NCBI Conserved Domain Search

Fibronectin type III domain;

162-222

8.22e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 50.88 E-value: 8.22e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915935   162 VSPTSVLLTWKHNDSGAS-------ECRIENKMESNLTFPV-KNQTSCNITGLSPGTSYTFSIISVTTN 222
Cdd:pfam00041   11 VTSTSLTVSWTPPPDGNGpitgyevEYRPKNSGEPWNEITVpGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

Name

Accession

Description

Interval

E-value

R-PTPc-J

cd14615

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

1083-1311

9.40e-171

Pssm-ID: 350463 [Multi-domain] Cd Length: 229 Bit Score: 507.05 E-value: 9.40e-171

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1083 NRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1162
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1163 CEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 1242
Cdd:cd14615    81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915935 1243 IPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14615   161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1054-1311

1.56e-120

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 375.46 E-value: 1.56e-120

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935   1054 GFAEEYEDLKLIGISLPKYT-AEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 1132
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935   1133 TLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLR 1210
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935   1211 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRM 1290
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQST--STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 568915935   1291 HRPLMVQTEDQYVFLNQCVLD 1311
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1079-1311

1.04e-110

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 347.69 E-value: 1.04e-110

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  1079 NRGKNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQ 1158
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  1159 GRTKCEEYWPSK--QAQDYGDITVAMTSEV-VLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 1235
Cdd:pfam00102   80 GREKCAQYWPEEegESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915935  1236 VRDYmKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:pfam00102  160 VRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

PHA02738

hypothetical protein; Provisional

1072-1304

2.54e-46

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 169.72 E-value: 2.54e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1072 YTAEIAeNRGKNRYNNVLPYDISRVKLSVQtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1151
Cdd:PHA02738   43 FNAEKK-NRKLNRYLDAVCFDHSRVILPAE-RNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVM 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1152 LTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNmQNSESHPLRQFHFTSWPDHGVPDTTDLL 1229
Cdd:PHA02738  121 LCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEF 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1230 INFRYLVRDYMKQIPPES-----------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQT 1298
Cdd:PHA02738  200 LNFVLEVRQCQKELAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFI 279


                  ....*.
gi 568915935 1299 EDQYVF 1304
Cdd:PHA02738  280 PFQYFF 285

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1069-1305

4.78e-45

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 164.49 E-value: 4.78e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1069 LPKYTAEIaENRGKNRYNNVLPYDISRVKlsvqthSTDDYINANYMPGYhSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 1148
Cdd:COG5599    33 DPQYLQNI-NGSPLNRFRDIQPYKETALR------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1149 IVMLTKCVE--QGRTKCEEYWPskQAQDYG--DITVAMTSEVVL-PEWTIRDFVVKNMQNS-ESHPLRQFHFTSWPDHGV 1222
Cdd:COG5599   105 LVVLASDDEisKPKVKMPVYFR--QDGEYGkyEVSSELTESIQLrDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1223 PDTTdLLINFRYLVRDYMK-QIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR-PLMVQT 1298
Cdd:COG5599   183 ISAE-ALKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQT 261


                  ....*..
gi 568915935 1299 EDQYVFL 1305
Cdd:COG5599   262 SEQLDVL 268

PTP_tm

pfam18861

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

849-979

1.40e-38

Pssm-ID: 465889 Cd Length: 126 Bit Score: 140.05 E-value: 1.40e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935   849 VKFSGFEASHGPIKAYAVILTTGE-AAQPSADVLKYTYEDFKRGASDTYVTYLIriEEKGQSQGlSEVLNYEIDVGNQST 927
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDsLNRPLKEYLNKTYYDWKYKKTDSYLATVT--PNPFTSPR-SSSRSLTVPVGTGSK 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568915935   928 TLGYYNGRLEPLGSYRACVAGFTNITYnlqNDGLINGDESYVSFSPYSEAVF 979
Cdd:pfam18861   78 WQGYCNGPLKPLGSYRFSVAAFTRLEF---DDGLIDGEESYVSFTPFSEPIA 126

FN3

COG3401

Fibronectin type 3 domain [General function prediction only];

199-699

4.13e-10

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 64.25 E-value: 4.13e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  199 TSCNITGLSPGTSYTFSIISVTTNETLNKTITTEPWPVSDLHVTSVGVTQARLTWSNANGTASYRMLIEELTTHSSVNIS 278
Cdd:COG3401    48 TKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  279 GLKPGTNNSFAFPESNETQADFAVAEEVPADANGTKRIPVTNLSQLHKNSLVSVDPPSGQDPSLTEILLTDLKPDTQYNA 358
Cdd:COG3401   128 ATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYY 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  359 TIYSQAANGtEGQPRNKVFKTNSTQV----SDVRAMNISASSMTLTWKSNYDGSRTS-IVYKIHVAGGTHSVNQTVNKTE 433
Cdd:COG3401   208 RVAATDTGG-ESAPSNEVSVTTPTTPpsapTGLTATADTPGSVTLSWDPVTESDATGyRVYRSNSGDGPFTKVATVTTTS 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  434 AIILGLSSSTLYN--ITVHPFLGQTEGTPGFLQVYTS---PDQVSDFRVTNVSTRAIGLAWRSNDS---KSFEIFIKQDG 505
Cdd:COG3401   287 YTDTGLTNGTTYYyrVTAVDAAGNESAPSNVVSVTTDltpPAAPSGLTATAVGSSSITLSWTASSDadvTGYNVYRSTSG 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  506 GEKHR--NASTGNQSYMVEDLKPGTSYHFEIIPRGPDGTEGLSS----------TVNGSTDPSAVTDIRVVNISTTEMQL 573
Cdd:COG3401   367 GGTYTkiAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSeevsattasaASGESLTASVDAVPLTDVAGATAAAS 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  574 EWQNTDDASGYTYHLVLESKSGSIirTNSSQKWITVGSLTPGTLYNVTIFPEVDQIQGISNSITQYTrPSSVSHIEVNTT 653
Cdd:COG3401   447 AASNPGVSAAVLADGGDTGNAVPF--TTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV-IGASAAAAVGGA 523

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 568915935  654 TTTAAIRWKNEDAASASYAYSVLILKTGDGSNVTSNFTKDPSILIP 699
Cdd:COG3401   524 PDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSG 569

fn3

Fibronectin type III domain;

162-222

8.22e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 50.88 E-value: 8.22e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915935   162 VSPTSVLLTWKHNDSGAS-------ECRIENKMESNLTFPV-KNQTSCNITGLSPGTSYTFSIISVTTN 222
Cdd:pfam00041   11 VTSTSLTVSWTPPPDGNGpitgyevEYRPKNSGEPWNEITVpGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

555-622

1.10e-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: 1.10e-06

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915935    555 PSAVTDIRVVNISTTEMQLEWQ--NTDDASGYTYHLVLESKSGS----IIRTNSSQKWITVGSLTPGTLYNVTI 622
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEppPDDGITGYIVGYRVEYREEGsewkEVNVTPSSTSYTLTGLKPGTEYEFRV 74

FN3

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

152-220

1.67e-06

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: 47.49 E-value: 1.67e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915935  152 PNPIFDIEA-VVSPTSVLLTWKHNDSGAS-------ECRIENKME-SNLTFPVKNQTSCNITGLSPGTSYTFSIISVT 220
Cdd:cd00063     1 PSPPTNLRVtDVTSTSVTLSWTPPEDDGGpitgyvvEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

FN3

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

555-640

2.26e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.11 E-value: 2.26e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  555 PSAVTDIRVVNISTTEMQLEWQNTDDA----SGYT--YHLVLESKSGSIIRTNSSQKWITVGSLTPGTLYNVTIFPEVDQ 628
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpiTGYVveYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 568915935  629 IQG-ISNSITQYT 640
Cdd:cd00063    81 GESpPSESVTVTT 93

fn3

Fibronectin type III domain;

383-460

2.49e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 2.49e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935   383 QVSDVRAMNISASSMTLTWKSNYDGSRTSIVYKIHVA---GGTHSVNQTV--NKTEAIILGLSSSTLYNITVHPFLGQTE 457
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRpknSGEPWNEITVpgTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568915935   458 GTP 460
Cdd:pfam00041   82 GPP 84

FN3

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

152-220

5.01e-06

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 46.07 E-value: 5.01e-06

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915935    152 PNPIFDIEAV-VSPTSVLLTWKHNDSGAS-----ECRIENKMESNLTFPVK---NQTSCNITGLSPGTSYTFSIISVT 220
Cdd:smart00060    1 PSPPSNLRVTdVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNvtpSSTSYTLTGLKPGTEYEFRVRAVN 78

Name

Accession

Description

Interval

E-value

R-PTPc-J

cd14615

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

1083-1311

9.40e-171

Pssm-ID: 350463 [Multi-domain] Cd Length: 229 Bit Score: 507.05 E-value: 9.40e-171

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1083 NRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1162
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1163 CEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 1242
Cdd:cd14615    81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915935 1243 IPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14615   161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

R3-PTPc

cd14548

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

1084-1307

7.21e-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: 414.83 E-value: 7.21e-136

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1084 RYNNVLPYDISRVKLSVQT-HSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1162
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINeEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1163 CEEYWPSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQnsESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMK 1241
Cdd:cd14548    81 CDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915935 1242 QipPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14548   159 Q--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1054-1311

1.56e-120

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 375.46 E-value: 1.56e-120

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935   1054 GFAEEYEDLKLIGISLPKYT-AEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 1132
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935   1133 TLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLR 1210
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935   1211 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRM 1290
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQST--STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 568915935   1291 HRPLMVQTEDQYVFLNQCVLD 1311
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1079-1311

1.04e-110

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 347.69 E-value: 1.04e-110

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  1079 NRGKNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQ 1158
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  1159 GRTKCEEYWPSK--QAQDYGDITVAMTSEV-VLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 1235
Cdd:pfam00102   80 GREKCAQYWPEEegESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915935  1236 VRDYmKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:pfam00102  160 VRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

R-PTPc-H

cd14619

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

1083-1313

7.37e-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: 329.16 E-value: 7.37e-104

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1083 NRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1161
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKpIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1162 KCEEYWP-SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYM 1240
Cdd:cd14619    81 KCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915935 1241 KQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1313
Cdd:cd14619   161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

R-PTPc-B

cd14617

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

1083-1307

7.65e-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: 7.65e-104

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1083 NRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1161
Cdd:cd14617     1 NRYNNILPYDSTRVKLSnVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1162 KCEEYWPSKQ-AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPL-RQFHFTSWPDHGVPDTTDLLINFRYLVRDY 1239
Cdd:cd14617    81 KCDHYWPADQdSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLvRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915935 1240 MKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14617   161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

PTPc

cd00047

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

1108-1307

6.42e-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: 6.42e-98

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSE 1185
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPleYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1186 VVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIA 1265
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK--PNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915935 1266 IDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd00047   159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-LAR-1

cd14553

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

1079-1313

3.90e-94

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: 302.78 E-value: 3.90e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1079 NRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVE 1157
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQpIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1158 QGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVR 1237
Cdd:cd14553    83 RSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915935 1238 DYMkqiPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1313
Cdd:cd14553   163 ACN---PPDAgPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236

R-PTPc-V

cd14618

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

1083-1310

1.55e-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: 1.55e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1083 NRYNNVLPYDISRVKLSV---QTHStdDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQG 1159
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQlggEPHS--DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1160 RTKCEEYWPSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 1238
Cdd:cd14618    79 RVLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568915935 1239 YMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1310
Cdd:cd14618   159 HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

R-PTPc-O

cd14614

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

1069-1310

1.35e-91

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: 296.03 E-value: 1.35e-91

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1069 LPKYTAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVY 1147
Cdd:cd14614     2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLvSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1148 AIVMLTKCVEQGRTKCEEYWP-SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKnmQNSESHPLRQFHFTSWPDHGVP--D 1224
Cdd:cd14614    82 IIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPtaN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1225 TTDLLINFRYLVRDymKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1304
Cdd:cd14614   160 AAESILQFVQMVRQ--QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                  ....*.
gi 568915935 1305 LNQCVL 1310
Cdd:cd14614   238 IHQCVQ 243

R5-PTPc-1

cd14549

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

1108-1305

8.61e-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: 286.17 E-value: 8.61e-89

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1187
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1188 LPEWTIRDFVVKNMQNSESHP------LRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRT 1260
Cdd:cd14549    81 LATYTVRTFSLKNLKLKKVKGrsservVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPPGAgPIVVHCSAGVGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915935 1261 GTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1305
Cdd:cd14549   158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202

PTPc-N9

cd14543

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

1054-1304

2.27e-83

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: 273.86 E-value: 2.27e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1054 GFAEEYEDLKLigiSLPKYTAEIAE---NRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGP 1129
Cdd:cd14543     4 GIYEEYEDIRR---EPPAGTFLCSLapaNQEKNRYGDVLCLDQSRVKLPkRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1130 LPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQ--AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESH 1207
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1208 PLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQI-----------PPESPILVHCSAGVGRTGTFIAIDRLIYQIENE 1276
Cdd:cd14543   161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                         250       260
                  ....*....|....*....|....*...
gi 568915935 1277 NTVDVYGIVYDLRMHRPLMVQTEDQYVF 1304
Cdd:cd14543   241 GTLNVMQTVRRMRTQRAFSIQTPDQYYF 268

R-PTPc-F-1

cd14626

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

1045-1311

5.27e-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: 259.20 E-value: 5.27e-78

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1045 KKQQADSNCGFAEEYEDLKlIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDF 1123
Cdd:cd14626     8 ERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILtSVDGVPGSDYINANYIDGYRKQNAY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1124 IATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQN 1203
Cdd:cd14626    87 IATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1204 SESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVY 1282
Cdd:cd14626   167 SEKREVRQFQFMAWPDHGVPEYPTPILAF---LRRVKACNPPDAgPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIY 243

                         250       260
                  ....*....|....*....|....*....
gi 568915935 1283 GIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14626   244 GHVTCMRSQRNYMVQTEDQYIFIHEALLE 272

PTPc-KIM

cd14547

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

1083-1307

1.75e-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: 252.70 E-value: 1.75e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1083 NRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEqGR 1160
Cdd:cd14547     1 NRYKTILPNEHSRVCLpSVDDDPLSSYINANYIRGYDGEeKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1161 TKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNmqNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYM 1240
Cdd:cd14547    80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEAR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915935 1241 KQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14547   158 QTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

R-PTPc-G-1

cd17667

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

1055-1313

8.40e-76

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: 252.65 E-value: 8.40e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1055 FAEEYEDLKLIGISLpKYTAEIA---ENRGKNRYNNVLPYDISRVKLSV-----QTHStdDYINANYMPGYHSKKDFIAT 1126
Cdd:cd17667     1 FSEDFEEVQRCTADM-NITAEHSnhpDNKHKNRYINILAYDHSRVKLRPlpgkdSKHS--DYINANYVDGYNKAKAYIAT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1127 QGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQ---N 1203
Cdd:cd17667    78 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1204 SESHP--------LRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIEN 1275
Cdd:cd17667   158 QKGNPkgrqnertVIQYHYTQWPDMGVPEYALPVLTF--VRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKD 235

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568915935 1276 ENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1313
Cdd:cd17667   236 KSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273

R-PTP-LAR-2

cd14554

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

1074-1310

1.35e-75

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: 250.52 E-value: 1.35e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1074 AEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVML 1152
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQpIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1153 TKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINF 1232
Cdd:cd14554    81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915935 1233 RYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1310
Cdd:cd14554   161 IGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238

R-PTPc-T-1

cd14630

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

1078-1311

2.92e-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: 249.56 E-value: 2.92e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1078 ENRGKNRYNNVLPYDISRVKLSV---QTHStdDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTK 1154
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLldgDPHS--DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1155 CVEQGRTKCEEYWPSkQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFry 1234
Cdd:cd14630    80 LVEVGRVKCVRYWPD-DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF-- 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915935 1235 lVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14630   157 -VRQVKFLNPPDAgPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233

R-PTPc-Q

cd14616

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

1083-1307

1.69e-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: 1.69e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1083 NRYNNVLPYDISRVKLSVQTHST-DDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1161
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1162 KCEEYWP--SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKnmQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRdy 1239
Cdd:cd14616    81 RCHQYWPedNKPVTVFGDIVITKLMEDVQIDWTIRDLKIE--RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR-- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915935 1240 MKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14616   157 ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

R-PTPc-M-1

cd14633

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

1054-1311

1.85e-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: 243.03 E-value: 1.85e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1054 GFAEEYEDLkLIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 1132
Cdd:cd14633    16 GFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLqPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1133 TLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSkQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQF 1212
Cdd:cd14633    95 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1213 HFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMH 1291
Cdd:cd14633   174 HFTGWPDHGVPYHATGLLGF---VRQVKSKSPPNAgPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSR 250

                         250       260
                  ....*....|....*....|
gi 568915935 1292 RPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14633   251 RVNMVQTEEQYVFIHDAILE 270

R-PTPc-D-1

cd14624

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

1043-1313

7.71e-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: 241.94 E-value: 7.71e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1043 YFKKQQADSNCGFAEEYEDLKlIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKK 1121
Cdd:cd14624    12 HIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSaIEGIPGSDYINANYIDGYRKQN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1122 DFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNM 1201
Cdd:cd14624    91 AYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKN 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1202 QNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVD 1280
Cdd:cd14624   171 GSSEKREVRQFQFTAWPDHGVPEHPTPFLAF---LRRVKTCNPPDAgPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVD 247

                         250       260       270
                  ....*....|....*....|....*....|...
gi 568915935 1281 VYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1313
Cdd:cd14624   248 IYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280

R-PTPc-S-1

cd14625

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

1035-1313

3.34e-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: 239.99 E-value: 3.34e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1035 IRVENFEAYFKKQQADSNCGFAEEYEDLKlIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANY 1113
Cdd:cd14625     4 IPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILqPIEGIMGSDYINANY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1114 MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTI 1193
Cdd:cd14625    83 IDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFCV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1194 RDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQ 1272
Cdd:cd14625   163 RTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAF---LRRVKTCNPPDAgPIVVHCSAGVGRTGCFIVIDAMLER 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 568915935 1273 IENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1313
Cdd:cd14625   240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280

R-PTPc-A-1

cd14621

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

1030-1311

1.07e-69

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: 236.07 E-value: 1.07e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1030 KKSKLIRVENFEAYFKKQQADSNCGFAEEYEDLKLIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDY 1108
Cdd:cd14621     3 RKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLtPVEGVPDSDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1109 INANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVL 1188
Cdd:cd14621    83 INASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1189 PEWTIRDFVVKNMQN-SESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPpeSPILVHCSAGVGRTGTFI 1264
Cdd:cd14621   163 VDYTVRKFCIQQVGDvTNKKPQRlitQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYA--GAIVVHCSAGVGRTGTFI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568915935 1265 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14621   241 VIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287

R-PTPc-typeIIb-1

cd14555

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

1108-1311

1.30e-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: 232.11 E-value: 1.30e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPsKQAQDYGDITVAMTSEVV 1187
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1188 LPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAI 1266
Cdd:cd14555    80 LAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGF---IRRVKASNPPSAgPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915935 1267 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14555   157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201

R-PTPc-C-1

cd14557

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

1108-1307

7.14e-69

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: 230.10 E-value: 7.14e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS--KQAQDYGDITVAMTSE 1185
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1186 VVLPEWTIRDFVVKNMQNSES-HPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIppESPILVHCSAGVGRTGTFI 1264
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFF--SGPIVVHCSAGVGRTGTYI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568915935 1265 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14557   159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

PTP_fungal

cd18533

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

1108-1305

4.84e-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: 4.84e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYM-PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD-YGDITVAM--T 1183
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGeYGDLTVELvsE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1184 SEVVLPEWTIRDFVVKnMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTF 1263
Cdd:cd18533    81 EENDDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915935 1264 IAIDRLIYQIEN--------ENTVD-VYGIVYDLRMHRPLMVQTEDQYVFL 1305
Cdd:cd18533   160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFL 210

R-PTPc-E-1

cd14620

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

1085-1311

1.14e-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: 224.82 E-value: 1.14e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1085 YNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKC 1163
Cdd:cd14620     1 YPNILPYDHSRVILSqLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1164 EEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVrdym 1240
Cdd:cd14620    81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRlvtQLHFTSWPDFGVPFTPIGMLKFLKKV---- 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915935 1241 KQIPP--ESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14620   157 KSVNPvhAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

PTPc-N11_6

cd14544

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

1079-1305

1.94e-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: 1.94e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1079 NRGKNRYNNVLPYDISRVKLSVQTHST--DDYINANYM-----PGYHSK--KDFIATQGPLPNTLKDFWRMVWEKNVYAI 1149
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVpgSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1150 VMLTKCVEQGRTKCEEYWPSK-QAQDYGDITVAMTSEVVLPEWTIRDFVVKNM-QNSESHPLRQFHFTSWPDHGVPDTTD 1227
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEgMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1228 LLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN---TVDVYGIVYDLRMHRPLMVQTEDQYVF 1304
Cdd:cd14544   161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                  .
gi 568915935 1305 L 1305
Cdd:cd14544   241 I 241

R-PTPc-U-1

cd14632

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

1108-1311

2.58e-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: 2.58e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPsKQAQDYGDITVAMTSEVV 1187
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1188 LPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAI 1266
Cdd:cd14632    80 LAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAF---IRRVKASTPPDAgPVVVHCSAGAGRTGCYIVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915935 1267 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14632   157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201

R-PTP-F-2

cd14629

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

1073-1313

3.32e-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: 225.76 E-value: 3.32e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1073 TAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1151
Cdd:cd14629    47 SANLPCNKFKNRLVNIMPYELTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1152 LTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLIN 1231
Cdd:cd14629   127 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1232 FRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14629   207 FIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286


                  ..
gi 568915935 1312 II 1313
Cdd:cd14629   287 YL 288

R-PTP-S-2

cd14627

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

1073-1313

4.20e-66

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

Pssm-ID: 350475 [Multi-domain] Cd Length: 290 Bit Score: 225.77 E-value: 4.20e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1073 TAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1151
Cdd:cd14627    47 SANLPCNKFKNRLVNIMPYETTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1152 LTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLIN 1231
Cdd:cd14627   127 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1232 FRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14627   207 FIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286


                  ..
gi 568915935 1312 II 1313
Cdd:cd14627   287 YL 288

R-PTP-D-2

cd14628

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

1035-1313

6.64e-66

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: 225.00 E-value: 6.64e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1035 IRVENFEAYFKK----QQADSNCGFAEEYEDLKLIGISLPKY-TAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDY 1108
Cdd:cd14628     3 VPARNLYAYIQKltqiETGENVTGMELEFKRLASSKAHTSRFiSANLPCNKFKNRLVNIMPYESTRVCLQpIRGVEGSDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1109 INANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVL 1188
Cdd:cd14628    83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1189 PEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDR 1268
Cdd:cd14628   163 PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSI 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 568915935 1269 LIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1313
Cdd:cd14628   243 VLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287

R-PTPc-Z-1

cd17668

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

1108-1306

9.53e-66

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: 221.39 E-value: 9.53e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1187
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1188 LPEWTIRDFVVKNMQ--------NSESHPLRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQIPPESPILVHCSAGVGR 1259
Cdd:cd17668    81 LAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTF--VRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568915935 1260 TGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 1306
Cdd:cd17668   159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205

PTPc-N20_13

cd14538

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

1108-1313

3.44e-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: 219.55 E-value: 3.44e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYM--PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS---KQAQDYGDITVAM 1182
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1183 TSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRdYMKQIPPESPILVHCSAGVGRTGT 1262
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRF---IR-YMRRIHNSGPIVVHCSAGIGRTGV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915935 1263 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1313
Cdd:cd14538   157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

PTPc-N12

cd14604

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

1070-1316

9.00e-65

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: 222.12 E-value: 9.00e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1070 PKYTAEIAENRGKNRYNNVLPYDISRVKLSVQTHSTD-DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 1148
Cdd:cd14604    48 PTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDsDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1149 IVMLTKCVEQGRTKCEEYWP--SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKnMQNsESHPLRQFHFTSWPDHGVPDTT 1226
Cdd:cd14604   128 IVMACREFEMGRKKCERYWPlyGEEPMTFGPFRISCEAEQARTDYFIRTLLLE-FQN-ETRRLYQFHYVNWPDHDVPSSF 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1227 DLLINFRYLVRDYmkQIPPESPILVHCSAGVGRTGTFIAID---RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYV 1303
Cdd:cd14604   206 DSILDMISLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYE 283

                         250
                  ....*....|...
gi 568915935 1304 FLNQCVLDIIRAQ 1316
Cdd:cd14604   284 LVHRAIAQLFEKQ 296

PTPc-N22_18_12

cd14542

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

1108-1307

3.14e-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: 216.52 E-value: 3.14e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSE 1185
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1186 vvlpEWTIRDFVVKNMQ---NSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYmkQIPPESPILVHCSAGVGRTGT 1262
Cdd:cd14542    81 ----KRVGPDFLIRTLKvtfQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568915935 1263 FIAIDR----LIYQIENENtVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14542   155 ICAIDYvwnlLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202

R-PTPc-A-E-2

cd14552

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

1108-1309

4.10e-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: 4.10e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1187
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1188 LPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFIAID 1267
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQ-SGNHPITVHCSAGAGRTGTFCALS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915935 1268 RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1309
Cdd:cd14552   160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

PTPc-N3

cd14600

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

1074-1314

3.57e-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: 216.64 E-value: 3.57e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1074 AEIAENRGKNRYNNVLPYDISRVKLsvqtHSTDDYINANYM----PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAI 1149
Cdd:cd14600    35 AKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1150 VMLTKCVEQGRTKCEEYWPSKQ-AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDL 1228
Cdd:cd14600   111 VMLTTLTERGRTKCHQYWPDPPdVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1229 LINFRYLVRDymKQIPPEsPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 1308
Cdd:cd14600   191 FLEFVNYVRS--KRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267


                  ....*.
gi 568915935 1309 VLDIIR 1314
Cdd:cd14600   268 ILRVYE 273

PTPc-N3_4

cd14541

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

1107-1310

8.99e-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: 212.96 E-value: 8.99e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1107 DYINANY----MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS-KQAQDYGDITVA 1181
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1182 MTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRdyMKQIPPESPILVHCSAGVGRTG 1261
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR--QNRVGMVEPTVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568915935 1262 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1310
Cdd:cd14541   159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207

PTPc-N1_2

cd14545

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

1082-1304

1.26e-62

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: 213.41 E-value: 1.26e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1082 KNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1161
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDND-YINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1162 KCEEYWPSKQAQDYG----DITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVR 1237
Cdd:cd14545    80 KCAQYWPQGEGNAMIfedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915935 1238 DYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENT--VDVYGIVYDLRMHRPLMVQTEDQYVF 1304
Cdd:cd14545   160 ESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228

PTPc-N18

cd14603

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

1078-1309

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 568915935 1078 ENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCV 1156
Cdd:cd14603    29 ENVKKNRYKDILPYDQTRVILSlLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1157 EQGRTKCEEYWPSKQAQ-DYGDITVAMTSEVVL-PEWTIRDFVVKNMQnsESHPLRQFHFTSWPDHGVPDTTDLLINFRY 1234
Cdd:cd14603   109 EMGKKKCERYWAQEQEPlQTGPFTITLVKEKRLnEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPDSPDCMLAMIE 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915935 1235 LVRDYMKQIPpeSPILVHCSAGVGRTGTFIAID---RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1309
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; ...

1108-1307

1.94e-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: 1.94e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1187
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1188 LPEWTIRDFVV-KNMQNSESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVrdyMKQIPPES-PILVHCSAGVGRTGT 1262
Cdd:cd14551    81 LVDYTTRKFCIqKVNRGIGEKRVRlvtQFHFTSWPDFGVPFTPIGMLKFLKKV---KSANPPRAgPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915935 1263 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

PTPc-N13

cd14597

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

1078-1313

2.85e-62

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: 212.38 E-value: 2.85e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1078 ENRGKNRYNNVLPYDISRVKLSVQthstDDYINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKC 1155
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGDE----GGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1156 VEQGRTKCEEYWP-----SKQAQDYGDITVAMTSEvvLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLI 1230
Cdd:cd14597    78 VEGGKIKCQRYWPeilgkTTMVDNRLQLTLVRMQQ--LKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1231 NFRylvrDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1310
Cdd:cd14597   156 TFI----SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231


                  ...
gi 568915935 1311 DII 1313
Cdd:cd14597   232 YVL 234

PTPc-N22

cd14602

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

1082-1312

4.64e-62

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: 211.62 E-value: 4.64e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1082 KNRYNNVLPYDISRVKLSVQTHSTD-DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGR 1160
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDsDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1161 TKCEEYW--PSKQAQDYGDITVAMTSEVVLPEWTIRdfVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 1238
Cdd:cd14602    81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915935 1239 YmkQIPPESPILVHCSAGVGRTGTFIAID---RLIYQ-IENENtVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDI 1312
Cdd:cd14602   159 Y--QEDDSVPICIHCSAGCGRTGVICAIDytwMLLKDgIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233

PTPc-N7

cd14612

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

1075-1305

5.57e-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: 212.00 E-value: 5.57e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1075 EIAENRGKNRYNNVLPYDISRVKLSVQTHS--TDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1151
Cdd:cd14612    11 DIPGHASKDRYKTILPNPQSRVCLRRAGSQeeEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1152 LTKcVEQGRTKCEEYWPSKQAQdYGDITVAMTSEVVLPEWTIRDFVVKnmQNSESHPLRQFHFTSWPDHGVPDTTDLLIN 1231
Cdd:cd14612    91 ITK-LKEKKEKCVHYWPEKEGT-YGRFEIRVQDMKECDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLR 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915935 1232 FRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1305
Cdd:cd14612   167 LVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240

R-PTPc-E-2

cd14622

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

1107-1311

1.61e-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: 1.61e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1107 DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEV 1186
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1187 VLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFIAI 1266
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQ-TGNHPIVVHCSAGAGRTGTFIAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915935 1267 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204

PTPc-N1

cd14608

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

1055-1304

1.80e-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: 211.81 E-value: 1.80e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1055 FAEEYEDLKLIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKLSVQThstDDYINANYMPGYHSKKDFIATQGPLPNTL 1134
Cdd:cd14608     1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED---NDYINASLIKMEEAQRSYILTQGPLPNTC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1135 KDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQ----DYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLR 1210
Cdd:cd14608    78 GHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKemifEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1211 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDR---LIYQIENENTVDVYGIVYD 1287
Cdd:cd14608   158 HFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLE 237

                         250
                  ....*....|....*..
gi 568915935 1288 LRMHRPLMVQTEDQYVF 1304
Cdd:cd14608   238 MRKFRMGLIQTADQLRF 254

R-PTPc-A-2

cd14623

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

1084-1309

2.60e-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: 2.60e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1084 RYNNVLPYDISRVKLSVQT-HSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1162
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRgEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1163 CEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 1242
Cdd:cd14623    81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915935 1243 iPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1309
Cdd:cd14623   161 -SGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226

R-PTPc-K-1

cd14631

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

1100-1311

1.26e-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: 1.26e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1100 VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPsKQAQDYGDIT 1179
Cdd:cd14631     7 VEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1180 VAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQIPPESPILVHCSAGVGR 1259
Cdd:cd14631    86 VTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSF--IRRVKLSNPPSAGPIVVHCSAGAGR 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568915935 1260 TGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14631   164 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215

PTPc-N11

cd14605

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

1078-1309

6.19e-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: 6.19e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1078 ENRGKNRYNNVLPYDISRVKLsvqtHSTD------DYINANY-MPGYHS-------KKDFIATQGPLPNTLKDFWRMVWE 1143
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVL----HDGDpnepvsDYINANIiMPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1144 KNVYAIVMLTKCVEQGRTKCEEYWPSKQA-QDYGDITVAMTSEVVLPEWTIRDFVVKNM-QNSESHPLRQFHFTSWPDHG 1221
Cdd:cd14605    77 ENSRVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1222 VPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENT---VDVYGIVYDLRMHRPLMVQT 1298
Cdd:cd14605   157 VPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQT 236

                         250
                  ....*....|.
gi 568915935 1299 EDQYVFLNQCV 1309
Cdd:cd14605   237 EAQYRFIYMAV 247

R-PTP-C-2

cd14558

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

1108-1305

8.56e-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: 8.56e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQaQDYGDITVAMTSEVV 1187
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEK-KTYGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1188 LPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPES----PILVHCSAGVGRTGTF 1263
Cdd:cd14558    80 SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHgrsvPIVVHCSDGSSRTGIF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915935 1264 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1305
Cdd:cd14558   160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFL 201

R-PTPc-R

cd14611

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

1082-1307

1.10e-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: 198.99 E-value: 1.10e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1082 KNRYNNVLPYDISRVKLSVQ--THSTDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQ 1158
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKnsNDSLSTYINANYIRGYGGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1159 GRtKCEEYWPSKQAQdYGDITVAMTSEVVLPEWTIRDFVVKnmQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 1238
Cdd:cd14611    82 NE-KCVLYWPEKRGI-YGKVEVLVNSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915935 1239 YMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14611   158 DRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

PTPc-N2

cd14607

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

1059-1304

1.52e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.

Pssm-ID: 350455 [Multi-domain] Cd Length: 257 Bit Score: 199.81 E-value: 1.52e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1059 YEDLKLIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKLSvqtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFW 1138
Cdd:cd14607     4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ---NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1139 RMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD--YGD--ITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHF 1214
Cdd:cd14607    81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1215 TSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR 1292
Cdd:cd14607   161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYR 240

                         250
                  ....*....|..
gi 568915935 1293 PLMVQTEDQYVF 1304
Cdd:cd14607   241 MGLIQTPDQLRF 252

R-PTP-N

cd14609

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

1073-1304

1.87e-57

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: 200.26 E-value: 1.87e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1073 TAEIAENRGKNRYNNVLPYDISRVKLSVQTH-STDDYINAN-------YMPGYhskkdfIATQGPLPNTLKDFWRMVWEK 1144
Cdd:cd14609    36 TAQGEANVKKNRNPDFVPYDHARIKLKAESNpSRSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWEN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1145 NVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPE-WTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVP 1223
Cdd:cd14609   110 GCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIP 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1224 DTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQY 1302
Cdd:cd14609   190 SSTRPLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQF 267


                  ..
gi 568915935 1303 VF 1304
Cdd:cd14609   268 EF 269

PTPc-N6

cd14606

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

1078-1313

4.72e-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: 195.87 E-value: 4.72e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1078 ENRGKNRYNNVLPYDISRVKLSVQTHST--DDYINANY-----MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIV 1150
Cdd:cd14606    17 ENKSKNRYKNILPFDHSRVILQGRDSNIpgSDYINANYvknqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1151 MLTKCVEQGRTKCEEYWPSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQNSES-HPLRQFHFTSWPDHGVPDTTDL 1228
Cdd:cd14606    97 MTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPGG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1229 LINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENT---VDVYGIVYDLRMHRPLMVQTEDQYVFL 1305
Cdd:cd14606   177 VLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFI 256


                  ....*...
gi 568915935 1306 NQCVLDII 1313
Cdd:cd14606   257 YVAIAQFI 264

R-PTP-N2

cd14610

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

1072-1315

8.60e-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: 195.66 E-value: 8.60e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1072 YTAEIAENRGKNRYNNVLPYDISRVKLSVQ-THSTDDYINANYMPGYHSKKD-FIATQGPLPNTLKDFWRMVWEKNVYAI 1149
Cdd:cd14610    37 NVAQREENVQKNRSLAVLPYDHSRIILKAEnSHSHSDYINASPIMDHDPRNPaYIATQGPLPATVADFWQMVWESGCVVI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1150 VMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPE-WTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDL 1228
Cdd:cd14610   117 VMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1229 LINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14610   197 LLDFRRKVNKCYRG--RSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                  ....*...
gi 568915935 1308 CVLDIIRA 1315
Cdd:cd14610   275 AVAEEVNA 282

PTPc-N4

cd14601

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

1107-1314

9.21e-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: 9.21e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1107 DYINANYM----PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQ-DYGDITVA 1181
Cdd:cd14601     1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSsSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1182 MTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDymKQIPPESPILVHCSAGVGRTG 1261
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568915935 1262 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIR 1314
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211

PTPc-N5

cd14613

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

1082-1306

2.79e-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: 190.46 E-value: 2.79e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1082 KNRYNNVLPYDISRVKLSvqTHSTDD----YINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcV 1156
Cdd:cd14613    28 KNRYKTILPNPHSRVCLT--SPDQDDplssYINANYIRGYGGEeKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN-I 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1157 EQGRTKCEEYWPSKQAQdYGDITVAMTSEVVLPEWTIRDFVVKNmqNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLV 1236
Cdd:cd14613   105 EEMNEKCTEYWPEEQVT-YEGIEITVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEV 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568915935 1237 RDYMKQIPPE-SPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 1306
Cdd:cd14613   182 EEARQQAEPNcGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252

PTPc-N20

cd14596

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

1108-1314

8.99e-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: 186.88 E-value: 8.99e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS--KQAQDYGDITVAMT 1183
Cdd:cd14596     1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1184 SEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRdYMKQIPPESPILVHCSAGVGRTGTF 1263
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKF---IC-YMRKVHNTGPIVVHCSAGIGRAGVL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915935 1264 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIR 1314
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207

PTPc-N21_14

cd14540

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

1108-1313

1.23e-51

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: 181.12 E-value: 1.23e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS----KQAQDYGDITVA 1181
Cdd:cd14540     1 YINASHitATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggeHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1182 MTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINF----RYLVRDYMKQIP---PESPILVHCS 1254
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeiNSVRRHTNQDVAghnRNPPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568915935 1255 AGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1313
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 ...

1108-1309

2.15e-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: 179.95 E-value: 2.15e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANY-------MPGYhskkdfIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITV 1180
Cdd:cd14546     1 YINASTiydhdprNPAY------IATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1181 AMTSEVVLPE-WTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLV-RDYMKQIppeSPILVHCSAGVG 1258
Cdd:cd14546    75 HLVSEHIWCDdYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568915935 1259 RTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1309
Cdd:cd14546   152 RTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

R-PTPc-typeIIb-2

cd14556

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

1108-1305

4.48e-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: 178.75 E-value: 4.48e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1187
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1188 LPEWTIRDFVVKNMQN-SESHPL-RQFHFTSWPDHG-VPDTTDLLINFRYLVRDYMKQIPpESPILVHCSAGVGRTGTFI 1264
Cdd:cd14556    80 DEDVISRIFRLQNTTRpQEGYRMvQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSG-EGPIVVHCLNGVGRSGVFC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 568915935 1265 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1305
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFC 199

PTP-N23

cd14539

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

1108-1304

1.13e-49

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: 1.13e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGY-HSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTS 1184
Cdd:cd14539     1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1185 EVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPE-SPILVHCSAGVGRTGTF 1263
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLqTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915935 1264 IAIDRLIYQIENEN-TVDVYGIVYDLRMHRPLMVQTEDQYVF 1304
Cdd:cd14539   161 CLLYAAVQEIEAGNgIPDLPQLVRKMRQQRKYMLQEKEHLKF 202

PTPc-N14

cd14599

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

1073-1314

8.43e-47

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: 169.79 E-value: 8.43e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1073 TAEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKD--FIATQGPLPNTLKDFWRMVWEKNVYAIV 1150
Cdd:cd14599    32 TATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1151 MLTKCVEQGRTKCEEYWP---SKQ-AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTT 1226
Cdd:cd14599   112 MVTAEEEGGRSKSHRYWPklgSKHsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1227 DLLINFRYLVRDYMKQIPPES--------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQT 1298
Cdd:cd14599   192 QGFLSYLEEIQSVRRHTNSMLdstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQT 271

                         250
                  ....*....|....*.
gi 568915935 1299 EDQYVFLNQCVLDIIR 1314
Cdd:cd14599   272 IAQYKFVYQVLIQFLK 287

PTPc_plant_PTP1

cd17658

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

1108-1304

1.89e-46

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: 165.72 E-value: 1.89e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYM--PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT-KCEEYWPSK--QAQDYGDITVAM 1182
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1183 ----TSEVVLpewTIRDFVVKNMQnSESHPLRQFH--FTSWPDHGVPDTTdllinfrYLVRDYMK---QIPP-ESPILVH 1252
Cdd:cd17658    81 kklkHSQHSI---TLRVLEVQYIE-SEEPPLSVLHiqYPEWPDHGVPKDT-------RSVRELLKrlyGIPPsAGPIVVH 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568915935 1253 CSAGVGRTGTFIAIDRLIYQI--ENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1304
Cdd:cd17658   150 CSAGIGRTGAYCTIHNTIRRIleGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203

PHA02738

hypothetical protein; Provisional

1072-1304

2.54e-46

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 169.72 E-value: 2.54e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1072 YTAEIAeNRGKNRYNNVLPYDISRVKLSVQtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1151
Cdd:PHA02738   43 FNAEKK-NRKLNRYLDAVCFDHSRVILPAE-RNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVM 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1152 LTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNmQNSESHPLRQFHFTSWPDHGVPDTTDLL 1229
Cdd:PHA02738  121 LCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEF 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1230 INFRYLVRDYMKQIPPES-----------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQT 1298
Cdd:PHA02738  200 LNFVLEVRQCQKELAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFI 279


                  ....*.
gi 568915935 1299 EDQYVF 1304
Cdd:PHA02738  280 PFQYFF 285

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1069-1305

4.78e-45

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 164.49 E-value: 4.78e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1069 LPKYTAEIaENRGKNRYNNVLPYDISRVKlsvqthSTDDYINANYMPGYhSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 1148
Cdd:COG5599    33 DPQYLQNI-NGSPLNRFRDIQPYKETALR------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1149 IVMLTKCVE--QGRTKCEEYWPskQAQDYG--DITVAMTSEVVL-PEWTIRDFVVKNMQNS-ESHPLRQFHFTSWPDHGV 1222
Cdd:COG5599   105 LVVLASDDEisKPKVKMPVYFR--QDGEYGkyEVSSELTESIQLrDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1223 PDTTdLLINFRYLVRDYMK-QIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR-PLMVQT 1298
Cdd:COG5599   183 ISAE-ALKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQT 261


                  ....*..
gi 568915935 1299 EDQYVFL 1305
Cdd:COG5599   262 SEQLDVL 268

PHA02747

protein tyrosine phosphatase; Provisional

1078-1305

1.48e-44

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 164.40 E-value: 1.48e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1078 ENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVML--TKC 1155
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLtpTKG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1156 VeQGRTKCEEYW-PSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFR 1233
Cdd:PHA02747  130 T-NGEEKCYQYWcLNEDGNiDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFI 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1234 YLV----RDYMKQIPPE----SPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1305
Cdd:PHA02747  209 KIIdinrKKSGKLFNPKdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFI 288

R5-PTP-2

cd14550

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

1108-1305

6.69e-43

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: 155.56 E-value: 6.69e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCveQGRTKCEEYWPSK-QAQDYGDITVAMTSEV 1186
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN--ELNEDEPIYWPTKeKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1187 VLPEW-----TIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLliNFRYLVRDYMKQipPESPILVHCSAGVGRTG 1261
Cdd:cd14550    79 HSCLSneirlIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVF--ELINTVQEWAQQ--RDGPIVVHDRYGGVQAA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568915935 1262 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1305
Cdd:cd14550   155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198

PHA02742

protein tyrosine phosphatase; Provisional

1078-1310

1.99e-42

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 157.86 E-value: 1.99e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1078 ENRGKNRYNNVLPYDISRVKLSVQThSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVE 1157
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILKIED-GGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1158 QGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 1235
Cdd:PHA02742  130 DGKEACYPYWMPHERGKatHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1236 VRDYM---------KQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 1306
Cdd:PHA02742  210 VREADlkadvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                  ....
gi 568915935 1307 QCVL 1310
Cdd:PHA02742  290 FIVL 293

PTPc_DSPc

smart00012

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

1208-1311

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 568915935   1208 PLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENE-NTVDVYGIVY 1286
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 568915935   1287 DLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

1208-1311

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 568915935   1208 PLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENE-NTVDVYGIVY 1286
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 568915935   1287 DLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105

PTP_tm

pfam18861

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

849-979

1.40e-38

Pssm-ID: 465889 Cd Length: 126 Bit Score: 140.05 E-value: 1.40e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935   849 VKFSGFEASHGPIKAYAVILTTGE-AAQPSADVLKYTYEDFKRGASDTYVTYLIriEEKGQSQGlSEVLNYEIDVGNQST 927
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDsLNRPLKEYLNKTYYDWKYKKTDSYLATVT--PNPFTSPR-SSSRSLTVPVGTGSK 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568915935   928 TLGYYNGRLEPLGSYRACVAGFTNITYnlqNDGLINGDESYVSFSPYSEAVF 979
Cdd:pfam18861   78 WQGYCNGPLKPLGSYRFSVAAFTRLEF---DDGLIDGEESYVSFTPFSEPIA 126

PTPc-N21

cd14598

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

1108-1314

1.68e-36

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: 137.80 E-value: 1.68e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKK--DFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD----YG--DIT 1179
Cdd:cd14598     1 YINASHIKVTVGGKewDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGrfKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1180 VAMTSEVVLpeWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDttDLLINFRYL-----VRDYMKQI----PPESPIL 1250
Cdd:cd14598    81 TRFRTDSGC--YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPE--DLKGFLSYLeeiqsVRRHTNSTidpkSPNPPVL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915935 1251 VHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIR 1314
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220

PHA02746

protein tyrosine phosphatase; Provisional

1078-1304

3.12e-36

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 140.55 E-value: 3.12e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1078 ENRGKNRYNNVLPYDISRVKLSVQTHST--------------------DDYINANYMPGYHSKKDFIATQGPLPNTLKDF 1137
Cdd:PHA02746   50 ENLKKNRFHDIPCWDHSRVVINAHESLKmfdvgdsdgkkievtsednaENYIHANFVDGFKEANKFICAQGPKEDTSEDF 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1138 WRMVWEKNVYAIVMLTKcVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFT 1215
Cdd:PHA02746  130 FKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSElaFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1216 SWPDHGVPDTTDLLINFRYLVRDYMKQIPPES--------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYD 1287
Cdd:PHA02746  209 DWPDNGIPTGMAEFLELINKVNEEQAELIKQAdndpqtlgPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLK 288

                         250
                  ....*....|....*..
gi 568915935 1288 LRMHRPLMVQTEDQYVF 1304
Cdd:PHA02746  289 IRKQRHSSVFLPEQYAF 305

R-PTP-Z-2

cd17669

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

1108-1310

1.94e-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: 131.27 E-value: 1.94e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCeEYWPSK-QAQDYGDITVAMTSE- 1185
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKdEPINCETFKVTLIAEe 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1186 -VVLP---EWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVP-DTTDLLINfryLVRDymKQIPPESPILVHCSAGVGRT 1260
Cdd:cd17669    80 hKCLSneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELIS---IIKE--EAANRDGPMIVHDEHGGVTA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915935 1261 GTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1310
Cdd:cd17669   155 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

R-PTP-G-2

cd17670

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

1108-1310

2.43e-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: 128.26 E-value: 2.43e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcvEQGRTKCEE-YWPSK-QAQDYGDITVAMTSE 1185
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSReESMNCEAFTVTLISK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1186 VVL-----PEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVP-DTTDLLINF---RYLVRDymkqippeSPILVHCSAG 1256
Cdd:cd17670    79 DRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVikeEALTRD--------GPTIVHDEFG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568915935 1257 VGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1310
Cdd:cd17670   151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

R-PTPc-T-2

cd14634

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

1108-1311

1.11e-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: 1.11e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTkcvEQGRTK-CEEYWPSKQAQDYGDITVAMTSEV 1186
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWPEKTSCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1187 VLPEWTIRDFVVKNMQNSES--HPLRQFHFTSWPDH--GVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGT 1262
Cdd:cd14634    78 IDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrdTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568915935 1263 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

R-PTPc-U-2

cd14637

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

1108-1311

3.44e-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: 125.02 E-value: 3.44e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT-KCEEYWPSKQAQDYGDITVAMTSEV 1186
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1187 VLPEWTIRDFVVKNM-QNSESHPL-RQFHFTSW-PDHGVPDTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTF 1263
Cdd:cd14637    81 ADEDIVTRLFRVQNItRLQEGHLMvRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRE-SGEGRTVVHCLNGGGRSGTY 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568915935 1264 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14637   160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207

R-PTPc-K-2

cd14636

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

1108-1304

3.92e-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: 3.92e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKC-VEQGrtkCEEYWPSKQAQDYGDITVAMTSEV 1186
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1187 VLPEWTIRDFVVKNMQNSESHPL--RQFHFTSWPDH-GVPDTTDLLINFRYLVRDYMKQIPP-ESPILVHCSAGVGRTGT 1262
Cdd:cd14636    78 MDCDVISRIFRICNLTRPQEGYLmvQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgEGRTIIHCLNGGGRSGM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915935 1263 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1304
Cdd:cd14636   158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199

R-PTPc-M-2

cd14635

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

1108-1311

7.80e-29

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

Pssm-ID: 350483 [Multi-domain] Cd Length: 206 Bit Score: 115.17 E-value: 7.80e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1108 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcVEQGRTkCEEYWPSKQAQDYGDITVAMTSEVV 1187
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWPENGVHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1188 LPEWTIRDFVVKNMQNSES--HPLRQFHFTSWPDHgvPDTTDLLINFRYLVRDYMKQIPP----ESPILVHCSAGVGRTG 1261
Cdd:cd14635    79 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMY--RDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915935 1262 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1311
Cdd:cd14635   157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206

PTP_YopH-like

cd14559

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

1083-1305

3.79e-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: 85.14 E-value: 3.79e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1083 NRYNNVLpydiSRVKLSVQTHstddyINANYMPgYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1162
Cdd:cd14559     1 NRFTNIQ----TRVSTPVGKN-----LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1163 CEEYWpsKQAQDYGDITVamTSEVVLPEWTIRDFVVK--NMQNSES---HPLRQFHFTSWPDHGVPDTTDLL-------- 1229
Cdd:cd14559    71 LPPYF--RQSGTYGSVTV--KSKKTGKDELVDGLKADmyNLKITDGnktITIPVVHVTNWPDHTAISSEGLKeladlvnk 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1230 -----INFRYL-----VRDYMKQIPpespiLVHCSAGVGRTGTFIAIdrlIYQIENENTVDVYGIVYDLRMHR-PLMVQT 1298
Cdd:cd14559   147 saeekRNFYKSkgssaINDKNKLLP-----VIHCRAGVGRTGQLAAA---MELNKSPNNLSVEDIVSDMRTSRnGKMVQK 218


                  ....*..
gi 568915935 1299 EDQYVFL 1305
Cdd:cd14559   219 DEQLDTL 225

PHA02740

protein tyrosine phosphatase; Provisional

1077-1307

1.48e-14

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 76.16 E-value: 1.48e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1077 AENRGKNRyNNVLP---YDISRVKLsvqtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLT 1153
Cdd:PHA02740   49 AENKAKDE-NLALHitrLLHRRIKL----FNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLIS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1154 KCVEQgrtKC-EEYWPSKQ--AQDYGDITVAMTSEVVLPEWTIRDFVVKNmQNSESHPLRQFHFTSWPDHGVPDTTDLLI 1230
Cdd:PHA02740  124 RHADK---KCfNQFWSLKEgcVITSDKFQIETLEIIIKPHFNLTLLSLTD-KFGQAQKISHFQYTAWPADGFSHDPDAFI 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935 1231 NFRYLVRDYMKQIPPES------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1304
Cdd:PHA02740  200 DFFCNIDDLCADLEKHKadgkiaPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVF 279


                  ...
gi 568915935 1305 LNQ 1307
Cdd:PHA02740  280 CYH 282

FN3

COG3401

Fibronectin type 3 domain [General function prediction only];

199-699

4.13e-10

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 64.25 E-value: 4.13e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  199 TSCNITGLSPGTSYTFSIISVTTNETLNKTITTEPWPVSDLHVTSVGVTQARLTWSNANGTASYRMLIEELTTHSSVNIS 278
Cdd:COG3401    48 TKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  279 GLKPGTNNSFAFPESNETQADFAVAEEVPADANGTKRIPVTNLSQLHKNSLVSVDPPSGQDPSLTEILLTDLKPDTQYNA 358
Cdd:COG3401   128 ATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYY 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  359 TIYSQAANGtEGQPRNKVFKTNSTQV----SDVRAMNISASSMTLTWKSNYDGSRTS-IVYKIHVAGGTHSVNQTVNKTE 433
Cdd:COG3401   208 RVAATDTGG-ESAPSNEVSVTTPTTPpsapTGLTATADTPGSVTLSWDPVTESDATGyRVYRSNSGDGPFTKVATVTTTS 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  434 AIILGLSSSTLYN--ITVHPFLGQTEGTPGFLQVYTS---PDQVSDFRVTNVSTRAIGLAWRSNDS---KSFEIFIKQDG 505
Cdd:COG3401   287 YTDTGLTNGTTYYyrVTAVDAAGNESAPSNVVSVTTDltpPAAPSGLTATAVGSSSITLSWTASSDadvTGYNVYRSTSG 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  506 GEKHR--NASTGNQSYMVEDLKPGTSYHFEIIPRGPDGTEGLSS----------TVNGSTDPSAVTDIRVVNISTTEMQL 573
Cdd:COG3401   367 GGTYTkiAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSeevsattasaASGESLTASVDAVPLTDVAGATAAAS 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  574 EWQNTDDASGYTYHLVLESKSGSIirTNSSQKWITVGSLTPGTLYNVTIFPEVDQIQGISNSITQYTrPSSVSHIEVNTT 653
Cdd:COG3401   447 AASNPGVSAAVLADGGDTGNAVPF--TTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV-IGASAAAAVGGA 523

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 568915935  654 TTTAAIRWKNEDAASASYAYSVLILKTGDGSNVTSNFTKDPSILIP 699
Cdd:COG3401   524 PDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSG 569

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

1205-1307

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 568915935 1205 ESHPLRQFHFTsWPDHGVPDTTDllinFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDrLIYQ-IENENTVDVyg 1283
Cdd:COG2453    44 EEAGLEYLHLP-IPDFGAPDDEQ----LQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAY-LVLLgLSAEEALAR-- 115

                          90       100
                  ....*....|....*....|....
gi 568915935 1284 ivydLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:COG2453   116 ----VRAARPGAVETPAQRAFLER 135

fn3

Fibronectin type III domain;

162-222

8.22e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 50.88 E-value: 8.22e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915935   162 VSPTSVLLTWKHNDSGAS-------ECRIENKMESNLTFPV-KNQTSCNITGLSPGTSYTFSIISVTTN 222
Cdd:pfam00041   11 VTSTSLTVSWTPPPDGNGpitgyevEYRPKNSGEPWNEITVpGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

PTP_DSP_cys

cd14494

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

1245-1305

7.03e-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: 7.03e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568915935 1245 PESPILVHCSAGVGRTGTFIAIDRLIYQieNENTVDVYGIVYDLRMHRplMVQTEDQYVFL 1305
Cdd:cd14494    55 PGEPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEAVRIVRLIRPGG--IPQTIEQLDFL 111

FN3

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

555-622

1.10e-06

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 47.61 E-value: 1.10e-06

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915935    555 PSAVTDIRVVNISTTEMQLEWQ--NTDDASGYTYHLVLESKSGS----IIRTNSSQKWITVGSLTPGTLYNVTI 622
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEppPDDGITGYIVGYRVEYREEGsewkEVNVTPSSTSYTLTGLKPGTEYEFRV 74

FN3

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

152-220

1.67e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.49 E-value: 1.67e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915935  152 PNPIFDIEA-VVSPTSVLLTWKHNDSGAS-------ECRIENKME-SNLTFPVKNQTSCNITGLSPGTSYTFSIISVT 220
Cdd:cd00063     1 PSPPTNLRVtDVTSTSVTLSWTPPEDDGGpitgyvvEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

FN3

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

555-640

2.26e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.11 E-value: 2.26e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  555 PSAVTDIRVVNISTTEMQLEWQNTDDA----SGYT--YHLVLESKSGSIIRTNSSQKWITVGSLTPGTLYNVTIFPEVDQ 628
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpiTGYVveYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 568915935  629 IQG-ISNSITQYT 640
Cdd:cd00063    81 GESpPSESVTVTT 93

fn3

Fibronectin type III domain;

383-460

2.49e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 2.49e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935   383 QVSDVRAMNISASSMTLTWKSNYDGSRTSIVYKIHVA---GGTHSVNQTV--NKTEAIILGLSSSTLYNITVHPFLGQTE 457
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRpknSGEPWNEITVpgTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568915935   458 GTP 460
Cdd:pfam00041   82 GPP 84

FN3

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

469-553

2.67e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.11 E-value: 2.67e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  469 PDQVSDFRVTNVSTRAIGLAWRSNDS-----KSFEIFIKQDGGEKHRNASTGN---QSYMVEDLKPGTSYHFEIIPRGPD 540
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDdggpiTGYVVEYREKGSGDWKEVEVTPgseTSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 568915935  541 GTEGLSSTVNGST 553
Cdd:cd00063    81 GESPPSESVTVTT 93

FN3

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

152-220

5.01e-06

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 46.07 E-value: 5.01e-06

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915935    152 PNPIFDIEAV-VSPTSVLLTWKHNDSGAS-----ECRIENKMESNLTFPVK---NQTSCNITGLSPGTSYTFSIISVT 220
Cdd:smart00060    1 PSPPSNLRVTdVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNvtpSSTSYTLTGLKPGTEYEFRVRAVN 78

FN3

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

384-458

9.95e-06

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.91 E-value: 9.95e-06

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935    384 VSDVRAMNISASSMTLTWKSNYDGSRTSIVYKIHVAGGT-----HSVNQTVNKTEAIILGLSSSTLYNITVHPFLGQTEG 458
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREegsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83

PTP_VSP_TPTE

cd14510

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

1218-1264

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 568915935 1218 PDHGVPdTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFI 1264
Cdd:cd14510    82 DDHNVP-TLDEMLSFTAEVREWMAA-DPKNVVAIHCKGGKGRTGTMV 126

FN3

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

469-541

1.99e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.14 E-value: 1.99e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935    469 PDQVSDFRVTNVSTRAIGLAWRSNDSKSFEIFI--------KQDGGEKHRNASTGNQSYMVEDLKPGTSYHFEIIPRGPD 540
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgyrveyrEEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    .
gi 568915935    541 G 541
Cdd:smart00060   81 G 81

FN3

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

384-460

2.20e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 44.41 E-value: 2.20e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  384 VSDVRAMNISASSMTLTWKSNYDGSRTSIVYKIHV----AGGTHSVN-QTVNKTEAIILGLSSSTLYNITVHPFLGQTEG 458
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYrekgSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83


                  ..
gi 568915935  459 TP 460
Cdd:cd00063    84 PP 85

fn3

Fibronectin type III domain;

470-535

2.73e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 43.94 E-value: 2.73e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915935   470 DQVSDFRVTNVSTRAIGLAWRSNDSKS-----FEIFIKQDGGE---KHRNASTGNQSYMVEDLKPGTSYHFEII 535
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpitgYEVEYRPKNSGepwNEITVPGTTTSVTLTGLKPGTEYEVRVQ 74

PTPlike_phytase

pfam14566

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

1218-1270

1.65e-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: 1.65e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568915935  1218 PDHGVPDTTDllinFRYLVrDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLI 1270
Cdd:pfam14566  109 TDEKAPLEED----FDALI-SIVKDAPEDTALVFNCQMGRGRTTTAMVIADLV 156

PTP_PTEN-like

cd14497

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

1217-1265

1.67e-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: 1.67e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568915935 1217 WPDHGVPdTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFIA 1265
Cdd:cd14497    68 FPDHHPP-PLGLLLEIVDDIDSWLSE-DPNNVAVVHCKAGKGRTGTVIC 114

CDKN3-like

cd14505

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

1205-1307

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 568915935 1205 ESHPLRQFHFtSWPDHGVPDTTDlliNFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAidRLIYQIENENTVDVygI 1284
Cdd:cd14505    69 QQAGITWHHL-PIPDGGVPSDIA---QWQELLEELLSALENGKKVLIHCKGGLGRTGLIAA--CLLLELGDTLDPEQ--A 140

                          90       100
                  ....*....|....*....|...
gi 568915935 1285 VYDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14505   141 IAAVRALRPGAIQTPKQENFLHQ 163

FN3

COG3401

Fibronectin type 3 domain [General function prediction only];

144-460

2.71e-04

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 45.38 E-value: 2.71e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  144 QVLCAGAAPNPIFDIEAVV-SPTSVLLTW-KHNDSGASECRIENKMESNLTF---PVKNQTSCNITGLSPGTSYTFSIIS 218
Cdd:COG3401   225 SVTTPTTPPSAPTGLTATAdTPGSVTLSWdPVTESDATGYRVYRSNSGDGPFtkvATVTTTSYTDTGLTNGTTYYYRVTA 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  219 VTTNETLN--------KTITTEPWPVSDLHVTSVGVTQARLTWSNA--NGTASYRM-----------LIEELTTHSSVNI 277
Cdd:COG3401   305 VDAAGNESapsnvvsvTTDLTPPAAPSGLTATAVGSSSITLSWTASsdADVTGYNVyrstsgggtytKIAETVTTTSYTD 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  278 SGLKPGTNNSFAF-------PESNETQADFAVAEEVPADANGTKRIPVTNLSQLHKNSLVSVDPPSGQDPSLTEILLTDL 350
Cdd:COG3401   385 TGLTPGTTYYYKVtavdaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDT 464

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915935  351 KPDTQYNATIYSQAANGTEGQPRNKVFKTNSTQVSDVRAMNISASSMTLTWKSNYDGSRTSivyKIHVAGGTHSVNQTVN 430
Cdd:COG3401   465 GNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPD---GTPNVTGASPVTVGAS 541

                         330       340       350
                  ....*....|....*....|....*....|
gi 568915935  431 KTEAIILGLSSSTLYNITVHPFLGQTEGTP 460
Cdd:COG3401   542 TGDVLITDLVSLTTSASSSVSGAGLGSGNL 571

PTP_PTPDC1

cd14506

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

1212-1305

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 568915935 1212 FHFTSWPDHGVPDTTDLLINFRylVRDYMKQipPESPILVHCSAGVGRTGTFIAIdRLIYqIENENTVDVYGIVydlRMH 1291
Cdd:cd14506    79 FYNFGWKDYGVPSLTTILDIVK--VMAFALQ--EGGKVAVHCHAGLGRTGVLIAC-YLVY-ALRMSADQAIRLV---RSK 149

                          90
                  ....*....|....
gi 568915935 1292 RPLMVQTEDQYVFL 1305
Cdd:cd14506   150 RPNSIQTRGQVLCV 163

TpbA-like

cd14529

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

1248-1287

8.99e-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: 8.99e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568915935 1248 PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYD 1287
Cdd:cd14529    91 PVLIHCKHGKDRTGLVSALYRIVYGGSKEEANEDYRLSNR 130

DUSP23

cd14504

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

1248-1307

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 568915935 1248 PILVHCSAGVGRTGTFIAidrlIYQIENENTVDVYGIVyDLRMHRPLMVQTEDQYVFLNQ 1307
Cdd:cd14504    84 AVLVHCLAGKGRTGTMLA----CYLVKTGKISAVDAIN-EIRRIRPGSIETSEQEKFVIQ 138

fn3

Fibronectin type III domain;

556-623

1.48e-03

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 38.94 E-value: 1.48e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915935   556 SAVTDIRVVNISTTEMQLEWQNTDDASG-YTYHLVLESKSGSI-----IRTNSSQKWITVGSLTPGTLYNVTIF 623
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpITGYEVEYRPKNSGepwneITVPGTTTSVTLTGLKPGTEYEVRVQ 74

PTPLP-like

cd14495

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

1213-1291

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 568915935 1213 HFtsWPDhgvPDTTDLLINFrylvrdyMKQIPPESPILVHCSAGVGRTGTFIAI-DRLIyqieNENTVDVYGIVYdlRMH 1291
Cdd:cd14495   165 HV--WPD---DEEIDAFVAF-------YRSLPADAWLHFHCRAGKGRTTTFMVMyDMLK----NPKDVSFDDIIA--RQY 226

FN3