128.96  E-value: 6.26e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613    70 ELLSGKFTILSVR--DPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSQYTNFEL 145
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678205613   146 DLSKKILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVKM---SELKEHLPRECLPEYLGGSLK 220
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGGTLD 158
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
305-560 8.19e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 132.52  E-value: 8.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 305 PYNQEKNRYGDVPCLDQTRVklakpysRPELTdYINASFMDGYKQRNaYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTR 384
Cdd:COG5599   40 INGSPLNRFRDIQPYKETAL-------RANLG-YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 385 LEEGGRR--KCGQYWPLekdfQVRYGALTI--TNLGVENLnhykKTILEIHSSETR------ERRLVSHFQYLSWPDYGV 454
Cdd:COG5599  111 DDEISKPkvKMPVYFRQ----DGEYGKYEVssELTESIQL----RDGIEARTYVLTikgtgqKKIEIPVLHVKNWPDHGA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 455 PSSAAtLIDFLGAVKQQQRVavsalgprfKGHPGGPPiVVHCSAGIGRTGTFCALdICLSQLQDVG---TLNIYQTVLRM 531
Cdd:COG5599  183 ISAEA-LKNLADLIDKKEKI---------KDPDKLLP-VVHCRAGVGRTGTLIAC-LALSKSINALvqiTLSVEEIVIDM 250

                        250       260       270
                 ....*....|....*....|....*....|
gi 678205613 532 RSQRAFSI-QTPEQYHFcyaaILEHAQRQG 560
Cdd:COG5599  251 RTSRNGGMvQTSEQLDV----LVKLAEQQI 276
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 72-218 1.58e-33

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: 125.14  E-value: 1.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613  72 LSGKFTILSVRDPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAVESFETQRNGLVFIYDMAGSQYTNF-ELDLSKK 150
Cdd:cd00170    7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLsDLSLLKK 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 151 ILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVK--MSELKEHLPRECLPEYLGGS 218
Cdd:cd00170   87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
73-217 3.96e-31

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 118.13  E-value: 3.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   73 SGKFTILSvRDPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAV-ESFETQRNGLVFIYDMAGSQYTNFE---LDLS 148
Cdd:pfam00650   1 GGKVYLHG-RDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALlLMPEGQVEGLTVIIDLKGLSLSNMDwwsISLL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 678205613  149 KKILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVK---MSELKEHLPRECLPEYLGG 217
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKnsnEEELEKYIPPEQLPKEYGG 151
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
1-48 1.48e-06

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 45.23  E-value: 1.48e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 678205613     1 QATKQFLEEINKWTGqYNVSPLSWNVAVKFLMARKFDVLRAIELFHSY 48
Cdd:smart01100   2 EALEELRELLEKHPD-LLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 279-549 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: 584.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 279 QKRGIYEEYEEIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPYSrPELTDYINASFMDGYKQRNAYIGTQG 358
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNG-DERTDYINANFMDGYKQKNAYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 359 PLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRER 438
Cdd:cd14543   80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 439 RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD 518
Cdd:cd14543  160 RQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLED 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 678205613 519 VGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14543  240 VGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
282-554 1.93e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 353.12  E-value: 1.93e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   282 GIYEEYEEIRR-RSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPysRPELTDYINASFMDGYKQRNAYIGTQGPL 360
Cdd:smart00194   1 GLEEEFEKLDRlKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPP--PGEGSDYINASYIDGPNGPKAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   361 ENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRL 440
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   441 VSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAvsalgprfkghpgGPPIVVHCSAGIGRTGTFCALDICLSQLQDVG 520
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTS-------------TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                          250       260       270
                   ....*....|....*....|....*....|....
gi 678205613   521 TLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:smart00194 226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
307-554 4.74e-115

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 341.14  E-value: 4.74e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613  307 NQEKNRYGDVPCLDQTRVKLAkpySRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 386
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT---GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613  387 EGGRRKCGQYWPLEKDFQVRYGALTITNLGVE-NLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFL 465
Cdd:pfam00102  78 EKGREKCAQYWPEEEGESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613  466 GAVKQQQRvavsalgprfkgHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQY 545
Cdd:pfam00102 158 RKVRKSSL------------DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQY 225


                  ....*....
gi 678205613  546 HFCYAAILE 554
Cdd:pfam00102 226 IFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 338-549 4.38e-98

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: 296.12  E-value: 4.38e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLGV 417
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavsalgprfkghPGGPPIVVHCS 497
Cdd:cd00047   81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR-------------KPNGPIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 678205613 498 AGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd00047  148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 307-554 5.30e-84

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: 261.56  E-value: 5.30e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 307 NQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 386
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVIL-QPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 387 EGGRRKCGQYWPLekDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLG 466
Cdd:cd14553   82 ERSRVKCDQYWPT--RGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 467 AVKqqqrvavsALGPRFKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYH 546
Cdd:cd14553  160 RVK--------ACNPPDAG-----PIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYI 226


                 ....*...
gi 678205613 547 FCYAAILE 554
Cdd:cd14553  227 FIHDALLE 234
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 305-553 6.86e-79

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: 248.21  E-value: 6.86e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 305 PYNQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTR 384
Cdd:cd14554    4 PCNKFKNRLVNILPYESTRVCL-QPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 385 LEEGGRRKCGQYWPLEKdfQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDF 464
Cdd:cd14554   83 LREMGREKCHQYWPAER--SARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 465 LGAV---KQQQrvavsalgprfkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQT 541
Cdd:cd14554  161 IGQVhktKEQF------------GQEG--PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQT 226

                        250
                 ....*....|..
gi 678205613 542 PEQYHFCYAAIL 553
Cdd:cd14554  227 EDQYQFCYRAAL 238
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 312-547 7.69e-76

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: 239.56  E-value: 7.69e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 312 RYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRR 391
Cdd:cd14548    1 RYTNILPYDHSRVKL-IPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 392 KCGQYWPLEKDfQVRYGALTITNLGVENLNHYkkTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQ 471
Cdd:cd14548   80 KCDHYWPFDQD-PVYYGDITVTMLSESVLPDW--TIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 678205613 472 QrvavsalgprfkgHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHF 547
Cdd:cd14548  157 I-------------KQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 338-549 8.12e-75

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: 236.48  E-value: 8.12e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPleKDFQVRYGALTITNLGV 417
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP--KEGTETYGNIQVTLLST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHY----------KKTILEIHSSEtrerRLVSHFQYLSWPDYGVPSSAATLIDFlgaVKQqqrvaVSALGPrfkghP 487
Cdd:cd14549   79 EVLATYtvrtfslknlKLKKVKGRSSE----RVVYQYHYTQWPDHGVPDYTLPVLSF---VRK-----SSAANP-----P 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 678205613 488 GGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14549  142 GAGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 338-549 9.78e-75

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: 236.38  E-value: 9.78e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMD-GYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPlEKDFQVRYGALTITNLG 416
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVELVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 417 VENLNHYKKTILEIH-SSETRERRLVSHFQYLSWPDYGVPSSAA---TLIDFLGAVKQQqrvavsalgprfkgHPGGPPI 492
Cdd:cd18533   80 EEENDDGGFIVREFElSKEDGKVKKVYHIQYKSWPDFGVPDSPEdllTLIKLKRELNDS--------------ASLDPPI 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 678205613 493 VVHCSAGIGRTGTFCALDICLSQLQDVGTLN---------IYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd18533  146 IVHCSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 270-556 6.73e-70

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: 226.07  E-value: 6.73e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 270 ELLDHVSH-KQKRGI--YEEYEEIrrrSPAGTFVC--SLAPYNQEKNRYGDVPCLDQTRVKLAKPYSRPElTDYINASFM 344
Cdd:cd14626    2 DLADNIERlKANDGLkfSQEYESI---DPGQQFTWenSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG-SDYINANYI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 345 DGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfQVRYGALTITNLGVENLNHYK 424
Cdd:cd14626   78 DGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRG--TETYGMIQVTLLDTVELATYS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 425 KTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsALGPrfkghPGGPPIVVHCSAGIGRTG 504
Cdd:cd14626  156 VRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVK--------ACNP-----PDAGPMVVHCSAGVGRTG 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 678205613 505 TFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILEHA 556
Cdd:cd14626  223 CFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 285-554 3.98e-69

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: 223.93  E-value: 3.98e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 285 EEYEEIRRRSPA----GTFVCSLA--PYNQEKNRYGDVPCLDQTRVKLAkPYSRPELTDYINASFMDGYKQRNAYIGTQG 358
Cdd:cd14603    2 GEFSEIRACSAAfkadYVCSTVAGgrKENVKKNRYKDILPYDQTRVILS-LLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 359 PLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDfQVRYGALTITNLGVENLNhyKKTILEIHS-SETRE 437
Cdd:cd14603   81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQE-PLQTGPFTITLVKEKRLN--EEVILRTLKvTFQKE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 438 RRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavsalgprfkghPGGPPIVVHCSAGIGRTGTFCALD-----IC 512
Cdd:cd14603  158 SRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQG-------------SGPEPLCVHCSAGCGRTGVICTVDyvrqlLL 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 678205613 513 LSQLQDvgTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14603  225 TQRIPP--DFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 310-549 9.68e-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: 221.50  E-value: 9.68e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 310 KNRYGDVPCLDQTRVKLakpYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGG 389
Cdd:cd14545    1 LNRYRDRDPYDHDRSRV---KLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 390 RRKCGQYWPLE--KDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGA 467
Cdd:cd14545   78 QIKCAQYWPQGegNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 468 VKQQqrvavsalGPRFKGHpgGPPiVVHCSAGIGRTGTFCALDICLSQL--QDVGTLNIYQTVLRMRSQRAFSIQTPEQY 545
Cdd:cd14545  158 VRES--------GSLSSDV--GPP-VVHCSAGIGRSGTFCLVDTCLVLIekGNPSSVDVKKVLLEMRKYRMGLIQTPDQL 226


                 ....
gi 678205613 546 HFCY 549
Cdd:cd14545  227 RFSY 230
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 264-552 7.52e-68

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 222.60  E-value: 7.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 264 KSVTLQELLDHVSH-KQKRGIYEEYEEIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLA-----KPY------- 330
Cdd:PHA02746   7 EIFNAFDFFDKTNHaKFCEFVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINaheslKMFdvgdsdg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 331 SRPELT------DYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGgRRKCGQYWPLEKDFQ 404
Cdd:PHA02746  87 KKIEVTsednaeNYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDD-DEKCFELWTKEEDSE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 405 VRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQR--VAVSALGPR 482
Cdd:PHA02746 166 LAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAelIKQADNDPQ 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 483 FKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAI 552
Cdd:PHA02746 246 TLG-----PIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 287-557 9.11e-68

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: 220.67  E-value: 9.11e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 287 YEEIRRRspAGTFVCSLA--PYNQEKNRYGDVPCLDQTRVKLAKpysrpELTDYINASFMDGYKQRNAYIGTQGPLENTY 364
Cdd:cd14608    5 YQDIRHE--ASDFPCRVAklPKNKNRNRYRDVSPFDHSRIKLHQ-----EDNDYINASLIKMEEAQRSYILTQGPLPNTC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 365 GDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRY--GALTITNLGVENLNHYKKTILEIHSSETRERRLVS 442
Cdd:cd14608   78 GHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELENLTTQETREIL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 443 HFQYLSWPDYGVPSSAATLIDFLGAVKQQqrvavSALGPRFKghpggpPIVVHCSAGIGRTGTFCALDICL---SQLQDV 519
Cdd:cd14608  158 HFHYTTWPDFGVPESPASFLNFLFKVRES-----GSLSPEHG------PVVVHCSAGIGRSGTFCLADTCLllmDKRKDP 226

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 678205613 520 GTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILEHAQ 557
Cdd:cd14608  227 SSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAK 264
PHA02738 PHA02738
hypothetical protein; Provisional
 283-552 4.02e-67

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 220.57  E-value: 4.02e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 283 IYEEYEEIRRRSPAGTFVCSLApyNQEKNRYGDVPCLDQTRVKLAKPYSRpelTDYINASFMDGYKQRNAYIGTQGPLEN 362
Cdd:PHA02738  27 ITREHQKVISEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERNR---GDYINANYVDGFEYKKKFICGQAPTRQ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 363 TYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLGVENLNHYKKTILEIhSSETRERRLVS 442
Cdd:PHA02738 102 TCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLL-TDGTSATQTVT 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 443 HFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavSALGPRFK-GHPGG--PPIVVHCSAGIGRTGTFCALDICLSQLQDV 519
Cdd:PHA02738 181 HFNFTAWPDHDVPKNTSEFLNFVLEVRQCQK---ELAQESLQiGHNRLqpPPIVVHCNAGLGRTPCYCVVDISISRFDAC 257

                        250       260       270
                 ....*....|....*....|....*....|...
gi 678205613 520 GTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAI 552
Cdd:PHA02738 258 ATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 338-552 9.92e-67

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: 215.21  E-value: 9.92e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPleKDFQVRYGALTITNLGV 417
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYkkTILEIHSSETRER--RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavsalgprfkgHPGGPPIVVH 495
Cdd:cd14552   79 TDYEDY--TLRDFLVTKGKGGstRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQ------------QSGNHPITVH 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 678205613 496 CSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAI 552
Cdd:cd14552  145 CSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 299-555 1.76e-66

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: 217.68  E-value: 1.76e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 299 FVCSLAPYNQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLV 378
Cdd:cd14627   45 FISANLPCNKFKNRLVNIMPYETTRVCL-QPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTI 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 379 IVMTTRLEEGGRRKCGQYWPLEKdfQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSA 458
Cdd:cd14627  124 VVMLTKLREMGREKCHQYWPAER--SARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSG 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 459 ATLIDFLGAVKQQQRvavsalgpRFkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFS 538
Cdd:cd14627  202 EGFIDFIGQVHKTKE--------QF-GQDG--PISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAM 270

                        250
                 ....*....|....*..
gi 678205613 539 IQTPEQYHFCYAAILEH 555
Cdd:cd14627  271 VQTEDEYQFCYQAALEY 287
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 307-557 1.88e-66

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: 216.17  E-value: 1.88e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 307 NQEKNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFM-------DGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVI 379
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 380 VMTTRLEEGGRRKCGQYWPLEKDfQVRYGALTITNLGVENLNHYKKTILEI-HSSETRERRLVSHFQYLSWPDYGVPSSA 458
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGM-QKQYGPYRVQNVSEHDTTDYTLRELQVsKLDQGDPIREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 459 ATLIDFLGAVKQQQrvavSALgprfkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVG---TLNIYQTVLRMRSQR 535
Cdd:cd14544  160 GGVLNFLEDVNQRQ----ESL-----PHAG--PIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQR 228

                        250       260
                 ....*....|....*....|..
gi 678205613 536 AFSIQTPEQYHFCYAAILEHAQ 557
Cdd:cd14544  229 SGMVQTEAQYKFIYVAVAQYIE 250
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 259-554 2.16e-66

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: 217.27  E-value: 2.16e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 259 HVPGPKSvTLQELLDHVSHKQKRGIYEEYEEIrrrSPAGTFVC--SLAPYNQEKNRYGDVPCLDQTRVKLaKPYSRPELT 336
Cdd:cd14625    1 HPPIPIS-ELAEHTERLKANDNLKLSQEYESI---DPGQQFTWehSNLEVNKPKNRYANVIAYDHSRVIL-QPIEGIMGS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 337 DYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfQVRYGALTITNLG 416
Cdd:cd14625   76 DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRG--TETYGMIQVTLLD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 417 VENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsALGPrfkghPGGPPIVVHC 496
Cdd:cd14625  154 TIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK--------TCNP-----PDAGPIVVHC 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 678205613 497 SAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14625  221 SAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 285-557 3.59e-66

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 217.56  E-value: 3.59e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 285 EEYEEIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAkpySRPELTDYINASFMDGYKQRNAYIGTQGPLENTY 364
Cdd:PHA02742  30 EEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILK---IEDGGDDFINASYVDGHNAKGRFICTQAPLEETA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 365 GDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHF 444
Cdd:PHA02742 107 LDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHF 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 445 QYLSWPDYGVPSSAATLIDFLGAVKQQQRVAvsALGPRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNI 524
Cdd:PHA02742 187 AYEDWPHGGLPRDPNKFLDFVLAVREADLKA--DVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPL 264

                        250       260       270
                 ....*....|....*....|....*....|...
gi 678205613 525 YQTVLRMRSQRAFSIQTPEQYHFCYAAILEHAQ 557
Cdd:PHA02742 265 LSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAK 297
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 285-554 1.72e-65

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: 214.51  E-value: 1.72e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 285 EEYEEIRRRSPAGTFVC--SLAPYNQEKNRYGDVPCLDQTRVKLAK-PYSRPELTDYINASFMDGYKQRNAYIGTQGPLE 361
Cdd:cd17667    3 EDFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYNKAKAYIATQGPLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 362 NTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQvrYGALTITNLGVENLNHYKKTILEIHSSETRE---- 437
Cdd:cd17667   83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEE--YGNIIVTLKSTKIHACYTVRRFSIRNTKVKKgqkg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 438 -------RRLVSHFQYLSWPDYGVPSSAATLIDFlgaVKQQQRVAVSALGprfkghpggpPIVVHCSAGIGRTGTFCALD 510
Cdd:cd17667  161 npkgrqnERTVIQYHYTQWPDMGVPEYALPVLTF---VRRSSAARTPEMG----------PVLVHCSAGVGRTGTYIVID 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 678205613 511 ICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd17667  228 SMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 299-555 2.63e-65

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: 214.98  E-value: 2.63e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 299 FVCSLAPYNQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLV 378
Cdd:cd14628   44 FISANLPCNKFKNRLVNIMPYESTRVCL-QPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 379 IVMTTRLEEGGRRKCGQYWPLEKdfQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSA 458
Cdd:cd14628  123 VVMLTKLREMGREKCHQYWPAER--SARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSG 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 459 ATLIDFLGAVKQQQRvavsalgpRFkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFS 538
Cdd:cd14628  201 EGFIDFIGQVHKTKE--------QF-GQDG--PISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAM 269

                        250
                 ....*....|....*..
gi 678205613 539 IQTPEQYHFCYAAILEH 555
Cdd:cd14628  270 VQTEDQYQFCYRAALEY 286
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 311-554 2.20e-64

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: 210.13  E-value: 2.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 311 NRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGR 390
Cdd:cd14619    1 NRFRNVLPYDWSRVPL-KPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 391 RKCGQYWPLekDFQ-VRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVK 469
Cdd:cd14619   80 VKCEHYWPL--DYTpCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 470 QQQRVAVSalgprfkghpGGPPiVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14619  158 QWLDQTMS----------GGPT-VVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLH 226


                 ....*
gi 678205613 550 AAILE 554
Cdd:cd14619  227 QCILD 231
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 311-547 2.68e-64

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 210.06  E-value: 2.68e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 311 NRYGDVPCLDQTRVKLAKPYSRPEltDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGR 390
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTD--DYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 391 RKCGQYWPLEKdfQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQ 470
Cdd:cd14615   79 TKCEEYWPSKQ--KKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 678205613 471 QqrvavsalgprFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHF 547
Cdd:cd14615  157 Y-----------MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 311-547 3.70e-64

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: 209.18  E-value: 3.70e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 311 NRYGDVPCLDQTRVKLAKPYSRPeLTDYINASFMDGYK-QRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGg 389
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDP-LSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 390 RRKCGQYWPLEKDfqVRYGALTITNLGVENLNHYKKTILEIHSSEtrERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVK 469
Cdd:cd14547   79 KEKCAQYWPEEEN--ETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678205613 470 QQQRVAvsalgprfkghPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHF 547
Cdd:cd14547  155 EARQTE-----------PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 299-555 3.99e-64

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: 211.51  E-value: 3.99e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 299 FVCSLAPYNQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLV 378
Cdd:cd14629   45 FISANLPCNKFKNRLVNIMPYELTRVCL-QPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTI 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 379 IVMTTRLEEGGRRKCGQYWPLEKdfQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSA 458
Cdd:cd14629  124 VVMLTKLREMGREKCHQYWPAER--SARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTG 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 459 ATLIDFLGAVKQQQRvavsalgpRFkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFS 538
Cdd:cd14629  202 EGFIDFIGQVHKTKE--------QF-GQDG--PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAM 270

                        250
                 ....*....|....*..
gi 678205613 539 IQTPEQYHFCYAAILEH 555
Cdd:cd14629  271 VQTEDQYQLCYRAALEY 287
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 334-554 4.77e-63

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: 206.43  E-value: 4.77e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 334 ELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPleKDFQVRYGALTIT 413
Cdd:cd14623   22 ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWP--SDGSVSYGDITIE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 414 NLGVENLNHYkkTILEIHSSETRER--RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavsalgprfkgHPGGPP 491
Cdd:cd14623  100 LKKEEECESY--TVRDLLVTNTRENksRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ------------QSGNHP 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 678205613 492 IVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14623  166 ITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 283-547 1.95e-62

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 207.93  E-value: 1.95e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 283 IYEEYEEIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKpySRPELTDYINASFMDGYKQRNAYIGTQGPLEN 362
Cdd:PHA02747  27 IRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS--GGGSTSDYIHANWIDGFEDDKKFIATQGPFAE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 363 TYGDFWRMVWEQNVLVIVMTTRLEE-GGRRKCGQYWPLEKDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLV 441
Cdd:PHA02747 105 TCADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 442 SHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRfkgHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGT 521
Cdd:PHA02747 185 SHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPK---DALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKA 261

                        250       260
                 ....*....|....*....|....*.
gi 678205613 522 LNIYQTVLRMRSQRAFSIQTPEQYHF 547
Cdd:PHA02747 262 ICLAKTAEKIREQRHAGIMNFDDYLF 287
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 311-549 2.22e-62

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: 204.77  E-value: 2.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 311 NRYGDVPCLDQTRVKLAKPYSRPeLTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGR 390
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDP-CSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 391 RKCGQYWPLEKDfQVRYGALTITNLGVENLNHYkkTILEIH---SSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGA 467
Cdd:cd14617   80 VKCDHYWPADQD-SLYYGDLIVQMLSESVLPEW--TIREFKicsEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 468 VKQQqrvavsalgprFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHF 547
Cdd:cd14617  157 VRDY-----------INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVY 225


                 ..
gi 678205613 548 CY 549
Cdd:cd14617  226 LH 227
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 287-552 4.28e-62

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: 205.20  E-value: 4.28e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 287 YEEIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPYSrpeltDYINASFMDGYKQRNAYIGTQGPLENTYGD 366
Cdd:cd14607    4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEN-----DYINASLVVIEEAQRSYILTQGPLPNTCCH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 367 FWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPL--EKDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHF 444
Cdd:cd14607   79 FWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTdeEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 445 QYLSWPDYGVPSSAATLIDFLGAVKQQqrvavSALGPRFKghpggpPIVVHCSAGIGRTGTFCALDICLSQLQ--DVGTL 522
Cdd:cd14607  159 HYTTWPDFGVPESPASFLNFLFKVRES-----GSLSPEHG------PAVVHCSAGIGRSGTFSLVDTCLVLMEkkDPDSV 227

                        250       260       270
                 ....*....|....*....|....*....|
gi 678205613 523 NIYQTVLRMRSQRAFSIQTPEQYHFCYAAI 552
Cdd:cd14607  228 DIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 259-554 4.79e-62

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: 206.12  E-value: 4.79e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 259 HVPGPksvtLQELLDHVSHKQKRG---IYEEYEEIrrrSPAGTFVC--SLAPYNQEKNRYGDVPCLDQTRVKLAKPYSRP 333
Cdd:cd14624    1 HPPIP----ILELADHIERLKANDnlkFSQEYESI---DPGQQFTWehSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 334 ElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfQVRYGALTIT 413
Cdd:cd14624   74 G-SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRG--TETYGLIQVT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 414 NLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsALGPrfkghPGGPPIV 493
Cdd:cd14624  151 LLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK--------TCNP-----PDAGPMV 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678205613 494 VHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14624  218 VHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 307-554 8.01e-62

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: 203.72  E-value: 8.01e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 307 NQEKNRYGDVPCLDQTRVKLAKPYSRPElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 386
Cdd:cd14630    3 NRNKNRYGNIISYDHSRVRLQLLDGDPH-SDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 387 EGGRRKCGQYWPLEKDFqvrYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLG 466
Cdd:cd14630   82 EVGRVKCVRYWPDDTEV---YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 467 AVKqqqrvavsalgprFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYH 546
Cdd:cd14630  159 QVK-------------FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYV 225


                 ....*...
gi 678205613 547 FCYAAILE 554
Cdd:cd14630  226 FVHDAILE 233
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 338-553 3.35e-61

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: 200.98  E-value: 3.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfQVRYGALTITNLGV 417
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADG--SEEYGNFLVTQKSV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHY-------KKTILEIHSSETRER-RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSalgprfkghpgg 489
Cdd:cd17668   79 QVLAYYtvrnftlRNTKIKKGSQKGRPSgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG------------ 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 678205613 490 pPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAIL 553
Cdd:cd17668  147 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 307-559 3.68e-61

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: 204.01  E-value: 3.68e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 307 NQEKNRYGDVPCLDQTRVKLAKPYSRPElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 386
Cdd:cd14604   57 NVKKNRYKDILPFDHSRVKLTLKTSSQD-SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 387 EGGRRKCGQYWPLEKDFQVRYGALTITNLGVENLNHY-KKTILEIHSSETRErrlVSHFQYLSWPDYGVPSSAATLIDFL 465
Cdd:cd14604  136 EMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYfIRTLLLEFQNETRR---LYQFHYVNWPDHDVPSSFDSILDMI 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 466 GAVKQ-QQRVAVsalgprfkghpggpPIVVHCSAGIGRTGTFCALDICLSQLQdVGTL----NIYQTVLRMRSQRAFSIQ 540
Cdd:cd14604  213 SLMRKyQEHEDV--------------PICIHCSAGCGRTGAICAIDYTWNLLK-AGKIpeefNVFNLIQEMRTQRHSAVQ 277

                        250
                 ....*....|....*....
gi 678205613 541 TPEQYHFCYAAILEHAQRQ 559
Cdd:cd14604  278 TKEQYELVHRAIAQLFEKQ 296
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 338-554 3.79e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 200.68  E-value: 3.79e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFM--DGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWP--LEKDFQVrYGALTIT 413
Cdd:cd14538    1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLIC-GGRLEVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 414 NLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsalgprfKGHPGGPpIV 493
Cdd:cd14538   80 LEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR--------------RIHNSGP-IV 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678205613 494 VHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14538  145 VHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 337-553 5.60e-61

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: 200.63  E-value: 5.60e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 337 DYINASFMD----GYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDfQVRYGALTI 412
Cdd:cd14541    1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 413 TNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqQQRVAVSalgprfkghpggPPI 492
Cdd:cd14541   80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR-QNRVGMV------------EPT 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 678205613 493 VVHCSAGIGRTGTFCALD--ICLSQL-QDVGTLNIyqtVLRMRSQRAFSIQTPEQYHFCYAAIL 553
Cdd:cd14541  147 VVHCSAGIGRTGVLITMEtaMCLIEAnEPVYPLDI---VRTMRDQRAMLIQTPSQYRFVCEAIL 207
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 305-549 9.69e-60

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: 198.52  E-value: 9.69e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 305 PYNQEKNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFMDGYKQR-NAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTT 383
Cdd:cd14612   13 PGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 384 RLEEGgRRKCGQYWPlEKdfQVRYGALTITNLGVENLNHYkkTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLID 463
Cdd:cd14612   93 KLKEK-KEKCVHYWP-EK--EGTYGRFEIRVQDMKECDGY--TIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 464 FLGAVKQQQRVAvsalgprfkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPE 543
Cdd:cd14612  167 LVAEVEESRQTA---------ASPG--PIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSE 235


                 ....*.
gi 678205613 544 QYHFCY 549
Cdd:cd14612  236 QYQFLH 241
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 311-553 1.99e-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: 197.09  E-value: 1.99e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 311 NRYGDVPCLDQTRVKLAKPYSRPElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGR 390
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPH-SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 391 RKCGQYWPLEKDfQVRYGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQ 470
Cdd:cd14618   80 VLCDHYWPSEST-PVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 471 QQRVAvsalgprfkghPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYA 550
Cdd:cd14618  159 HVQAT-----------KGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                 ...
gi 678205613 551 AIL 553
Cdd:cd14618  228 CIL 230
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 305-554 2.07e-59

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: 198.18  E-value: 2.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 305 PYNQEKNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFM------DGYKQRNaYIGTQGPLENTYGDFWRMVWEQNVLV 378
Cdd:cd14606   16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 379 IVMTTRLEEGGRRKCGQYWPlEKDFQVRYGALTITNLGVENLNHYKKTILE---IHSSETreRRLVSHFQYLSWPDYGVP 455
Cdd:cd14606   95 IVMTTREVEKGRNKCVPYWP-EVGMQRAYGPYSVTNCGEHDTTEYKLRTLQvspLDNGEL--IREIWHYQYLSWPDHGVP 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 456 SSAATLIDFLGAVKQQQrvavsalgprfKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGT---LNIYQTVLRMR 532
Cdd:cd14606  172 SEPGGVLSFLDQINQRQ-----------ESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVR 240

                        250       260
                 ....*....|....*....|..
gi 678205613 533 SQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14606  241 AQRSGMVQTEAQYKFIYVAIAQ 262
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 338-545 2.70e-59

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: 195.82  E-value: 2.70e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLGV 417
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEI-HSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFlgavkqqqRVAVSALGPRFKGhpggpPIVVHC 496
Cdd:cd14557   81 KICPDYIIRKLNInNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKL--------RRRVNAFNNFFSG-----PIVVHC 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 678205613 497 SAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQY 545
Cdd:cd14557  148 SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 337-552 6.04e-59

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: 194.84  E-value: 6.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 337 DYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfQVRYGALTITNLG 416
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG--SVTHGEITIEIKN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 417 VENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavsalgprfkgHPGGPPIVVHC 496
Cdd:cd14622   79 DTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQ------------QTGNHPIVVHC 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 678205613 497 SAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAI 552
Cdd:cd14622  147 SAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 310-554 1.01e-58

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: 195.44  E-value: 1.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 310 KNRYGDVPCLDQTRVKLAKPYSrPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGG 389
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITS-DEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 390 RRKCGQYWPLEKDFQVRYGALTITNLGVENLNHYKKTILEIHSSEtrERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVK 469
Cdd:cd14602   80 KKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 470 QQQrvavsalgprfkgHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD---VGTLNIYQTVLRMRSQRAFSIQTPEQYH 546
Cdd:cd14602  158 CYQ-------------EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIQEMRTQRPSLVQTKEQYE 224


                 ....*...
gi 678205613 547 FCYAAILE 554
Cdd:cd14602  225 LVYNAVIE 232
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 338-549 3.82e-58

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: 192.64  E-value: 3.82e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLGV 417
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHyKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsalgpRFKGHpGGPPIVVHCS 497
Cdd:cd14542   81 KRVGP-DFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVR------------DYQGS-EDVPICVHCS 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 678205613 498 AGIGRTGTFCALDICLSQLQDVG---TLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14542  147 AGCGRTGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 286-553 7.72e-58

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: 194.30  E-value: 7.72e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 286 EYEEIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAkpysrpELTDYINASFMD----GYKQRNAYIGTQGPLE 361
Cdd:cd14600   19 QFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQ------GNEDYINASYVNmeipSANIVNKYIATQGPLP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 362 NTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQvRYGALTITnLGVENLN-HYKKTILEIHSSETRERRL 440
Cdd:cd14600   93 HTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVM-EYGGFRVQ-CHSEDCTiAYVFREMLLTNTQTGEERT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 441 VSHFQYLSWPDYGVPSSAATLIDFLGAVKqQQRVAvsalgprfkghpgGPPIVVHCSAGIGRTGTFCALD--ICLSQL-Q 517
Cdd:cd14600  171 VTHLQYVAWPDHGVPDDSSDFLEFVNYVR-SKRVE-------------NEPVLVHCSAGIGRTGVLVTMEtaMCLTERnQ 236

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 678205613 518 DVGTLNIyqtVLRMRSQRAFSIQTPEQYHFCYAAIL 553
Cdd:cd14600  237 PVYPLDI---VRKMRDQRAMMVQTSSQYKFVCEAIL 269
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 338-549 1.39e-57

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: 191.28  E-value: 1.39e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPleKDFQVRYGALTITNLGV 417
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP--DQGCWTYGNLRVRVEDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHY--KKTILEIHSSETRER--RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsALGPRFKGhpggpPIV 493
Cdd:cd14551   79 VVLVDYttRKFCIQKVNRGIGEKrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVK--------SANPPRAG-----PIV 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 678205613 494 VHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14551  146 VHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 307-555 2.39e-57

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: 194.09  E-value: 2.39e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 307 NQEKNRYGDVPCLDQTRVKLAKPYSRPElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 386
Cdd:cd14621   52 NKEKNRYVNILPYDHSRVHLTPVEGVPD-SDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 387 EGGRRKCGQYWPLEKDFQvrYGALTITNLGVENLNHY---KKTILEIHS-SETRERRLVSHFQYLSWPDYGVPSSAATLI 462
Cdd:cd14621  131 ERKECKCAQYWPDQGCWT--YGNIRVSVEDVTVLVDYtvrKFCIQQVGDvTNKKPQRLITQFHFTSWPDFGVPFTPIGML 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 463 DFLGAVKqqqrvavsALGPRFKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTP 542
Cdd:cd14621  209 KFLKKVK--------NCNPQYAG-----AIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTD 275

                        250
                 ....*....|...
gi 678205613 543 EQYHFCYAAILEH 555
Cdd:cd14621  276 MQYVFIYQALLEH 288
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 338-549 3.05e-57

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: 190.29  E-value: 3.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNA-YIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVRYGALTITNLG 416
Cdd:cd14539    1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 417 VENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVK---QQQRvavsalgprfkghPGGPPIV 493
Cdd:cd14539   81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshyLQQR-------------SLQTPIV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 494 VHCSAGIGRTGTFCALdicLSQLQDV----GTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14539  148 VHCSSGVGRTGAFCLL---YAAVQEIeagnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 270-554 4.11e-57

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 192.56  E-value: 4.11e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 270 ELLDHVSH---KQKRGIYEEYEEIrrrspagtFVCSLAPY-------NQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYI 339
Cdd:cd14633    1 DLLQHITQmkcAEGYGFKEEYESF--------FEGQSAPWdsakkdeNRMKNRYGNIIAYDHSRVRL-QPIEGETSSDYI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 340 NASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFqvrYGALTITNLGVEN 419
Cdd:cd14633   72 NGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI---YKDIKVTLIETEL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 420 LNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQqqrvavsalgprfKGHPGGPPIVVHCSAG 499
Cdd:cd14633  149 LAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-------------KSPPNAGPLVVHCSAG 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 678205613 500 IGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14633  216 AGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 338-556 1.05e-56

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: 189.59  E-value: 1.05e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINAS---FMDGYKQRNaYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKD--FQVRYGALTI 412
Cdd:cd14540    1 YINAShitATVGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGehDALTFGEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 413 TNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGprfkGHPGGPPI 492
Cdd:cd14540   80 STKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVA----GHNRNPPT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 678205613 493 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILEHA 556
Cdd:cd14540  156 LVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 338-554 1.17e-56

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: 188.97  E-value: 1.17e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFqvrYGALTITNLGV 417
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLVET 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsalgprFKGHPGGPPIVVHCS 497
Cdd:cd14555   78 EPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK-------------ASNPPSAGPIVVHCS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 678205613 498 AGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14555  145 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 305-553 2.78e-56

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: 189.33  E-value: 2.78e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 305 PYNQEKNRYGDVPCLDQTRVKLAKPYSRpELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTR 384
Cdd:cd14614   10 PVNRCKNRYTNILPYDFSRVKLVSMHEE-EGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 385 LEEGGRRKCGQYWPLEKDfQVRYGALTITNLGVENLNHYkkTILEIHSSETRERRLVSHFQYLSWPDYGVPS--SAATLI 462
Cdd:cd14614   89 CNEKRRVKCDHYWPFTEE-PVAYGDITVEMLSEEEQPDW--AIREFRVSYADEVQDVMHFNYTAWPDHGVPTanAAESIL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 463 DFLGAVKQQQRvavsalgpRFKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTP 542
Cdd:cd14614  166 QFVQMVRQQAV--------KSKG-----PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTE 232

                        250
                 ....*....|.
gi 678205613 543 EQYHFCYAAIL 553
Cdd:cd14614  233 EQYIFIHQCVQ 243
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 338-549 2.79e-56

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: 187.99  E-value: 2.79e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDfqvRYGALTITNLGV 417
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK---TYGDIEVELKDT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQrvavsalGPRFKGHPGGPPIVVHCS 497
Cdd:cd14558   78 EKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKL-------PYKNSKHGRSVPIVVHCS 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 678205613 498 AGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14558  151 DGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 307-552 3.34e-56

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: 189.46  E-value: 3.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 307 NQEKNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFM--------DGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLV 378
Cdd:cd14605    2 NKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 379 IVMTTRLEEGGRRKCGQYWPLEKDFQvRYGALTITNLGvENLNHyKKTILEIHSSETRE---RRLVSHFQYLSWPDYGVP 455
Cdd:cd14605   82 IVMTTKEVERGKSKCVKYWPDEYALK-EYGVMRVRNVK-ESAAH-DYILRELKLSKVGQgntERTVWQYHFRTWPDHGVP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 456 SSAATLIDFLGAVKQQQrvavsalgprfKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGT---LNIYQTVLRMR 532
Cdd:cd14605  159 SDPGGVLDFLEEVHHKQ-----------ESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVR 227

                        250       260
                 ....*....|....*....|
gi 678205613 533 SQRAFSIQTPEQYHFCYAAI 552
Cdd:cd14605  228 SQRSGMVQTEAQYRFIYMAV 247
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 313-554 5.63e-56

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: 187.84  E-value: 5.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 313 YGDVPCLDQTRVKLAKPYSRPeLTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRK 392
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIP-CSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 393 CGQYWPLEKDFQvrYGALTITNLGVENLNHY---KKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVK 469
Cdd:cd14620   80 CYQYWPDQGCWT--YGNIRVAVEDCVVLVDYtirKFCIQPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 470 qqqrvavsALGPRFKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14620  158 --------SVNPVHAG-----PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIY 224


                 ....*
gi 678205613 550 AAILE 554
Cdd:cd14620  225 QALLE 229
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 283-557 7.21e-55

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: 187.13  E-value: 7.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 283 IYEEYEEIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPYSRPelTDYINASFMD---GYKQRNaYIGTQGP 359
Cdd:cd14599   14 VFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN--TGYINASHIKvtvGGEEWH-YIATQGP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 360 LENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPL--EKDFQVRYGALTITNLGVENLNHYKKTILEIHSSETRE 437
Cdd:cd14599   91 LPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 438 RRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRFKGHpggPPIVVHCSAGIGRTGTFCALDICLSQLQ 517
Cdd:cd14599  171 ERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCN---PPIVVHCSAGVGRTGVVILTELMIGCLE 247

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 678205613 518 DVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILEHAQ 557
Cdd:cd14599  248 HNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 338-554 1.85e-54

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: 183.33  E-value: 1.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDfqvRYGALTITNLGV 417
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD---TYGDIKITLLKT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLgavkqqQRVAVSAlgprfkgHPGGPPIVVHCS 497
Cdd:cd14632   78 ETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFI------RRVKAST-------PPDAGPVVVHCS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 678205613 498 AGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14632  145 AGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 307-553 9.13e-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: 182.34  E-value: 9.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 307 NQEKNRYGDVPCLDQTRVKLAkpysrpELTDYINASF--MDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTR 384
Cdd:cd14597    3 NRKKNRYKNILPYDTTRVPLG------DEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 385 LEEGGRRKCGQYWP--LEKDFQVRyGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLI 462
Cdd:cd14597   77 EVEGGKIKCQRYWPeiLGKTTMVD-NRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 463 DFLGAVKQQqrvavsalgprfkgHPGGpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTP 542
Cdd:cd14597  156 TFISYMRHI--------------HKSG-PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTE 220

                        250
                 ....*....|.
gi 678205613 543 EQYHFCYAAIL 553
Cdd:cd14597  221 DQYIFCYQVIL 231
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 310-552 1.47e-53

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: 182.75  E-value: 1.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 310 KNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFMDGY-KQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEG 388
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 389 GRrKCGQYWPLEkdfQVRYGALTITNLGVENLNHYKKTILEIHSSEtrERRLVSHFQYLSWPDYGVPSSAATLIDFLGAV 468
Cdd:cd14613  108 NE-KCTEYWPEE---QVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEV 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 469 KQQqrvavsalgpRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFC 548
Cdd:cd14613  182 EEA----------RQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFV 251


                 ....
gi 678205613 549 YAAI 552
Cdd:cd14613  252 HHVL 255
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 328-554 1.14e-52

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: 179.06  E-value: 1.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 328 KPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFqvrY 407
Cdd:cd14631    5 QPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV---Y 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 408 GALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLgavkqqQRVAVSalgprfkGHP 487
Cdd:cd14631   82 GDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFI------RRVKLS-------NPP 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 678205613 488 GGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14631  149 SAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 311-547 4.45e-52

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: 177.41  E-value: 4.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 311 NRYGDVPCLDQTRVKLAKPYSRPElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGR 390
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPG-SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 391 RKCGQYWPLEKDFQVRYGALTITNLgVENLNHyKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVkq 470
Cdd:cd14616   80 IRCHQYWPEDNKPVTVFGDIVITKL-MEDVQI-DWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLV-- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 678205613 471 qqrvavsalgpRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHF 547
Cdd:cd14616  156 -----------RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 338-554 2.02e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 175.32  E-value: 2.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASF--MDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWP--LEKDFQVRYGALTIT 413
Cdd:cd14596    1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPetLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 414 NLGVenLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsalgprfKGHPGGPpIV 493
Cdd:cd14596   81 NYQA--LQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR--------------KVHNTGP-IV 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678205613 494 VHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14596  144 VHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 338-554 2.58e-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: 174.94  E-value: 2.58e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRN-AYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPlEKDFQVrYGALTItNLG 416
Cdd:cd14546    1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-EEGSEV-YHIYEV-HLV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 417 VENL--NHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSalgprfkghpggpPIVV 494
Cdd:cd14546   78 SEHIwcDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSC-------------PIVV 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678205613 495 HCSAGIGRTGTFCALDICLSQL-QDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14546  145 HCSDGAGRTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 338-550 9.48e-51

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: 173.42  E-value: 9.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRN--AYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRR-KCGQYWPLEKDFQVRYGALTITN 414
Cdd:cd17658    1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 415 LGVENLNH-YKKTILEIHSSETRERRL-VSHFQYLSWPDYGVPSSAATLIDFLGAVkqqqrvavsalgprFKGHPGGPPI 492
Cdd:cd17658   81 KKLKHSQHsITLRVLEVQYIESEEPPLsVLHIQYPEWPDHGVPKDTRSVRELLKRL--------------YGIPPSAGPI 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 493 VVHCSAGIGRTGTFCALDICLSQ--LQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYA 550
Cdd:cd17658  147 VVHCSAGIGRTGAYCTIHNTIRRilEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 337-554 2.32e-49

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: 169.74  E-value: 2.32e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 337 DYINASFMD----GYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPlEKDFQVRYGALTI 412
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 413 TNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQrvavsalgprfKGHPggPPI 492
Cdd:cd14601   80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKR-----------AGKD--EPV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 678205613 493 VVHCSAGIGRTGTFCALD--ICLSQL-QDVGTLNIYQTvlrMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14601  147 VVHCSAGIGRTGVLITMEtaMCLIECnQPVYPLDIVRT---MRDQRAMMIQTPSQYRFVCEAILK 208
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 268-554 3.43e-49

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: 171.78  E-value: 3.43e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 268 LQELLDHVSHKQKrgIYEEYEEI--RRRSPAGTFVcSLAPYNQEKNRYGDVPCLDQTRV--KLAKPYSRpelTDYINASF 343
Cdd:cd14610    6 LSYMEDHLKNKNR--LEKEWEALcaYQAEPNATNV-AQREENVQKNRSLAVLPYDHSRIilKAENSHSH---SDYINASP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 344 MDGYKQRN-AYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKD--FQVRYGALTITNLGVENL 420
Cdd:cd14610   80 IMDHDPRNpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSnlYHIYEVNLVSEHIWCEDF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 421 ---NHYKKTIleihssETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQqrvavsalgprFKGHpgGPPIVVHCS 497
Cdd:cd14610  160 lvrSFYLKNL------QTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKC-----------YRGR--SCPIIVHCS 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 678205613 498 AGIGRTGTFCALDICLSQL-QDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14610  221 DGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 310-549 1.16e-48

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: 168.56  E-value: 1.16e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 310 KNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFMDGYK-QRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEG 388
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 389 GRrKCGQYWPLEKDFqvrYGALTITNLGVENLNHYkkTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAV 468
Cdd:cd14611   82 NE-KCVLYWPEKRGI---YGKVEVLVNSVKECDNY--TIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 469 KQQQrvavsalgprfKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFC 548
Cdd:cd14611  156 EEDR-----------LASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                 .
gi 678205613 549 Y 549
Cdd:cd14611  225 H 225
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 301-554 2.21e-47

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: 166.75  E-value: 2.21e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 301 CSLAP--YNQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQR-NAYIGTQGPLENTYGDFWRMVWEQNVL 377
Cdd:cd14609   34 CSTAQgeANVKKNRNPDFVPYDHARIKL-KAESNPSRSDYINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWENGCT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 378 VIVMTTRLEEGGRRKCGQYWPLEKD--FQVRYGALTITNLGVENL---NHYKKTIleihssETRERRLVSHFQYLSWPDY 452
Cdd:cd14609  113 VIVMLTPLVEDGVKQCDRYWPDEGSslYHIYEVNLVSEHIWCEDFlvrSFYLKNV------QTQETRTLTQFHFLSWPAE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 453 GVPSSAATLIDFLGAVKQQqrvavsalgprFKGHpgGPPIVVHCSAGIGRTGTFCALDICLSQL-QDVGTLNIYQTVLRM 531
Cdd:cd14609  187 GIPSSTRPLLDFRRKVNKC-----------YRGR--SCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHV 253

                        250       260
                 ....*....|....*....|...
gi 678205613 532 RSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14609  254 RDQRPGMVRTKDQFEFALTAVAE 276
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 338-549 3.04e-46

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: 161.04  E-value: 3.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGrRKCGQYWPLEKdfQVRYGALTITNLGV 417
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKD-QSCPQYWPDEG--SGTYGPIQVEFVST 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEIHSS--ETRERRLVSHFQYLSWPDYG-VPSSAATLIDFLGAVKQQQRvavsalgprfkgHPGGPPIVV 494
Cdd:cd14556   78 TIDEDVISRIFRLQNTtrPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQE------------QSGEGPIVV 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 678205613 495 HCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14556  146 HCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 338-554 3.27e-45

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: 158.99  E-value: 3.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMD---GYKQRNaYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPL--EKDFQVRYGALTI 412
Cdd:cd14598    1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgSRHNTVTYGRFKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 413 TNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRfkghPGGPPI 492
Cdd:cd14598   80 TTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPK----SPNPPV 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 678205613 493 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14598  156 LVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
441-554 6.00e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 135.18  E-value: 6.00e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   441 VSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQrvavsalgprfKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD-V 519
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNL-----------NQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 678205613   520 GTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:smart00404  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 441-554 6.00e-38

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: 135.18  E-value: 6.00e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   441 VSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQrvavsalgprfKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD-V 519
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNL-----------NQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 678205613   520 GTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:smart00012  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 70-220 6.26e-35

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: 128.96  E-value: 6.26e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613    70 ELLSGKFTILSVR--DPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSQYTNFEL 145
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 678205613   146 DLSKKILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVKM---SELKEHLPRECLPEYLGGSLK 220
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGGTLD 158
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
305-560 8.19e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 132.52  E-value: 8.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 305 PYNQEKNRYGDVPCLDQTRVklakpysRPELTdYINASFMDGYKQRNaYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTR 384
Cdd:COG5599   40 INGSPLNRFRDIQPYKETAL-------RANLG-YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 385 LEEGGRR--KCGQYWPLekdfQVRYGALTI--TNLGVENLnhykKTILEIHSSETR------ERRLVSHFQYLSWPDYGV 454
Cdd:COG5599  111 DDEISKPkvKMPVYFRQ----DGEYGKYEVssELTESIQL----RDGIEARTYVLTikgtgqKKIEIPVLHVKNWPDHGA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 455 PSSAAtLIDFLGAVKQQQRVavsalgprfKGHPGGPPiVVHCSAGIGRTGTFCALdICLSQLQDVG---TLNIYQTVLRM 531
Cdd:COG5599  183 ISAEA-LKNLADLIDKKEKI---------KDPDKLLP-VVHCRAGVGRTGTLIAC-LALSKSINALvqiTLSVEEIVIDM 250

                        250       260       270
                 ....*....|....*....|....*....|
gi 678205613 532 RSQRAFSI-QTPEQYHFcyaaILEHAQRQG 560
Cdd:COG5599  251 RTSRNGGMvQTSEQLDV----LVKLAEQQI 276
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 338-554 1.42e-34

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: 129.76  E-value: 1.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGgrRKCGQYWPlEKDfQVRYGALTITNLGV 417
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA--QLCMQYWP-EKT-SCCYGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEIHSSETRER--RLVSHFQYLSWPDY-GVPSSAATLIDFLGAVKQQQRvavsalgpRFKGHPGgpPIVV 494
Cdd:cd14634   77 DIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQE--------QYDGREG--RTVV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 495 HCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14634  147 HCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 338-549 7.72e-34

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: 127.44  E-value: 7.72e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGrrKCGQYWPLEKD------FQVRYGALT 411
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKplecetFKVTLSGED 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 412 ITNLGVENLNHYKKTILEihsSETRERRL-VSHFQYLSWPDYGVPSSaaTLIDFLGAVKQ--QQRVAvsalgprfkghpg 488
Cdd:cd14550   79 HSCLSNEIRLIVRDFILE---STQDDYVLeVRQFQCPSWPNPCSPIH--TVFELINTVQEwaQQRDG------------- 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678205613 489 gpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCY 549
Cdd:cd14550  141 --PIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 72-218 1.58e-33

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: 125.14  E-value: 1.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613  72 LSGKFTILSVRDPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAVESFETQRNGLVFIYDMAGSQYTNF-ELDLSKK 150
Cdd:cd00170    7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLsDLSLLKK 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 151 ILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVK--MSELKEHLPRECLPEYLGGS 218
Cdd:cd00170   87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
73-217 3.96e-31

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 118.13  E-value: 3.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   73 SGKFTILSvRDPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAV-ESFETQRNGLVFIYDMAGSQYTNFE---LDLS 148
Cdd:pfam00650   1 GGKVYLHG-RDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALlLMPEGQVEGLTVIIDLKGLSLSNMDwwsISLL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 678205613  149 KKILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVK---MSELKEHLPRECLPEYLGG 217
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKnsnEEELEKYIPPEQLPKEYGG 151
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 338-554 6.35e-31

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: 119.36  E-value: 6.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGgrRKCGQYWPLEKdfQVRYGALTITNLGV 417
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWPEEG--MLRYGPIQVECMSC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEIhSSETRERR---LVSHFQYLSWPDY-GVPSSAATLIDFLGAVKQQQRvavsalgprfKGHPGGPPIV 493
Cdd:cd14636   77 SMDCDVISRIFRI-CNLTRPQEgylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQE----------ECDEGEGRTI 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678205613 494 VHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14636  146 IHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 338-554 2.04e-30

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: 118.25  E-value: 2.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGgrRKCGQYWPleKDFQVRYGALTITNLGV 417
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWP--ENGVHRHGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEIHSSETRER--RLVSHFQYLSWPDY-GVPSSAATLIDFLGAVKQQQRvavsalgpRFKGHPGgpPIVV 494
Cdd:cd14635   77 DLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQE--------EYNGGEG--RTVV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 495 HCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14635  147 HCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 338-554 2.72e-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: 117.70  E-value: 2.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRR-KCGQYWPlEKDFQvRYGALTITNLG 416
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQ-QYGPMEVEFVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 417 VENLNHYKKTILEIH--SSETRERRLVSHFQYLSWPDY-GVPSSAATLIDFLGAVKQQQRvavsalgprfkgHPGGPPIV 493
Cdd:cd14637   79 GSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSAYrDTPDSKKAFLHLLASVEKWQR------------ESGEGRTV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678205613 494 VHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAILE 554
Cdd:cd14637  147 VHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 339-552 1.39e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 118.53  E-value: 1.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 339 INASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEggrRKC-GQYWPLEKDFQVRYGALTITNLGV 417
Cdd:PHA02740  79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSLKEGCVITSDKFQIETLEI 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEIHSSETRERRLvSHFQYLSWPDYGVPSSAATLIDFLGAVKQ-----QQRVAVSALGPrfkghpggppI 492
Cdd:PHA02740 156 IIKPHFNLTLLSLTDKFGQAQKI-SHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadlEKHKADGKIAP----------I 224

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 493 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAI 552
Cdd:PHA02740 225 IIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 338-553 2.33e-27

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: 109.31  E-value: 2.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCgQYWPlEKDFQVRYGALTITNLGV 417
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWP-NKDEPINCETFKVTLIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 EN--LNHYKKTILE---IHSSETRERRLVSHFQYLSWPDYGVPSSAAtlIDFLGAVKQQqrvAVSALGprfkghpggpPI 492
Cdd:cd17669   79 EHkcLSNEEKLIIQdfiLEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEE---AANRDG----------PM 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678205613 493 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAIL 553
Cdd:cd17669  144 IVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 338-553 3.05e-25

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: 103.60  E-value: 3.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 338 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRlEEGGRRKCGQYWPlEKDFQVRYGALTITNLGV 417
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWP-SREESMNCEAFTVTLISK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 418 ENLNHYKKTILEIHS---SETRERRL--VSHFQYLSWPDYGVPSSAAtlIDFLGAVKQQqrvAVSALGprfkghpggpPI 492
Cdd:cd17670   79 DRLCLSNEEQIIIHDfilEATQDDYVleVRHFQCPKWPNPDAPISST--FELINVIKEE---ALTRDG----------PT 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 678205613 493 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHFCYAAIL 553
Cdd:cd17670  144 IVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 86-222 5.52e-14

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: 69.28  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613   86 GASIALFTAKLHHPSKSVQHVVLQALFYLLDRAVESFETQrnGLVFIYDMAGSQYTNFE-LDLSKKILNLLKGAFPARLK 164
Cdd:pfam13716   1 GRPVLVFISKLLPSRPASLDDLDRLLFYLLKTLSEKLKGK--PFVVVVDHTGVTSENFPsLSFLKKAYDLLPRAFKKNLK 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613  165 KVFIVGAPMWFRVPYSII-SLLLKEKLRERVQMV-KMSELKEHLPRECLPEYLGGSLKLD 222
Cdd:pfam13716  79 AVYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHYVsSLSELWEGIDREQLPTELPGVLSYD 138
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 488-549 4.81e-12

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: 62.75  E-value: 4.81e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 678205613 488 GGPPIVVHCSAGIGRTGTFCALDICLSQLqdvgtLNIYQTVLRMRSQRAFSI-QTPEQYHFCY 549
Cdd:cd14494   55 PGEPVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRPGGIpQTIEQLDFLI 112
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
429-547 2.17e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 50.35  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 429 EIHSSETRERRLVshFQYLSWPDYGVPSsAATLIDFLGAVKQQQRvavsalgprfkghpGGPPIVVHCSAGIGRTGTFCA 508
Cdd:COG2453   37 ELLLGLLEEAGLE--YLHLPIPDFGAPD-DEQLQEAVDFIDEALR--------------EGKKVLVHCRGGIGRTGTVAA 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 678205613 509 ldiCLSQLQDVGTLNIYQTVLRMRSQrafSIQTPEQYHF 547
Cdd:COG2453  100 ---AYLVLLGLSAEEALARVRAARPG---AVETPAQRAF 132
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 434-544 4.91e-07

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: 50.43  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 434 ETRERRLVSHFQYlSWPDYGVPSsAATLIDflgAVKqqqrVAVSALGPRFKghpggppIVVHCSAGIGRTGTF--CALdi 511
Cdd:cd14506   70 EAFMRAGIYFYNF-GWKDYGVPS-LTTILD---IVK----VMAFALQEGGK-------VAVHCHAGLGRTGVLiaCYL-- 131

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 678205613 512 clsqlqdVGTLNIY--QTVLRMRSQRAFSIQTPEQ 544
Cdd:cd14506  132 -------VYALRMSadQAIRLVRSKRPNSIQTRGQ 159
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 351-545 1.12e-06

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: 49.71  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 351 NAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfqvRYGALTITNLGV--------ENLNH 422
Cdd:cd14559   29 NVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSG----TYGSVTVKSKKTgkdelvdgLKADM 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 423 YKktiLEIHSSETRERRLVSHFQylSWPDYGVPSSAAT--LIDFLGAVKQQQRVAVSALGPRFKGHPGGPPIVVHCSAGI 500
Cdd:cd14559  105 YN---LKITDGNKTITIPVVHVT--NWPDHTAISSEGLkeLADLVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGV 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 678205613 501 GRTGTFCAlDICLSQLQDvgTLNIYQTVLRMRSQR-AFSIQTPEQY 545
Cdd:cd14559  180 GRTGQLAA-AMELNKSPN--NLSVEDIVSDMRTSRnGKMVQKDEQL 222
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
1-48 1.48e-06

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 45.23  E-value: 1.48e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 678205613     1 QATKQFLEEINKWTGqYNVSPLSWNVAVKFLMARKFDVLRAIELFHSY 48
Cdd:smart01100   2 EALEELRELLEKHPD-LLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 420-547 1.86e-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: 48.03  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 420 LNHYK-KTILEIhsseTRERRLVSHfqYLSWPDYGVPSSAA---TLIDFL-GAVKQQQRVavsalgprfkghpggppiVV 494
Cdd:cd14505   56 LEELGvPDLLEQ----YQQAGITWH--HLPIPDGGVPSDIAqwqELLEELlSALENGKKV------------------LI 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 678205613 495 HCSAGIGRTGTFCALdiCLSQLQDvgTLNIYQTVLRMRSQRAFSIQTPEQYHF 547
Cdd:cd14505  112 HCKGGLGRTGLIAAC--LLLELGD--TLDPEQAIAAVRALRPGAIQTPKQENF 160
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 425-509 4.52e-04

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: 40.82  E-value: 4.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 678205613 425 KTILEIHSSETRERRLV-----SHFQYLSWPdygvpsSAATLIDfLGAVKQQQRVAVSALGPRfkghpggpPIVVHCSAG 499
Cdd:cd14529   35 KTVIDLRGADERAASEEaaakiDGVKYVNLP------LSATRPT-ESDVQSFLLIMDLKLAPG--------PVLIHCKHG 99

                         90
                 ....*....|
gi 678205613 500 IGRTGTFCAL 509
Cdd:cd14529  100 KDRTGLVSAL 109
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 489-547 6.95e-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: 39.95  E-value: 6.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 678205613 489 GPPIVVHCSAGIGRTGTFCAldiCLsqLQDVGTLNIYQTVLRMRSQRAFSIQTPEQYHF 547
Cdd:cd14504   82 NEAVLVHCLAGKGRTGTMLA---CY--LVKTGKISAVDAINEIRRIRPGSIETSEQEKF 135
 
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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