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Conserved domains on  [gi|1709536963|ref|XP_029871270|]
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tyrosine-protein phosphatase non-receptor type 9 [Aquila chrysaetos chrysaetos]

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 ...
 289-560 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 1709536963 289 QKRGIYEEYEDIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPYSrPELTDYINASFMDGYKQRNAYIGTQG 368
Cdd:cd14543     1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNG-DERTDYINANFMDGYKQKNAYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 369 PLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLGVENLNHYKKTILEIHSSETRER 448
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDES 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 449 RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD 528
Cdd:cd14543   160 RQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLED 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1709536963 529 VGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYT 560
Cdd:cd14543   240 VGTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 80-230 3.32e-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: 129.73  E-value: 3.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963   80 ELLSGKFTILSVR--DPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSQYTNFEL 155
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709536963  156 DLSKKILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVKM---SELKEHLPRECLPEYLGGSLK 230
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGGTLD 158
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
10-58 3.12e-07

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 47.16  E-value: 3.12e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1709536963   10 EQATKQFLEEINKWTGqYNVSPLSWNVAVKFLMARKFDVLRAIELFHSY 58
Cdd:smart01100   1 EEALEELRELLEKHPD-LLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 289-560 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 1709536963 289 QKRGIYEEYEDIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPYSrPELTDYINASFMDGYKQRNAYIGTQG 368
Cdd:cd14543     1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNG-DERTDYINANFMDGYKQKNAYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 369 PLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLGVENLNHYKKTILEIHSSETRER 448
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDES 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 449 RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD 528
Cdd:cd14543   160 RQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLED 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1709536963 529 VGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYT 560
Cdd:cd14543   240 VGTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
292-564 4.93e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 353.12  E-value: 4.93e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  292 GIYEEYEDIRR-RSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPysRPELTDYINASFMDGYKQRNAYIGTQGPL 370
Cdd:smart00194   1 GLEEEFEKLDRlKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPP--PGEGSDYINASYIDGPNGPKAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  371 ENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLGVENLNHYKKTILEIHSSETRERRL 450
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  451 VSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAvsalgprfkghpgGPPIVVHCSAGIGRTGTFCALDICLSQLQDVG 530
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTS-------------TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1709536963  531 TLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:smart00194 226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
317-564 1.67e-114

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 340.37  E-value: 1.67e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 317 NQEKNRYGDVPCLDQTRVKLAkpySRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 396
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT---GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 397 EGGRRKCGQYWPLEKDFQVCFGALTITNLGVE-NLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFL 475
Cdd:pfam00102  78 EKGREKCAQYWPEEEGESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 476 GAVKQQQRvavsalgprfkgHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQY 555
Cdd:pfam00102 158 RKVRKSSL------------DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQY 225


                  ....*....
gi 1709536963 556 YFCYTAILE 564
Cdd:pfam00102 226 IFLYDAILE 234
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 274-562 2.50e-67

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 221.83  E-value: 2.50e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 274 KSVTLQELLDHVSH-KQKRGIYEEYEDIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLA-----KPY------- 340
Cdd:PHA02746    7 EIFNAFDFFDKTNHaKFCEFVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINaheslKMFdvgdsdg 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 341 SRPELT------DYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGgRRKCGQYWPLEKDFQ 414
Cdd:PHA02746   87 KKIEVTsednaeNYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDD-DEKCFELWTKEEDSE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 415 VCFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQR--VAVSALGPR 492
Cdd:PHA02746  166 LAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAelIKQADNDPQ 245

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 493 FKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAI 562
Cdd:PHA02746  246 TLG-----PIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 80-230 3.32e-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: 129.73  E-value: 3.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963   80 ELLSGKFTILSVR--DPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSQYTNFEL 155
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709536963  156 DLSKKILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVKM---SELKEHLPRECLPEYLGGSLK 230
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGGTLD 158
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
315-555 4.25e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 130.98  E-value: 4.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 315 PYNQEKNRYGDVPCLDQTRVklakpysRPELTdYINASFMDGYKQRNaYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTR 394
Cdd:COG5599    40 INGSPLNRFRDIQPYKETAL-------RANLG-YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 395 LEEGGRR--KCGQYWPLEKDfqvcFGALTI--TNLGVENLnhykKTILEIHSSETR------ERRLVSHFQYLSWPDYGV 464
Cdd:COG5599   111 DDEISKPkvKMPVYFRQDGE----YGKYEVssELTESIQL----RDGIEARTYVLTikgtgqKKIEIPVLHVKNWPDHGA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 465 PSSAAtLIDFLGAVKQQQRVavsalgprfKGHPGGPPiVVHCSAGIGRTGTFCALdICLSQLQDVG---TLNIYQTVLRM 541
Cdd:COG5599   183 ISAEA-LKNLADLIDKKEKI---------KDPDKLLP-VVHCRAGVGRTGTLIAC-LALSKSINALvqiTLSVEEIVIDM 250

                         250
                  ....*....|....*
gi 1709536963 542 RTQRAFSI-QTPEQY 555
Cdd:COG5599   251 RTSRNGGMvQTSEQL 265
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 82-228 7.94e-34

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: 125.91  E-value: 7.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  82 LSGKFTILSVRDPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAVESFETQRNGLVFIYDMAGSQYTNF-ELDLSKK 160
Cdd:cd00170     7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLsDLSLLKK 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 161 ILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVK--MSELKEHLPRECLPEYLGGS 228
Cdd:cd00170    87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
83-227 2.34e-31

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 118.90  E-value: 2.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  83 SGKFTILSvRDPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAV-ESFETQRNGLVFIYDMAGSQYTNFE---LDLS 158
Cdd:pfam00650   1 GGKVYLHG-RDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALlLMPEGQVEGLTVIIDLKGLSLSNMDwwsISLL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709536963 159 KKILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVK---MSELKEHLPRECLPEYLGG 227
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKnsnEEELEKYIPPEQLPKEYGG 151
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
10-58 3.12e-07

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 47.16  E-value: 3.12e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1709536963   10 EQATKQFLEEINKWTGqYNVSPLSWNVAVKFLMARKFDVLRAIELFHSY 58
Cdd:smart01100   1 EEALEELRELLEKHPD-LLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 289-560 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 1709536963 289 QKRGIYEEYEDIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPYSrPELTDYINASFMDGYKQRNAYIGTQG 368
Cdd:cd14543     1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNG-DERTDYINANFMDGYKQKNAYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 369 PLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLGVENLNHYKKTILEIHSSETRER 448
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDES 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 449 RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD 528
Cdd:cd14543   160 RQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLED 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1709536963 529 VGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYT 560
Cdd:cd14543   240 VGTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
292-564 4.93e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 353.12  E-value: 4.93e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  292 GIYEEYEDIRR-RSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPysRPELTDYINASFMDGYKQRNAYIGTQGPL 370
Cdd:smart00194   1 GLEEEFEKLDRlKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPP--PGEGSDYINASYIDGPNGPKAYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  371 ENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLGVENLNHYKKTILEIHSSETRERRL 450
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  451 VSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAvsalgprfkghpgGPPIVVHCSAGIGRTGTFCALDICLSQLQDVG 530
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTS-------------TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1709536963  531 TLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:smart00194 226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
317-564 1.67e-114

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 340.37  E-value: 1.67e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 317 NQEKNRYGDVPCLDQTRVKLAkpySRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 396
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT---GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 397 EGGRRKCGQYWPLEKDFQVCFGALTITNLGVE-NLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFL 475
Cdd:pfam00102  78 EKGREKCAQYWPEEEGESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 476 GAVKQQQRvavsalgprfkgHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQY 555
Cdd:pfam00102 158 RKVRKSSL------------DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQY 225


                  ....*....
gi 1709536963 556 YFCYTAILE 564
Cdd:pfam00102 226 IFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 348-559 4.95e-97

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: 294.19  E-value: 4.95e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLGV 427
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavsalgprfkghPGGPPIVVHCS 507
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR-------------KPNGPIVVHCS 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1709536963 508 AGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCY 559
Cdd:cd00047   148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 317-564 4.20e-83

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: 259.64  E-value: 4.20e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 317 NQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 396
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVIL-QPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 397 EGGRRKCGQYWPLEKDFQvcFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLG 476
Cdd:cd14553    82 ERSRVKCDQYWPTRGTET--YGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 477 AVKqqqrvavsALGPRFKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYY 556
Cdd:cd14553   160 RVK--------ACNPPDAG-----PIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYI 226


                  ....*...
gi 1709536963 557 FCYTAILE 564
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 ...
 315-563 1.69e-76

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: 242.82  E-value: 1.69e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 315 PYNQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTR 394
Cdd:cd14554     4 PCNKFKNRLVNILPYESTRVCL-QPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 395 LEEGGRRKCGQYWPLEKDFQvcFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDF 474
Cdd:cd14554    83 LREMGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 475 LGAV---KQQQrvavsalgprfkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQT 551
Cdd:cd14554   161 IGQVhktKEQF------------GQEG--PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQT 226

                         250
                  ....*....|..
gi 1709536963 552 PEQYYFCYTAIL 563
Cdd:cd14554   227 EDQYQFCYRAAL 238
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 322-557 2.53e-75

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: 238.79  E-value: 2.53e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 322 RYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRR 401
Cdd:cd14548     1 RYTNILPYDHSRVKL-IPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 402 KCGQYWPLEKDfQVCFGALTITNLGVENLNHYkkTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQ 481
Cdd:cd14548    80 KCDHYWPFDQD-PVYYGDITVTMLSESVLPDW--TIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709536963 482 QrvavsalgprfkgHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYF 557
Cdd:cd14548   157 I-------------KQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 348-559 9.05e-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: 236.86  E-value: 9.05e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQvcFGALTITNLGV 427
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTET--YGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHY----------KKTILEIHSSEtrerRLVSHFQYLSWPDYGVPSSAATLIDFlgaVKQqqrvaVSALGPrfkghP 497
Cdd:cd14549    79 EVLATYtvrtfslknlKLKKVKGRSSE----RVVYQYHYTQWPDHGVPDYTLPVLSF---VRK-----SSAANP-----P 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709536963 498 GGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCY 559
Cdd:cd14549   142 GAGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 348-559 2.16e-74

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: 235.99  E-value: 2.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMD-GYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPlEKDFQVCFGALTITNLG 426
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 427 VENLNHYKKTILEIH-SSETRERRLVSHFQYLSWPDYGVPSSAA---TLIDFLGAVKQQqrvavsalgprfkgHPGGPPI 502
Cdd:cd18533    80 EEENDDGGFIVREFElSKEDGKVKKVYHIQYKSWPDFGVPDSPEdllTLIKLKRELNDS--------------ASLDPPI 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709536963 503 VVHCSAGIGRTGTFCALDICLSQLQDVGTLN---------IYQTVLRMRTQRAFSIQTPEQYYFCY 559
Cdd:cd18533   146 IVHCSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 320-559 4.98e-70

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: 225.35  E-value: 4.98e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 320 KNRYGDVPCLDQTRVKLakpYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGG 399
Cdd:cd14545     1 LNRYRDRDPYDHDRSRV---KLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 400 RRKCGQYWPLEKDFQVCF--GALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGA 477
Cdd:cd14545    78 QIKCAQYWPQGEGNAMIFedTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 478 VKQQqrvavsalGPRFKGHpgGPPiVVHCSAGIGRTGTFCALDICLSQL--QDVGTLNIYQTVLRMRTQRAFSIQTPEQY 555
Cdd:cd14545   158 VRES--------GSLSSDV--GPP-VVHCSAGIGRSGTFCLVDTCLVLIekGNPSSVDVKKVLLEMRKYRMGLIQTPDQL 226


                  ....
gi 1709536963 556 YFCY 559
Cdd:cd14545   227 RFSY 230
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 280-566 6.44e-69

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: 224.14  E-value: 6.44e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 280 ELLDHVSH-KQKRGI--YEEYEDIrrrSPAGTFVC--SLAPYNQEKNRYGDVPCLDQTRVKLAKPYSRPElTDYINASFM 354
Cdd:cd14626     2 DLADNIERlKANDGLkfSQEYESI---DPGQQFTWenSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG-SDYINANYI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 355 DGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfQVCFGALTITNLGVENLNHYK 434
Cdd:cd14626    78 DGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRG--TETYGMIQVTLLDTVELATYS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 435 KTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsALGPrfkghPGGPPIVVHCSAGIGRTG 514
Cdd:cd14626   156 VRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVK--------ACNP-----PDAGPMVVHCSAGVGRTG 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1709536963 515 TFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILEHA 566
Cdd:cd14626   223 CFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 295-564 3.30e-68

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: 222.01  E-value: 3.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 295 EEYEDIRRRSPA----GTFVCSLA--PYNQEKNRYGDVPCLDQTRVKLAkPYSRPELTDYINASFMDGYKQRNAYIGTQG 368
Cdd:cd14603     2 GEFSEIRACSAAfkadYVCSTVAGgrKENVKKNRYKDILPYDQTRVILS-LLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 369 PLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDfQVCFGALTITNLGVENLNhyKKTILEIHS-SETRE 447
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQE-PLQTGPFTITLVKEKRLN--EEVILRTLKvTFQKE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 448 RRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavsalgprfkghPGGPPIVVHCSAGIGRTGTFCALD-----IC 522
Cdd:cd14603   158 SRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQG-------------SGPEPLCVHCSAGCGRTGVICTVDyvrqlLL 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1709536963 523 LSQLQDvgTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14603   225 TQRIPP--DFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 297-567 3.38e-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: 222.59  E-value: 3.38e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 297 YEDIRRRspAGTFVCSLA--PYNQEKNRYGDVPCLDQTRVKLAKpysrpELTDYINASFMDGYKQRNAYIGTQGPLENTY 374
Cdd:cd14608     5 YQDIRHE--ASDFPCRVAklPKNKNRNRYRDVSPFDHSRIKLHQ-----EDNDYINASLIKMEEAQRSYILTQGPLPNTC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 375 GDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCF--GALTITNLGVENLNHYKKTILEIHSSETRERRLVS 452
Cdd:cd14608    78 GHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELENLTTQETREIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 453 HFQYLSWPDYGVPSSAATLIDFLGAVKQQqrvavSALGPRFKghpggpPIVVHCSAGIGRTGTFCALDICL---SQLQDV 529
Cdd:cd14608   158 HFHYTTWPDFGVPESPASFLNFLFKVRES-----GSLSPEHG------PVVVHCSAGIGRSGTFCLADTCLllmDKRKDP 226

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1709536963 530 GTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILEHAQ 567
Cdd:cd14608   227 SSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAK 264
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 274-562 2.50e-67

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 221.83  E-value: 2.50e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 274 KSVTLQELLDHVSH-KQKRGIYEEYEDIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLA-----KPY------- 340
Cdd:PHA02746    7 EIFNAFDFFDKTNHaKFCEFVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINaheslKMFdvgdsdg 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 341 SRPELT------DYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGgRRKCGQYWPLEKDFQ 414
Cdd:PHA02746   87 KKIEVTsednaeNYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDD-DEKCFELWTKEEDSE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 415 VCFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQR--VAVSALGPR 492
Cdd:PHA02746  166 LAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAelIKQADNDPQ 245

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 493 FKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAI 562
Cdd:PHA02746  246 TLG-----PIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02738 PHA02738
hypothetical protein; Provisional
 293-562 1.06e-66

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 219.80  E-value: 1.06e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 293 IYEEYEDIRRRSPAGTFVCSLApyNQEKNRYGDVPCLDQTRVKLAKPYSRpelTDYINASFMDGYKQRNAYIGTQGPLEN 372
Cdd:PHA02738   27 ITREHQKVISEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERNR---GDYINANYVDGFEYKKKFICGQAPTRQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 373 TYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLGVENLNHYKKTILEIhSSETRERRLVS 452
Cdd:PHA02738  102 TCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLL-TDGTSATQTVT 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 453 HFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavSALGPRFK-GHPGG--PPIVVHCSAGIGRTGTFCALDICLSQLQDV 529
Cdd:PHA02738  181 HFNFTAWPDHDVPKNTSEFLNFVLEVRQCQK---ELAQESLQiGHNRLqpPPIVVHCNAGLGRTPCYCVVDISISRFDAC 257

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1709536963 530 GTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAI 562
Cdd:PHA02738  258 ATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 348-562 9.44e-66

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: 213.28  E-value: 9.44e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPleKDFQVCFGALTITNLGV 427
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYkkTILEIHSSETRER--RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavsalgprfkgHPGGPPIVVH 505
Cdd:cd14552    79 TDYEDY--TLRDFLVTKGKGGstRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQ------------QSGNHPITVH 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1709536963 506 CSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAI 562
Cdd:cd14552   145 CSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 295-567 2.12e-65

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 216.02  E-value: 2.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 295 EEYEDIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAkpySRPELTDYINASFMDGYKQRNAYIGTQGPLENTY 374
Cdd:PHA02742   30 EEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILK---IEDGGDDFINASYVDGHNAKGRFICTQAPLEETA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 375 GDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHF 454
Cdd:PHA02742  107 LDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHF 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 455 QYLSWPDYGVPSSAATLIDFLGAVKQQQRVAvsALGPRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNI 534
Cdd:PHA02742  187 AYEDWPHGGLPRDPNKFLDFVLAVREADLKA--DVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPL 264

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1709536963 535 YQTVLRMRTQRAFSIQTPEQYYFCYTAILEHAQ 567
Cdd:PHA02742  265 LSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAK 297
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 317-567 2.14e-65

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: 214.25  E-value: 2.14e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 317 NQEKNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFM-------DGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVI 389
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 390 VMTTRLEEGGRRKCGQYWPLEKDfQVCFGALTITNLGVENLNHYKKTILEI-HSSETRERRLVSHFQYLSWPDYGVPSSA 468
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGM-QKQYGPYRVQNVSEHDTTDYTLRELQVsKLDQGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 469 ATLIDFLGAVKQQQrvavSALgprfkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVG---TLNIYQTVLRMRTQR 545
Cdd:cd14544   160 GGVLNFLEDVNQRQ----ESL-----PHAG--PIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQR 228

                         250       260
                  ....*....|....*....|..
gi 1709536963 546 AFSIQTPEQYYFCYTAILEHAQ 567
Cdd:cd14544   229 SGMVQTEAQYKFIYVAVAQYIE 250
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 321-564 2.22e-65

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: 213.60  E-value: 2.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 321 NRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGR 400
Cdd:cd14619     1 NRFRNVLPYDWSRVPL-KPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 401 RKCGQYWPLekDFQVC-FGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVK 479
Cdd:cd14619    80 VKCEHYWPL--DYTPCtYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 480 QQQRVAVSalgprfkghpGGPPiVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCY 559
Cdd:cd14619   158 QWLDQTMS----------GGPT-VVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLH 226


                  ....*
gi 1709536963 560 TAILE 564
Cdd:cd14619   227 QCILD 231
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 269-564 4.26e-65

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: 214.57  E-value: 4.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 269 HVPGPKSvTLQELLDHVSHKQKRGIYEEYEDIrrrSPAGTFVC--SLAPYNQEKNRYGDVPCLDQTRVKLaKPYSRPELT 346
Cdd:cd14625     1 HPPIPIS-ELAEHTERLKANDNLKLSQEYESI---DPGQQFTWehSNLEVNKPKNRYANVIAYDHSRVIL-QPIEGIMGS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 347 DYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfQVCFGALTITNLG 426
Cdd:cd14625    76 DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRG--TETYGMIQVTLLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 427 VENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsALGPrfkghPGGPPIVVHC 506
Cdd:cd14625   154 TIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK--------TCNP-----PDAGPIVVHC 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1709536963 507 SAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14625   221 SAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 295-564 5.88e-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: 213.74  E-value: 5.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 295 EEYEDIRRRSPAGTFVC--SLAPYNQEKNRYGDVPCLDQTRVKLAK-PYSRPELTDYINASFMDGYKQRNAYIGTQGPLE 371
Cdd:cd17667     3 EDFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYNKAKAYIATQGPLK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 372 NTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQvcFGALTITNLGVENLNHYKKTILEIHSSETRE---- 447
Cdd:cd17667    83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEE--YGNIIVTLKSTKIHACYTVRRFSIRNTKVKKgqkg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 448 -------RRLVSHFQYLSWPDYGVPSSAATLIDFlgaVKQQQRVAVSALGprfkghpggpPIVVHCSAGIGRTGTFCALD 520
Cdd:cd17667   161 npkgrqnERTVIQYHYTQWPDMGVPEYALPVLTF---VRRSSAARTPEMG----------PVLVHCSAGVGRTGTYIVID 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1709536963 521 ICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd17667   228 SMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 309-565 7.55e-65

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 214.21  E-value: 7.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 309 FVCSLAPYNQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLV 388
Cdd:cd14627    45 FISANLPCNKFKNRLVNIMPYETTRVCL-QPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 389 IVMTTRLEEGGRRKCGQYWPLEKDFQvcFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSA 468
Cdd:cd14627   124 VVMLTKLREMGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSG 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 469 ATLIDFLGAVKQQQRvavsalgpRFkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFS 548
Cdd:cd14627   202 EGFIDFIGQVHKTKE--------QF-GQDG--PISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAM 270

                         250
                  ....*....|....*..
gi 1709536963 549 IQTPEQYYFCYTAILEH 565
Cdd:cd14627   271 VQTEDEYQFCYQAALEY 287
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 321-557 2.51e-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: 210.44  E-value: 2.51e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 321 NRYGDVPCLDQTRVKLAKPYSRPEltDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGR 400
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTD--DYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 401 RKCGQYWPLEKdfQVCFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQ 480
Cdd:cd14615    79 TKCEEYWPSKQ--KKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709536963 481 QqrvavsalgprFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYF 557
Cdd:cd14615   157 Y-----------MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 309-565 7.33e-64

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 211.51  E-value: 7.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 309 FVCSLAPYNQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLV 388
Cdd:cd14628    44 FISANLPCNKFKNRLVNIMPYESTRVCL-QPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 389 IVMTTRLEEGGRRKCGQYWPLEKDFQvcFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSA 468
Cdd:cd14628   123 VVMLTKLREMGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSG 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 469 ATLIDFLGAVKQQQRvavsalgpRFkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFS 548
Cdd:cd14628   201 EGFIDFIGQVHKTKE--------QF-GQDG--PISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAM 269

                         250
                  ....*....|....*..
gi 1709536963 549 IQTPEQYYFCYTAILEH 565
Cdd:cd14628   270 VQTEDQYQFCYRAALEY 286
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 321-559 5.90e-63

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: 207.08  E-value: 5.90e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 321 NRYGDVPCLDQTRVKLAKPYSRPeLTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGR 400
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDP-CSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 401 RKCGQYWPLEKDfQVCFGALTITNLGVENLNHYkkTILEIH---SSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGA 477
Cdd:cd14617    80 VKCDHYWPADQD-SLYYGDLIVQMLSESVLPEW--TIREFKicsEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 478 VKQQqrvavsalgprFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYF 557
Cdd:cd14617   157 VRDY-----------INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVY 225


                  ..
gi 1709536963 558 CY 559
Cdd:cd14617   226 LH 227
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 321-557 8.28e-63

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 206.48  E-value: 8.28e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 321 NRYGDVPCLDQTRVKLAKPYSRPeLTDYINASFMDGYK-QRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGg 399
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDP-LSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 400 RRKCGQYWPLEKDFQvcFGALTITNLGVENLNHYKKTILEIHSSEtrERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVK 479
Cdd:cd14547    79 KEKCAQYWPEEENET--YGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709536963 480 QQQRVAvsalgprfkghPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYF 557
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 ...
 309-565 1.54e-62

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 208.04  E-value: 1.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 309 FVCSLAPYNQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLV 388
Cdd:cd14629    45 FISANLPCNKFKNRLVNIMPYELTRVCL-QPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 389 IVMTTRLEEGGRRKCGQYWPLEKDFQvcFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSA 468
Cdd:cd14629   124 VVMLTKLREMGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTG 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 469 ATLIDFLGAVKQQQRvavsalgpRFkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFS 548
Cdd:cd14629   202 EGFIDFIGQVHKTKE--------QF-GQDG--PITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAM 270

                         250
                  ....*....|....*..
gi 1709536963 549 IQTPEQYYFCYTAILEH 565
Cdd:cd14629   271 VQTEDQYQLCYRAALEY 287
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 344-564 3.49e-62

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: 204.89  E-value: 3.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 344 ELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPleKDFQVCFGALTIT 423
Cdd:cd14623    22 ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWP--SDGSVSYGDITIE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 424 NLGVENLNHYkkTILEIHSSETRER--RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavsalgprfkgHPGGPP 501
Cdd:cd14623   100 LKKEEECESY--TVRDLLVTNTRENksRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ------------QSGNHP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709536963 502 IVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14623   166 ITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 293-557 4.84e-62

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 207.55  E-value: 4.84e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 293 IYEEYEDIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKpySRPELTDYINASFMDGYKQRNAYIGTQGPLEN 372
Cdd:PHA02747   27 IRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS--GGGSTSDYIHANWIDGFEDDKKFIATQGPFAE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 373 TYGDFWRMVWEQNVLVIVMTTRLEE-GGRRKCGQYWPLEKDFQVCFGALTITNLGVENLNHYKKTILEIHSSETRERRLV 451
Cdd:PHA02747  105 TCADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 452 SHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRfkgHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGT 531
Cdd:PHA02747  185 SHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPK---DALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKA 261

                         250       260
                  ....*....|....*....|....*.
gi 1709536963 532 LNIYQTVLRMRTQRAFSIQTPEQYYF 557
Cdd:PHA02747  262 ICLAKTAEKIREQRHAGIMNFDDYLF 287
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 297-562 1.30e-61

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: 204.43  E-value: 1.30e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 297 YEDIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPYSrpeltDYINASFMDGYKQRNAYIGTQGPLENTYGD 376
Cdd:cd14607     4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEN-----DYINASLVVIEEAQRSYILTQGPLPNTCCH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 377 FWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFG--ALTITNLGVENLNHYKKTILEIHSSETRERRLVSHF 454
Cdd:cd14607    79 FWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKetGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 455 QYLSWPDYGVPSSAATLIDFLGAVKQQqrvavSALGPRFKghpggpPIVVHCSAGIGRTGTFCALDICLSQLQ--DVGTL 532
Cdd:cd14607   159 HYTTWPDFGVPESPASFLNFLFKVRES-----GSLSPEHG------PAVVHCSAGIGRSGTFSLVDTCLVLMEkkDPDSV 227

                         250       260       270
                  ....*....|....*....|....*....|
gi 1709536963 533 NIYQTVLRMRTQRAFSIQTPEQYYFCYTAI 562
Cdd:cd14607   228 DIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 348-564 1.67e-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: 202.22  E-value: 1.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFM--DGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLE-KDFQVCFGALTITN 424
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSlNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 425 LGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsalgprfKGHPGGPpIVV 504
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR--------------RIHNSGP-IVV 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 505 HCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14538   146 HCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 269-564 1.74e-61

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 204.97  E-value: 1.74e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 269 HVPGPksvtLQELLDHVSHKQKRG---IYEEYEDIrrrSPAGTFVC--SLAPYNQEKNRYGDVPCLDQTRVKLAKPYSRP 343
Cdd:cd14624     1 HPPIP----ILELADHIERLKANDnlkFSQEYESI---DPGQQFTWehSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 344 ElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfQVCFGALTIT 423
Cdd:cd14624    74 G-SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRG--TETYGLIQVT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 424 NLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsALGPrfkghPGGPPIV 503
Cdd:cd14624   151 LLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK--------TCNP-----PDAGPMV 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709536963 504 VHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14624   218 VHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 317-564 3.89e-61

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: 202.56  E-value: 3.89e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 317 NQEKNRYGDVPCLDQTRVKLAKPYSRPElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 396
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPH-SDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 397 EGGRRKCGQYWPLEKDfqvCFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLG 476
Cdd:cd14630    82 EVGRVKCVRYWPDDTE---VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 477 AVKqqqrvavsalgprFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYY 556
Cdd:cd14630   159 QVK-------------FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYV 225


                  ....*...
gi 1709536963 557 FCYTAILE 564
Cdd:cd14630   226 FVHDAILE 233
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 317-569 5.45e-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: 5.45e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 317 NQEKNRYGDVPCLDQTRVKLAKPYSRPElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 396
Cdd:cd14604    57 NVKKNRYKDILPFDHSRVKLTLKTSSQD-SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 397 EGGRRKCGQYWPLEKDFQVCFGALTITNLGVENLNHY-KKTILEIHSSETRErrlVSHFQYLSWPDYGVPSSAATLIDFL 475
Cdd:cd14604   136 EMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYfIRTLLLEFQNETRR---LYQFHYVNWPDHDVPSSFDSILDMI 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 476 GAVKQ-QQRVAVsalgprfkghpggpPIVVHCSAGIGRTGTFCALDICLSQLQdVGTL----NIYQTVLRMRTQRAFSIQ 550
Cdd:cd14604   213 SLMRKyQEHEDV--------------PICIHCSAGCGRTGAICAIDYTWNLLK-AGKIpeefNVFNLIQEMRTQRHSAVQ 277

                         250
                  ....*....|....*....
gi 1709536963 551 TPEQYYFCYTAILEHAQRE 569
Cdd:cd14604   278 TKEQYELVHRAIAQLFEKQ 296
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 348-563 7.59e-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: 200.59  E-value: 7.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQvcFGALTITNLGV 427
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE--YGNFLVTQKSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHY-------KKTILEIHSSETRER-RLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSalgprfkghpgg 499
Cdd:cd17668    79 QVLAYYtvrnftlRNTKIKKGSQKGRPSgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG------------ 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709536963 500 pPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAIL 563
Cdd:cd17668   147 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 347-563 1.66e-60

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: 199.86  E-value: 1.66e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 347 DYINASFMD----GYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDfQVCFGALTI 422
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 423 TNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqQQRVAVSalgprfkghpggPPI 502
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR-QNRVGMV------------EPT 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709536963 503 VVHCSAGIGRTGTFCALD--ICLSQL-QDVGTLNIyqtVLRMRTQRAFSIQTPEQYYFCYTAIL 563
Cdd:cd14541   147 VVHCSAGIGRTGVLITMEtaMCLIEAnEPVYPLDI---VRTMRDQRAMLIQTPSQYRFVCEAIL 207
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 348-560 1.65e-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: 196.97  E-value: 1.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLGV 427
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEI-HSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFlgavkqqqRVAVSALGPRFKGhpggpPIVVHC 506
Cdd:cd14557    81 KICPDYIIRKLNInNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKL--------RRRVNAFNNFFSG-----PIVVHC 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1709536963 507 SAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYT 560
Cdd:cd14557   148 SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 348-559 2.34e-59

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: 196.49  E-value: 2.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLGV 427
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHyKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsalgpRFKGHpGGPPIVVHCS 507
Cdd:cd14542    81 KRVGP-DFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVR------------DYQGS-EDVPICVHCS 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709536963 508 AGIGRTGTFCALDICLSQLQDVG---TLNIYQTVLRMRTQRAFSIQTPEQYYFCY 559
Cdd:cd14542   147 AGCGRTGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 315-559 2.39e-59

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: 198.14  E-value: 2.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 315 PYNQEKNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFMDGYKQR-NAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTT 393
Cdd:cd14612    13 PGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 394 RLEEGgRRKCGQYWPlEKdfQVCFGALTITNLGVENLNHYkkTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLID 473
Cdd:cd14612    93 KLKEK-KEKCVHYWP-EK--EGTYGRFEIRVQDMKECDGY--TIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 474 FLGAVKQQQRVAvsalgprfkGHPGgpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPE 553
Cdd:cd14612   167 LVAEVEESRQTA---------ASPG--PIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSE 235


                  ....*.
gi 1709536963 554 QYYFCY 559
Cdd:cd14612   236 QYQFLH 241
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 347-562 3.38e-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: 196.38  E-value: 3.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 347 DYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfQVCFGALTITNLG 426
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG--SVTHGEITIEIKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 427 VENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRvavsalgprfkgHPGGPPIVVHC 506
Cdd:cd14622    79 DTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQ------------QTGNHPIVVHC 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1709536963 507 SAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAI 562
Cdd:cd14622   147 SAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 321-563 3.60e-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: 3.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 321 NRYGDVPCLDQTRVKLAKPYSRPElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGR 400
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPH-SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 401 RKCGQYWPLEKDfQVCFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQ 480
Cdd:cd14618    80 VLCDHYWPSEST-PVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 481 QQRVAvsalgprfkghPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYT 560
Cdd:cd14618   159 HVQAT-----------KGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                  ...
gi 1709536963 561 AIL 563
Cdd:cd14618   228 CIL 230
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 320-564 4.56e-59

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: 196.98  E-value: 4.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 320 KNRYGDVPCLDQTRVKLAKPYSrPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGG 399
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITS-DEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 400 RRKCGQYWPLEKDFQVCFGALTITNLGVENLNHYKKTILEIHSSEtrERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVK 479
Cdd:cd14602    80 KKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 480 QQQrvavsalgprfkgHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD---VGTLNIYQTVLRMRTQRAFSIQTPEQYY 556
Cdd:cd14602   158 CYQ-------------EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIQEMRTQRPSLVQTKEQYE 224


                  ....*...
gi 1709536963 557 FCYTAILE 564
Cdd:cd14602   225 LVYNAVIE 232
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 315-564 8.25e-58

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: 194.71  E-value: 8.25e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 315 PYNQEKNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFM------DGYKQRNaYIGTQGPLENTYGDFWRMVWEQNVLV 388
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 389 IVMTTRLEEGGRRKCGQYWPlEKDFQVCFGALTITNLGVENLNHYKKTILE---IHSSETreRRLVSHFQYLSWPDYGVP 465
Cdd:cd14606    95 IVMTTREVEKGRNKCVPYWP-EVGMQRAYGPYSVTNCGEHDTTEYKLRTLQvspLDNGEL--IREIWHYQYLSWPDHGVP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 466 SSAATLIDFLGAVKQQQrvavsalgprfKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGT---LNIYQTVLRMR 542
Cdd:cd14606   172 SEPGGVLSFLDQINQRQ-----------ESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVR 240

                         250       260
                  ....*....|....*....|..
gi 1709536963 543 TQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14606   241 AQRSGMVQTEAQYKFIYVAIAQ 262
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 348-559 6.78e-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: 190.12  E-value: 6.78e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLE-----KDFQVCFGALTI 422
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQgcwtyGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 423 TnlgvenLNHYKKTIL---EIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsALGPRFKGhpgg 499
Cdd:cd14551    81 L------VDYTTRKFCiqkVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVK--------SANPPRAG---- 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 500 pPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCY 559
Cdd:cd14551   143 -PIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 317-565 9.36e-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: 192.93  E-value: 9.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 317 NQEKNRYGDVPCLDQTRVKLAKPYSRPElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLE 396
Cdd:cd14621    52 NKEKNRYVNILPYDHSRVHLTPVEGVPD-SDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLK 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 397 EGGRRKCGQYWPlekdFQVC--FGALTITNLGVENLNHY---KKTILEIHS-SETRERRLVSHFQYLSWPDYGVPSSAAT 470
Cdd:cd14621   131 ERKECKCAQYWP----DQGCwtYGNIRVSVEDVTVLVDYtvrKFCIQQVGDvTNKKPQRLITQFHFTSWPDFGVPFTPIG 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 471 LIDFLGAVKqqqrvavsALGPRFKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQ 550
Cdd:cd14621   207 MLKFLKKVK--------NCNPQYAG-----AIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQ 273

                         250
                  ....*....|....*
gi 1709536963 551 TPEQYYFCYTAILEH 565
Cdd:cd14621   274 TDMQYVFIYQALLEH 288
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 296-563 2.87e-56

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: 190.83  E-value: 2.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 296 EYEDIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAkpysrpELTDYINASFMD----GYKQRNAYIGTQGPLE 371
Cdd:cd14600    19 QFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQ------GNEDYINASYVNmeipSANIVNKYIATQGPLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 372 NTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDfqVC-FGALTITnLGVENLN-HYKKTILEIHSSETRERR 449
Cdd:cd14600    93 HTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPD--VMeYGGFRVQ-CHSEDCTiAYVFREMLLTNTQTGEER 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 450 LVSHFQYLSWPDYGVPSSAATLIDFLGAVKqQQRVAvsalgprfkghpgGPPIVVHCSAGIGRTGTFCALD--ICLSQL- 526
Cdd:cd14600   170 TVTHLQYVAWPDHGVPDDSSDFLEFVNYVR-SKRVE-------------NEPVLVHCSAGIGRTGVLVTMEtaMCLTERn 235

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1709536963 527 QDVGTLNIyqtVLRMRTQRAFSIQTPEQYYFCYTAIL 563
Cdd:cd14600   236 QPVYPLDI---VRKMRDQRAMMVQTSSQYKFVCEAIL 269
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 315-563 2.92e-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: 189.71  E-value: 2.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 315 PYNQEKNRYGDVPCLDQTRVKLAKPYSRpELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTR 394
Cdd:cd14614    10 PVNRCKNRYTNILPYDFSRVKLVSMHEE-EGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 395 LEEGGRRKCGQYWPLEKDfQVCFGALTITNLGVENLNHYkkTILEIHSSETRERRLVSHFQYLSWPDYGVPS--SAATLI 472
Cdd:cd14614    89 CNEKRRVKCDHYWPFTEE-PVAYGDITVEMLSEEEQPDW--AIREFRVSYADEVQDVMHFNYTAWPDHGVPTanAAESIL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 473 DFLGAVKQQQRvavsalgpRFKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTP 552
Cdd:cd14614   166 QFVQMVRQQAV--------KSKG-----PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTE 232

                         250
                  ....*....|.
gi 1709536963 553 EQYYFCYTAIL 563
Cdd:cd14614   233 EQYIFIHQCVQ 243
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 280-564 3.13e-56

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: 190.64  E-value: 3.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 280 ELLDHVSH---KQKRGIYEEYEDIrrrspagtFVCSLAPY-------NQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYI 349
Cdd:cd14633     1 DLLQHITQmkcAEGYGFKEEYESF--------FEGQSAPWdsakkdeNRMKNRYGNIIAYDHSRVRL-QPIEGETSSDYI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 350 NASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFqvcFGALTITNLGVEN 429
Cdd:cd14633    72 NGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI---YKDIKVTLIETEL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 430 LNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQqqrvavsalgprfKGHPGGPPIVVHCSAG 509
Cdd:cd14633   149 LAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-------------KSPPNAGPLVVHCSAG 215

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709536963 510 IGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14633   216 AGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 348-566 5.53e-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: 188.05  E-value: 5.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINAS---FMDGYKQRNaYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKD--FQVCFGALTI 422
Cdd:cd14540     1 YINAShitATVGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGehDALTFGEYKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 423 TNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGprfkGHPGGPPI 502
Cdd:cd14540    80 STKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVA----GHNRNPPT 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709536963 503 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILEHA 566
Cdd:cd14540   156 LVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 348-559 5.72e-56

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: 187.59  E-value: 5.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNA-YIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFQVCFGALTITNLG 426
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 427 VENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVK---QQQRvavsalgprfkghPGGPPIV 503
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshyLQQR-------------SLQTPIV 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 504 VHCSAGIGRTGTFCALdicLSQLQDV----GTLNIYQTVLRMRTQRAFSIQTPEQYYFCY 559
Cdd:cd14539   148 VHCSSGVGRTGAFCLL---YAAVQEIeagnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 348-564 1.12e-55

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: 186.66  E-value: 1.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDfqvCFGALTITNLGV 427
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE---VYGDIKVTLVET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsalgprFKGHPGGPPIVVHCS 507
Cdd:cd14555    78 EPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK-------------ASNPPSAGPIVVHCS 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1709536963 508 AGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14555   145 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 323-564 1.59e-55

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: 187.46  E-value: 1.59e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 323 YGDVPCLDQTRVKLAKPYSRPeLTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRK 402
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIP-CSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 403 CGQYWPlekdFQVC--FGALTITNLGVENLNHY---KKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGA 477
Cdd:cd14620    80 CYQYWP----DQGCwtYGNIRVAVEDCVVLVDYtirKFCIQPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 478 VKqqqrvavsALGPRFKGhpggpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYF 557
Cdd:cd14620   156 VK--------SVNPVHAG-----PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSF 222


                  ....*..
gi 1709536963 558 CYTAILE 564
Cdd:cd14620   223 IYQALLE 229
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 348-560 2.26e-55

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: 186.06  E-value: 2.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDfqvCFGALTITNLGV 427
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK---TYGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQrvavsalGPRFKGHPGGPPIVVHCS 507
Cdd:cd14558    78 EKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKL-------PYKNSKHGRSVPIVVHCS 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1709536963 508 AGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYT 560
Cdd:cd14558   151 DGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 317-562 3.08e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 184.84  E-value: 3.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 317 NQEKNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFM--------DGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLV 388
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 389 IVMTTRLEEGGRRKCGQYWPLEKDFQVcFGALTITNLGvENLNHyKKTILEIHSSETRE---RRLVSHFQYLSWPDYGVP 465
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPDEYALKE-YGVMRVRNVK-ESAAH-DYILRELKLSKVGQgntERTVWQYHFRTWPDHGVP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 466 SSAATLIDFLGAVKQQQrvavsalgprfKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGT---LNIYQTVLRMR 542
Cdd:cd14605   159 SDPGGVLDFLEEVHHKQ-----------ESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVR 227

                         250       260
                  ....*....|....*....|
gi 1709536963 543 TQRAFSIQTPEQYYFCYTAI 562
Cdd:cd14605   228 SQRSGMVQTEAQYRFIYMAV 247
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 317-563 8.71e-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: 182.72  E-value: 8.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 317 NQEKNRYGDVPCLDQTRVKLAkpysrpELTDYINASF--MDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTR 394
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPLG------DEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 395 LEEGGRRKCGQYWPLE-KDFQVCFGALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLID 473
Cdd:cd14597    77 EVEGGKIKCQRYWPEIlGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 474 FLGAVKQQqrvavsalgprfkgHPGGpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPE 553
Cdd:cd14597   157 FISYMRHI--------------HKSG-PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221

                         250
                  ....*....|
gi 1709536963 554 QYYFCYTAIL 563
Cdd:cd14597   222 QYIFCYQVIL 231
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 348-564 1.36e-53

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: 181.40  E-value: 1.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDfqvCFGALTITNLGV 427
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD---TYGDIKITLLKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLgavkqqQRVAVSAlgprfkgHPGGPPIVVHCS 507
Cdd:cd14632    78 ETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFI------RRVKAST-------PPDAGPVVVHCS 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1709536963 508 AGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14632   145 AGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 293-567 1.99e-53

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: 183.66  E-value: 1.99e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 293 IYEEYEDIRRRSPAGTFVCSLAPYNQEKNRYGDVPCLDQTRVKLAKPYSRPelTDYINASFMD---GYKQRNaYIGTQGP 369
Cdd:cd14599    14 VFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN--TGYINASHIKvtvGGEEWH-YIATQGP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 370 LENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPL--EKDFQVCFGALTITNLGVENLNHYKKTILEIHSSETRE 447
Cdd:cd14599    91 LPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 448 RRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRFKGHpggPPIVVHCSAGIGRTGTFCALDICLSQLQ 527
Cdd:cd14599   171 ERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCN---PPIVVHCSAGVGRTGVVILTELMIGCLE 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1709536963 528 DVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILEHAQ 567
Cdd:cd14599   248 HNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 320-562 1.31e-52

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: 180.44  E-value: 1.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 320 KNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFMDGY-KQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEG 398
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 399 GRrKCGQYWPLEkdfQVCFGALTITNLGVENLNHYKKTILEIHSSEtrERRLVSHFQYLSWPDYGVPSSAATLIDFLGAV 478
Cdd:cd14613   108 NE-KCTEYWPEE---QVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 479 KQQqrvavsalgpRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFC 558
Cdd:cd14613   182 EEA----------RQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFV 251


                  ....
gi 1709536963 559 YTAI 562
Cdd:cd14613   252 HHVL 255
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 321-557 2.36e-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: 178.56  E-value: 2.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 321 NRYGDVPCLDQTRVKLAKPYSRPElTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGR 400
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPG-SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 401 RKCGQYWPLEKDFQVCFGALTITNLgVENLNHyKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVkq 480
Cdd:cd14616    80 IRCHQYWPEDNKPVTVFGDIVITKL-MEDVQI-DWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLV-- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709536963 481 qqrvavsalgpRFKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYF 557
Cdd:cd14616   156 -----------RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 338-564 6.73e-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: 177.13  E-value: 6.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 338 KPYSRPELTDYINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKDFqvcF 417
Cdd:cd14631     5 QPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV---Y 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 418 GALTITNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLgavkqqQRVAVSalgprfkGHP 497
Cdd:cd14631    82 GDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFI------RRVKLS-------NPP 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709536963 498 GGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14631   149 SAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 348-564 2.59e-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: 175.33  E-value: 2.59e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRN-AYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKdfQVCFGALTItNLG 426
Cdd:cd14546     1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEG--SEVYHIYEV-HLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 427 VENL--NHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSalgprfkghpggpPIVV 504
Cdd:cd14546    78 SEHIwcDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSC-------------PIVV 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709536963 505 HCSAGIGRTGTFCALDICLSQL-QDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14546   145 HCSDGAGRTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 348-564 4.06e-50

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: 172.24  E-value: 4.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASF--MDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWP--LEKDFQVCFGALTIT 423
Cdd:cd14596     1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPetLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 424 NLGVenLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKqqqrvavsalgprfKGHPGGPpIV 503
Cdd:cd14596    81 NYQA--LQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR--------------KVHNTGP-IV 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709536963 504 VHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14596   144 VHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 278-564 5.82e-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: 5.82e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 278 LQELLDHVSHKQKrgIYEEYEDI--RRRSPAGTFVcSLAPYNQEKNRYGDVPCLDQTRV--KLAKPYSRpelTDYINASF 353
Cdd:cd14610     6 LSYMEDHLKNKNR--LEKEWEALcaYQAEPNATNV-AQREENVQKNRSLAVLPYDHSRIilKAENSHSH---SDYINASP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 354 MDGYKQRN-AYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPLEKD--FQVCFGALTITNLGVENL 430
Cdd:cd14610    80 IMDHDPRNpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSnlYHIYEVNLVSEHIWCEDF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 431 ---NHYKKTIleihssETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQqrvavsalgprFKGHpgGPPIVVHCS 507
Cdd:cd14610   160 lvrSFYLKNL------QTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKC-----------YRGR--SCPIIVHCS 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1709536963 508 AGIGRTGTFCALDICLSQL-QDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14610   221 DGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 348-559 6.29e-49

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: 168.80  E-value: 6.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRN--AYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRR-KCGQYWPLEKDFQVCFGALTITN 424
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 425 LGVENLNH-YKKTILEIHSSETRERRL-VSHFQYLSWPDYGVPSSAATLIDFLGAVkqqqrvavsalgprFKGHPGGPPI 502
Cdd:cd17658    81 KKLKHSQHsITLRVLEVQYIESEEPPLsVLHIQYPEWPDHGVPKDTRSVRELLKRL--------------YGIPPSAGPI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1709536963 503 VVHCSAGIGRTGTFCALDICLSQ--LQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCY 559
Cdd:cd17658   147 VVHCSAGIGRTGAYCTIHNTIRRilEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 347-564 2.59e-48

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: 167.43  E-value: 2.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 347 DYINASFMD----GYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPlEKDFQVCFGALTI 422
Cdd:cd14601     1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 423 TNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQrvavsalgprfKGHPggPPI 502
Cdd:cd14601    80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKR-----------AGKD--EPV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709536963 503 VVHCSAGIGRTGTFCALD--ICLSQL-QDVGTLNIYQTvlrMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14601   147 VVHCSAGIGRTGVLITMEtaMCLIECnQPVYPLDIVRT---MRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 320-559 5.41e-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: 167.02  E-value: 5.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 320 KNRYGDVPCLDQTRVKLAKPYSRPELTDYINASFMDGYK-QRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEG 398
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 399 GRrKCGQYWPLEKDFqvcFGALTITNLGVENLNHYkkTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAV 478
Cdd:cd14611    82 NE-KCVLYWPEKRGI---YGKVEVLVNSVKECDNY--TIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 479 KQQQrvavsalgprfKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFC 558
Cdd:cd14611   156 EEDR-----------LASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                  .
gi 1709536963 559 Y 559
Cdd:cd14611   225 H 225
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 311-564 2.56e-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: 167.14  E-value: 2.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 311 CSLAP--YNQEKNRYGDVPCLDQTRVKLaKPYSRPELTDYINASFMDGYKQR-NAYIGTQGPLENTYGDFWRMVWEQNVL 387
Cdd:cd14609    34 CSTAQgeANVKKNRNPDFVPYDHARIKL-KAESNPSRSDYINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWENGCT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 388 VIVMTTRLEEGGRRKCGQYWPLEKD--FQVCFGALTITNLGVENL---NHYKKTIleihssETRERRLVSHFQYLSWPDY 462
Cdd:cd14609   113 VIVMLTPLVEDGVKQCDRYWPDEGSslYHIYEVNLVSEHIWCEDFlvrSFYLKNV------QTQETRTLTQFHFLSWPAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 463 GVPSSAATLIDFLGAVKQQqrvavsalgprFKGHpgGPPIVVHCSAGIGRTGTFCALDICLSQL-QDVGTLNIYQTVLRM 541
Cdd:cd14609   187 GIPSSTRPLLDFRRKVNKC-----------YRGR--SCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHV 253

                         250       260
                  ....*....|....*....|...
gi 1709536963 542 RTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14609   254 RDQRPGMVRTKDQFEFALTAVAE 276
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 348-559 7.79e-45

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: 157.57  E-value: 7.79e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGrRKCGQYWPLEKdfQVCFGALTITNLGV 427
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKD-QSCPQYWPDEG--SGTYGPIQVEFVST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEIHSS--ETRERRLVSHFQYLSWPDYG-VPSSAATLIDFLGAVKQQQRvavsalgprfkgHPGGPPIVV 504
Cdd:cd14556    78 TIDEDVISRIFRLQNTtrPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQE------------QSGEGPIVV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709536963 505 HCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCY 559
Cdd:cd14556   146 HCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 348-564 3.05e-44

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: 156.67  E-value: 3.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMD---GYKQRNaYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCGQYWPL--EKDFQVCFGALTI 422
Cdd:cd14598     1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgSRHNTVTYGRFKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 423 TNLGVENLNHYKKTILEIHSSETRERRLVSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQRVAVSALGPRfkghPGGPPI 502
Cdd:cd14598    80 TTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPK----SPNPPV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709536963 503 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14598   156 LVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
451-564 1.42e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 1.42e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  451 VSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQrvavsalgprfKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD-V 529
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNL-----------NQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1709536963  530 GTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:smart00404  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 451-564 1.42e-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: 137.10  E-value: 1.42e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  451 VSHFQYLSWPDYGVPSSAATLIDFLGAVKQQQrvavsalgprfKGHPGGPPIVVHCSAGIGRTGTFCALDICLSQLQD-V 529
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNL-----------NQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1709536963  530 GTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:smart00012  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 80-230 3.32e-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: 129.73  E-value: 3.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963   80 ELLSGKFTILSVR--DPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSQYTNFEL 155
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709536963  156 DLSKKILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVKM---SELKEHLPRECLPEYLGGSLK 230
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGGTLD 158
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 348-564 3.45e-35

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: 131.68  E-value: 3.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGgrRKCGQYWPlEKDfQVCFGALTITNLGV 427
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA--QLCMQYWP-EKT-SCCYGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEIHSSETRER--RLVSHFQYLSWPDY-GVPSSAATLIDFLGAVKQQQRvavsalgpRFKGHPGgpPIVV 504
Cdd:cd14634    77 DIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQE--------QYDGREG--RTVV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 505 HCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14634   147 HCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 348-560 3.60e-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: 128.59  E-value: 3.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGrrKCGQYWPLEKD------FQVCFGALT 421
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKplecetFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 422 ITNLGVENLNHYKKTILEihsSETRERRL-VSHFQYLSWPDYGVPSSaaTLIDFLGAVKQ--QQRVAvsalgprfkghpg 498
Cdd:cd14550    79 HSCLSNEIRLIVRDFILE---STQDDYVLeVRQFQCPSWPNPCSPIH--TVFELINTVQEwaQQRDG------------- 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709536963 499 gpPIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYT 560
Cdd:cd14550   141 --PIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
315-555 4.25e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 130.98  E-value: 4.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 315 PYNQEKNRYGDVPCLDQTRVklakpysRPELTdYINASFMDGYKQRNaYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTR 394
Cdd:COG5599    40 INGSPLNRFRDIQPYKETAL-------RANLG-YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 395 LEEGGRR--KCGQYWPLEKDfqvcFGALTI--TNLGVENLnhykKTILEIHSSETR------ERRLVSHFQYLSWPDYGV 464
Cdd:COG5599   111 DDEISKPkvKMPVYFRQDGE----YGKYEVssELTESIQL----RDGIEARTYVLTikgtgqKKIEIPVLHVKNWPDHGA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 465 PSSAAtLIDFLGAVKQQQRVavsalgprfKGHPGGPPiVVHCSAGIGRTGTFCALdICLSQLQDVG---TLNIYQTVLRM 541
Cdd:COG5599   183 ISAEA-LKNLADLIDKKEKI---------KDPDKLLP-VVHCRAGVGRTGTLIAC-LALSKSINALvqiTLSVEEIVIDM 250

                         250
                  ....*....|....*
gi 1709536963 542 RTQRAFSI-QTPEQY 555
Cdd:COG5599   251 RTSRNGGMvQTSEQL 265
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 82-228 7.94e-34

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: 125.91  E-value: 7.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  82 LSGKFTILSVRDPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAVESFETQRNGLVFIYDMAGSQYTNF-ELDLSKK 160
Cdd:cd00170     7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLsDLSLLKK 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 161 ILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVK--MSELKEHLPRECLPEYLGGS 228
Cdd:cd00170    87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
83-227 2.34e-31

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 118.90  E-value: 2.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  83 SGKFTILSvRDPSGASIALFTAKLHHPSKSVQHVVLQALFYLLDRAV-ESFETQRNGLVFIYDMAGSQYTNFE---LDLS 158
Cdd:pfam00650   1 GGKVYLHG-RDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALlLMPEGQVEGLTVIIDLKGLSLSNMDwwsISLL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709536963 159 KKILNLLKGAFPARLKKVFIVGAPMWFRVPYSIISLLLKEKLRERVQMVK---MSELKEHLPRECLPEYLGG 227
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKnsnEEELEKYIPPEQLPKEYGG 151
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 349-562 3.05e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 117.76  E-value: 3.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 349 INASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEggrRKC-GQYWPLEKDFQVCFGALTITNLGV 427
Cdd:PHA02740   79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSLKEGCVITSDKFQIETLEI 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEIHSSETRERRLvSHFQYLSWPDYGVPSSAATLIDFLGAVKQ-----QQRVAVSALGPrfkghpggppI 502
Cdd:PHA02740  156 IIKPHFNLTLLSLTDKFGQAQKI-SHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadlEKHKADGKIAP----------I 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 503 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAI 562
Cdd:PHA02740  225 IIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 348-564 5.01e-29

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: 114.35  E-value: 5.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGgrRKCGQYWPLEKDFQvcFGALTITNLGV 427
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWPEEGMLR--YGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEIhSSETRERR---LVSHFQYLSWPDY-GVPSSAATLIDFLGAVKQQQRvavsalgprfKGHPGGPPIV 503
Cdd:cd14636    77 SMDCDVISRIFRI-CNLTRPQEgylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQE----------ECDEGEGRTI 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709536963 504 VHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14636   146 IHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 348-564 1.00e-28

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: 113.63  E-value: 1.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGgrRKCGQYWPLEKDFQvcFGALTITNLGV 427
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPENGVHR--HGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEIHSSETRER--RLVSHFQYLSWPDY-GVPSSAATLIDFLGAVKQQQRvavsalgpRFKGHPGgpPIVV 504
Cdd:cd14635    77 DLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQE--------EYNGGEG--RTVV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 505 HCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14635   147 HCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 348-564 9.37e-28

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: 110.77  E-value: 9.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRR-KCGQYWP---LEK--DFQVCFGALT 421
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPepgLQQygPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 422 ITNLGVENLNHYKKTileihSSETRERRLVSHFQYLSWPDY-GVPSSAATLIDFLGAVKQQQRvavsalgprfkgHPGGP 500
Cdd:cd14637    81 ADEDIVTRLFRVQNI-----TRLQEGHLMVRHFQFLRWSAYrDTPDSKKAFLHLLASVEKWQR------------ESGEG 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709536963 501 PIVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAILE 564
Cdd:cd14637   144 RTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 348-563 3.86e-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: 108.93  E-value: 3.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRLEEGGRRKCgQYWPLEKDFQVCFGaLTITNLGV 427
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCET-FKVTLIAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 EN--LNHYKKTILE---IHSSETRERRLVSHFQYLSWPDYGVPSSAAtlIDFLGAVKQQqrvAVSALGprfkghpggpPI 502
Cdd:cd17669    79 EHkcLSNEEKLIIQdfiLEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEE---AANRDG----------PM 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709536963 503 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAIL 563
Cdd:cd17669   144 IVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 348-563 2.14e-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: 103.99  E-value: 2.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 348 YINASFMDGYKQRNAYIGTQGPLENTYGDFWRMVWEQNVLVIVMTTRlEEGGRRKCGQYWPLEKDFQVCFgALTITNLGV 427
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYWPSREESMNCE-AFTVTLISK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 428 ENLNHYKKTILEIHS---SETRERRL--VSHFQYLSWPDYGVPSSAAtlIDFLGAVKQQqrvAVSALGprfkghpggpPI 502
Cdd:cd17670    79 DRLCLSNEEQIIIHDfilEATQDDYVleVRHFQCPKWPNPDAPISST--FELINVIKEE---ALTRDG----------PT 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709536963 503 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNIYQTVLRMRTQRAFSIQTPEQYYFCYTAIL 563
Cdd:cd17670   144 IVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 96-232 3.31e-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: 70.05  E-value: 3.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963  96 GASIALFTAKLHHPSKSVQHVVLQALFYLLDRAVESFETQrnGLVFIYDMAGSQYTNFE-LDLSKKILNLLKGAFPARLK 174
Cdd:pfam13716   1 GRPVLVFISKLLPSRPASLDDLDRLLFYLLKTLSEKLKGK--PFVVVVDHTGVTSENFPsLSFLKKAYDLLPRAFKKNLK 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 175 KVFIVGAPMWFRVPYSII-SLLLKEKLRERVQMV-KMSELKEHLPRECLPEYLGGSLKLD 232
Cdd:pfam13716  79 AVYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHYVsSLSELWEGIDREQLPTELPGVLSYD 138
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 498-559 3.69e-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: 63.14  E-value: 3.69e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709536963 498 GGPPIVVHCSAGIGRTGTFCALDICLSQLqdvgtLNIYQTVLRMRTQRAFSI-QTPEQYYFCY 559
Cdd:cd14494    55 PGEPVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRPGGIpQTIEQLDFLI 112
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
10-58 3.12e-07

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 47.16  E-value: 3.12e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1709536963   10 EQATKQFLEEINKWTGqYNVSPLSWNVAVKFLMARKFDVLRAIELFHSY 58
Cdd:smart01100   1 EEALEELRELLEKHPD-LLPPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 459-555 8.52e-07

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: 50.09  E-value: 8.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 459 WPDYGVPSSAAT--LIDFLGAVKQQQRVAVSALGPRFKGHPGGPPIVVHCSAGIGRTGTFCAlDICLSQLQDvgTLNIYQ 536
Cdd:cd14559   126 WPDHTAISSEGLkeLADLVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLAA-AMELNKSPN--NLSVED 202

                          90       100
                  ....*....|....*....|
gi 1709536963 537 TVLRMRTQR-AFSIQTPEQY 555
Cdd:cd14559   203 IVSDMRTSRnGKMVQKDEQL 222
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
439-557 1.64e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 47.66  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 439 EIHSSETRERRLVshFQYLSWPDYGVPSsAATLIDFLGAVKQQQRvavsalgprfkghpGGPPIVVHCSAGIGRTGTFCA 518
Cdd:COG2453    37 ELLLGLLEEAGLE--YLHLPIPDFGAPD-DEQLQEAVDFIDEALR--------------EGKKVLVHCRGGIGRTGTVAA 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1709536963 519 LDICLSQlqdvgtLNIYQTVLRMRTQRAFSIQTPEQYYF 557
Cdd:COG2453   100 AYLVLLG------LSAEEALARVRAARPGAVETPAQRAF 132
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 399-560 1.71e-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: 48.41  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 399 GRRKCGQYWPLEKDFQV---CFGALTITNLGVENLNHYK-KTILEIhsseTRERRLVSHfqYLSWPDYGVPSSAA---TL 471
Cdd:cd14505    22 GCKFKDHRRDLQADLEElkdQGVDDVVTLCTDGELEELGvPDLLEQ----YQQAGITWH--HLPIPDGGVPSDIAqwqEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 472 IDFL-GAVKQQQRVavsalgprfkghpggppiVVHCSAGIGRTGTFCALdiCLSQLQDvgTLNIYQTVLRMRTQRAFSIQ 550
Cdd:cd14505    96 LEELlSALENGKKV------------------LIHCKGGLGRTGLIAAC--LLLELGD--TLDPEQAIAAVRALRPGAIQ 153

                         170
                  ....*....|
gi 1709536963 551 TPEQYYFCYT 560
Cdd:cd14505   154 TPKQENFLHQ 163
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 444-554 1.81e-06

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: 48.88  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 444 ETRERRLVSHFQYlSWPDYGVPSsAATLIDflgAVKqqqrVAVSALGPRFKghpggppIVVHCSAGIGRTGTF--CALdi 521
Cdd:cd14506    70 EAFMRAGIYFYNF-GWKDYGVPS-LTTILD---IVK----VMAFALQEGGK-------VAVHCHAGLGRTGVLiaCYL-- 131

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1709536963 522 clsqlqdVGTLNIY--QTVLRMRTQRAFSIQTPEQ 554
Cdd:cd14506   132 -------VYALRMSadQAIRLVRSKRPNSIQTRGQ 159
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 499-554 4.08e-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: 40.72  E-value: 4.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1709536963 499 GPPIVVHCSAGIGRTGTFCAldiCLsqLQDVGTLNIYQTVLRMRTQRAFSIQTPEQ 554
Cdd:cd14504    82 NEAVLVHCLAGKGRTGTMLA---CY--LVKTGKISAVDAINEIRRIRPGSIETSEQ 132
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 435-519 4.40e-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: 41.21  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709536963 435 KTILEIHSSETRERRLV-----SHFQYLSWPdygvpsSAATLIDfLGAVKQQQRVAVSALGPRfkghpggpPIVVHCSAG 509
Cdd:cd14529    35 KTVIDLRGADERAASEEaaakiDGVKYVNLP------LSATRPT-ESDVQSFLLIMDLKLAPG--------PVLIHCKHG 99

                          90
                  ....*....|
gi 1709536963 510 IGRTGTFCAL 519
Cdd:cd14529   100 KDRTGLVSAL 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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