NCBI Conserved Domain Search

Fibronectin type III domain;

642-719

1.43e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 41.63 E-value: 1.43e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  642 PSNVSYIEVNTNTtvAAIQWKNLDAASASY-SYSVLILKAGDGSNVTSR--VRDIPSVTIPGLIPGVSYEVKIFTKIRNT 718
Cdd:pfam00041    3 PSNLTVTDVTSTS--LTVSWTPPPDGNGPItGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   .
gi 1958760896  719 E 719
Cdd:pfam00041   81 E 81

Name

Accession

Description

Interval

E-value

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

1084-1312

7.43e-172

Pssm-ID: 350463 [Multi-domain] Cd Length: 229 Bit Score: 509.74 E-value: 7.43e-172

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1084 NRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1163
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1164 CEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 1243
Cdd:cd14615     81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760896 1244 IPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14615    161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1055-1312

2.42e-120

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 375.07 E-value: 2.42e-120

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  1055 GFAEEYEDLKLIGISLPKYA-AEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 1133
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  1134 TLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLR 1211
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  1212 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRM 1291
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQST--STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1958760896  1292 HRPLMVQTEDQYVFLNQCVLD 1312
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1080-1312

2.29e-111

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 349.62 E-value: 2.29e-111

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1080 NRGKNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQ 1159
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1160 GRTKCEEYWPSK--QAQDYGDITVAMTSEV-VLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 1236
Cdd:pfam00102   80 GREKCAQYWPEEegESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760896 1237 VRDYmKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:pfam00102  160 VRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

PHA02738

hypothetical protein; Provisional

1073-1305

3.46e-46

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 169.34 E-value: 3.46e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1073 YAAEIAeNRGKNRYNNVLPYDISRVKLSVQtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1152
Cdd:PHA02738    43 FNAEKK-NRKLNRYLDAVCFDHSRVILPAE-RNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVM 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1153 LTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNmQSSESHPLRQFHFTSWPDHGVPDTTDLL 1230
Cdd:PHA02738   121 LCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEF 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1231 INFRYLVRDYMKQIPPES-----------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQT 1299
Cdd:PHA02738   200 LNFVLEVRQCQKELAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFI 279


                   ....*.
gi 1958760896 1300 EDQYVF 1305
Cdd:PHA02738   280 PFQYFF 285

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1070-1306

8.91e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 166.81 E-value: 8.91e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1070 LPKYAAEIaENRGKNRYNNVLPYDISRVKlsvqthSTDDYINANYMPGYhSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 1149
Cdd:COG5599     33 DPQYLQNI-NGSPLNRFRDIQPYKETALR------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPV 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1150 IVMLTKCVE--QGRTKCEEYWPskQAQDYG--DITVAMTSEVVL-PEWTIRDFVVKNMQSS-ESHPLRQFHFTSWPDHGV 1223
Cdd:COG5599    105 LVVLASDDEisKPKVKMPVYFR--QDGEYGkyEVSSELTESIQLrDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGA 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1224 PDTTdLLINFRYLVRDYMK-QIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR-PLMVQT 1299
Cdd:COG5599    183 ISAE-ALKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQT 261


                   ....*..
gi 1958760896 1300 EDQYVFL 1306
Cdd:COG5599    262 SEQLDVL 268

PTP_tm

pfam18861

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...

850-980

3.89e-39

Pssm-ID: 465889 Cd Length: 126 Bit Score: 141.97 E-value: 3.89e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  850 VKFSGFEASHGPIKAYAVLLTTGEAG-QPSTDVLKYTYEDFKKGASDTYVTYLIriEEKGQSQGlSEALNYEIDVGNQST 928
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDSLnRPLKEYLNKTYYDWKYKKTDSYLATVT--PNPFTSPR-SSSRSLTVPVGTGSK 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958760896  929 TLGYYNGRLEPLGSYRACVAGFTNITYnlqNDGLINGDESYVSFSPYSEAVS 980
Cdd:pfam18861   78 WQGYCNGPLKPLGSYRFSVAAFTRLEF---DDGLIDGEESYVSFTPFSEPIA 126

FN3

COG3401

Fibronectin type 3 domain [General function prediction only];

169-659

3.24e-11

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 67.72 E-value: 3.24e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  169 LTWKHNDSATSEYKINEGNTLRYTVKNQTSFNITGLSPATSYKFSITLGTVNETSGKP-TYKNITTEPWPVSDLQVAYIG 247
Cdd:COG3401      9 LDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGlGTGGRAGTTSGVAAVAVAAAP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  248 VTQALLAW--SNANGTASYRMQIVELTTNSSGGISDLKPGTHKSLAVQGSNETQHDLWVTE-----GVSDANGTEGSPVA 320
Cdd:COG3401     89 PTATGLTTltGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGvdganASGTTASSVAGAGV 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  321 NISQLHKNSLASADPPSARDPSLTEVLLTELKPDTQYKVTIYSqAADGTEGQPGNKV----FKTNPIQVSDIRAVNISDS 396
Cdd:COG3401    169 VVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAA-TDTGGESAPSNEVsvttPTTPPSAPTGLTATADTPG 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  397 NMTLTWKSNNNESHASftYKIYVAGGSDSINE---TVNETQAVIRGLSSSTLYN--ITVLPFLGQTAGIPGFLQVYTS-- 469
Cdd:COG3401    248 SVTLSWDPVTESDATG--YRVYRSNSGDGPFTkvaTVTTTSYTDTGLTNGTTYYyrVTAVDAAGNESAPSNVVSVTTDlt 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  470 -PRPVSDFRVTNVSLREIGLAWRSNDSE---SFEIF--ITQEGSEKRWNASTGDLSYIVENLKPGTSYQFEIFPRGPNGT 543
Cdd:COG3401    326 pPAAPSGLTATAVGSSSITLSWTASSDAdvtGYNVYrsTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  544 EGPSQTVVgrtdcSAVTDIRVVSVSTTEIQLEWQNTDSASGYTYHLVLESENGSIKTNSSQKWITVGGLTPGTLYNVTIF 623
Cdd:COG3401    406 ESAPSEEV-----SATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTAT 480

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1958760896  624 PE--VDQMEGNSSSITQYTRPSNVSYIEVNTNTTVAAI 659
Cdd:COG3401    481 TTdtTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAA 518

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

470-554

3.48e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.42 E-value: 3.48e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  470 PRPVSDFRVTNVSLREIGLAWRSNDSE-----SFEIFITQEGSEKRWNASTG---DLSYIVENLKPGTSYQFEIFPRGPN 541
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpitGYVVEYREKGSGDWKEVEVTpgsETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1958760896  542 GTEGPSQTVVGRT 554
Cdd:cd00063     81 GESPPSESVTVTT 93

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

557-631

1.33e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 47.61 E-value: 1.33e-06

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896   557 SAVTDIRVVSVSTTEIQLEWQNTDSASGYTYHLVLESENGS-------IKTNSSQKWITVGGLTPGTLYNVTIFPEVDQM 629
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREegsewkeVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1958760896   630 EG 631
Cdd:smart00060   82 EG 83

fn3

Fibronectin type III domain;

472-536

3.81e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 43.56 E-value: 3.81e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760896  472 PVSDFRVTNVSLREIGLAWRSNDS-----ESFEIFITQEGSEKRWNASTGDL---SYIVENLKPGTSYQFEIF 536
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDgngpiTGYEVEYRPKNSGEPWNEITVPGtttSVTLTGLKPGTEYEVRVQ 74

fn3

Fibronectin type III domain;

642-719

1.43e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 41.63 E-value: 1.43e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  642 PSNVSYIEVNTNTtvAAIQWKNLDAASASY-SYSVLILKAGDGSNVTSR--VRDIPSVTIPGLIPGVSYEVKIFTKIRNT 718
Cdd:pfam00041    3 PSNLTVTDVTSTS--LTVSWTPPPDGNGPItGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   .
gi 1958760896  719 E 719
Cdd:pfam00041   81 E 81

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

642-711

4.29e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 37.86 E-value: 4.29e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760896  642 PSNVSYIEVNTNTtvAAIQWKNLDAASA---SYSYSVLILKAGDGSNVTSRVRDIPSVTIPGLIPGVSYEVKI 711
Cdd:cd00063      4 PTNLRVTDVTSTS--VTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRV 74

Name

Accession

Description

Interval

E-value

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

1084-1312

7.43e-172

Pssm-ID: 350463 [Multi-domain] Cd Length: 229 Bit Score: 509.74 E-value: 7.43e-172

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1084 NRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1163
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1164 CEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 1243
Cdd:cd14615     81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760896 1244 IPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14615    161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

1085-1308

2.66e-136

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: 415.99 E-value: 2.66e-136

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1085 RYNNVLPYDISRVKLSVQT-HSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1163
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINeEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1164 CEEYWPSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQssESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMK 1242
Cdd:cd14548     81 CDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760896 1243 QipPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd14548    159 Q--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1055-1312

2.42e-120

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 375.07 E-value: 2.42e-120

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  1055 GFAEEYEDLKLIGISLPKYA-AEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 1133
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  1134 TLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLR 1211
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  1212 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRM 1291
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQST--STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1958760896  1292 HRPLMVQTEDQYVFLNQCVLD 1312
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1080-1312

2.29e-111

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 349.62 E-value: 2.29e-111

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1080 NRGKNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQ 1159
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1160 GRTKCEEYWPSK--QAQDYGDITVAMTSEV-VLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 1236
Cdd:pfam00102   80 GREKCAQYWPEEegESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958760896 1237 VRDYmKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:pfam00102  160 VRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

1084-1314

5.01e-104

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: 329.54 E-value: 5.01e-104

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1084 NRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1162
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKpIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1163 KCEEYWP-SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYM 1241
Cdd:cd14619     81 KCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760896 1242 KQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1314
Cdd:cd14619    161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

1084-1308

8.04e-104

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: 328.80 E-value: 8.04e-104

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1084 NRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1162
Cdd:cd14617      1 NRYNNILPYDSTRVKLSnVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1163 KCEEYWPSKQ-AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPL-RQFHFTSWPDHGVPDTTDLLINFRYLVRDY 1240
Cdd:cd14617     81 KCDHYWPADQdSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLvRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760896 1241 MKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd14617    161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

1109-1308

6.87e-98

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.

Pssm-ID: 350343 [Multi-domain] Cd Length: 200 Bit Score: 311.53 E-value: 6.87e-98

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSE 1186
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPleYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1187 VVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIA 1266
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK--PNGPIVVHCSAGVGRTGTFIA 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958760896 1267 IDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd00047    159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

1080-1314

5.24e-95

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: 305.09 E-value: 5.24e-95

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1080 NRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVE 1158
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQpIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1159 QGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVR 1238
Cdd:cd14553     83 RSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760896 1239 DYMkqiPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1314
Cdd:cd14553    163 ACN---PPDAgPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

1084-1311

1.37e-93

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: 300.71 E-value: 1.37e-93

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1084 NRYNNVLPYDISRVKLSV---QTHStdDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQG 1160
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQlggEPHS--DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1161 RTKCEEYWPSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 1239
Cdd:cd14618     79 RVLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958760896 1240 YMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1311
Cdd:cd14618    159 HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

1070-1311

1.77e-92

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: 298.34 E-value: 1.77e-92

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1070 LPKYAAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVY 1148
Cdd:cd14614      2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLvSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1149 AIVMLTKCVEQGRTKCEEYWP-SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKnmQSSESHPLRQFHFTSWPDHGVP--D 1225
Cdd:cd14614     82 IIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPtaN 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1226 TTDLLINFRYLVRDymKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1305
Cdd:cd14614    160 AAESILQFVQMVRQ--QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                   ....*.
gi 1958760896 1306 LNQCVL 1311
Cdd:cd14614    238 IHQCVQ 243

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

1109-1306

3.57e-89

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: 287.33 E-value: 3.57e-89

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1188
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1189 LPEWTIRDFVVKNMQSSESHP------LRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRT 1261
Cdd:cd14549     81 LATYTVRTFSLKNLKLKKVKGrsservVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPPGAgPIVVHCSAGVGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958760896 1262 GTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1306
Cdd:cd14549    158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

1055-1305

2.14e-84

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: 276.94 E-value: 2.14e-84

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1055 GFAEEYEDLKLIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 1133
Cdd:cd14543      4 GIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPkRNGDERTDYINANFMDGYKQKNAYIATQGPLPK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1134 TLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQ--AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLR 1211
Cdd:cd14543     84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1212 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQI-----------PPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTV 1280
Cdd:cd14543    164 HFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTL 243

                          250       260
                   ....*....|....*....|....*
gi 1958760896 1281 DVYGIVYDLRMHRPLMVQTEDQYVF 1305
Cdd:cd14543    244 NVMQTVRRMRTQRAFSIQTPDQYYF 268

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

1046-1312

2.88e-78

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: 259.58 E-value: 2.88e-78

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1046 KKQQADSNCGFAEEYEDLKlIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDF 1124
Cdd:cd14626      8 ERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILtSVDGVPGSDYINANYIDGYRKQNAY 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1125 IATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQS 1204
Cdd:cd14626     87 IATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGS 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1205 SESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVY 1283
Cdd:cd14626    167 SEKREVRQFQFMAWPDHGVPEYPTPILAF---LRRVKACNPPDAgPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIY 243

                          250       260
                   ....*....|....*....|....*....
gi 1958760896 1284 GIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14626    244 GHVTCMRSQRNYMVQTEDQYIFIHEALLE 272

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

1084-1308

5.44e-76

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: 251.16 E-value: 5.44e-76

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1084 NRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEqGR 1161
Cdd:cd14547      1 NRYKTILPNEHSRVCLpSVDDDPLSSYINANYIRGYDGEeKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1162 TKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNmqSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYM 1241
Cdd:cd14547     80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEAR 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760896 1242 KQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd14547    158 QTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

1075-1311

8.99e-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: 251.29 E-value: 8.99e-76

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1075 AEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVML 1153
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQpIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1154 TKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINF 1233
Cdd:cd14554     81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760896 1234 RYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1311
Cdd:cd14554    161 IGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

1079-1312

1.69e-75

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: 250.33 E-value: 1.69e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1079 ENRGKNRYNNVLPYDISRVKLSV---QTHStdDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTK 1155
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLldgDPHS--DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1156 CVEQGRTKCEEYWPSkQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFry 1235
Cdd:cd14630     80 LVEVGRVKCVRYWPD-DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF-- 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760896 1236 lVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14630    157 -VRQVKFLNPPDAgPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

1056-1314

3.14e-75

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: 251.11 E-value: 3.14e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1056 FAEEYEDLK--LIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKLSV-----QTHStdDYINANYMPGYHSKKDFIATQ 1128
Cdd:cd17667      1 FSEDFEEVQrcTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPlpgkdSKHS--DYINANYVDGYNKAKAYIATQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1129 GPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQ---SS 1205
Cdd:cd17667     79 GPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkGQ 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1206 ESHP--------LRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENE 1277
Cdd:cd17667    159 KGNPkgrqnertVIQYHYTQWPDMGVPEYALPVLTF--VRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDK 236

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1958760896 1278 NTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1314
Cdd:cd17667    237 STVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

1055-1312

1.10e-72

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: 243.80 E-value: 1.10e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1055 GFAEEYEDLkLIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 1133
Cdd:cd14633     16 GFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLqPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1134 TLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSkQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQF 1213
Cdd:cd14633     95 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQF 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1214 HFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMH 1292
Cdd:cd14633    174 HFTGWPDHGVPYHATGLLGF---VRQVKSKSPPNAgPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSR 250

                          250       260
                   ....*....|....*....|
gi 1958760896 1293 RPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14633    251 RVNMVQTEEQYVFIHDAILE 270

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

1084-1308

1.38e-72

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: 241.35 E-value: 1.38e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1084 NRYNNVLPYDISRVKLSVQTHST-DDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1162
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1163 KCEEYWP--SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKnmQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRdy 1240
Cdd:cd14616     81 RCHQYWPedNKPVTVFGDIVITKLMEDVQIDWTIRDLKIE--RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR-- 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760896 1241 MKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd14616    157 ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

1044-1314

2.48e-72

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: 243.10 E-value: 2.48e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1044 YFKKQQADSNCGFAEEYEDLKlIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKK 1122
Cdd:cd14624     12 HIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSaIEGIPGSDYINANYIDGYRKQN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1123 DFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNM 1202
Cdd:cd14624     91 AYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKN 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1203 QSSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVD 1281
Cdd:cd14624    171 GSSEKREVRQFQFTAWPDHGVPEHPTPFLAF---LRRVKTCNPPDAgPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVD 247

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1958760896 1282 VYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1314
Cdd:cd14624    248 IYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

1036-1314

1.05e-71

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: 241.15 E-value: 1.05e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1036 IRVENFEAYFKKQQADSNCGFAEEYEDLKlIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANY 1114
Cdd:cd14625      4 IPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILqPIEGIMGSDYINANY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1115 MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTI 1194
Cdd:cd14625     83 IDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFCV 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1195 RDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQ 1273
Cdd:cd14625    163 RTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAF---LRRVKTCNPPDAgPIVVHCSAGVGRTGCFIVIDAMLER 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1958760896 1274 IENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1314
Cdd:cd14625    240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280

R-PTPc-A-1

cd14621

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...

1031-1312

5.12e-70

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: 237.23 E-value: 5.12e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1031 KKSKLIRVENFEAYFKKQQADSNCGFAEEYEDLKLIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDY 1109
Cdd:cd14621      3 RKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLtPVEGVPDSDY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1110 INANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVL 1189
Cdd:cd14621     83 INASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1190 PEWTIRDFVVKNM-QSSESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPpeSPILVHCSAGVGRTGTFI 1265
Cdd:cd14621    163 VDYTVRKFCIQQVgDVTNKKPQRlitQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYA--GAIVVHCSAGVGRTGTFI 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958760896 1266 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14621    241 VIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

1109-1312

1.07e-69

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: 232.50 E-value: 1.07e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPsKQAQDYGDITVAMTSEVV 1188
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1189 LPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAI 1267
Cdd:cd14555     80 LAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGF---IRRVKASNPPSAgPIVVHCSAGAGRTGCYIVI 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958760896 1268 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14555    157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

1109-1308

1.19e-68

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: 229.33 E-value: 1.19e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS--KQAQDYGDITVAMTSE 1186
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1187 VVLPEWTIRDFVVKNMQSSES-HPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIppESPILVHCSAGVGRTGTFI 1265
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFF--SGPIVVHCSAGVGRTGTYI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958760896 1266 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd14557    159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

1109-1306

5.13e-67

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.

Pssm-ID: 350509 [Multi-domain] Cd Length: 212 Bit Score: 225.21 E-value: 5.13e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYM-PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD-YGDITVAM--T 1184
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGeYGDLTVELvsE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1185 SEVVLPEWTIRDFVVKnMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTF 1264
Cdd:cd18533     81 EENDDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTF 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958760896 1265 IAIDRLIYQIEN--------ENTVD-VYGIVYDLRMHRPLMVQTEDQYVFL 1306
Cdd:cd18533    160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFL 210

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

1086-1312

1.34e-66

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: 224.43 E-value: 1.34e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1086 YNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKC 1164
Cdd:cd14620      1 YPNILPYDHSRVILSqLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1165 EEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVrdym 1241
Cdd:cd14620     81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRlvtQLHFTSWPDFGVPFTPIGMLKFLKKV---- 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760896 1242 KQIPP--ESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14620    157 KSVNPvhAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

1080-1306

1.85e-66

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.

Pssm-ID: 350392 [Multi-domain] Cd Length: 251 Bit Score: 225.03 E-value: 1.85e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1080 NRGKNRYNNVLPYDISRVKLSVQTHST--DDYINANYM-----PGYHSK--KDFIATQGPLPNTLKDFWRMVWEKNVYAI 1150
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNVpgSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1151 VMLTKCVEQGRTKCEEYWPSK-QAQDYGDITVAMTSEVVLPEWTIRDFVVKNM-QSSESHPLRQFHFTSWPDHGVPDTTD 1228
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEgMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1229 LLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN---TVDVYGIVYDLRMHRPLMVQTEDQYVF 1305
Cdd:cd14544    161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                   .
gi 1958760896 1306 L 1306
Cdd:cd14544    241 I 241

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

1109-1312

2.24e-66

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: 223.00 E-value: 2.24e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPsKQAQDYGDITVAMTSEVV 1188
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1189 LPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAI 1267
Cdd:cd14632     80 LAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAF---IRRVKASTPPDAgPVVVHCSAGAGRTGCYIVL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958760896 1268 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14632    157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

1074-1314

9.07e-66

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: 224.60 E-value: 9.07e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1074 AAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1152
Cdd:cd14629     47 SANLPCNKFKNRLVNIMPYELTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1153 LTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLIN 1232
Cdd:cd14629    127 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1233 FRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14629    207 FIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286


                   ..
gi 1958760896 1313 II 1314
Cdd:cd14629    287 YL 288

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

1109-1314

1.01e-65

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: 221.09 E-value: 1.01e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYM--PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS---KQAQDYGDITVAM 1183
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1184 TSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRdYMKQIPPESPILVHCSAGVGRTGT 1263
Cdd:cd14538     81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRF---IR-YMRRIHNSGPIVVHCSAGIGRTGV 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958760896 1264 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1314
Cdd:cd14538    157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

R-PTPc-Z-1

cd17668

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...

1109-1307

1.23e-65

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: 221.01 E-value: 1.23e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1188
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1189 LPEWTIRDFVVKNMQ--------SSESHPLRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQIPPESPILVHCSAGVGR 1260
Cdd:cd17668     81 LAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTF--VRKASYAKRHAVGPVVVHCSAGVGR 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958760896 1261 TGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 1307
Cdd:cd17668    159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

1074-1314

1.55e-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: 223.84 E-value: 1.55e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1074 AAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1152
Cdd:cd14627     47 SANLPCNKFKNRLVNIMPYETTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1153 LTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLIN 1232
Cdd:cd14627    127 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1233 FRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14627    207 FIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286


                   ..
gi 1958760896 1313 II 1314
Cdd:cd14627    287 YL 288

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

1036-1314

1.85e-65

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

Pssm-ID: 350476 [Multi-domain] Cd Length: 292 Bit Score: 223.84 E-value: 1.85e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1036 IRVENFEAYFKK----QQADSNCGFAEEYEDLKLIGISLPKY-AAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDY 1109
Cdd:cd14628      3 VPARNLYAYIQKltqiETGENVTGMELEFKRLASSKAHTSRFiSANLPCNKFKNRLVNIMPYESTRVCLQpIRGVEGSDY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1110 INANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVL 1189
Cdd:cd14628     83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNM 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1190 PEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDR 1269
Cdd:cd14628    163 PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSI 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1958760896 1270 LIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1314
Cdd:cd14628    243 VLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

1109-1310

3.59e-64

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: 216.37 E-value: 3.59e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1188
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1189 LPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFIAID 1268
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQ-SGNHPITVHCSAGAGRTGTFCALS 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958760896 1269 RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1310
Cdd:cd14552    160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

PTPc-N22_18_12

cd14542

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...

1109-1308

7.90e-64

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: 215.36 E-value: 7.90e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSE 1186
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1187 vvlpEWTIRDFVVKNMQ---SSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYmkQIPPESPILVHCSAGVGRTGT 1263
Cdd:cd14542     81 ----KRVGPDFLIRTLKvtfQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958760896 1264 FIAIDR----LIYQIENENtVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd14542    155 ICAIDYvwnlLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

1071-1317

1.13e-63

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: 219.03 E-value: 1.13e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1071 PKYAAEIAENRGKNRYNNVLPYDISRVKLSVQTHSTD-DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 1149
Cdd:cd14604     48 PTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDsDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAI 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1150 IVMLTKCVEQGRTKCEEYWP--SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQssESHPLRQFHFTSWPDHGVPDTT 1227
Cdd:cd14604    128 IVMACREFEMGRKKCERYWPlyGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQN--ETRRLYQFHYVNWPDHDVPSSF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1228 DLLINFRYLVRDYmkQIPPESPILVHCSAGVGRTGTFIAID---RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYV 1304
Cdd:cd14604    206 DSILDMISLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYE 283

                          250
                   ....*....|...
gi 1958760896 1305 FLNQCVLDIIRAQ 1317
Cdd:cd14604    284 LVHRAIAQLFEKQ 296

PTPc-N3

cd14600

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...

1075-1315

1.43e-63

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: 217.80 E-value: 1.43e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1075 AEIAENRGKNRYNNVLPYDISRVKLsvqtHSTDDYINANYM----PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAI 1150
Cdd:cd14600     35 AKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1151 VMLTKCVEQGRTKCEEYWPSKQ-AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDL 1229
Cdd:cd14600    111 VMLTTLTERGRTKCHQYWPDPPdVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1230 LINFRYLVRDymKQIPPEsPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 1309
Cdd:cd14600    191 FLEFVNYVRS--KRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267


                   ....*.
gi 1958760896 1310 VLDIIR 1315
Cdd:cd14600    268 ILRVYE 273

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

1083-1305

3.88e-63

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: 214.56 E-value: 3.88e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1083 KNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1162
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGDND-YINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1163 KCEEYWPSKQAQDYG----DITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVR 1238
Cdd:cd14545     80 KCAQYWPQGEGNAMIfedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVR 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760896 1239 DYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENT--VDVYGIVYDLRMHRPLMVQTEDQYVF 1305
Cdd:cd14545    160 ESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228

PTPc-N3_4

cd14541

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

1108-1311

4.44e-63

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: 213.73 E-value: 4.44e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1108 DYINANY----MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS-KQAQDYGDITVA 1182
Cdd:cd14541      1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1183 MTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRdyMKQIPPESPILVHCSAGVGRTG 1262
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR--QNRVGMVEPTVVHCSAGIGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958760896 1263 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1311
Cdd:cd14541    159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

1079-1314

9.04e-63

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: 213.92 E-value: 9.04e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1079 ENRGKNRYNNVLPYDISRVKLSVQthstDDYINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKC 1156
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPLGDE----GGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1157 VEQGRTKCEEYWP-----SKQAQDYGDITVAMTSEvvLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLI 1231
Cdd:cd14597     78 VEGGKIKCQRYWPeilgkTTMVDNRLQLTLVRMQQ--LKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1232 NFRylvrDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1311
Cdd:cd14597    156 TFI----SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231


                   ...
gi 1958760896 1312 DII 1314
Cdd:cd14597    232 YVL 234

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

1079-1310

1.61e-62

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: 214.30 E-value: 1.61e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1079 ENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCV 1157
Cdd:cd14603     29 ENVKKNRYKDILPYDQTRVILSlLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREI 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1158 EQGRTKCEEYWPSKQAQ-DYGDITVAMTSEVVL-PEWTIRDFVVKNMQssESHPLRQFHFTSWPDHGVPDTTDLLINFRY 1235
Cdd:cd14603    109 EMGKKKCERYWAQEQEPlQTGPFTITLVKEKRLnEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPDSPDCMLAMIE 186

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760896 1236 LVRDYMKQIPpeSPILVHCSAGVGRTGTFIAID---RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1310
Cdd:cd14603    187 LARRLQGSGP--EPLCVHCSAGCGRTGVICTVDyvrQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTV 262

R-PTPc-A-E-1

cd14551

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...

1109-1308

2.02e-62

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: 211.69 E-value: 2.02e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1188
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1189 LPEWTIRDFVV-KNMQSSESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVrdyMKQIPPES-PILVHCSAGVGRTGT 1263
Cdd:cd14551     81 LVDYTTRKFCIqKVNRGIGEKRVRlvtQFHFTSWPDFGVPFTPIGMLKFLKKV---KSANPPRAgPIVVHCSAGVGRTGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958760896 1264 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd14551    158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

1076-1306

7.67e-62

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: 211.62 E-value: 7.67e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1076 EIAENRGKNRYNNVLPYDISRVKLSVQTHS--TDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1152
Cdd:cd14612     11 DIPGHASKDRYKTILPNPQSRVCLRRAGSQeeEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1153 LTKcVEQGRTKCEEYWPSKQAQdYGDITVAMTSEVVLPEWTIRDFVVKnmQSSESHPLRQFHFTSWPDHGVPDTTDLLIN 1232
Cdd:cd14612     91 ITK-LKEKKEKCVHYWPEKEGT-YGRFEIRVQDMKECDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLR 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958760896 1233 FRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1306
Cdd:cd14612    167 LVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

1056-1305

1.19e-61

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: 212.19 E-value: 1.19e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1056 FAEEYEDLKLIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKLSVQThstDDYINANYMPGYHSKKDFIATQGPLPNTL 1135
Cdd:cd14608      1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED---NDYINASLIKMEEAQRSYILTQGPLPNTC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1136 KDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQ----DYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLR 1211
Cdd:cd14608     78 GHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKemifEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREIL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1212 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDR---LIYQIENENTVDVYGIVYD 1288
Cdd:cd14608    158 HFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLE 237

                          250
                   ....*....|....*..
gi 1958760896 1289 LRMHRPLMVQTEDQYVF 1305
Cdd:cd14608    238 MRKFRMGLIQTADQLRF 254

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

1108-1312

1.53e-61

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: 209.09 E-value: 1.53e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1108 DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEV 1187
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1188 VLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFIAI 1267
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQ-TGNHPIVVHCSAGAGRTGTFIAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958760896 1268 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14622    160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204

PTPc-N22

cd14602

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...

1083-1313

1.76e-61

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: 210.08 E-value: 1.76e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1083 KNRYNNVLPYDISRVKLSVQTHSTD-DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGR 1161
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDsDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1162 TKCEEYW--PSKQAQDYGDITVAMTSEVVLPEWTIRdfVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 1239
Cdd:cd14602     81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760896 1240 YmkQIPPESPILVHCSAGVGRTGTFIAID---RLIYQ-IENENtVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDI 1313
Cdd:cd14602    159 Y--QEDDSVPICIHCSAGCGRTGVICAIDytwMLLKDgIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

1085-1310

2.48e-61

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: 209.52 E-value: 2.48e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1085 RYNNVLPYDISRVKLSVQT-HSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1163
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRgEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1164 CEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 1243
Cdd:cd14623     81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958760896 1244 iPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1310
Cdd:cd14623    161 -SGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

1101-1312

1.28e-59

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: 204.10 E-value: 1.28e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1101 VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPsKQAQDYGDIT 1180
Cdd:cd14631      7 VEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFK 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1181 VAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQIPPESPILVHCSAGVGR 1260
Cdd:cd14631     86 VTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSF--IRRVKLSNPPSAGPIVVHCSAGAGR 163

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958760896 1261 TGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14631    164 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215

PTPc-N11

cd14605

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...

1079-1310

5.96e-59

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: 203.71 E-value: 5.96e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1079 ENRGKNRYNNVLPYDISRVKLsvqtHSTD------DYINANY-MPGYHS-------KKDFIATQGPLPNTLKDFWRMVWE 1144
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVL----HDGDpnepvsDYINANIiMPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1145 KNVYAIVMLTKCVEQGRTKCEEYWPSKQA-QDYGDITVAMTSEVVLPEWTIRDFVVKNM-QSSESHPLRQFHFTSWPDHG 1222
Cdd:cd14605     77 ENSRVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHG 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1223 VPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENT---VDVYGIVYDLRMHRPLMVQT 1299
Cdd:cd14605    157 VPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQT 236

                          250
                   ....*....|.
gi 1958760896 1300 EDQYVFLNQCV 1310
Cdd:cd14605    237 EAQYRFIYMAV 247

PTPc-N2

cd14607

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...

1060-1305

5.78e-58

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: 200.96 E-value: 5.78e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1060 YEDLKLIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKLSvqtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFW 1139
Cdd:cd14607      4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ---NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1140 RMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD--YGD--ITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHF 1215
Cdd:cd14607     81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1216 TSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR 1293
Cdd:cd14607    161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYR 240

                          250
                   ....*....|..
gi 1958760896 1294 PLMVQTEDQYVF 1305
Cdd:cd14607    241 MGLIQTPDQLRF 252

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

1109-1306

8.33e-58

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: 198.39 E-value: 8.33e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQaQDYGDITVAMTSEVV 1188
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEK-KTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1189 LPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPES----PILVHCSAGVGRTGTF 1264
Cdd:cd14558     80 SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHgrsvPIVVHCSDGSSRTGIF 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958760896 1265 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1306
Cdd:cd14558    160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFL 201

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

1074-1305

8.40e-58

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: 201.42 E-value: 8.40e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1074 AAEIAENRGKNRYNNVLPYDISRVKLSVQTH-STDDYINAN-------YMPGYhskkdfIATQGPLPNTLKDFWRMVWEK 1145
Cdd:cd14609     36 TAQGEANVKKNRNPDFVPYDHARIKLKAESNpSRSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWEN 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1146 NVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPE-WTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVP 1224
Cdd:cd14609    110 GCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIP 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1225 DTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQY 1303
Cdd:cd14609    190 SSTRPLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQF 267


                   ..
gi 1958760896 1304 VF 1305
Cdd:cd14609    268 EF 269

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

1083-1308

1.35e-57

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: 198.60 E-value: 1.35e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1083 KNRYNNVLPYDISRVKLSVQ--THSTDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQ 1159
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKnsNDSLSTYINANYIRGYGGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1160 GRtKCEEYWPSKQAQdYGDITVAMTSEVVLPEWTIRDFVVKnmQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 1239
Cdd:cd14611     82 NE-KCVLYWPEKRGI-YGKVEVLVNSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760896 1240 YMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd14611    158 DRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

1075-1316

5.42e-56

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: 196.43 E-value: 5.42e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1075 AEIAENRGKNRYNNVLPYDISRVKLSVQ-THSTDDYINANYMPGYHSKKD-FIATQGPLPNTLKDFWRMVWEKNVYAIVM 1152
Cdd:cd14610     39 AQREENVQKNRSLAVLPYDHSRIILKAEnSHSHSDYINASPIMDHDPRNPaYIATQGPLPATVADFWQMVWESGCVVIVM 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1153 LTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPE-WTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLI 1231
Cdd:cd14610    119 LTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLL 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1232 NFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1310
Cdd:cd14610    199 DFRRKVNKCYRG--RSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 276


                   ....*.
gi 1958760896 1311 LDIIRA 1316
Cdd:cd14610    277 AEEVNA 282

PTPc-N6

cd14606

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...

1079-1314

8.18e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.

Pssm-ID: 350454 [Multi-domain] Cd Length: 266 Bit Score: 195.10 E-value: 8.18e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1079 ENRGKNRYNNVLPYDISRVKLSVQTHST--DDYINANY-----MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIV 1151
Cdd:cd14606     17 ENKSKNRYKNILPFDHSRVILQGRDSNIpgSDYINANYvknqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1152 MLTKCVEQGRTKCEEYWPSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQSSES-HPLRQFHFTSWPDHGVPDTTDL 1229
Cdd:cd14606     97 MTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPGG 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1230 LINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENT---VDVYGIVYDLRMHRPLMVQTEDQYVFL 1306
Cdd:cd14606    177 VLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFI 256


                   ....*...
gi 1958760896 1307 NQCVLDII 1314
Cdd:cd14606    257 YVAIAQFI 264

PTPc-N4

cd14601

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...

1108-1315

8.53e-55

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: 190.16 E-value: 8.53e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1108 DYINANYM----PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQ-DYGDITVA 1182
Cdd:cd14601      1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSsSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1183 MTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDymKQIPPESPILVHCSAGVGRTG 1262
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958760896 1263 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIR 1315
Cdd:cd14601    159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

1109-1315

2.33e-54

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: 188.42 E-value: 2.33e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS--KQAQDYGDITVAMT 1184
Cdd:cd14596      1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1185 SEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRdYMKQIPPESPILVHCSAGVGRTGTF 1264
Cdd:cd14596     81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKF---IC-YMRKVHNTGPIVVHCSAGIGRAGVL 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958760896 1265 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIR 1315
Cdd:cd14596    157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

1083-1307

3.79e-54

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: 190.07 E-value: 3.79e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1083 KNRYNNVLPYDISRVKLSvqTHSTDD----YINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcV 1157
Cdd:cd14613     28 KNRYKTILPNPHSRVCLT--SPDQDDplssYINANYIRGYGGEeKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN-I 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1158 EQGRTKCEEYWPSKQAQdYGDITVAMTSEVVLPEWTIRDFVVKNmqSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLV 1237
Cdd:cd14613    105 EEMNEKCTEYWPEEQVT-YEGIEITVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEV 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958760896 1238 RDYMKQIPPE-SPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 1307
Cdd:cd14613    182 EEARQQAEPNcGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252

PTPc-N21_14

cd14540

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

1109-1314

3.17e-52

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: 183.04 E-value: 3.17e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS----KQAQDYGDITVA 1182
Cdd:cd14540      1 YINASHitATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggeHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1183 MTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINF----RYLVRDYMKQIP---PESPILVHCS 1255
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeiNSVRRHTNQDVAghnRNPPTLVHCS 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958760896 1256 AGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1314
Cdd:cd14540    161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219

R-PTP-N-N2

cd14546

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...

1109-1310

5.39e-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: 179.18 E-value: 5.39e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANY-------MPGYhskkdfIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITV 1181
Cdd:cd14546      1 YINASTiydhdprNPAY------IATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1182 AMTSEVVLPE-WTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLV-RDYMKQIppeSPILVHCSAGVG 1259
Cdd:cd14546     75 HLVSEHIWCDdYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958760896 1260 RTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1310
Cdd:cd14546    152 RTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

1109-1306

9.53e-51

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: 177.98 E-value: 9.53e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1188
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1189 LPEWTIRDFVVKNM-QSSESHPL-RQFHFTSWPDHG-VPDTTDLLINFRYLVRDYMKQIPpESPILVHCSAGVGRTGTFI 1265
Cdd:cd14556     80 DEDVISRIFRLQNTtRPQEGYRMvQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSG-EGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958760896 1266 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1306
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFC 199

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

1109-1305

8.86e-50

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: 175.26 E-value: 8.86e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGY-HSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTS 1185
Cdd:cd14539      1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1186 EVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPE-SPILVHCSAGVGRTGTF 1264
Cdd:cd14539     81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLqTPIVVHCSSGVGRTGAF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958760896 1265 IAIDRLIYQIENEN-TVDVYGIVYDLRMHRPLMVQTEDQYVF 1305
Cdd:cd14539    161 CLLYAAVQEIEAGNgIPDLPQLVRKMRQQRKYMLQEKEHLKF 202

PTPc_plant_PTP1

cd17658

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...

1109-1305

7.40e-47

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: 166.87 E-value: 7.40e-47

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYM--PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT-KCEEYWPSK--QAQDYGDITVAM 1183
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1184 ----TSEVVLpewTIRDFVVKNMQSSEShPLRQFH--FTSWPDHGVPDTTdllinfrYLVRDYMK---QIPP-ESPILVH 1253
Cdd:cd17658     81 kklkHSQHSI---TLRVLEVQYIESEEP-PLSVLHiqYPEWPDHGVPKDT-------RSVRELLKrlyGIPPsAGPIVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958760896 1254 CSAGVGRTGTFIAIDRLIYQI--ENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1305
Cdd:cd17658    150 CSAGIGRTGAYCTIHNTIRRIleGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203

PTPc-N14

cd14599

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...

1075-1315

1.30e-46

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: 169.41 E-value: 1.30e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1075 AEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKD--FIATQGPLPNTLKDFWRMVWEKNVYAIVM 1152
Cdd:cd14599     33 ATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1153 LTKCVEQGRTKCEEYWP---SKQ-AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTD 1228
Cdd:cd14599    113 VTAEEEGGRSKSHRYWPklgSKHsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQ 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1229 LLINFRYLVRDYMKQIPPES--------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTE 1300
Cdd:cd14599    193 GFLSYLEEIQSVRRHTNSMLdstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTI 272

                          250
                   ....*....|....*
gi 1958760896 1301 DQYVFLNQCVLDIIR 1315
Cdd:cd14599    273 AQYKFVYQVLIQFLK 287

PHA02738

hypothetical protein; Provisional

1073-1305

3.46e-46

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 169.34 E-value: 3.46e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1073 YAAEIAeNRGKNRYNNVLPYDISRVKLSVQtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1152
Cdd:PHA02738    43 FNAEKK-NRKLNRYLDAVCFDHSRVILPAE-RNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVM 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1153 LTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNmQSSESHPLRQFHFTSWPDHGVPDTTDLL 1230
Cdd:PHA02738   121 LCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEF 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1231 INFRYLVRDYMKQIPPES-----------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQT 1299
Cdd:PHA02738   200 LNFVLEVRQCQKELAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFI 279


                   ....*.
gi 1958760896 1300 EDQYVF 1305
Cdd:PHA02738   280 PFQYFF 285

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1070-1306

8.91e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 166.81 E-value: 8.91e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1070 LPKYAAEIaENRGKNRYNNVLPYDISRVKlsvqthSTDDYINANYMPGYhSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 1149
Cdd:COG5599     33 DPQYLQNI-NGSPLNRFRDIQPYKETALR------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPV 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1150 IVMLTKCVE--QGRTKCEEYWPskQAQDYG--DITVAMTSEVVL-PEWTIRDFVVKNMQSS-ESHPLRQFHFTSWPDHGV 1223
Cdd:COG5599    105 LVVLASDDEisKPKVKMPVYFR--QDGEYGkyEVSSELTESIQLrDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGA 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1224 PDTTdLLINFRYLVRDYMK-QIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR-PLMVQT 1299
Cdd:COG5599    183 ISAE-ALKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQT 261


                   ....*..
gi 1958760896 1300 EDQYVFL 1306
Cdd:COG5599    262 SEQLDVL 268

PHA02747

protein tyrosine phosphatase; Provisional

1079-1306

2.77e-45

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 166.33 E-value: 2.77e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1079 ENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVML--TKC 1156
Cdd:PHA02747    50 ENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLtpTKG 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1157 VeQGRTKCEEYW-PSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFR 1234
Cdd:PHA02747   130 T-NGEEKCYQYWcLNEDGNiDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFI 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1235 YLV----RDYMKQIPPE----SPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1306
Cdd:PHA02747   209 KIIdinrKKSGKLFNPKdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFI 288

PHA02742

protein tyrosine phosphatase; Provisional

1079-1311

1.04e-42

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 158.63 E-value: 1.04e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1079 ENRGKNRYNNVLPYDISRVKLSVQThSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVE 1158
Cdd:PHA02742    51 KNMKKCRYPDAPCFDRNRVILKIED-GGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1159 QGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 1236
Cdd:PHA02742   130 DGKEACYPYWMPHERGKatHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1237 VRDYM---------KQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 1307
Cdd:PHA02742   210 VREADlkadvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                   ....
gi 1958760896 1308 QCVL 1311
Cdd:PHA02742   290 FIVL 293

R5-PTP-2

cd14550

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

1109-1306

1.16e-42

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: 154.79 E-value: 1.16e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCveQGRTKCEEYWPSK-QAQDYGDITVAMTSEV 1187
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN--ELNEDEPIYWPTKeKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1188 VLPEW-----TIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLliNFRYLVRDYMKQipPESPILVHCSAGVGRTG 1262
Cdd:cd14550     79 HSCLSneirlIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVF--ELINTVQEWAQQ--RDGPIVVHDRYGGVQAA 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958760896 1263 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1306
Cdd:cd14550    155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

1209-1312

2.25e-41

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 147.51 E-value: 2.25e-41

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  1209 PLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENE-NTVDVYGIVY 1287
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1958760896  1288 DLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

1209-1312

2.25e-41

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: 147.51 E-value: 2.25e-41

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  1209 PLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENE-NTVDVYGIVY 1287
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1958760896  1288 DLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105

PTP_tm

pfam18861

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...

850-980

3.89e-39

Pssm-ID: 465889 Cd Length: 126 Bit Score: 141.97 E-value: 3.89e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  850 VKFSGFEASHGPIKAYAVLLTTGEAG-QPSTDVLKYTYEDFKKGASDTYVTYLIriEEKGQSQGlSEALNYEIDVGNQST 928
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDSLnRPLKEYLNKTYYDWKYKKTDSYLATVT--PNPFTSPR-SSSRSLTVPVGTGSK 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958760896  929 TLGYYNGRLEPLGSYRACVAGFTNITYnlqNDGLINGDESYVSFSPYSEAVS 980
Cdd:pfam18861   78 WQGYCNGPLKPLGSYRFSVAAFTRLEF---DDGLIDGEESYVSFTPFSEPIA 126

PTPc-N21

cd14598

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...

1109-1315

6.28e-37

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: 138.95 E-value: 6.28e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKK--DFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD----YG--DIT 1180
Cdd:cd14598      1 YINASHIKVTVGGKewDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGrfKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1181 VAMTSEVVLpeWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDttDLLINFRYL-----VRDYMKQI----PPESPIL 1251
Cdd:cd14598     81 TRFRTDSGC--YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPE--DLKGFLSYLeeiqsVRRHTNSTidpkSPNPPVL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958760896 1252 VHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIR 1315
Cdd:cd14598    157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220

PHA02746

protein tyrosine phosphatase; Provisional

1079-1305

6.75e-37

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 142.48 E-value: 6.75e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1079 ENRGKNRYNNVLPYDISRVKLSVQTHST--------------------DDYINANYMPGYHSKKDFIATQGPLPNTLKDF 1138
Cdd:PHA02746    50 ENLKKNRFHDIPCWDHSRVVINAHESLKmfdvgdsdgkkievtsednaENYIHANFVDGFKEANKFICAQGPKEDTSEDF 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1139 WRMVWEKNVYAIVMLTKcVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFT 1216
Cdd:PHA02746   130 FKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSElaFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFP 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1217 SWPDHGVPDTTDLLINFRYLVRDYMKQIPPES--------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYD 1288
Cdd:PHA02746   209 DWPDNGIPTGMAEFLELINKVNEEQAELIKQAdndpqtlgPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLK 288

                          250
                   ....*....|....*..
gi 1958760896 1289 LRMHRPLMVQTEDQYVF 1305
Cdd:PHA02746   289 IRKQRHSSVFLPEQYAF 305

R-PTP-Z-2

cd17669

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

1109-1311

3.31e-34

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: 130.50 E-value: 3.31e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCeEYWPSK-QAQDYGDITVAMTSE- 1186
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKdEPINCETFKVTLIAEe 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1187 -VVLP---EWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVP-DTTDLLINfryLVRDymKQIPPESPILVHCSAGVGRT 1261
Cdd:cd17669     80 hKCLSneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELIS---IIKE--EAANRDGPMIVHDEHGGVTA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1262 GTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1311
Cdd:cd17669    155 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

1109-1311

3.72e-33

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: 127.87 E-value: 3.72e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcvEQGRTKCEE-YWPSK-QAQDYGDITVAMTSE 1186
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSReESMNCEAFTVTLISK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1187 VVL-----PEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVP-DTTDLLINF---RYLVRDymkqippeSPILVHCSAG 1257
Cdd:cd17670     79 DRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVikeEALTRD--------GPTIVHDEFG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958760896 1258 VGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1311
Cdd:cd17670    151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

R-PTPc-T-2

cd14634

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...

1109-1312

1.24e-32

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: 126.29 E-value: 1.24e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTkcvEQGRTK-CEEYWPSKQAQDYGDITVAMTSEV 1187
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWPEKTSCCYGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1188 VLPEWTIRDFVVKNMQSSES--HPLRQFHFTSWPDH--GVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGT 1263
Cdd:cd14634     78 IDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrdTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958760896 1264 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14634    158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

R-PTPc-U-2

cd14637

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...

1109-1312

2.81e-32

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: 125.41 E-value: 2.81e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT-KCEEYWPSKQAQDYGDITVAMTSEV 1187
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1188 VLPEWTIRDFVVKNM-QSSESHPL-RQFHFTSW-PDHGVPDTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTF 1264
Cdd:cd14637     81 ADEDIVTRLFRVQNItRLQEGHLMvRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRE-SGEGRTVVHCLNGGGRSGTY 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958760896 1265 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14637    160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207

R-PTPc-K-2

cd14636

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...

1109-1305

4.36e-30

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: 118.97 E-value: 4.36e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKC-VEQGrtkCEEYWPSKQAQDYGDITVAMTSEV 1187
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1188 VLPEWTIRDFVVKNMQSSESHPL--RQFHFTSWPDH-GVPDTTDLLINFRYLVRDYMKQIPP-ESPILVHCSAGVGRTGT 1263
Cdd:cd14636     78 MDCDVISRIFRICNLTRPQEGYLmvQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgEGRTIIHCLNGGGRSGM 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958760896 1264 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1305
Cdd:cd14636    158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199

R-PTPc-M-2

cd14635

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...

1109-1312

1.03e-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: 114.78 E-value: 1.03e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1109 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcVEQGRTkCEEYWPSKQAQDYGDITVAMTSEVV 1188
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWPENGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1189 LPEWTIRDFVVKNMQSSES--HPLRQFHFTSWPDHgvPDTTDLLINFRYLVRDYMKQIPP----ESPILVHCSAGVGRTG 1262
Cdd:cd14635     79 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMY--RDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1263 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1312
Cdd:cd14635    157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206

PTP_YopH-like

cd14559

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...

1084-1306

2.10e-18

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: 85.91 E-value: 2.10e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1084 NRYNNVLpydiSRVKLSVQTHstddyINANYMPgYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1163
Cdd:cd14559      1 NRFTNIQ----TRVSTPVGKN-----LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1164 CEEYWpsKQAQDYGDITVamTSEVVL-----PEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLL-------- 1230
Cdd:cd14559     71 LPPYF--RQSGTYGSVTV--KSKKTGkdelvDGLKADMYNLKITDGNKTITIPVVHVTNWPDHTAISSEGLKeladlvnk 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1231 -----INFRYL-----VRDYMKQIPpespiLVHCSAGVGRTGTFIAIdrlIYQIENENTVDVYGIVYDLRMHR-PLMVQT 1299
Cdd:cd14559    147 saeekRNFYKSkgssaINDKNKLLP-----VIHCRAGVGRTGQLAAA---MELNKSPNNLSVEDIVSDMRTSRnGKMVQK 218


                   ....*..
gi 1958760896 1300 EDQYVFL 1306
Cdd:cd14559    219 DEQLDTL 225

PHA02740

protein tyrosine phosphatase; Provisional

1078-1308

1.40e-14

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 76.16 E-value: 1.40e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1078 AENRGKNRyNNVLP---YDISRVKLsvqtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLT 1154
Cdd:PHA02740    49 AENKAKDE-NLALHitrLLHRRIKL----FNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLIS 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1155 KCVEQgrtKC-EEYWPSKQ--AQDYGDITVAMTSEVVLPEWTIRDFVVKNmQSSESHPLRQFHFTSWPDHGVPDTTDLLI 1231
Cdd:PHA02740   124 RHADK---KCfNQFWSLKEgcVITSDKFQIETLEIIIKPHFNLTLLSLTD-KFGQAQKISHFQYTAWPADGFSHDPDAFI 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1232 NFRYLVRDYMKQIPPES------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1305
Cdd:PHA02740   200 DFFCNIDDLCADLEKHKadgkiaPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVF 279


                   ...
gi 1958760896 1306 LNQ 1308
Cdd:PHA02740   280 CYH 282

FN3

COG3401

Fibronectin type 3 domain [General function prediction only];

169-659

3.24e-11

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 67.72 E-value: 3.24e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  169 LTWKHNDSATSEYKINEGNTLRYTVKNQTSFNITGLSPATSYKFSITLGTVNETSGKP-TYKNITTEPWPVSDLQVAYIG 247
Cdd:COG3401      9 LDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGlGTGGRAGTTSGVAAVAVAAAP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  248 VTQALLAW--SNANGTASYRMQIVELTTNSSGGISDLKPGTHKSLAVQGSNETQHDLWVTE-----GVSDANGTEGSPVA 320
Cdd:COG3401     89 PTATGLTTltGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGvdganASGTTASSVAGAGV 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  321 NISQLHKNSLASADPPSARDPSLTEVLLTELKPDTQYKVTIYSqAADGTEGQPGNKV----FKTNPIQVSDIRAVNISDS 396
Cdd:COG3401    169 VVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAA-TDTGGESAPSNEVsvttPTTPPSAPTGLTATADTPG 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  397 NMTLTWKSNNNESHASftYKIYVAGGSDSINE---TVNETQAVIRGLSSSTLYN--ITVLPFLGQTAGIPGFLQVYTS-- 469
Cdd:COG3401    248 SVTLSWDPVTESDATG--YRVYRSNSGDGPFTkvaTVTTTSYTDTGLTNGTTYYyrVTAVDAAGNESAPSNVVSVTTDlt 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  470 -PRPVSDFRVTNVSLREIGLAWRSNDSE---SFEIF--ITQEGSEKRWNASTGDLSYIVENLKPGTSYQFEIFPRGPNGT 543
Cdd:COG3401    326 pPAAPSGLTATAVGSSSITLSWTASSDAdvtGYNVYrsTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGN 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  544 EGPSQTVVgrtdcSAVTDIRVVSVSTTEIQLEWQNTDSASGYTYHLVLESENGSIKTNSSQKWITVGGLTPGTLYNVTIF 623
Cdd:COG3401    406 ESAPSEEV-----SATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTAT 480

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1958760896  624 PE--VDQMEGNSSSITQYTRPSNVSYIEVNTNTTVAAI 659
Cdd:COG3401    481 TTdtTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAA 518

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

1206-1308

2.07e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 57.29 E-value: 2.07e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1206 ESHPLRQFHFTsWPDHGVPDTTDllinFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDrLIYQ-IENENTVDVyg 1284
Cdd:COG2453     44 EEAGLEYLHLP-IPDFGAPDDEQ----LQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAY-LVLLgLSAEEALAR-- 115

                           90       100
                   ....*....|....*....|....
gi 1958760896 1285 ivydLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:COG2453    116 ----VRAARPGAVETPAQRAFLER 135

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

470-554

3.48e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.42 E-value: 3.48e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  470 PRPVSDFRVTNVSLREIGLAWRSNDSE-----SFEIFITQEGSEKRWNASTG---DLSYIVENLKPGTSYQFEIFPRGPN 541
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpitGYVVEYREKGSGDWKEVEVTpgsETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1958760896  542 GTEGPSQTVVGRT 554
Cdd:cd00063     81 GESPPSESVTVTT 93

PTP_DSP_cys

cd14494

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...

1246-1306

7.04e-07

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: 49.27 E-value: 7.04e-07

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958760896 1246 PESPILVHCSAGVGRTGTFIAIDRLIYQieNENTVDVYGIVYDLRMHRplMVQTEDQYVFL 1306
Cdd:cd14494     55 PGEPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEAVRIVRLIRPGG--IPQTIEQLDFL 111

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

152-233

1.26e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.88 E-value: 1.26e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  152 PSPVFDVEA-VTSPTSVVLTWKHNDSATSE---YKI-------NEGNTLRYTVKNQTSFNITGLSPATSYKFSITLGTVN 220
Cdd:cd00063      1 PSPPTNLRVtDVTSTSVTLSWTPPEDDGGPitgYVVeyrekgsGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1958760896  221 ETSGKPTYKNITT 233
Cdd:cd00063     81 GESPPSESVTVTT 93

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

557-631

1.33e-06

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 47.61 E-value: 1.33e-06

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896   557 SAVTDIRVVSVSTTEIQLEWQNTDSASGYTYHLVLESENGS-------IKTNSSQKWITVGGLTPGTLYNVTIFPEVDQM 629
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREegsewkeVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1958760896   630 EG 631
Cdd:smart00060   82 EG 83

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

470-542

1.76e-06

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 47.22 E-value: 1.76e-06

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896   470 PRPVSDFRVTNVSLREIGLAWRSNDSESFEIFITQ--------EGSEKRWNASTGDLSYIVENLKPGTSYQFEIFPRGPN 541
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGyrveyreeGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    .
gi 1958760896   542 G 542
Cdd:smart00060   81 G 81

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

557-640

2.54e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.11 E-value: 2.54e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  557 SAVTDIRVVSVSTTEIQLEWQNTDSA----SGYTYHLVLESENGSIK---TNSSQKWITVGGLTPGTLYNVTIFPEVDQM 629
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEYREKGSGDWKEvevTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|.
gi 1958760896  630 EGNSSSITQYT 640
Cdd:cd00063     82 ESPPSESVTVT 92

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

382-450

9.57e-06

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 45.30 E-value: 9.57e-06

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958760896   382 PIQVSDIRAVNISDSNMTLTWKSNNNESHASFTYKIYVAGGSDS-----INETVNETQAVIRGLSSSTLYNITV 450
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGsewkeVNVTPSSTSYTLTGLKPGTEYEFRV 74

PTP_VSP_TPTE

cd14510

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...

1219-1265

1.10e-05

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.

Pssm-ID: 350360 [Multi-domain] Cd Length: 177 Bit Score: 47.36 E-value: 1.10e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958760896 1219 PDHGVPdTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFI 1265
Cdd:cd14510     82 DDHNVP-TLDEMLSFTAEVREWMAA-DPKNVVAIHCKGGKGRTGTMV 126

FN3

COG3401

Fibronectin type 3 domain [General function prediction only];

144-447

1.29e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 49.62 E-value: 1.29e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  144 QVVCAGAAPSPVFDVEAV-TSPTSVVLTW-KHNDSATSEYKI-----NEGNTLRYTVKNQTSFNITGLSPATSYKFSIT- 215
Cdd:COG3401    225 SVTTPTTPPSAPTGLTATaDTPGSVTLSWdPVTESDATGYRVyrsnsGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTa 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  216 LGTVNETSGKPTYKNITTE---PWPVSDLQVAYIGVTQALLAWSNA--NGTASYRM-----------QIVELTTNSSGGI 279
Cdd:COG3401    305 VDAAGNESAPSNVVSVTTDltpPAAPSGLTATAVGSSSITLSWTASsdADVTGYNVyrstsgggtytKIAETVTTTSYTD 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  280 SDLKPGTHKSLAVQ----GSNETQHDLWVTEGVSDANGTEGSPVANISQLHKNSLASADPPSARDPSLTEVLLTELKPDT 355
Cdd:COG3401    385 TGLTPGTTYYYKVTavdaAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDT 464

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  356 QYKVTIYS----QAADGTEGQPGNKVFKTNPIQVSDIRAVNISDSNMTLTWKSNNNESHASFTYKIYVAGGSDSINETVN 431
Cdd:COG3401    465 GNAVPFTTtsstVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGD 544

                          330
                   ....*....|....*.
gi 1958760896  432 ETQAVIRGLSSSTLYN 447
Cdd:COG3401    545 VLITDLVSLTTSASSS 560

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

382-461

3.28e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 44.02 E-value: 3.28e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  382 PIQVSDIRAVNISDSNMTLTWKSNNNESHASFTYKIYVAGGSDSINETVN-----ETQAVIRGLSSSTLYNITVLPFLGQ 456
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEvtpgsETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ....*
gi 1958760896  457 TAGIP 461
Cdd:cd00063     81 GESPP 85

fn3

Fibronectin type III domain;

472-536

3.81e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 43.56 E-value: 3.81e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958760896  472 PVSDFRVTNVSLREIGLAWRSNDS-----ESFEIFITQEGSEKRWNASTGDL---SYIVENLKPGTSYQFEIF 536
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDgngpiTGYEVEYRPKNSGEPWNEITVPGtttSVTLTGLKPGTEYEVRVQ 74

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

152-215

5.63e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 42.99 E-value: 5.63e-05

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958760896   152 PSPVFDVEAV-TSPTSVVLTWKH-----NDSATSEYKINEGNTLR-----YTVKNQTSFNITGLSPATSYKFSIT 215
Cdd:smart00060    1 PSPPSNLRVTdVTSTSVTLSWEPppddgITGYIVGYRVEYREEGSewkevNVTPSSTSYTLTGLKPGTEYEFRVR 75

fn3

Fibronectin type III domain;

153-226

6.22e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.79 E-value: 6.22e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  153 SPVFDVEAV-TSPTSVVLTWKHNDSATSE---YKI------NEGNTLRYTV-KNQTSFNITGLSPATSYKFSITlgTVNE 221
Cdd:pfam00041    1 SAPSNLTVTdVTSTSLTVSWTPPPDGNGPitgYEVeyrpknSGEPWNEITVpGTTTSVTLTGLKPGTEYEVRVQ--AVNG 78


                   ....*
gi 1958760896  222 TSGKP 226
Cdd:pfam00041   79 GGEGP 83

COG3979

Chitodextrinase [Carbohydrate transport and metabolism];

162-460

1.04e-04

Chitodextrinase [Carbohydrate transport and metabolism];

Pssm-ID: 443178 [Multi-domain] Cd Length: 369 Bit Score: 46.30 E-value: 1.04e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  162 TSPTSVVLTWkhnDSATS-----EYKINEGNTLRYTVKNQTSFNITGLSPATSYKFSI----TLGTVNETSGKPTYKNIT 232
Cdd:COG3979     14 VTSSSVSLSW---DASTDnvgvtGYDVYRGGDQVATVTGLTAWTVTGLTPGTEYTFTVgacdAAGNVSAASGTSTAMFGG 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  233 TEPWPVSDLQVAYIGVTQAL----LAWSNANGTASYRMQIVELTTNSSGGISDLKPGTHKSLAVQGSNETQHDLWVTEGV 308
Cdd:COG3979     91 SSTTLGSAEGVADTSGNLAAsgafFGVTTPPTPSSTLVVDGTTTVNAAATANGGTGGSGGTTTIITTGVEGGGGSKTAQS 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  309 SDANGTEGSPVANISQLHKNSLASADPPSARDPSLTEVLLTE------LKPDTQYKVTIYSQAADGTEGQPGNKVFKTNP 382
Cdd:COG3979    171 LNAITAAGTAALNGGVVGGADEVLTCSAVKDDGSGGAGAGNTywalntLGVSDTPSGTTATGGTVGITSAYGAGVSGNAA 250

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760896  383 IQVSDIRAVNISDSNMTLTWKSNNNESHASFTYKIYVAGGSDSINETVNETQAVIRGLSSSTLYNITVLPFLGQTAGI 460
Cdd:COG3979    251 VNVNAGFVVGNVGGAAGNTGTTSGTATSDAATNDVGDAAVTGLNDGAANGPTGGYGATGTTVAGAAGVGGTKSGTGAL 328

fn3

Fibronectin type III domain;

642-719

1.43e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 41.63 E-value: 1.43e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  642 PSNVSYIEVNTNTtvAAIQWKNLDAASASY-SYSVLILKAGDGSNVTSR--VRDIPSVTIPGLIPGVSYEVKIFTKIRNT 718
Cdd:pfam00041    3 PSNLTVTDVTSTS--LTVSWTPPPDGNGPItGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   .
gi 1958760896  719 E 719
Cdd:pfam00041   81 E 81

PTPlike_phytase

pfam14566

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...

1184-1271

1.56e-04

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.

Pssm-ID: 464208 [Multi-domain] Cd Length: 157 Bit Score: 43.45 E-value: 1.56e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1184 TSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSwPDHGVPDTTDllinFRYLVrDYMKQIPPESPILVHCSAGVGRTGT 1263
Cdd:pfam14566   75 TVVDVWESDVQTPEEVYERLKAEGPGVDYRRIPI-TDEKAPLEED----FDALI-SIVKDAPEDTALVFNCQMGRGRTTT 148


                   ....*...
gi 1958760896 1264 FIAIDRLI 1271
Cdd:pfam14566  149 AMVIADLV 156

PTP_PTEN-like

cd14497

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...

1218-1266

1.68e-04

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.

Pssm-ID: 350347 [Multi-domain] Cd Length: 160 Bit Score: 43.34 E-value: 1.68e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958760896 1218 WPDHGVPdTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFIA 1266
Cdd:cd14497     68 FPDHHPP-PLGLLLEIVDDIDSWLSE-DPNNVAVVHCKAGKGRTGTVIC 114

CDKN3-like

cd14505

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...

1206-1308

1.97e-04

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: 43.41 E-value: 1.97e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1206 ESHPLRQFHFtSWPDHGVPDTTDlliNFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAidRLIYQIENENTVDVygI 1285
Cdd:cd14505     69 QQAGITWHHL-PIPDGGVPSDIA---QWQELLEELLSALENGKKVLIHCKGGLGRTGLIAA--CLLLELGDTLDPEQ--A 140

                           90       100
                   ....*....|....*....|...
gi 1958760896 1286 VYDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd14505    141 IAAVRALRPGAIQTPKQENFLHQ 163

fn3

Fibronectin type III domain;

557-634

2.57e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 41.25 E-value: 2.57e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896  557 SAVTDIRVVSVSTTEIQLEWQNTDSASGY--TYHLVLESENG-----SIKTNSSQKWITVGGLTPGTLYNVTIFPEVDQM 629
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPitGYEVEYRPKNSgepwnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1958760896  630 EGNSS 634
Cdd:pfam00041   81 EGPPS 85

PTP_PTPDC1

cd14506

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...

1213-1306

3.69e-04

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.

Pssm-ID: 350356 [Multi-domain] Cd Length: 206 Bit Score: 43.49 E-value: 3.69e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1213 FHFTSWPDHGVPDTTDLLINFRylVRDYMKQipPESPILVHCSAGVGRTGTFIAIdRLIYqIENENTVDVYGIVydlRMH 1292
Cdd:cd14506     79 FYNFGWKDYGVPSLTTILDIVK--VMAFALQ--EGGKVAVHCHAGLGRTGVLIAC-YLVY-ALRMSADQAIRLV---RSK 149

                           90
                   ....*....|....
gi 1958760896 1293 RPLMVQTEDQYVFL 1306
Cdd:cd14506    150 RPNSIQTRGQVLCV 163

TpbA-like

cd14529

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...

1249-1288

9.00e-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: 9.00e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958760896 1249 PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYD 1288
Cdd:cd14529     91 PVLIHCKHGKDRTGLVSALYRIVYGGSKEEANEDYRLSNR 130

DUSP23

cd14504

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...

1249-1308

1.23e-03

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.

Pssm-ID: 350354 [Multi-domain] Cd Length: 142 Bit Score: 40.72 E-value: 1.23e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1249 PILVHCSAGVGRTGTFIAidrlIYQIENENTVDVYGIVyDLRMHRPLMVQTEDQYVFLNQ 1308
Cdd:cd14504     84 AVLVHCLAGKGRTGTMLA----CYLVKTGKISAVDAIN-EIRRIRPGSIETSEQEKFVIQ 138

PTPLP-like

cd14495

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...

1214-1292

2.07e-03

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.

Pssm-ID: 350345 Cd Length: 278 Bit Score: 41.59 E-value: 2.07e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760896 1214 HFtsWPDhgvPDTTDLLINFrylvrdyMKQIPPESPILVHCSAGVGRTGTFIAI-DRLIyqieNENTVDVYGIVYdlRMH 1292
Cdd:cd14495    165 HV--WPD---DEEIDAFVAF-------YRSLPADAWLHFHCRAGKGRTTTFMVMyDMLK----NPKDVSFDDIIA--RQY 226

fn3

Fibronectin type III domain;

384-450

2.33e-03

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 38.55 E-value: 2.33e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958760896  384 QVSDIRAVNISDSNMTLTWKSNNNESHASFTYKIYVA---GGSDSINETV--NETQAVIRGLSSSTLYNITV 450
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRpknSGEPWNEITVpgTTTSVTLTGLKPGTEYEVRV 73

DSPc

pfam00782

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...

1249-1290

2.45e-03

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.

Pssm-ID: 395632 [Multi-domain] Cd Length: 127 Bit Score: 39.55 E-value: 2.45e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958760896 1249 PILVHCSAGVGRTGTFIAidRLIYQIENENTVDVYGIVYDLR 1290
Cdd:pfam00782   71 KVLVHCQAGISRSATLII--AYLMKTRNLSLNEAYSFVKERR 110

FN3