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Conserved domains on  [gi|71990705|ref|NP_001022208|]
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Receptor-type tyrosine-protein phosphatase [Caenorhabditis elegans]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 11511050)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
792-1071 1.54e-93

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 302.27  E-value: 1.54e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     792 LFAQEYESLPHFQLD---TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDySDYINANFIKSWKEKKLFIAAQAPVD 868
Cdd:smart00194    1 GLEEEFEKLDRLKPDdesCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     869 ATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQIT--RYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvi 946
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGC------ 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     947 pngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISI 1026
Cdd:smart00194  154 -------------------SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAI 214

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*
gi 71990705    1027 DSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:smart00194  215 DILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1134-1402 2.38e-83

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 273.77  E-value: 2.38e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1134 GLEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPtIGHADSSYINASHIKGY--FFDYIAAQDPVs 1211
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPngPKAYIATQGPL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1212 EGTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDN 1289
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTelVEKGREKCAQYWPDEEGEPLTY-----GDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1290 ESmpaNQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQR 1369
Cdd:smart00194  154 SE---TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQST---STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE 226

                           250       260       270
                    ....*....|....*....|....*....|...
gi 71990705    1370 IDVFQTVKGLQSHRPMMFTRFEQYSFCYRALAD 1402
Cdd:smart00194  227 VDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 368-488 1.24e-07

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 50.96  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  368 PFPPkeEDVRVLNSGSAlSCEVEWKSPAEPNGRITKYFVSVRgamrksdgsltPDDLPAAVEVDKRCANwdgdentskhn 447
Cdd:cd00063    1 PSPP--TNLRVTDVTST-SVTLSWTPPEDDGGPITGYVVEYR-----------EKGSGDWKEVEVTPGS----------- 55

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 71990705  448 ginpidfaneFYSCKFGPLKPNRNYTVTVWAENSAGRSLPA 488
Cdd:cd00063   56 ----------ETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
792-1071 1.54e-93

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 302.27  E-value: 1.54e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     792 LFAQEYESLPHFQLD---TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDySDYINANFIKSWKEKKLFIAAQAPVD 868
Cdd:smart00194    1 GLEEEFEKLDRLKPDdesCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     869 ATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQIT--RYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvi 946
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGC------ 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     947 pngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISI 1026
Cdd:smart00194  154 -------------------SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAI 214

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*
gi 71990705    1027 DSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:smart00194  215 DILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
815-1071 5.55e-87

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 282.98  E-value: 5.55e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    815 NAIKNRYNDIRAFDDTRVKLKKINGDdySDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTE 894
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    895 KNRQQCAKYWPD--EQITRYGDIIVEPASFSFH-SDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRI 971
Cdd:pfam00102   79 KGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDeKDYTVRTLEVSNGGS-------------------------EETRTV 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    972 LQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFN-NSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRR 1050
Cdd:pfam00102  134 KHFHYTGWPDHGVPESPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRS 213

                          250       260
                   ....*....|....*....|.
gi 71990705   1051 QRNLMVQSLEQYVFIYKALAE 1071
Cdd:pfam00102  214 QRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1134-1402 2.38e-83

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 273.77  E-value: 2.38e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1134 GLEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPtIGHADSSYINASHIKGY--FFDYIAAQDPVs 1211
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPngPKAYIATQGPL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1212 EGTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDN 1289
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTelVEKGREKCAQYWPDEEGEPLTY-----GDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1290 ESmpaNQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQR 1369
Cdd:smart00194  154 SE---TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQST---STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE 226

                           250       260       270
                    ....*....|....*....|....*....|...
gi 71990705    1370 IDVFQTVKGLQSHRPMMFTRFEQYSFCYRALAD 1402
Cdd:smart00194  227 VDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 845-1067 2.38e-83

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: 271.08  E-value: 2.38e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDE--QITRYGDIIVEPASF 922
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEggKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  923 SFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP 1002
Cdd:cd00047   81 EELSDYTIRTLELSPKGC-------------------------SESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEA 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1003 QFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1067
Cdd:cd00047  136 RKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1160-1402 8.49e-75

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 248.31  E-value: 8.49e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   1160 NLLKNRYEAAVPFDKYRVILPPTIGHADssYINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDET 1237
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD--YINASYIDGYKkpKKYIATQGPLPN-TVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   1238 DWSDV--EKYWPIDgSGTECHFGSernsVNVTCVSEE-HHQDFIIRNLSYSMKDNEsmpANQEVVQYSYTGWPsDSIVPK 1314
Cdd:pfam00102   78 EKGREkcAQYWPEE-EGESLEYGD----FTVTLKKEKeDEKDYTVRTLEVSNGGSE---ETRTVKHFHYTGWP-DHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   1315 SANSLMNLIEMVlqRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1394
Cdd:pfam00102  149 SPNSLLDLLRKV--RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                   ....*...
gi 71990705   1395 FCYRALAD 1402
Cdd:pfam00102  227 FLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1190-1398 1.65e-62

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: 211.76  E-value: 1.65e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVML--SDETDWSDVEKYWPIDGsGTECHFGSernsVN 1265
Cdd:cd00047    1 YINASYIDGYRGPkeYIATQGPLPN-TVEDFWRMVWEQKVSVIVMLtnLVEKGREKCERYWPEEG-GKPLEYGD----IT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIRNLSYSMKDNESmpaNQEVVQYSYTGWPSDSIVPksanSLMNLIEMVLQRQSSLMGSQAPIVVHCR 1345
Cdd:cd00047   75 VTLVSEEELSDYTIRTLELSPKGCSE---SREVTHLHYTGWPDHGVPS----SPEDLLALVRRVRKEARKPNGPIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 71990705 1346 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1398
Cdd:cd00047  148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 807-1065 8.84e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 141.68  E-value: 8.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   807 TVASNRK-ENAIKNRYNDIRAFDDTRVKLKKINGDDySDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYL 885
Cdd:PHA02747   42 LIANFEKpENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   886 IVMVANLTEKN-RQQCAKYW-PDEQitryGDIIVEpasfsfhsDYAIRAFDIAhigecgpdVIPngngvEYANVPI-VKG 962
Cdd:PHA02747  121 IVMLTPTKGTNgEEKCYQYWcLNED----GNIDME--------DFRIETLKTS--------VRA-----KYILTLIeITD 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   963 QFANNSRRILQYHFTNWNDYKAPECSTGLLRFM-----YRLRELPQFNN-----SPVVIHCSAGVGRTGTFISIDSMLDQ 1032
Cdd:PHA02747  176 KILKDSRKISHFQCSEWFEDETPSDHPDFIKFIkiidiNRKKSGKLFNPkdallCPIVVHCSDGVGKTGIFCAVDICLNQ 255

                         250       260       270
                  ....*....|....*....|....*....|...
gi 71990705  1033 CLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFI 1065
Cdd:PHA02747  256 LVKRKAICLAKTAEKIREQRHAGIMNFDDYLFI 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
798-1073 4.19e-36

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 138.69  E-value: 4.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  798 ESLPHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKlkkINGDdysdYINANFIKSwKEKKLFIAAQAPVDATIGDFWRM 877
Cdd:COG5599   25 NELAPSHNDPQYLQNINGSPLNRFRDIQPYKETALR---ANLG----YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  878 VWEQESYLIVMVANLTE--KNRQQCAKYWPdeQITRYGDIIVEpasfsfhsdyairafdIAHIgecgpDVIPNGNGVEYA 955
Cdd:COG5599   97 LFDNNTPVLVVLASDDEisKPKVKMPVYFR--QDGEYGKYEVS----------------SELT-----ESIQLRDGIEAR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  956 NVPIVKGQFANNSRRILQYHFTNWNDYKAPEcSTGLLRFMYRLRE---LPQFNNSPVVIHCSAGVGRTGTFISIDSMLD- 1031
Cdd:COG5599  154 TYVLTIKGTGQKKIEIPVLHVKNWPDHGAIS-AEALKNLADLIDKkekIKDPDKLLPVVHCRAGVGRTGTLIACLALSKs 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 71990705 1032 -QCLAEDKANIFEFVCNLRRQRN-LMVQSLEQYVFIyKALAEWH 1073
Cdd:COG5599  233 iNALVQITLSVEEIVIDMRTSRNgGMVQTSEQLDVL-VKLAEQQ 275
PHA02738 PHA02738
hypothetical protein; Provisional
 1126-1407 3.10e-27

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 114.25  E-value: 3.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1126 MTTSNGETGLEEEFKKLernLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADssYINASHIKGYFFD--Y 1203
Cdd:PHA02738   18 MEKSDCEEVITREHQKV---ISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVILPAERNRGD--YINANYVDGFEYKkkF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1204 IAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETD---------WSDVEkywpidgsGTECHFGSERnsvnVTCVSEEHH 1274
Cdd:PHA02738   93 ICGQAPTRQ-TCYDFYRMLWMEHVQIIVMLCKKKEngrekcfpyWSDVE--------QGSIRFGKFK----ITTTQVETH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1275 QDFIIRNLSYSmkdnESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSL------MGSQA----PIVVHC 1344
Cdd:PHA02738  160 PHYVKSTLLLT----DGTSATQTVTHFNFTAWP-DHDVPKNTSEFLNFVLEVRQCQKELaqeslqIGHNRlqppPIVVHC 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990705  1345 RNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYISKT 1407
Cdd:PHA02738  235 NAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLT 297
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 368-488 1.24e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 50.96  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  368 PFPPkeEDVRVLNSGSAlSCEVEWKSPAEPNGRITKYFVSVRgamrksdgsltPDDLPAAVEVDKRCANwdgdentskhn 447
Cdd:cd00063    1 PSPP--TNLRVTDVTST-SVTLSWTPPEDDGGPITGYVVEYR-----------EKGSGDWKEVEVTPGS----------- 55

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 71990705  448 ginpidfaneFYSCKFGPLKPNRNYTVTVWAENSAGRSLPA 488
Cdd:cd00063   56 ----------ETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
792-1071 1.54e-93

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 302.27  E-value: 1.54e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     792 LFAQEYESLPHFQLD---TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDySDYINANFIKSWKEKKLFIAAQAPVD 868
Cdd:smart00194    1 GLEEEFEKLDRLKPDdesCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     869 ATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQIT--RYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvi 946
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGC------ 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     947 pngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISI 1026
Cdd:smart00194  154 -------------------SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAI 214

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*
gi 71990705    1027 DSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:smart00194  215 DILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
815-1071 5.55e-87

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 282.98  E-value: 5.55e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    815 NAIKNRYNDIRAFDDTRVKLKKINGDdySDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTE 894
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    895 KNRQQCAKYWPD--EQITRYGDIIVEPASFSFH-SDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRI 971
Cdd:pfam00102   79 KGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDeKDYTVRTLEVSNGGS-------------------------EETRTV 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    972 LQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFN-NSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRR 1050
Cdd:pfam00102  134 KHFHYTGWPDHGVPESPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRS 213

                          250       260
                   ....*....|....*....|.
gi 71990705   1051 QRNLMVQSLEQYVFIYKALAE 1071
Cdd:pfam00102  214 QRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1134-1402 2.38e-83

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 273.77  E-value: 2.38e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1134 GLEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPtIGHADSSYINASHIKGY--FFDYIAAQDPVs 1211
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPngPKAYIATQGPL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1212 EGTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDN 1289
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTelVEKGREKCAQYWPDEEGEPLTY-----GDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1290 ESmpaNQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQR 1369
Cdd:smart00194  154 SE---TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQST---STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE 226

                           250       260       270
                    ....*....|....*....|....*....|...
gi 71990705    1370 IDVFQTVKGLQSHRPMMFTRFEQYSFCYRALAD 1402
Cdd:smart00194  227 VDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 845-1067 2.38e-83

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: 271.08  E-value: 2.38e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDE--QITRYGDIIVEPASF 922
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEggKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  923 SFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP 1002
Cdd:cd00047   81 EELSDYTIRTLELSPKGC-------------------------SESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEA 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1003 QFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1067
Cdd:cd00047  136 RKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1160-1402 8.49e-75

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 248.31  E-value: 8.49e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   1160 NLLKNRYEAAVPFDKYRVILPPTIGHADssYINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDET 1237
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD--YINASYIDGYKkpKKYIATQGPLPN-TVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   1238 DWSDV--EKYWPIDgSGTECHFGSernsVNVTCVSEE-HHQDFIIRNLSYSMKDNEsmpANQEVVQYSYTGWPsDSIVPK 1314
Cdd:pfam00102   78 EKGREkcAQYWPEE-EGESLEYGD----FTVTLKKEKeDEKDYTVRTLEVSNGGSE---ETRTVKHFHYTGWP-DHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   1315 SANSLMNLIEMVlqRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1394
Cdd:pfam00102  149 SPNSLLDLLRKV--RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                   ....*...
gi 71990705   1395 FCYRALAD 1402
Cdd:pfam00102  227 FLYDAILE 234
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 773-1079 1.12e-74

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: 250.33  E-value: 1.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  773 IPVDDLPTEYVVRHRDTDFLFAQEYESLPH--FQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANF 850
Cdd:cd14621    8 LPVDKLEEEINRRMADDNKLFREEFNALPAcpIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  851 IKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAI 930
Cdd:cd14621   88 INGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  931 RAFDIAHIGEcgpdvipngngveyanvpiVKGQfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLREL-PQFnNSPV 1009
Cdd:cd14621  168 RKFCIQQVGD-------------------VTNK--KPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCnPQY-AGAI 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1010 VIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEWHMYGDTD 1079
Cdd:cd14621  226 VVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTE 295
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 793-1071 1.54e-73

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: 246.49  E-value: 1.54e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  793 FAQEYESLPHFQLD----TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDD--YSDYINANFIKSWKEKKLFIAAQAP 866
Cdd:cd17667    1 FSEDFEEVQRCTADmnitAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDskHSDYINANYVDGYNKAKAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  867 VDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIahigecgpdvi 946
Cdd:cd17667   81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSI----------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  947 pngngveyANVPIVKGQFAN-----NSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTG 1021
Cdd:cd17667  150 --------RNTKVKKGQKGNpkgrqNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTG 221

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 71990705 1022 TFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd17667  222 TYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 820-1067 2.07e-73

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: 243.80  E-value: 2.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  820 RYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQ 899
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  900 CAKYWP-DEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGECgpdvipngngveyanvpivkgqfannsRRILQYHFTN 978
Cdd:cd14548   81 CDHYWPfDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEV---------------------------RSVRQFHFTA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  979 WNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQS 1058
Cdd:cd14548  134 WPDHGVPEAPDSLLRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQT 213


                 ....*....
gi 71990705 1059 LEQYVFIYK 1067
Cdd:cd14548  214 EAQYIFLHQ 222
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 845-1066 1.37e-72

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 240.72  E-value: 1.37e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSF 924
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFDIAHIGecgpdvipngngveyanvpIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFmyrLRELPQF 1004
Cdd:cd14549   81 LATYTVRTFSLKNLK-------------------LKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAA 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1005 NN---SPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIY 1066
Cdd:cd14549  139 NPpgaGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 815-1071 1.98e-71

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: 238.84  E-value: 1.98e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  815 NAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTE 894
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  895 KNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQY 974
Cdd:cd14553   83 RSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNG-------------------------SSEKREVRQF 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  975 HFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNL 1054
Cdd:cd14553  138 QFTAWPDHGVPEHPTPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNY 217

                        250
                 ....*....|....*..
gi 71990705 1055 MVQSLEQYVFIYKALAE 1071
Cdd:cd14553  218 MVQTEDQYIFIHDALLE 234
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 821-1071 4.66e-68

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: 228.67  E-value: 4.66e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  821 YNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQC 900
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  901 AKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIA--HIGECGPdvipngngveyanvpivkgqfannSRRILQYHFTN 978
Cdd:cd14620   81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqLPDGCKA------------------------PRLVTQLHFTS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  979 WNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQS 1058
Cdd:cd14620  137 WPDFGVPFTPIGMLKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQT 216

                        250
                 ....*....|...
gi 71990705 1059 LEQYVFIYKALAE 1071
Cdd:cd14620  217 DMQYSFIYQALLE 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 809-1067 4.74e-67

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: 227.63  E-value: 4.74e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  809 ASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVM 888
Cdd:cd14543   23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  889 VANLTEKNRQQCAKYWPDEQ--ITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaN 966
Cdd:cd14543  103 TTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTET-------------------------D 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  967 NSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNS-------------PVVIHCSAGVGRTGTFISIDSMLDQC 1033
Cdd:cd14543  158 ESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQL 237

                        250       260       270
                 ....*....|....*....|....*....|....
gi 71990705 1034 LAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1067
Cdd:cd14543  238 EDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 793-1071 1.35e-63

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: 217.98  E-value: 1.35e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  793 FAQEYESL-PHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATI 871
Cdd:cd14626   18 FSQEYESIdPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  872 GDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngng 951
Cdd:cd14626   98 SDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNG------------ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  952 veyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLD 1031
Cdd:cd14626  166 -------------SSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 71990705 1032 QCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14626  233 RMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 819-1065 2.14e-63

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 215.45  E-value: 2.14e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  819 NRYNDIRAFDDTRVKLKkINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ 898
Cdd:cd14615    1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  899 QCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTN 978
Cdd:cd14615   80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQT-------------------------NESRTVRHFHFTS 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  979 WNDYKAPECSTGLLRFMYRLRELPQFN--NSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMV 1056
Cdd:cd14615  135 WPDHGVPETTDLLINFRHLVREYMKQNppNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMV 214


                 ....*....
gi 71990705 1057 QSLEQYVFI 1065
Cdd:cd14615  215 QTEDQYVFL 223
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 819-1066 9.59e-63

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


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 213.41  E-value: 9.59e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  819 NRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWK-EKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNr 897
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  898 QQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfannSRRILQYHFT 977
Cdd:cd14547   80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGE---------------------------KRYLKHYWYT 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  978 NWNDYKAPECSTGLLRFMYRLRELPQFNNS--PVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLM 1055
Cdd:cd14547  133 SWPDHKTPEAAQPLLSLVQEVEEARQTEPHrgPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGM 212

                        250
                 ....*....|.
gi 71990705 1056 VQSLEQYVFIY 1066
Cdd:cd14547  213 VQTAEQYEFVH 223
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1190-1398 1.65e-62

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: 211.76  E-value: 1.65e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVML--SDETDWSDVEKYWPIDGsGTECHFGSernsVN 1265
Cdd:cd00047    1 YINASYIDGYRGPkeYIATQGPLPN-TVEDFWRMVWEQKVSVIVMLtnLVEKGREKCERYWPEEG-GKPLEYGD----IT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIRNLSYSMKDNESmpaNQEVVQYSYTGWPSDSIVPksanSLMNLIEMVLQRQSSLMGSQAPIVVHCR 1345
Cdd:cd00047   75 VTLVSEEELSDYTIRTLELSPKGCSE---SREVTHLHYTGWPDHGVPS----SPEDLLALVRRVRKEARKPNGPIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 71990705 1346 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1398
Cdd:cd00047  148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 845-1067 1.01e-61

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: 209.77  E-value: 1.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSF 924
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFDIAhigecgpdvipngngveyanvPIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQF 1004
Cdd:cd14551   81 LVDYTTRKFCIQ---------------------KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPP 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990705 1005 NNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1067
Cdd:cd14551  140 RAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 814-1071 1.92e-61

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 210.27  E-value: 1.92e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  814 ENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLT 893
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  894 EKNRQQCAKYWPDEQITrYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQ 973
Cdd:cd14630   82 EVGRVKCVRYWPDDTEV-YGDIKVTLIETEPLAEYVIRTFTVQKKG-------------------------YHEIREIRQ 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  974 YHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRN 1053
Cdd:cd14630  136 FHFTSWPDHGVPCYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRV 215

                        250
                 ....*....|....*...
gi 71990705 1054 LMVQSLEQYVFIYKALAE 1071
Cdd:cd14630  216 NMVQTEEQYVFVHDAILE 233
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 773-1071 1.24e-60

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 209.56  E-value: 1.24e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  773 IPVDDLpTEYVVRHRDTDFL-FAQEYESL-PHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANF 850
Cdd:cd14625    4 IPISEL-AEHTERLKANDNLkLSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  851 IKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAI 930
Cdd:cd14625   83 IDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFCV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  931 RAFDIahigecgpdvipNGNGveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVV 1010
Cdd:cd14625  163 RTFSL------------HKNG-------------SSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIV 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990705 1011 IHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14625  218 VHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 845-1069 6.36e-60

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: 204.83  E-value: 6.36e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSF 924
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFDIAhigecgpdvipngngveyaNVPIVKG--QFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP 1002
Cdd:cd17668   81 LAYYTVRNFTLR-------------------NTKIKKGsqKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAK 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705 1003 QFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1069
Cdd:cd17668  142 RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 793-1071 1.58e-59

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: 206.05  E-value: 1.58e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  793 FAQEYESLPHFQLDTVASNRK-ENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATI 871
Cdd:cd14633   17 FKEEYESFFEGQSAPWDSAKKdENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  872 GDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQiTRYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngng 951
Cdd:cd14633   97 YDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDT-EIYKDIKVTLIETELLAEYVIRTFAVEKRG------------ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  952 veyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLD 1031
Cdd:cd14633  164 -------------VHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLD 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 71990705 1032 QCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14633  231 MAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 815-1068 2.12e-59

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: 204.30  E-value: 2.12e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  815 NAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTE 894
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  895 KNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkGQfannSRRILQY 974
Cdd:cd14554   86 MGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD---------------------GQ----SRTVRQF 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  975 HFTNWNDYKAPECSTGLLRFMYRL-RELPQFN-NSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQR 1052
Cdd:cd14554  141 QFTDWPEQGVPKSGEGFIDFIGQVhKTKEQFGqEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQR 220

                        250
                 ....*....|....*.
gi 71990705 1053 NLMVQSLEQYVFIYKA 1068
Cdd:cd14554  221 PAMVQTEDQYQFCYRA 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 845-1066 3.11e-59

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: 202.86  E-value: 3.11e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIK-SWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQIT-RYGDIIVEPASF 922
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  923 SFHSDYA--IRAFDIAHigecgpdvipngNGVEyanvpivkgqfannSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRE 1000
Cdd:cd18533   81 EENDDGGfiVREFELSK------------EDGK--------------VKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRE 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705 1001 LPQ--FNNSPVVIHCSAGVGRTGTFISIDSMLD---------QCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIY 1066
Cdd:cd18533  135 LNDsaSLDPPIIVHCSAGVGRTGTFIALDSLLDelkrglsdsQDLEDSEDPVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 773-1071 1.68e-58

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 203.42  E-value: 1.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  773 IPVDDLpTEYVVRHRDTDFL-FAQEYESL-PHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANF 850
Cdd:cd14624    4 IPILEL-ADHIERLKANDNLkFSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  851 IKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAI 930
Cdd:cd14624   83 IDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  931 RAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVV 1010
Cdd:cd14624  163 RTFALYKNG-------------------------SSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMV 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990705 1011 IHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14624  218 VHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 819-1067 2.32e-58

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: 200.92  E-value: 2.32e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  819 NRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ 898
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  899 QCAKYWP-DEQITRYGDIIVEPASFSFHSDYAIRAFDIahigeCGPDVIpngngveyanvpivkgqfaNNSRRILQYHFT 977
Cdd:cd14617   81 KCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKI-----CSEEQL-------------------DAPRLVRHFHYT 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  978 NWNDYKAPECSTGLLRFMYRLRELPQFNNS--PVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLM 1055
Cdd:cd14617  137 VWPDHGVPETTQSLIQFVRTVRDYINRTPGsgPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHM 216

                        250
                 ....*....|..
gi 71990705 1056 VQSLEQYVFIYK 1067
Cdd:cd14617  217 VQTECQYVYLHQ 228
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 819-1069 6.68e-58

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: 199.73  E-value: 6.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  819 NRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ 898
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  899 QCAKYWP-DEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGECGpdvipngngveyanvpivkgqfannSRRILQYHFT 977
Cdd:cd14619   81 KCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQK-------------------------TLSVRHFHFT 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  978 NWNDYKAPECSTGLLRFMYRLREL--PQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLM 1055
Cdd:cd14619  136 AWPDHGVPSSTDTLLAFRRLLRQWldQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLM 215

                        250
                 ....*....|....
gi 71990705 1056 VQSLEQYVFIYKAL 1069
Cdd:cd14619  216 VQTESQYVFLHQCI 229
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 845-1067 2.34e-57

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 196.97  E-value: 2.34e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWP--DEQITRYGDIIVEPASF 922
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  923 SFHSDYAIRAFDIAHIGECGpdvipngngveyanvpivkgqfanNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP 1002
Cdd:cd14557   81 KICPDYIIRKLNINNKKEKG------------------------SGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFN 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1003 QFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1067
Cdd:cd14557  137 NFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 815-1072 7.39e-56

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: 194.60  E-value: 7.39e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  815 NAIKNRYNDIRAFDDTRVKLKKINGD-DYSDYINANFIKS-------WKEKKLFIAAQAPVDATIGDFWRMVWEQESYLI 886
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIRNenegpttDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  887 VMVANLTEKNRQQCAKYWPDEQITR-YGDIIVEPASFSFHSDYAIRAFDIAHIGECGPdvipngngveyanvpivkgqfa 965
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQKqYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDP---------------------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  966 nnSRRILQYHFTNWNDYKAPECSTGLLRFMYRL-RELPQFNNS-PVVIHCSAGVGRTGTFISIDSMLDQC----LAEDkA 1039
Cdd:cd14544  139 --IREIWHYQYLSWPDHGVPSDPGGVLNFLEDVnQRQESLPHAgPIVVHCSAGIGRTGTFIVIDMLLDQIkrkgLDCD-I 215

                        250       260       270
                 ....*....|....*....|....*....|...
gi 71990705 1040 NIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1072
Cdd:cd14544  216 DIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQY 248
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 800-1067 1.32e-55

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: 193.57  E-value: 1.32e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  800 LPHFqldtvASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVW 879
Cdd:cd14614    2 IPHF-----AADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  880 EQESYLIVMVANLTEKNRQQCAKYWP-DEQITRYGDIIVEPASFSFHSDYAIRAFDIAhigecgpdvipngngveyanvp 958
Cdd:cd14614   77 QQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVS---------------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  959 ivkgqFANNSRRILQYHFTNWNDYKAPECSTG--LLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAE 1036
Cdd:cd14614  135 -----YADEVQDVMHFNYTAWPDHGVPTANAAesILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH 209

                        250       260       270
                 ....*....|....*....|....*....|.
gi 71990705 1037 DKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1067
Cdd:cd14614  210 EFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 819-1069 1.55e-54

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: 190.15  E-value: 1.55e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  819 NRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ 898
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  899 QCAKYWPDEQI-TRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFT 977
Cdd:cd14618   81 LCDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKLWHEDL-------------------------RKERRVKHLHYT 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  978 NWNDYKAPECSTGLLRFMYRLRELPQF--NNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLM 1055
Cdd:cd14618  136 AWPDHGIPESTSSLMAFRELVREHVQAtkGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLM 215

                        250
                 ....*....|....
gi 71990705 1056 VQSLEQYVFIYKAL 1069
Cdd:cd14618  216 IQTLSQYIFLHSCI 229
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 805-1071 1.04e-53

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: 189.27  E-value: 1.04e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  805 LDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESY 884
Cdd:cd14603   20 CSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  885 LIVMVANLTEKNRQQCAKYWPDEQitrygdiivEPASFSfhsdyairAFDIAHIGE--CGPDVIpngngveyanVPIVKG 962
Cdd:cd14603  100 VILMACREIEMGKKKCERYWAQEQ---------EPLQTG--------PFTITLVKEkrLNEEVI----------LRTLKV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  963 QFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAE---DKA 1039
Cdd:cd14603  153 TFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQripPDF 232

                        250       260       270
                 ....*....|....*....|....*....|..
gi 71990705 1040 NIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14603  233 SIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 845-1069 9.33e-53

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: 184.01  E-value: 9.33e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSF 924
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFdiahigecgpdVIPNGNGveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRL-RELPQ 1003
Cdd:cd14552   81 YEDYTLRDF-----------LVTKGKG--------------GSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQ 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71990705 1004 FNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1069
Cdd:cd14552  136 SGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 816-1070 1.53e-52

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 185.04  E-value: 1.53e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  816 AIKNRYNDIRAFDDTRVKLKKI-NGDDYSDYINANFIKSWK-EKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLT 893
Cdd:cd14612   16 ASKDRYKTILPNPQSRVCLRRAgSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  894 EKNrQQCAKYWPDEQITrYGDIIVEPASFSFHSDYAIRAFDIAHIGECgpdvipngngveyanvpivkgqfannsRRILQ 973
Cdd:cd14612   96 EKK-EKCVHYWPEKEGT-YGRFEIRVQDMKECDGYTIRDLTIQLEEES---------------------------RSVKH 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  974 YHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNS--PVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQ 1051
Cdd:cd14612  147 YWFSSWPDHQTPESAGPLLRLVAEVEESRQTAASpgPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLD 226

                        250
                 ....*....|....*....
gi 71990705 1052 RNLMVQSLEQYVFIYKALA 1070
Cdd:cd14612  227 RGGMIQTSEQYQFLHHTLA 245
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 845-1071 2.02e-52

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 183.19  E-value: 2.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITrYGDIIVEPASFSF 924
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV-YGDIKVTLVETEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQF 1004
Cdd:cd14555   80 LAEYVVRTFALERRG-------------------------YHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPP 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705 1005 NNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14555  135 SAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 807-1071 4.92e-52

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: 185.52  E-value: 4.92e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  807 TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLI 886
Cdd:cd14604   49 TATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAII 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  887 VMVANLTEKNRQQCAKYWP--DEQITRYGDIIVEPASFSFHSDYAIRAFDIahigecgpdvipngngveyanvpivkgQF 964
Cdd:cd14604  129 VMACREFEMGRKKCERYWPlyGEEPMTFGPFRISCEAEQARTDYFIRTLLL---------------------------EF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  965 ANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISID---SMLDQCLAEDKANI 1041
Cdd:cd14604  182 QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNV 261

                        250       260       270
                 ....*....|....*....|....*....|
gi 71990705 1042 FEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14604  262 FNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 831-1071 6.43e-52

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


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 182.14  E-value: 6.43e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  831 RVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQiT 910
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDT-E 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  911 RYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTG 990
Cdd:cd14631   80 VYGDFKVTCVEMEPLAEYVVRTFTLERRG-------------------------YNEIREVKQFHFTGWPDHGVPYHATG 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  991 LLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALA 1070
Cdd:cd14631  135 LLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214


                 .
gi 71990705 1071 E 1071
Cdd:cd14631  215 E 215
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 808-1072 1.06e-51

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: 184.16  E-value: 1.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  808 VASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIV 887
Cdd:cd14628   45 ISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  888 MVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkGQfann 967
Cdd:cd14628  125 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD---------------------GQ---- 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  968 SRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP-QF-NNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFV 1045
Cdd:cd14628  180 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKeQFgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTV 259

                        250       260
                 ....*....|....*....|....*..
gi 71990705 1046 CNLRRQRNLMVQSLEQYVFIYKALAEW 1072
Cdd:cd14628  260 KMLRTQRPAMVQTEDQYQFCYRAALEY 286
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 808-1072 2.69e-51

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: 183.01  E-value: 2.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  808 VASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIV 887
Cdd:cd14627   46 ISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  888 MVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkGQfann 967
Cdd:cd14627  126 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD---------------------GQ---- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  968 SRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP-QF-NNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFV 1045
Cdd:cd14627  181 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKeQFgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTV 260

                        250       260
                 ....*....|....*....|....*..
gi 71990705 1046 CNLRRQRNLMVQSLEQYVFIYKALAEW 1072
Cdd:cd14627  261 KMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 819-1067 6.19e-51

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: 179.33  E-value: 6.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  819 NRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ 898
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  899 QCAKYWPDEQ--ITRYGDIIVEPASFSFHSDYAIRAFDIAHIGECgpdvipngngveyanvpivkgqfannsRRILQYHF 976
Cdd:cd14616   81 RCHQYWPEDNkpVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDY---------------------------MMVRQCNF 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  977 TNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMV 1056
Cdd:cd14616  134 TSWPEHGVPESSAPLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMV 213

                        250
                 ....*....|.
gi 71990705 1057 QSLEQYVFIYK 1067
Cdd:cd14616  214 QNLAQYIFLHQ 224
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 818-1067 2.03e-50

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: 178.35  E-value: 2.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  818 KNRYNDIRAFDDTRVKLKKINGDdySDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNR 897
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  898 QQCAKYWPDEQITrygDIIVEPASFSF-------HSDYAIRAFDIAHIgecgpdvipngngveyanvpivKGQFannSRR 970
Cdd:cd14545   79 IKCAQYWPQGEGN---AMIFEDTGLKVtllseedKSYYTVRTLELENL----------------------KTQE---TRE 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  971 ILQYHFTNWNDYKAPECSTGLLRFMYRLRE--LPQFNNSPVVIHCSAGVGRTGTFisidSMLDQCLAE------DKANIF 1042
Cdd:cd14545  131 VLHFHYTTWPDFGVPESPAAFLNFLQKVREsgSLSSDVGPPVVHCSAGIGRSGTF----CLVDTCLVLiekgnpSSVDVK 206

                        250       260
                 ....*....|....*....|....*
gi 71990705 1043 EFVCNLRRQRNLMVQSLEQYVFIYK 1067
Cdd:cd14545  207 KVLLEMRKYRMGLIQTPDQLRFSYL 231
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 808-1072 2.03e-50

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: 180.69  E-value: 2.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  808 VASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIV 887
Cdd:cd14629   46 ISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  888 MVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkGQfann 967
Cdd:cd14629  126 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD---------------------GQ---- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  968 SRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP-QF-NNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFV 1045
Cdd:cd14629  181 SRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKeQFgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTV 260

                        250       260
                 ....*....|....*....|....*..
gi 71990705 1046 CNLRRQRNLMVQSLEQYVFIYKALAEW 1072
Cdd:cd14629  261 KTLRTQRPAMVQTEDQYQLCYRAALEY 287
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 820-1071 5.85e-50

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: 176.77  E-value: 5.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  820 RYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQ 899
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  900 CAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNW 979
Cdd:cd14623   81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRE-------------------------NKSRQIRQFHFHGW 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  980 NDYKAPECSTGLLRFMYRL-RELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQS 1058
Cdd:cd14623  136 PEVGIPSDGKGMINIIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQT 215

                        250
                 ....*....|...
gi 71990705 1059 LEQYVFIYKALAE 1071
Cdd:cd14623  216 LEQYEFCYKVVQE 228
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 814-1072 1.71e-49

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: 176.36  E-value: 1.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  814 ENAIKNRYNDIRAFDDTRVKLKkiNGD---DYSDYINANFI--------KSWKEKKLFIAAQAPVDATIGDFWRMVWEQE 882
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLH--DGDpnePVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQEN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  883 SYLIVMVANLTEKNRQQCAKYWPDE-QITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivk 961
Cdd:cd14605   79 SRVIVMTTKEVERGKSKCVKYWPDEyALKEYGVMRVRNVKESAAHDYILRELKLSKVGQ--------------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  962 gqfANNSRRILQYHFTNWNDYKAPECSTGLLRFM--YRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDqcLAEDKA 1039
Cdd:cd14605  138 ---GNTERTVWQYHFRTWPDHGVPSDPGGVLDFLeeVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILID--IIREKG 212

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 71990705 1040 -----NIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1072
Cdd:cd14605  213 vdcdiDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHY 250
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 844-1072 2.52e-49

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: 174.04  E-value: 2.52e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  844 DYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFS 923
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  924 FHSDYAIRAFdiahigecgpdvipngngveyanvpIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRL-RELP 1002
Cdd:cd14622   81 LLETISIRDF-------------------------LVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQ 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1003 QFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1072
Cdd:cd14622  136 QTGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 818-1070 2.60e-49

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: 176.21  E-value: 2.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  818 KNRYNDIRAFDDTRVKLKKINGDDY-SDYINANFIKSW-KEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEK 895
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  896 NrQQCAKYWPDEQITrYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfannSRRILQYH 975
Cdd:cd14613  108 N-EKCTEYWPEEQVT-YEGIEITVKQVIHADDYRLRLITLKSGGE---------------------------ERGLKHYW 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  976 FTNWNDYKAPECSTGLLRFMYRLRELPQ---FNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQR 1052
Cdd:cd14613  159 YTSWPDQKTPDNAPPLLQLVQEVEEARQqaePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDR 238

                        250
                 ....*....|....*...
gi 71990705 1053 NLMVQSLEQYVFIYKALA 1070
Cdd:cd14613  239 GGMIQTCEQYQFVHHVLS 256
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1160-1399 1.10e-48

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: 173.48  E-value: 1.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1160 NLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLS--D 1235
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRgaYIATQGPLAE-TTEDFWRMLWEHNSTIIVMLTklR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1236 ETDWSDVEKYWPIDGSGTECHFgsernsvNVTCVSEEHHQDFIIRNLSYS-MKDNESmpanQEVVQYSYTGWPsDSIVPK 1314
Cdd:cd14554   85 EMGREKCHQYWPAERSARYQYF-------VVDPMAEYNMPQYILREFKVTdARDGQS----RTVRQFQFTDWP-EQGVPK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1315 SANSLMNLIEMVlQRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1394
Cdd:cd14554  153 SGEGFIDFIGQV-HKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQ 231


                 ....*
gi 71990705 1395 FCYRA 1399
Cdd:cd14554  232 FCYRA 236
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 782-1071 1.17e-48

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: 175.24  E-value: 1.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  782 YVVRHRDTDFLFAQEYESLPHFQLDTVASN---RKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKK 858
Cdd:cd14610    8 YMEDHLKNKNRLEKEWEALCAYQAEPNATNvaqREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  859 -LFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGdiIVEPASFSFH---SDYAIRAFd 934
Cdd:cd14610   88 pAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYH--IYEVNLVSEHiwcEDFLVRSF- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  935 iahigecgpdvipngngveyanvpIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCS 1014
Cdd:cd14610  165 ------------------------YLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCS 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 71990705 1015 AGVGRTGTFISIDSMLDQCLAEDKA-NIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14610  221 DGAGRSGTYILIDMVLNKMAKGAKEiDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 845-1071 7.61e-48

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: 169.85  E-value: 7.61e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITrYGDIIVEPASFSF 924
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT-YGDIKITLLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQF 1004
Cdd:cd14632   80 LAEYSVRTFALERRG-------------------------YSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPP 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705 1005 NNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14632  135 DAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 818-1071 1.32e-46

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: 167.32  E-value: 1.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  818 KNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNR 897
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  898 QQCAKYW--PDEQITRYGDIIVEPASFSFHSDYAIRafdiahigecgpdvipngngveyanvpIVKGQFANNSRRILQYH 975
Cdd:cd14602   81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIR---------------------------TLKVKFNSETRTIYQFH 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  976 FTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISID---SMLDQCLAEDKANIFEFVCNLRRQR 1052
Cdd:cd14602  134 YKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDytwMLLKDGIIPENFSVFSLIQEMRTQR 213

                        250
                 ....*....|....*....
gi 71990705 1053 NLMVQSLEQYVFIYKALAE 1071
Cdd:cd14602  214 PSLVQTKEQYELVYNAVIE 232
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 812-1072 2.76e-46

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: 167.75  E-value: 2.76e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  812 RKENAIKNRYNDIRAFDDTRVKLKkiNGDDY---SDYINANFIKS--W---KEKKLFIAAQAPVDATIGDFWRMVWEQES 883
Cdd:cd14606   15 RPENKSKNRYKNILPFDHSRVILQ--GRDSNipgSDYINANYVKNqlLgpdENAKTYIASQGCLEATVNDFWQMAWQENS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  884 YLIVMVANLTEKNRQQCAKYWPDEQITR-YGDIIVEPASFSFHSDYAIRafdiaHIGECGPDvipNGNGVeyanvpivkg 962
Cdd:cd14606   93 RVIVMTTREVEKGRNKCVPYWPEVGMQRaYGPYSVTNCGEHDTTEYKLR-----TLQVSPLD---NGELI---------- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  963 qfannsRRILQYHFTNWNDYKAPECSTGLLRFM----YRLRELPqfNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAED- 1037
Cdd:cd14606  155 ------REIWHYQYLSWPDHGVPSEPGGVLSFLdqinQRQESLP--HAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGl 226

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 71990705 1038 --KANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1072
Cdd:cd14606  227 dcDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQF 263
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 813-1069 6.10e-46

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: 165.39  E-value: 6.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  813 KENAIKNRYNDIRAFDDTRVKLkkinGDDySDYINANFIK--SWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVA 890
Cdd:cd14597    1 KENRKKNRYKNILPYDTTRVPL----GDE-GGYINASFIKmpVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  891 NLTEKNRQQCAKYWPDEqiTRYGDIIVEPASFSFHSDYAIRAFDIAHIgecgpdvipngngvEYANVPivkgqfANNSRR 970
Cdd:cd14597   76 QEVEGGKIKCQRYWPEI--LGKTTMVDNRLQLTLVRMQQLKNFVIRVL--------------ELEDIQ------TREVRH 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  971 ILQYHFTNWNDYKAPECSTGLLRFMYRLRELpqFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRR 1050
Cdd:cd14597  134 ITHLNFTAWPDHDTPSQPEQLLTFISYMRHI--HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRL 211

                        250
                 ....*....|....*....
gi 71990705 1051 QRNLMVQSLEQYVFIYKAL 1069
Cdd:cd14597  212 QRHGMVQTEDQYIFCYQVI 230
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 845-1066 1.50e-45

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: 163.33  E-value: 1.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITrYGDIIVEPASFSF 924
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT-YGDIEVELKDTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRE-LPQ 1003
Cdd:cd14558   80 SPTYTVRVFEITHLKR-------------------------KDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQkLPY 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71990705 1004 FN-----NSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIY 1066
Cdd:cd14558  135 KNskhgrSVPIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 845-1071 1.87e-45

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: 162.93  E-value: 1.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIK--SWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPD---EQITRYGDIIVEP 919
Cdd:cd14538    1 YINASHIRipVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  920 ASFSFHSDYAIRAFDIAHI--GEcgpdvipngngveyanvpivkgqfannSRRILQYHFTNWNDYKAPECSTGLLRFMYR 997
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKetGE---------------------------VHHITHLNFTTWPDHGTPQSADPLLRFIRY 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990705  998 LRELpqFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14538  134 MRRI--HNSGPIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 818-1066 2.37e-45

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: 163.55  E-value: 2.37e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  818 KNRYNDIRAFDDTRVKLKKINGDDY-SDYINANFIKSWK-EKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEK 895
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  896 NrQQCAKYWPdEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGECgpdvipngngveyanvpivkgqfannsRRILQYH 975
Cdd:cd14611   82 N-EKCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQS---------------------------RSVKHYW 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  976 FTNWNDYKAPECSTGLLRFMYRLRE--LPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRN 1053
Cdd:cd14611  133 YTSWPDHKTPDSAQPLLQLMLDVEEdrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRG 212

                        250
                 ....*....|...
gi 71990705 1054 LMVQSLEQYVFIY 1066
Cdd:cd14611  213 GMVQTSEQYEFVH 225
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 845-1067 4.85e-45

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: 161.82  E-value: 4.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQ--ITRYGDIIVEPASF 922
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeeQLQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  923 SFHS-DYAIRAfdiahigecgpdvipngngveyanvpiVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLREL 1001
Cdd:cd14542   81 KRVGpDFLIRT---------------------------LKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1002 PQFNNSPVVIHCSAGVGRTGTFISID----SMLDQCLAEDkANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1067
Cdd:cd14542  134 QGSEDVPICVHCSAGCGRTGTICAIDyvwnLLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 814-1084 5.23e-45

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: 164.43  E-value: 5.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  814 ENAIKNRYNDIRAFDDTRVKLKKinGDDysDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLT 893
Cdd:cd14608   24 KNKNRNRYRDVSPFDHSRIKLHQ--EDN--DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVM 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  894 EKNRQQCAKYWP----DEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSR 969
Cdd:cd14608  100 EKGSLKCAQYWPqkeeKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLT-------------------------TQETR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  970 RILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFN--NSPVVIHCSAGVGRTGTFISIDS---MLDQCLAEDKANIFEF 1044
Cdd:cd14608  155 EILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSpeHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKV 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 71990705 1045 VCNLRRQRNLMVQSLEQYVFIYKALAEWHMYGDTDEDVRD 1084
Cdd:cd14608  235 LLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQD 274
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1165-1395 8.02e-44

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: 159.06  E-value: 8.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1165 RYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVsEGTAFDFWRMIADQNVTTVVMLSD--ETDWS 1240
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSprEFIATQGPL-PGTKDDFWRMVWEQNSHTIVMLTQcmEKGRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1241 DVEKYWPIDGsgTECHFGSernsVNVTCVSEEHHQDFIIRNLSYSMKDnESMPanqeVVQYSYTGWPsDSIVPKSANSLM 1320
Cdd:cd14548   80 KCDHYWPFDQ--DPVYYGD----ITVTMLSESVLPDWTIREFKLERGD-EVRS----VRQFHFTAWP-DHGVPEAPDSLL 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705 1321 NLIEMVLQRqssLMGSQAPIVVHCRNGSSESGIFicISLLWLRQK--AEQRIDVFQTVKGLQSHRPMMFTRFEQYSF 1395
Cdd:cd14548  148 RFVRLVRDY---IKQEKGPTIVHCSAGVGRTGTF--IALDRLLQQieSEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1118-1404 1.33e-42

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: 157.97  E-value: 1.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1118 AIVSSRESMTTSNGETGLEEEFKKL---ERNLTTPLSSNFAAkdeNLLKNRYEAAVPFDKYRVILPPTIGHADSSYINAS 1194
Cdd:cd14628   10 AYIQKLTQIETGENVTGMELEFKRLassKAHTSRFISANLPC---NKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINAS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1195 HIKGYFFD--YIAAQDPVSEGTAfDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTECHFgsernsvNVTCVS 1270
Cdd:cd14628   87 FIDGYRQQkaYIATQGPLAETTE-DFWRMLWEHNSTIVVMLTKlrEMGREKCHQYWPAERSARYQYF-------VVDPMA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1271 EEHHQDFIIRNLSYS-MKDNESmpanQEVVQYSYTGWPSDSiVPKSANSLMNLIEMVlQRQSSLMGSQAPIVVHCRNGSS 1349
Cdd:cd14628  159 EYNMPQYILREFKVTdARDGQS----RTVRQFQFTDWPEQG-VPKSGEGFIDFIGQV-HKTKEQFGQDGPISVHCSAGVG 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1350 ESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1404
Cdd:cd14628  233 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1133-1404 2.02e-42

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: 157.59  E-value: 2.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1133 TGLEEEFKKL---ERNLTTPLSSNFAAkdeNLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQ 1207
Cdd:cd14627   26 TGMELEFKRLansKAHTSRFISANLPC---NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQkaYIATQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1208 DPVSEGTAfDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTECHFgsernsvNVTCVSEEHHQDFIIRNLSYS 1285
Cdd:cd14627  103 GPLAETTE-DFWRMLWENNSTIVVMLTKlrEMGREKCHQYWPAERSARYQYF-------VVDPMAEYNMPQYILREFKVT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1286 -MKDNESmpanQEVVQYSYTGWPSDSiVPKSANSLMNLIEMVlQRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQ 1364
Cdd:cd14627  175 dARDGQS----RTVRQFQFTDWPEQG-VPKSGEGFIDFIGQV-HKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERM 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 71990705 1365 KAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1404
Cdd:cd14627  249 RYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 796-1069 2.06e-42

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: 156.28  E-value: 2.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  796 EYESLPHfqldTVASNrKENAIKNRYNDIRAFDDTRVKLKKINgddySDYINANFIKSWKEKKLFIAAQAPVDATIGDFW 875
Cdd:cd14607   10 ESHDYPH----RVAKY-PENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  876 RMVWEQESYLIVMVANLTEKNRQQCAKYWP--DEQITRYGD--IIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngng 951
Cdd:cd14607   81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPtdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENIN------------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  952 veyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFN--NSPVVIHCSAGVGRTGTFisidSM 1029
Cdd:cd14607  149 -------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSpeHGPAVVHCSAGIGRSGTF----SL 211

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 71990705 1030 LDQCLA------EDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1069
Cdd:cd14607  212 VDTCLVlmekkdPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1131-1397 2.50e-42

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: 156.37  E-value: 2.50e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1131 GETGLEEEFKKLeRNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQD 1208
Cdd:cd14543    1 QKRGIYEEYEDI-RREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKnaYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1209 PVsEGTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGTEcHFGsernSVNVTCVSEEHHQDFIIRNLS-YS 1285
Cdd:cd14543   80 PL-PKTYSDFWRMVWEQKVLVIVMTTrvVERGRVKCGQYWPLEEGSSL-RYG----DLTVTNLSVENKEHYKKTTLEiHN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1286 MKDNESmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSL---MGSQ-------APIVVHCRNGSSESGIF- 1354
Cdd:cd14543  154 TETDES----RQVTHFQFTSWP-DFGVPSSAAALLDFLGEVRQQQALAvkaMGDRwkghppgPPIVVHCSAGIGRTGTFc 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 71990705 1355 ---ICISllwlRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd14543  229 tldICLS----QLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 844-1068 3.48e-42

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: 154.02  E-value: 3.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  844 DYINANFIK------SWKEKklFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPD-EQITRYGDII 916
Cdd:cd14541    1 DYINANYVNmeipgsGIVNR--YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  917 VEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMY 996
Cdd:cd14541   79 ITCVSEEVTPSFAFREFILTNTNT-------------------------GEERHITQMQYLAWPDHGVPDDSSDFLDFVK 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71990705  997 RLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKA 1068
Cdd:cd14541  134 RVRQNRVGMVEPTVVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEA 205
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 814-1069 5.85e-42

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: 155.39  E-value: 5.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  814 ENAIKNRYNDIRAFDDTRVKLkkiNGDDysDYINANFIK----SWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMV 889
Cdd:cd14600   39 QNMDKNRYKDVLPYDATRVVL---QGNE--DYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  890 ANLTEKNRQQCAKYWPDEQ-ITRYGDIIVEPASFSFHSDYAIRAFDIAHIgECGpdvipngngveyanvpivkgqfanNS 968
Cdd:cd14600  114 TTLTERGRTKCHQYWPDPPdVMEYGGFRVQCHSEDCTIAYVFREMLLTNT-QTG------------------------EE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  969 RRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQfNNSPVVIHCSAGVGRTGTFISIDSMLdqCLAEDKANIF--EFVC 1046
Cdd:cd14600  169 RTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTMETAM--CLTERNQPVYplDIVR 245

                        250       260
                 ....*....|....*....|...
gi 71990705 1047 NLRRQRNLMVQSLEQYVFIYKAL 1069
Cdd:cd14600  246 KMRDQRAMMVQTSSQYKFVCEAI 268
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1190-1397 1.03e-41

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: 152.16  E-value: 1.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTEchfgsernSVN 1265
Cdd:cd14558    1 YINASFIDGYWGpkSLIATQGPLPD-TIADFWQMIFQKKVKVIVMLTElkEGDQEQCAQYWGDEKKTYG--------DIE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIRNLS-YSMKDNESmpanQEVVQYSYTGWpSDSIVPKSANSLMNLIEMVLQRQ---SSLMGSQAPIV 1341
Cdd:cd14558   72 VELKDTEKSPTYTVRVFEiTHLKRKDS----RTVYQYQYHKW-KGEELPEKPKDLVDMIKSIKQKLpykNSKHGRSVPIV 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 71990705 1342 VHCRNGSSESGIFICislLW-LRQKA--EQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd14558  147 VHCSDGSSRTGIFCA---LWnLLESAetEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 845-1072 2.23e-41

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: 151.84  E-value: 2.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIK-SWKEKKLF-IAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQI----TRYGDIIVE 918
Cdd:cd14540    1 YINASHITaTVGGKQRFyIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGehdaLTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  919 PASFSFHSDYAIRAFDIAHIGECgpdvipngngveyanvpivkgqfanNSRRILQYHFTNWNDYKAPECSTGLLRFMYRL 998
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSG-------------------------QSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEI 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  999 REL---------PQFNNSPVVIHCSAGVGRTGTFISIDSMLdQCLAED-KANIFEFVCNLRRQRNLMVQSLEQYVFIYKA 1068
Cdd:cd14540  136 NSVrrhtnqdvaGHNRNPPTLVHCSAGVGRTGVVILADLML-YCLDHNeELDIPRVLALLRHQRMLLVQTLAQYKFVYNV 214


                 ....
gi 71990705 1069 LAEW 1072
Cdd:cd14540  215 LIQY 218
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 784-1071 3.21e-41

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: 153.65  E-value: 3.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  784 VRHRDTdflFAQEYESLPHFQLD---TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINAN-FIKSWKEKKL 859
Cdd:cd14609   11 LRNRDR---LAKEWQALCAYQAEpntCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  860 FIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGdiIVEPASFSFH---SDYAIRAFDIA 936
Cdd:cd14609   88 YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYH--IYEVNLVSEHiwcEDFLVRSFYLK 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  937 HIGecgpdvipngngveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAG 1016
Cdd:cd14609  166 NVQ-------------------------TQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDG 220

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1017 VGRTGTFISIDSMLDQcLAE-----DKANIFEFVcnlRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14609  221 AGRTGTYILIDMVLNR-MAKgvkeiDIAATLEHV---RDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1126-1406 4.08e-41

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: 153.93  E-value: 4.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1126 MTTSNGETGLEEEFKKLERnLTTPLSS------NFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGY 1199
Cdd:cd14604   18 STDHNGEDNFASDFMRLRR-LSTKYRTekiyptATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1200 F--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDW--SDVEKYWPIDGSGTeCHFGSERnsvnVTCVSEEHHQ 1275
Cdd:cd14604   97 YgpKAYIATQGPLAN-TVIDFWRMIWEYNVAIIVMACREFEMgrKKCERYWPLYGEEP-MTFGPFR----ISCEAEQART 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1276 DFIIRNLSYSMkDNESmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFI 1355
Cdd:cd14604  171 DYFIRTLLLEF-QNET----RRLYQFHYVNWP-DHDVPSSFDSILDMISLMRKYQEH---EDVPICIHCSAGCGRTGAIC 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71990705 1356 CISLLWLRQKA---EQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYISK 1406
Cdd:cd14604  242 AIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEK 295
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1133-1404 2.84e-40

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: 151.42  E-value: 2.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1133 TGLEEEFKKL---ERNLTTPLSSNFAAkdeNLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQ 1207
Cdd:cd14629   26 TAMELEFKLLansKAHTSRFISANLPC---NKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQkaYIATQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1208 DPVSEGTAfDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTECHFgsernsvNVTCVSEEHHQDFIIRNLSYS 1285
Cdd:cd14629  103 GPLAETTE-DFWRMLWEHNSTIVVMLTKlrEMGREKCHQYWPAERSARYQYF-------VVDPMAEYNMPQYILREFKVT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1286 -MKDNESmpanQEVVQYSYTGWPSDSiVPKSANSLMNLIEMVlQRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQ 1364
Cdd:cd14629  175 dARDGQS----RTIRQFQFTDWPEQG-VPKTGEGFIDFIGQV-HKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERM 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 71990705 1365 KAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1404
Cdd:cd14629  249 RYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1160-1405 2.01e-39

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: 146.77  E-value: 2.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1160 NLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDET 1237
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQnaYIATQGPLPE-TFGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1238 DWSDV--EKYWPIDGSGTechFGSernsVNVTCVSEEHHQDFIIRNLSYSMkdnESMPANQEVVQYSYTGWPsDSIVPKS 1315
Cdd:cd14553   82 ERSRVkcDQYWPTRGTET---YGL----IQVTLLDTVELATYTVRTFALHK---NGSSEKREVRQFQFTAWP-DHGVPEH 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1316 ANSLMnlieMVLQRQSSLMGSQA-PIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1394
Cdd:cd14553  151 PTPFL----AFLRRVKACNPPDAgPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYI 226

                        250
                 ....*....|.
gi 71990705 1395 FCYRALADYIS 1405
Cdd:cd14553  227 FIHDALLEAVT 237
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1160-1404 3.63e-39

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: 146.45  E-value: 3.63e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1160 NLLKNRYEAAVPFDKYRVIL---PPTIGHADssYINASHIK---------GYFFDYIAAQDPVsEGTAFDFWRMIADQNV 1227
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILkdrDPNVPGSD--YINANYIRnenegpttdENAKTYIATQGCL-ENTVSDFWSMVWQENS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1228 TTVVMLSDETDW--SDVEKYWPIDGSGTEchFGSERnsvnVTCVSEEHHQDFIIRNLSYSMKDNESMPanQEVVQYSYTG 1305
Cdd:cd14544   78 RVIVMTTKEVERgkNKCVRYWPDEGMQKQ--YGPYR----VQNVSEHDTTDYTLRELQVSKLDQGDPI--REIWHYQYLS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1306 WPsDSIVPKSANSLMNLIEMVLQRQSSLMgSQAPIVVHCRNGSSESGIFICISLLwLRQKAEQ----RIDVFQTVKGLQS 1381
Cdd:cd14544  150 WP-DHGVPSDPGGVLNFLEDVNQRQESLP-HAGPIVVHCSAGIGRTGTFIVIDML-LDQIKRKgldcDIDIQKTIQMVRS 226

                        250       260
                 ....*....|....*....|...
gi 71990705 1382 HRPMMFTRFEQYSFCYRALADYI 1404
Cdd:cd14544  227 QRSGMVQTEAQYKFIYVAVAQYI 249
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1170-1402 4.38e-39

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: 145.57  E-value: 4.38e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1170 VPFDKYRVILPPTIGHADSSYINASHIKGY--FFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKY 1245
Cdd:cd14623    6 IPYEFNRVIIPVKRGEENTDYVNASFIDGYrqKDSYIASQGPLQH-TIEDFWRMIWEWKSCSIVMLTEleERGQEKCAQY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1246 WPIDGSGTechFGSernsVNVTCVSEEHHQDFIIRNLSYS-MKDNESmpanQEVVQYSYTGWPSDSIvPKSANSLMNLIE 1324
Cdd:cd14623   85 WPSDGSVS---YGD----ITIELKKEEECESYTVRDLLVTnTRENKS----RQIRQFHFHGWPEVGI-PSDGKGMINIIA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71990705 1325 MVlQRQSSLMGSQaPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALAD 1402
Cdd:cd14623  153 AV-QKQQQQSGNH-PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1190-1400 8.06e-39

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: 143.95  E-value: 8.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTEchfgserNSVN 1265
Cdd:cd14552    1 YINASFIDGYRQKdaYIATQGPLDH-TVEDFWRMIWEWKSCSIVMLTEikERSQNKCAQYWPEDGSVSS-------GDIT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIRNLSYSMKDNESMpanQEVVQYSYTGWPSDSIvPKSANSLMNLIEMVlQRQSSLMGSQaPIVVHCR 1345
Cdd:cd14552   73 VELKDQTDYEDYTLRDFLVTKGKGGST---RTVRQFHFHGWPEVGI-PDNGKGMIDLIAAV-QKQQQQSGNH-PITVHCS 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1346 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd14552  147 AGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 845-1071 1.01e-38

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: 143.73  E-value: 1.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFI--KSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEqitrygdiIVEPASF 922
Cdd:cd14596    1 YINASYItmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPET--------LQEPMEL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  923 SfhsDYAIRafdiahigecgpdvIPNGNGVEYANVPIVK--GQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRE 1000
Cdd:cd14596   73 E---NYQLR--------------LENYQALQYFIIRIIKlvEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRK 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990705 1001 LpqFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14596  136 V--HNTGPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 845-1071 3.07e-38

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: 142.58  E-value: 3.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKK-LFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPAS-F 922
Cdd:cd14546    1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSeH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  923 SFHSDYAIRAFdiahigecgpdvipngngveyanvpIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP 1002
Cdd:cd14546   81 IWCDDYLVRSF-------------------------YLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1003 QFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKA-NIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14546  136 RGRSCPIVVHCSDGAGRTGTYILIDMVLNRMAKGAKEiDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1190-1397 4.03e-38

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: 141.78  E-value: 4.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFFD--YIAAQDPVsEGTAFDFWRMIADQNVTTVVMLS--DETDWSdVEKYWPIDGSGTechFGSernsVN 1265
Cdd:cd14556    1 YINAALLDSYKQPaaFIVTQHPL-PNTVTDFWRLVYDYGCTSIVMLNqlDPKDQS-CPQYWPDEGSGT---YGP----IQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIR--NLSYSMKDNEsmpANQEVVQYSYTGWPSDSIVPKSANSLMNLIEMV--LQRQSSlmgsQAPIV 1341
Cdd:cd14556   72 VEFVSTTIDEDVISRifRLQNTTRPQE---GYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVekWQEQSG----EGPIV 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 71990705 1342 VHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd14556  145 VHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1164-1404 1.55e-37

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: 141.18  E-value: 1.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1164 NRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSD 1241
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSsqEFIATQGPLPQ-TVGDFWRMIWEQQSSTIVMLTNCMEAGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1242 V--EKYWPIDGsgTECHFGSERnsvnVTCVSEEHHQDFIIRNLSYSMKDNESmpaNQEVVQYSYTGWPsDSIVPKSANSL 1319
Cdd:cd14619   80 VkcEHYWPLDY--TPCTYGHLR----VTVVSEEVMENWTVREFLLKQVEEQK---TLSVRHFHFTAWP-DHGVPSSTDTL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1320 MNLIEMVLQRQSSLMgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRA 1399
Cdd:cd14619  150 LAFRRLLRQWLDQTM-SGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQC 228


                 ....*
gi 71990705 1400 LADYI 1404
Cdd:cd14619  229 ILDFL 233
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 796-1072 1.77e-37

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: 142.83  E-value: 1.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  796 EYESLPHFQLDTVASNRK--ENAIKNRYNDIRAFDDTRVKLKKiNGDDYSDYINANFIK------SWKekklFIAAQAPV 867
Cdd:cd14599   17 EYEQIPKKKADGVFTTATlpENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKvtvggeEWH----YIATQGPL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  868 DATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWP----DEQITRYGDIIVepaSFSFHSD---YAIRAFDIAHige 940
Cdd:cd14599   92 PHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgsKHSSATYGKFKV---TTKFRTDsgcYATTGLKVKH--- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  941 cgpdvipngngveyanvpIVKGQfannSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNS----------PVV 1010
Cdd:cd14599  166 ------------------LLSGQ----ERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIV 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990705 1011 IHCSAGVGRTGTFISIDSMLdQCLAE-DKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1072
Cdd:cd14599  224 VHCSAGVGRTGVVILTELMI-GCLEHnEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1134-1400 3.48e-37

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: 141.72  E-value: 3.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1134 GLEEEFKKLERNLTTPLSSnfAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVS 1211
Cdd:cd14633   16 GFKEEYESFFEGQSAPWDS--AKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRpnHYIATQGPMQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1212 EgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPIDgsgTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDN 1289
Cdd:cd14633   94 E-TIYDFWRMVWHENTASIIMVTNLVEVGRVKccKYWPDD---TEIY-----KDIKVTLIETELLAEYVIRTFAVEKRGV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1290 ESMpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQR 1369
Cdd:cd14633  165 HEI---REIRQFHFTGWP-DHGVPYHATGLLGFVRQV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV 237

                        250       260       270
                 ....*....|....*....|....*....|.
gi 71990705 1370 IDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd14633  238 VDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 844-1069 4.71e-37

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: 139.31  E-value: 4.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  844 DYINANFIK----SWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQIT-RYGDIIVE 918
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSsSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  919 PASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRL 998
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNLEK-------------------------NESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLV 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990705  999 RELPQFNNSPVVIHCSAGVGRTGTFISIDSMLdqCLAEDKANIF--EFVCNLRRQRNLMVQSLEQYVFIYKAL 1069
Cdd:cd14601  136 RNKRAGKDEPVVVHCSAGIGRTGVLITMETAM--CLIECNQPVYplDIVRTMRDQRAMMIQTPSQYRFVCEAI 206
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 845-1066 8.02e-37

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: 137.92  E-value: 8.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVaNLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSF 924
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFDIAHIgecgpdvipngngveyanvpivkGQFANNSRRILQYHFTNWNDYKapECSTGLLRFMYRLREL--- 1001
Cdd:cd14556   80 DEDVISRIFRLQNT-----------------------TRPQEGYRMVQQFQFLGWPRDR--DTPPSKRALLKLLSEVekw 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71990705 1002 -PQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIY 1066
Cdd:cd14556  135 qEQSGEGPIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 807-1065 8.84e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 141.68  E-value: 8.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   807 TVASNRK-ENAIKNRYNDIRAFDDTRVKLKKINGDDySDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYL 885
Cdd:PHA02747   42 LIANFEKpENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   886 IVMVANLTEKN-RQQCAKYW-PDEQitryGDIIVEpasfsfhsDYAIRAFDIAhigecgpdVIPngngvEYANVPI-VKG 962
Cdd:PHA02747  121 IVMLTPTKGTNgEEKCYQYWcLNED----GNIDME--------DFRIETLKTS--------VRA-----KYILTLIeITD 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   963 QFANNSRRILQYHFTNWNDYKAPECSTGLLRFM-----YRLRELPQFNN-----SPVVIHCSAGVGRTGTFISIDSMLDQ 1032
Cdd:PHA02747  176 KILKDSRKISHFQCSEWFEDETPSDHPDFIKFIkiidiNRKKSGKLFNPkdallCPIVVHCSDGVGKTGIFCAVDICLNQ 255

                         250       260       270
                  ....*....|....*....|....*....|...
gi 71990705  1033 CLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFI 1065
Cdd:PHA02747  256 LVKRKAICLAKTAEKIREQRHAGIMNFDDYLFI 288
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 971-1071 9.50e-37

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: 134.41  E-value: 9.50e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     971 ILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQF--NNSPVVIHCSAGVGRTGTFISIDSMLDQCLAE-DKANIFEFVCN 1047
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 71990705    1048 LRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
971-1071 9.50e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 134.41  E-value: 9.50e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705     971 ILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQF--NNSPVVIHCSAGVGRTGTFISIDSMLDQCLAE-DKANIFEFVCN 1047
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 71990705    1048 LRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1150-1402 1.19e-36

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: 139.96  E-value: 1.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1150 LSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNV 1227
Cdd:cd14603   20 CSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSraYIATQGPLSH-TVLDFWRMIWQYGV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1228 TTVVMLSDETDWS--DVEKYWPIDGSGTEchFGsernSVNVTCVSEEH-HQDFIIRNLSYSMKDNEsmpanQEVVQYSYT 1304
Cdd:cd14603   99 KVILMACREIEMGkkKCERYWAQEQEPLQ--TG----PFTITLVKEKRlNEEVILRTLKVTFQKES-----RSVSHFQYM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1305 GWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIfIC----ISLLWLRQKAEQRIDVFQTVKGLQ 1380
Cdd:cd14603  168 AWP-DHGIPDSPDCMLAMIELARRLQGS---GPEPLCVHCSAGCGRTGV-ICtvdyVRQLLLTQRIPPDFSIFDVVLEMR 242

                        250       260
                 ....*....|....*....|..
gi 71990705 1381 SHRPMMFTRFEQYSFCYRALAD 1402
Cdd:cd14603  243 KQRPAAVQTEEQYEFLYHTVAQ 264
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
798-1073 4.19e-36

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 138.69  E-value: 4.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  798 ESLPHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKlkkINGDdysdYINANFIKSwKEKKLFIAAQAPVDATIGDFWRM 877
Cdd:COG5599   25 NELAPSHNDPQYLQNINGSPLNRFRDIQPYKETALR---ANLG----YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  878 VWEQESYLIVMVANLTE--KNRQQCAKYWPdeQITRYGDIIVEpasfsfhsdyairafdIAHIgecgpDVIPNGNGVEYA 955
Cdd:COG5599   97 LFDNNTPVLVVLASDDEisKPKVKMPVYFR--QDGEYGKYEVS----------------SELT-----ESIQLRDGIEAR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  956 NVPIVKGQFANNSRRILQYHFTNWNDYKAPEcSTGLLRFMYRLRE---LPQFNNSPVVIHCSAGVGRTGTFISIDSMLD- 1031
Cdd:COG5599  154 TYVLTIKGTGQKKIEIPVLHVKNWPDHGAIS-AEALKNLADLIDKkekIKDPDKLLPVVHCRAGVGRTGTLIACLALSKs 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 71990705 1032 -QCLAEDKANIFEFVCNLRRQRN-LMVQSLEQYVFIyKALAEWH 1073
Cdd:COG5599  233 iNALVQITLSVEEIVIDMRTSRNgGMVQTSEQLDVL-VKLAEQQ 275
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 812-1069 6.16e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 139.78  E-value: 6.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   812 RKENAIKNRYNDIRAFDDTRVKL----------------KKI---NGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIG 872
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgKKIevtSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   873 DFWRMVWEQESYLIVMVANlTEKNRQQCAKYW--PDEQITRYGDIIVEPASFSFHSDYAIRAFDIAhigecgpDVIpngn 950
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFTKTRLMIT-------DKI---- 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   951 gveyanvpivkgqfANNSRRILQYHFTNWNDYKAPecsTGLLRFM--------YRLRELPQFNNS-----PVVIHCSAGV 1017
Cdd:PHA02746  196 --------------SDTSREIHHFWFPDWPDNGIP---TGMAEFLelinkvneEQAELIKQADNDpqtlgPIVVHCSAGI 258

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 71990705  1018 GRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1069
Cdd:PHA02746  259 GRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1190-1403 1.10e-35

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: 135.13  E-value: 1.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYF-FDY-IAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTechFGSernsVN 1265
Cdd:cd14622    2 YINASFIDGYRqKDYfIATQGPLAH-TVEDFWRMVWEWKCHTIVMLTElqEREQEKCVQYWPSEGSVT---HGE----IT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIRNLSYSMKDNESmpaNQEVVQYSYTGWPSDSIvPKSANSLMNLIEMVlQRQSSLMGSQaPIVVHCR 1345
Cdd:cd14622   74 IEIKNDTLLETISIRDFLVTYNQEKQ---TRLVRQFHFHGWPEIGI-PAEGKGMIDLIAAV-QKQQQQTGNH-PIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 71990705 1346 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADY 1403
Cdd:cd14622  148 AGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1164-1402 2.14e-35

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 134.94  E-value: 2.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1164 NRYEAAVPFDKYRVILPpTIGHADSSYINASHIKGYFF--DYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSD--ETDW 1239
Cdd:cd14615    1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSkkEFIAAQGPLP-NTVKDFWRMVWEKNVYAIVMLTKcvEQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1240 SDVEKYWPIDGSGTechfgseRNSVNVTCVSEEHHQDFIIRNLSY-SMKDNESMPanqeVVQYSYTGWPsDSIVPKSANS 1318
Cdd:cd14615   79 TKCEEYWPSKQKKD-------YGDITVTMTSEIVLPEWTIRDFTVkNAQTNESRT----VRHFHFTSWP-DHGVPETTDL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1319 LMNLIEMVLQ--RQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFC 1396
Cdd:cd14615  147 LINFRHLVREymKQNP---PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223


                 ....*.
gi 71990705 1397 YRALAD 1402
Cdd:cd14615  224 NQCALD 229
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1190-1397 5.40e-35

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: 133.14  E-value: 5.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIK---GYFFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDwSDVEK---YWPidgsgtECHFGSERNS 1263
Cdd:cd18533    1 YINASYITlpgTSSKRYIATQGPLPA-TIGDFWKMIWQNNVGVIVMLTPLVE-NGREKcdqYWP------SGEYEGEYGD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1264 VNVTCVSEEHHQD--FIIRNLSYSMKDNESmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMV--LQRQSSLMGsqaP 1339
Cdd:cd18533   73 LTVELVSEEENDDggFIVREFELSKEDGKV----KKVYHIQYKSWP-DFGVPDSPEDLLTLIKLKreLNDSASLDP---P 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705 1340 IVVHCRNGSSESGIFICI--------SLLWLRQKAEQRID-VFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd18533  145 IIVHCSAGVGRTGTFIALdslldelkRGLSDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1135-1405 9.67e-35

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: 134.80  E-value: 9.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1135 LEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYffD-----YIAAQDP 1209
Cdd:cd14610   19 LEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDH--DprnpaYIATQGP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1210 VSeGTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTECHFGSERNSVNVTCvseehhQDFIIRnlSYSMK 1287
Cdd:cd14610   97 LP-ATVADFWQMVWESGCVVIVMLTPlaENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWC------EDFLVR--SFYLK 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1288 dNESMPANQEVVQYSYTGWpSDSIVPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQ-KA 1366
Cdd:cd14610  168 -NLQTNETRTVTQFHFLSW-NDQGVPASTRSLLDFRRKV---NKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKG 242

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 71990705 1367 EQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYIS 1405
Cdd:cd14610  243 AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVN 281
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1164-1400 2.61e-34

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: 131.99  E-value: 2.61e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1164 NRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSD 1241
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSpqEFIATQGPLKK-TIEDFWRLVWEQQVCNIIMLTVGMENGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1242 V--EKYWPIDGsgTECHFGSernsVNVTCVSEEHHQDFIIRNLSYSmkdNESMPANQEVVQYSYTGWPsDSIVPKSANSL 1319
Cdd:cd14618   80 VlcDHYWPSES--TPVSYGH----ITVHLLAQSSEDEWTRREFKLW---HEDLRKERRVKHLHYTAWP-DHGIPESTSSL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1320 MNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRA 1399
Cdd:cd14618  150 MAFRELVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                 .
gi 71990705 1400 L 1400
Cdd:cd14618  229 I 229
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 845-1066 3.39e-34

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: 130.66  E-value: 3.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKL--FIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ-QCAKYWPDE--QITRYGDIIVEP 919
Cdd:cd17658    1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  920 ASFSfHSDYAI--RAFDIAHIgecgpdvipngngvEYANVPivkgqfannsRRILQYHFTNWNDYKAPECSTGLLRFMYR 997
Cdd:cd17658   81 KKLK-HSQHSItlRVLEVQYI--------------ESEEPP----------LSVLHIQYPEWPDHGVPKDTRSVRELLKR 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990705  998 LRELPQfNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKA--NIFEFVCNLRRQRNLMVQSLEQYVFIY 1066
Cdd:cd17658  136 LYGIPP-SAGPIVVHCSAGIGRTGAYCTIHNTIRRILEGDMSavDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1166-1400 4.84e-34

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: 131.22  E-value: 4.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1166 YEAAVPFDKYRVILPPTIGHADSSYINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSD 1241
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKekNKFIAAQGPKQE-TVNDFWRMVWEQKSATIVMLTNlkERKEEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1242 VEKYWPIDGSGTechFGSERNSVNVTCVSeehhQDFIIRNLSYSMKDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMN 1321
Cdd:cd14620   80 CYQYWPDQGCWT---YGNIRVAVEDCVVL----VDYTIRKFCIQPQLPDGCKAPRLVTQLHFTSWP-DFGVPFTPIGMLK 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990705 1322 LIEMVLQRQSSLMGsqaPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd14620  152 FLKKVKSVNPVHAG---PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1190-1397 6.76e-34

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 129.75  E-value: 6.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPIDGSGTEChfgserNSVNVT 1267
Cdd:cd14550    1 YINASYLQGYRRsnEFIITQHPLEH-TIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEKPLEC------ETFKVT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1268 CVSEEH----------HQDFIIRnlsySMKDNESMpanqEVVQYSYTGWPsDSIVPKSanSLMNLIEMVLQRQSSlmgSQ 1337
Cdd:cd14550   74 LSGEDHsclsneirliVRDFILE----STQDDYVL----EVRQFQCPSWP-NPCSPIH--TVFELINTVQEWAQQ---RD 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1338 APIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd14550  140 GPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1135-1403 8.60e-34

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: 132.45  E-value: 8.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1135 LEEEFKKLErnlTTPL--SSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGY--FFDYIAAQDPv 1210
Cdd:cd14621   28 FREEFNALP---ACPIqaTCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYqeKNKFIAAQGP- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1211 SEGTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTechFGSERNSVNVTCVSeehhQDFIIRNLSYSMKD 1288
Cdd:cd14621  104 KEETVNDFWRMIWEQNTATIVMVTNlkERKECKCAQYWPDQGCWT---YGNIRVSVEDVTVL----VDYTVRKFCIQQVG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1289 NESMPANQEVV-QYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGsqaPIVVHCRNGSSESGIFICISLLWLRQKAE 1367
Cdd:cd14621  177 DVTNKKPQRLItQFHFTSWP-DFGVPFTPIGMLKFLKKVKNCNPQYAG---AIVVHCSAGVGRTGTFIVIDAMLDMMHAE 252

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 71990705 1368 QRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADY 1403
Cdd:cd14621  253 RKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1152-1398 8.61e-34

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: 130.78  E-value: 8.61e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1152 SNFAAK-DENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVT 1228
Cdd:cd14614    3 PHFAADlPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSpqEYIATQGPLPE-TRNDFWKMVLQQKSQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1229 TVVMLS--DETDWSDVEKYWPidgsgtechFGSE---RNSVNVTCVSEEHHQDFIIRNLSYSMKDnesmpANQEVVQYSY 1303
Cdd:cd14614   82 IIVMLTqcNEKRRVKCDHYWP---------FTEEpvaYGDITVEMLSEEEQPDWAIREFRVSYAD-----EVQDVMHFNY 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1304 TGWPsDSIVP--KSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQS 1381
Cdd:cd14614  148 TAWP-DHGVPtaNAAESILQFVQMVRQQAVK---SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRS 223

                        250
                 ....*....|....*..
gi 71990705 1382 HRPMMFTRFEQYSFCYR 1398
Cdd:cd14614  224 YRMSMVQTEEQYIFIHQ 240
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1190-1400 1.66e-33

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: 128.65  E-value: 1.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIK----GYFFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDV--EKYWPiDGSGTECHFGserNS 1263
Cdd:cd14538    1 YINASHIRipvgGDTYHYIACQGPLPN-TTGDFWQMVWEQKSEVIAMVTQDVEGGKVkcHRYWP-DSLNKPLICG---GR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1264 VNVTCVSEEHHQDFIIRNLSysMKDNESmPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqRQSSLMGsqaPIVVH 1343
Cdd:cd14538   76 LEVSLEKYQSLQDFVIRRIS--LRDKET-GEVHHITHLNFTTWP-DHGTPQSADPLLRFIRYM--RRIHNSG---PIVVH 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705 1344 CRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd14538  147 CSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PHA02738 PHA02738
hypothetical protein; Provisional
 788-1069 2.39e-33

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 131.97  E-value: 2.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   788 DTDFLFAQEYESLPHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKinGDDYSDYINANFIKSWKEKKLFIAAQAPV 867
Cdd:PHA02738   22 DCEEVITREHQKVISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVILPA--ERNRGDYINANYVDGFEYKKKFICGQAPT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   868 DATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDeqitrygdiiVEPASFSFhSDYAIRAFDIAHIgecgpdvip 947
Cdd:PHA02738  100 RQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSD----------VEQGSIRF-GKFKITTTQVETH--------- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   948 ngngVEYANVPIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLR----ELPQ--FNNS-------PVVIHCS 1014
Cdd:PHA02738  160 ----PHYVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkELAQesLQIGhnrlqppPIVVHCN 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 71990705  1015 AGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1069
Cdd:PHA02738  236 AGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1176-1400 3.78e-33

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: 128.21  E-value: 3.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1176 RVILPPTIGHADSSYINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPIDgs 1251
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQrpSHYIATQGPVHE-TVYDFWRMIWQEQSACIVMVTNLVEVGRVKcyKYWPDD-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1252 gTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDNESMpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqrQS 1331
Cdd:cd14631   78 -TEVY-----GDFKVTCVEMEPLAEYVVRTFTLERRGYNEI---REVKQFHFTGWP-DHGVPYHATGLLSFIRRV---KL 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990705 1332 SLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd14631  145 SNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 845-1072 6.48e-33

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: 127.40  E-value: 6.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIK------SWKekklFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWP----DEQITRYGD 914
Cdd:cd14598    1 YINASHIKvtvggkEWD----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  915 IIVepaSFSFHSD---YAIRAFDIAHigecgpdvipngngveyanvpIVKGQfannSRRILQYHFTNWNDYKAPECSTGL 991
Cdd:cd14598   77 FKI---TTRFRTDsgcYATTGLKIKH---------------------LLTGQ----ERTVWHLQYTDWPEHGCPEDLKGF 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  992 LRFMYRLREL---------PQFNNSPVVIHCSAGVGRTGTFISIDSMLdQCLAEDKANIFEFVCN-LRRQRNLMVQSLEQ 1061
Cdd:cd14598  129 LSYLEEIQSVrrhtnstidPKSPNPPVLVHCSAGVGRTGVVILSEIMI-ACLEHNEMLDIPRVLDmLRQQRMMMVQTLSQ 207

                        250
                 ....*....|.
gi 71990705 1062 YVFIYKALAEW 1072
Cdd:cd14598  208 YTFVYKVLIQF 218
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1163-1400 7.04e-33

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: 128.03  E-value: 7.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1163 KNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDW- 1239
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPraYIATQGPLST-TLLDFWRMIWEYSVLIIVMACMEFEMg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1240 -SDVEKYWPIDGSgTECHFGsernSVNVTCVSEEHHQDFIIRNLSYSMKDnesmpANQEVVQYSYTGWPsDSIVPKSANS 1318
Cdd:cd14602   80 kKKCERYWAEPGE-MQLEFG----PFSVTCEAEKRKSDYIIRTLKVKFNS-----ETRTIYQFHYKNWP-DHDVPSSIDP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1319 LMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQK---AEQRIDVFQTVKGLQSHRPMMFTRFEQYSF 1395
Cdd:cd14602  149 ILELIWDVRCYQED---DSVPICIHCSAGCGRTGVICAIDYTWMLLKdgiIPENFSVFSLIQEMRTQRPSLVQTKEQYEL 225


                 ....*
gi 71990705 1396 CYRAL 1400
Cdd:cd14602  226 VYNAV 230
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 845-1067 7.62e-33

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: 126.73  E-value: 7.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKL-FIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDE--QITRYGDIIVEPAS 921
Cdd:cd14539    1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  922 FSFHSDYAIRAFDIAHIGECGpdvipngngveyanvpivkgqfannSRRILQYHFTNWNDYKAPECSTGLLRFMYRLREL 1001
Cdd:cd14539   81 VRTTPTHVERIISIQHKDTRL-------------------------SRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSH 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1002 PQFNNS---PVVIHCSAGVGRTGTFISIDSMLDQCLAEDK-ANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1067
Cdd:cd14539  136 YLQQRSlqtPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNGiPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1190-1397 1.38e-32

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: 125.93  E-value: 1.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTechFGSernsVN 1265
Cdd:cd14549    1 YINANYVDGYNKAraYIATQGPLPS-TFDDFWRMVWEQNSAIIVMITNlvERGRRKCDQYWPKEGTET---YGN----IQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIRNLSYSM---KDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIemvlqRQSSL--MGSQAPI 1340
Cdd:cd14549   73 VTLLSTEVLATYTVRTFSLKNlklKKVKGRSSERVVYQYHYTQWP-DHGVPDYTLPVLSFV-----RKSSAanPPGAGPI 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705 1341 VVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd14549  147 VVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1135-1405 1.93e-32

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: 128.23  E-value: 1.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1135 LEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGY---FFDYIAAQDPVS 1211
Cdd:cd14609   17 LAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHdprMPAYIATQGPLS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1212 EGTAfDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSgtechfgSERNSVNVTCVSEehH---QDFIIRnlSYSM 1286
Cdd:cd14609   97 HTIA-DFWQMVWENGCTVIVMLTPlvEDGVKQCDRYWPDEGS-------SLYHIYEVNLVSE--HiwcEDFLVR--SFYL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1287 KDNESMpANQEVVQYSYTGWPSDSIvPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQ-K 1365
Cdd:cd14609  165 KNVQTQ-ETRTLTQFHFLSWPAEGI-PSSTRPLLDFRRKV---NKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 71990705 1366 AEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYIS 1405
Cdd:cd14609  240 GVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVN 279
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1159-1404 2.87e-32

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: 126.67  E-value: 2.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1159 ENLLKNRYEAAVPFDKYRVILPP-TIGHADSSYINASHIKGYF----------FDYIAAQDPVsEGTAFDFWRMIADQNV 1227
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDgDPNEPVSDYINANIIMPEFetkcnnskpkKSYIATQGCL-QNTVNDFWRMVFQENS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1228 TTVVMLSDETDW--SDVEKYWPIDGSGTEchFGSERnsvnVTCVSEEHHQDFIIRNLSYSMKDNESMpaNQEVVQYSYTG 1305
Cdd:cd14605   80 RVIVMTTKEVERgkSKCVKYWPDEYALKE--YGVMR----VRNVKESAAHDYILRELKLSKVGQGNT--ERTVWQYHFRT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1306 WPsDSIVPKSANSLMNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLW--LRQKA-EQRIDVFQTVKGLQSH 1382
Cdd:cd14605  152 WP-DHGVPSDPGGVLDFLEEVHHKQESIMDA-GPVVVHCSAGIGRTGTFIVIDILIdiIREKGvDCDIDVPKTIQMVRSQ 229

                        250       260
                 ....*....|....*....|..
gi 71990705 1383 RPMMFTRFEQYSFCYRALADYI 1404
Cdd:cd14605  230 RSGMVQTEAQYRFIYMAVQHYI 251
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1135-1405 4.15e-32

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: 127.13  E-value: 4.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1135 LEEEFKKLERNLTTPLSSNFAAKDE-------------NLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF 1201
Cdd:cd14625    9 LAEHTERLKANDNLKLSQEYESIDPgqqftwehsnlevNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1202 D--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPidGSGTECHfgserNSVNVTCVSEEHHQDF 1277
Cdd:cd14625   89 QnaYIATQGPLPE-TFGDFWRMVWEQRSATVVMMTklEEKSRIKCDQYWP--SRGTETY-----GMIQVTLLDTIELATF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1278 IIRnlSYSMKDNESmPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGsqaPIVVHCRNGSSESGIFICI 1357
Cdd:cd14625  161 CVR--TFSLHKNGS-SEKREVRQFQFTAWP-DHGVPEYPTPFLAFLRRVKTCNPPDAG---PIVVHCSAGVGRTGCFIVI 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 71990705 1358 SLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYIS 1405
Cdd:cd14625  234 DAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1158-1400 5.34e-32

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: 125.52  E-value: 5.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1158 DENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD 1235
Cdd:cd14630    1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPrhYIATQGPMQE-TVKDFWRMIWQENSASVVMVTN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1236 ETDWSDVE--KYWPIDgsgTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDNESMpanQEVVQYSYTGWPsDSIVP 1313
Cdd:cd14630   80 LVEVGRVKcvRYWPDD---TEVY-----GDIKVTLIETEPLAEYVIRTFTVQKKGYHEI---REIRQFHFTSWP-DHGVP 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1314 KSANSLMNLIemvlqRQSSLMG--SQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFE 1391
Cdd:cd14630  148 CYATGLLGFV-----RQVKFLNppDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEE 222


                 ....*....
gi 71990705 1392 QYSFCYRAL 1400
Cdd:cd14630  223 QYVFVHDAI 231
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1164-1398 5.64e-32

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: 124.82  E-value: 5.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1164 NRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD---YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWS 1240
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEekaYIATQGPLPN-TVADFWRMVWQEKTPIIVMITNLTEAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1241 D-VEKYWPIDgsgtechFGSERNSVNVTCVSEEHHQDFIIRNLSYsmkdnESMPANQEVVQYSYTGWPsDSIVPKSANSL 1319
Cdd:cd14547   80 EkCAQYWPEE-------ENETYGDFEVTVQSVKETDGYTVRKLTL-----KYGGEKRYLKHYWYTSWP-DHKTPEAAQPL 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990705 1320 MNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1398
Cdd:cd14547  147 LSLVQEVEEARQTEPHR-GPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1160-1400 3.02e-31

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: 124.76  E-value: 3.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1160 NLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDET 1237
Cdd:cd14626   41 NKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQnaYIATQGPLPE-TLSDFWRMVWEQRTATIVMMTRLE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1238 DWSDV--EKYWPIDGSGTechFGsernSVNVTCVSEEHHQDFIIRNLS-YSMKDNEsmpaNQEVVQYSYTGWPsDSIVPK 1314
Cdd:cd14626  120 EKSRVkcDQYWPIRGTET---YG----MIQVTLLDTVELATYSVRTFAlYKNGSSE----KREVRQFQFMAWP-DHGVPE 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1315 SANSLMNLIEMVLQRQSSLMGsqaPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1394
Cdd:cd14626  188 YPTPILAFLRRVKACNPPDAG---PMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYI 264


                 ....*.
gi 71990705 1395 FCYRAL 1400
Cdd:cd14626  265 FIHEAL 270
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1190-1400 8.15e-30

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: 118.10  E-value: 8.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPIDgsgTECHfgserNSVN 1265
Cdd:cd14555    1 YINANYIDGYHRPnhYIATQGPMQE-TVYDFWRMVWQENSASIVMVTNLVEVGRVKcsRYWPDD---TEVY-----GDIK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIRNLSYSMKdneSMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHCR 1345
Cdd:cd14555   72 VTLVETEPLAEYVVRTFALERR---GYHEIREVRQFHFTGWP-DHGVPYHATGLLGFIRRV---KASNPPSAGPIVVHCS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1346 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd14555  145 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1159-1400 1.44e-29

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: 118.39  E-value: 1.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1159 ENLLKNRYEAAVPFDKYRVILpptigHADSSYINASHIK----GYFFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLS 1234
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFIKmpvgDEEFVYIACQGPLPT-TVADFWQMVWEQKSTVIAMMT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1235 DETDWSDV--EKYWP-IDGSGTEChfgSERnsVNVTCVSEEHHQDFIIRNLsySMKDNESMPAnQEVVQYSYTGWPsDSI 1311
Cdd:cd14597   76 QEVEGGKIkcQRYWPeILGKTTMV---DNR--LQLTLVRMQQLKNFVIRVL--ELEDIQTREV-RHITHLNFTAWP-DHD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1312 VPKSANSLMNLIEMVLQRQSSlmgsqAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFE 1391
Cdd:cd14597  147 TPSQPEQLLTFISYMRHIHKS-----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221


                 ....*....
gi 71990705 1392 QYSFCYRAL 1400
Cdd:cd14597  222 QYIFCYQVI 230
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1190-1398 2.21e-29

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: 116.75  E-value: 2.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWS--DVEKYWPIDGSGTEChFGsernSVN 1265
Cdd:cd14542    1 YINANFIKGVSGSkaYIATQGPLPN-TVLDFWRMIWEYNVQVIVMACREFEMGkkKCERYWPEEGEEQLQ-FG----PFK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEH-HQDFIIRNLSYSMkDNESmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHC 1344
Cdd:cd14542   75 ISLEKEKRvGPDFLIRTLKVTF-QKES----RTVYQFHYTAWP-DHGVPSSVDPILDLVRLVRDYQGS---EDVPICVHC 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705 1345 RNGSSESGIFICISLLW---LRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1398
Cdd:cd14542  146 SAGCGRTGTICAIDYVWnllKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1137-1404 2.25e-29

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: 118.98  E-value: 2.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1137 EEFKKLER-----NLTTPLSSNfaakDENLLKNRYEAAVPFDKYRVILPPTIG----HADssYINASHIKGY--FFDYIA 1205
Cdd:cd17667    3 EDFEEVQRctadmNITAEHSNH----PDNKHKNRYINILAYDHSRVKLRPLPGkdskHSD--YINANYVDGYnkAKAYIA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1206 AQDPVsEGTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSgtechfgSERNSVNVTCVSEEHHQDFIIRNLS 1283
Cdd:cd17667   77 TQGPL-KSTFEDFWRMIWEQNTGIIVMITNlvEKGRRKCDQYWPTENS-------EEYGNIIVTLKSTKIHACYTVRRFS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1284 Y-SMKDNESMPAN-------QEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGsqaPIVVHCRNGSSESGIFI 1355
Cdd:cd17667  149 IrNTKVKKGQKGNpkgrqneRTVIQYHYTQWP-DMGVPEYALPVLTFVRRSSAARTPEMG---PVLVHCSAGVGRTGTYI 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 71990705 1356 CISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1404
Cdd:cd17667  225 VIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1164-1395 3.16e-29

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: 116.93  E-value: 3.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1164 NRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSD--ETDW 1239
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCpnEFIATQGPLP-GTVGDFWRMVWETRAKTIVMLTQcfEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1240 SDVEKYWPIDGSGTEChFGsernSVNVTCVSEEHHQDFIIRNLSYSMKDNESMpanqeVVQYSYTGWPSDSiVPKSANSL 1319
Cdd:cd14616   80 IRCHQYWPEDNKPVTV-FG----DIVITKLMEDVQIDWTIRDLKIERHGDYMM-----VRQCNFTSWPEHG-VPESSAPL 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71990705 1320 MNLIEMVlqrQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSF 1395
Cdd:cd14616  149 IHFVKLV---RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1190-1400 4.22e-29

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: 116.23  E-value: 4.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFFD--YIAAQDPVsEGTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTECHFGSERNSVN 1265
Cdd:cd17668    1 YINANYVDGYNKPkaYIAAQGPL-KSTAEDFWRMIWEHNVEVIVMITNlvEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHqdFIIRNLSYSMKDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGsqaPIVVHCR 1345
Cdd:cd17668   80 VLAYYTVRN--FTLRNTKIKKGSQKGRPSGRVVTQYHYTQWP-DMGVPEYTLPVLTFVRKASYAKRHAVG---PVVVHCS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1346 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd17668  154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1297-1402 4.61e-29

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 112.45  E-value: 4.61e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1297 EVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLWLRQKAEQR-IDVFQT 1375
Cdd:smart00404    1 TVKHYHYTGWP-DHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 71990705    1376 VKGLQSHRPMMFTRFEQYSFCYRALAD 1402
Cdd:smart00404   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1297-1402 4.61e-29

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: 112.45  E-value: 4.61e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705    1297 EVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLWLRQKAEQR-IDVFQT 1375
Cdd:smart00012    1 TVKHYHYTGWP-DHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 71990705    1376 VKGLQSHRPMMFTRFEQYSFCYRALAD 1402
Cdd:smart00012   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1159-1404 5.65e-29

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: 117.67  E-value: 5.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1159 ENLLKNRYEAAVPFDKYRVIL----PPTIGhadSSYINASHIKGYFF-------DYIAAQDPVsEGTAFDFWRMIADQNV 1227
Cdd:cd14606   17 ENKSKNRYKNILPFDHSRVILqgrdSNIPG---SDYINANYVKNQLLgpdenakTYIASQGCL-EATVNDFWQMAWQENS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1228 TTVVMLSDEtdwsdVEK-------YWPidGSGTECHFGsernSVNVTCVSEEHHQDFIIRNLSYSMKDNESMPanQEVVQ 1300
Cdd:cd14606   93 RVIVMTTRE-----VEKgrnkcvpYWP--EVGMQRAYG----PYSVTNCGEHDTTEYKLRTLQVSPLDNGELI--REIWH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1301 YSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlMGSQAPIVVHCRNGSSESGIFICISLLW--LRQKA-EQRIDVFQTVK 1377
Cdd:cd14606  160 YQYLSWP-DHGVPSEPGGVLSFLDQINQRQES-LPHAGPIIVHCSAGIGRTGTIIVIDMLMenISTKGlDCDIDIQKTIQ 237

                        250       260
                 ....*....|....*....|....*..
gi 71990705 1378 GLQSHRPMMFTRFEQYSFCYRALADYI 1404
Cdd:cd14606  238 MVRAQRSGMVQTEAQYKFIYVAIAQFI 264
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1190-1397 1.09e-28

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: 114.79  E-value: 1.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKG---YFFDYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSDETDWSD--VEKYWPIDgSGTECHFGSernsV 1264
Cdd:cd14539    1 YINASLIEDltpYCPRFIATQAPLP-GTAADFWLMVYEQQVSVIVMLVSEQENEKqkVHRYWPTE-RGQALVYGA----I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1265 NVTCVSEEHHQDFIIRNLSYSMKDNESMpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVHC 1344
Cdd:cd14539   75 TVSLQSVRTTPTHVERIISIQHKDTRLS---RSVVHLQFTTWP-ELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHC 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1345 RNGSSESGIFiCISLLWLRQKAEQR--IDVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd14539  151 SSGVGRTGAF-CLLYAAVQEIEAGNgiPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1152-1403 1.25e-28

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: 116.09  E-value: 1.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1152 SNFAAKDE-----NLLKNRYEAAVPFDKYRVILP-PTIGHADSSYINASHIKGYFFD---YIAAQDPVSEgTAFDFWRMI 1222
Cdd:cd14612    2 PNFVSPEEldipgHASKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIRGYDGKekaYIATQGPMLN-TVSDFWEMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1223 ADQNVTTVVMLSDETDWSD-VEKYWPiDGSGTECHFGsernsVNVTCVSEehHQDFIIRNLSYSMKDnesmpANQEVVQY 1301
Cdd:cd14612   81 WQEECPIIVMITKLKEKKEkCVHYWP-EKEGTYGRFE-----IRVQDMKE--CDGYTIRDLTIQLEE-----ESRSVKHY 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1302 SYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQS 1381
Cdd:cd14612  148 WFSSWP-DHQTPESAGPLLRLVAEVEESRQT-AASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRL 225

                        250       260
                 ....*....|....*....|..
gi 71990705 1382 HRPMMFTRFEQYSFCYRALADY 1403
Cdd:cd14612  226 DRGGMIQTSEQYQFLHHTLALY 247
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1135-1403 1.74e-28

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: 116.12  E-value: 1.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1135 LEEEFKKLERNLTTPLSSNFAAKdenLLKNRYEAAVPFDKYRVIL-PPTIGHADSSYINASHIKGYFFD---YIAAQDPV 1210
Cdd:cd14613    3 LQAEFFEIPMNFVDPKEYDIPGL---VRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYGGEekvYIATQGPT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1211 SEgTAFDFWRMIADQNVTTVVMLSD-ETDWSDVEKYWPIDGSGTEchfgsernSVNVTCVSEEHHQDFIIRNLSYSMKDN 1289
Cdd:cd14613   80 VN-TVGDFWRMVWQERSPIIVMITNiEEMNEKCTEYWPEEQVTYE--------GIEITVKQVIHADDYRLRLITLKSGGE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1290 EsmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQR 1369
Cdd:cd14613  151 E-----RGLKHYWYTSWP-DQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV 224

                        250       260       270
                 ....*....|....*....|....*....|....
gi 71990705 1370 IDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADY 1403
Cdd:cd14613  225 VDILRTTCQLRLDRGGMIQTCEQYQFVHHVLSLY 258
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1190-1400 2.10e-28

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: 113.94  E-value: 2.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE-KYWPIDGSGTEChfgserNSVNV 1266
Cdd:cd17669    1 YINASYIMGYYQsnEFIITQHPLLH-TIKDFWRMIWDHNAQLIVMLPDGQNMAEDEfVYWPNKDEPINC------ETFKV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1267 TCVSEEHH----------QDFIIRnlsySMKDNESMpanqEVVQYSYTGWPS-DSIVPKSanslMNLIEMVLQRQSSLMG 1335
Cdd:cd17669   74 TLIAEEHKclsneekliiQDFILE----ATQDDYVL----EVRHFQCPKWPNpDSPISKT----FELISIIKEEAANRDG 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1336 sqaPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd17669  142 ---PMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 814-1066 2.38e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 117.03  E-value: 2.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   814 ENAIKNRYNDIRAFDDTRVKLKKINGDDysDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLT 893
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILKIEDGGD--DFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   894 EKNRQQCAKYW-PDEQIT-RYGDIIVEPASFSFHSDYAIRAFDIAhigecgpdvipNGNgveyanvpivkgqfANNSRRI 971
Cdd:PHA02742  129 EDGKEACYPYWmPHERGKaTHGEFKIKTKKIKSFRNYAVTNLCLT-----------DTN--------------TGASLDI 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   972 LQYHFTNWNDYKAPECSTGLLRFMYRLREL-----------PQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKAN 1040
Cdd:PHA02742  184 KHFAYEDWPHGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIP 263

                         250       260
                  ....*....|....*....|....*.
gi 71990705  1041 IFEFVCNLRRQRNLMVQSLEQYVFIY 1066
Cdd:PHA02742  264 LLSIVRDLRKQRHNCLSLPQQYIFCY 289
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1190-1404 2.84e-28

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: 114.09  E-value: 2.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIK----GYFFDYIAAQDPVsEGTAFDFWRMIADQNVTTVVMLSDETDWS--DVEKYWPIDGSGTECHFGSERNS 1263
Cdd:cd14540    1 YINASHITatvgGKQRFYIAAQGPL-QNTVGDFWQMVWEQGVYLVVMVTAEEEGGreKCFRYWPTLGGEHDALTFGEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1264 VNVTCVSEEHhqdFIIRNLSYsmkdnESMPANQE--VVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGSQA--- 1338
Cdd:cd14540   80 STKFSVSSGC---YTTTGLRV-----KHTLSGQSrtVWHLQYTDWP-DHGCPEDVSGFLDFLEEINSVRRHTNQDVAghn 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990705 1339 ---PIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1404
Cdd:cd14540  151 rnpPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1190-1398 5.64e-28

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: 112.61  E-value: 5.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGTECHfgserNSVN 1265
Cdd:cd14557    1 YINASYIDGFKepRKYIAAQGPKDE-TVDDFWRMIWEQKSTVIVMVTrcEEGNRNKCAQYWPSMEEGSRAF-----GDVV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIRNLSYSMKDNESmpANQEVVQYSYTGWPsDSIVPKSANSLMNLiemvLQRQSSLMGS-QAPIVVHC 1344
Cdd:cd14557   75 VKINEEKICPDYIIRKLNINNKKEKG--SGREVTHIQFTSWP-DHGVPEDPHLLLKL----RRRVNAFNNFfSGPIVVHC 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71990705 1345 RNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1398
Cdd:cd14557  148 SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1164-1398 6.02e-28

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: 113.48  E-value: 6.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1164 NRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSDETDWSD 1241
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFrrEYIATQGPLP-GTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1242 V--EKYWPIDGSGTecHFGsernSVNVTCVSEEHHQDFIIRNlsYSMKDNESMPANQEVVQYSYTGWPsDSIVPKSANSL 1319
Cdd:cd14617   80 VkcDHYWPADQDSL--YYG----DLIVQMLSESVLPEWTIRE--FKICSEEQLDAPRLVRHFHYTVWP-DHGVPETTQSL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990705 1320 MNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1398
Cdd:cd14617  151 IQFVRTVRDYINRTPGS-GPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1160-1405 7.38e-28

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: 114.83  E-value: 7.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1160 NLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDET 1237
Cdd:cd14624   47 NKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQnaYIATQGALPE-TFGDFWRMIWEQRSATVVMMTKLE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1238 DWSDV--EKYWPidGSGTECHfgserNSVNVTCVSEEHHQDFIIRnlSYSMKDNESmPANQEVVQYSYTGWPsDSIVPKS 1315
Cdd:cd14624  126 ERSRVkcDQYWP--SRGTETY-----GLIQVTLLDTVELATYCVR--TFALYKNGS-SEKREVRQFQFTAWP-DHGVPEH 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1316 ANSLMNLIEMVlqrQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSF 1395
Cdd:cd14624  195 PTPFLAFLRRV---KTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIF 271

                        250
                 ....*....|
gi 71990705 1396 CYRALADYIS 1405
Cdd:cd14624  272 IHDALLEAVT 281
PHA02738 PHA02738
hypothetical protein; Provisional
 1126-1407 3.10e-27

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 114.25  E-value: 3.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1126 MTTSNGETGLEEEFKKLernLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADssYINASHIKGYFFD--Y 1203
Cdd:PHA02738   18 MEKSDCEEVITREHQKV---ISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVILPAERNRGD--YINANYVDGFEYKkkF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1204 IAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETD---------WSDVEkywpidgsGTECHFGSERnsvnVTCVSEEHH 1274
Cdd:PHA02738   93 ICGQAPTRQ-TCYDFYRMLWMEHVQIIVMLCKKKEngrekcfpyWSDVE--------QGSIRFGKFK----ITTTQVETH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1275 QDFIIRNLSYSmkdnESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSL------MGSQA----PIVVHC 1344
Cdd:PHA02738  160 PHYVKSTLLLT----DGTSATQTVTHFNFTAWP-DHDVPKNTSEFLNFVLEVRQCQKELaqeslqIGHNRlqppPIVVHC 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990705  1345 RNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYISKT 1407
Cdd:PHA02738  235 NAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLT 297
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1190-1402 3.38e-27

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: 110.61  E-value: 3.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIkgYFFD-----YIAAQDPVSEGTAfDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSgtECHFGSErn 1262
Cdd:cd14546    1 YINASTI--YDHDprnpaYIATQGPLPHTIA-DFWQMIWEQGCVVIVMLTrlQENGVKQCARYWPEEGS--EVYHIYE-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1263 svnVTCVSEehH---QDFIIRNLsY--SMKDNESmpanQEVVQYSYTGWPSDSIvPKSANSLMNLIEMVlqrQSSLMGSQ 1337
Cdd:cd14546   74 ---VHLVSE--HiwcDDYLVRSF-YlkNLQTSET----RTVTQFHFLSWPDEGI-PASAKPLLEFRRKV---NKSYRGRS 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71990705 1338 APIVVHCRNGSSESGIFICISLLWLR-QKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALAD 1402
Cdd:cd14546  140 CPIVVHCSDGAGRTGTYILIDMVLNRmAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1190-1398 7.49e-27

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: 109.62  E-value: 7.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGY--FFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTechFGSERNSVN 1265
Cdd:cd14551    1 YINASYIDGYqeKNKFIAAQGPKDE-TVNDFWRMIWEQGSATIVMVTNlkERKEKKCSQYWPDQGCWT---YGNLRVRVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHH-QDFIIRNLSysmkDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHC 1344
Cdd:cd14551   77 DTVVLVDYTtRKFCIQKVN----RGIGEKRVRLVTQFHFTSWP-DFGVPFTPIGMLKFLKKV---KSANPPRAGPIVVHC 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71990705 1345 RNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1398
Cdd:cd14551  149 SAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1190-1400 8.43e-27

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: 109.37  E-value: 8.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPiDGSGTechFGSernsVN 1265
Cdd:cd14632    1 YINANYIDGYHRSnhFIATQGPKQE-MVYDFWRMVWQEHCSSIVMITKLVEVGRVKcsKYWP-DDSDT---YGD----IK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIRNLSYsmkDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHCR 1345
Cdd:cd14632   72 ITLLKTETLAEYSVRTFAL---ERRGYSARHEVKQFHFTSWP-EHGVPYHATGLLAFIRRV---KASTPPDAGPVVVHCS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1346 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd14632  145 AGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1163-1397 1.09e-26

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: 109.79  E-value: 1.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1163 KNRYEAAVPFDKYRVILPPTIGhaDSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETD 1238
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINASLVEVEEAKrsYILTQGPLPN-TSGHFWQMVWEQNSKAVIMLNKlmEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1239 WSDVEKYWPIDGSGTEChfgSERNSVNVTCVSEEHHQDFIIRNLSY-SMKDNESmpanQEVVQYSYTGWPsDSIVPKSAN 1317
Cdd:cd14545   78 QIKCAQYWPQGEGNAMI---FEDTGLKVTLLSEEDKSYYTVRTLELeNLKTQET----REVLHFHYTTWP-DFGVPESPA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1318 SLMNLIEMVlqRQS-SLMGSQAPIVVHCRNGSSESGIFICI--SLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1394
Cdd:cd14545  150 AFLNFLQKV--RESgSLSSDVGPPVVHCSAGIGRSGTFCLVdtCLVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLR 227


                 ...
gi 71990705 1395 FCY 1397
Cdd:cd14545  228 FSY 230
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 845-1071 2.70e-26

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: 108.18  E-value: 2.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMvanLTEKNRQQ-CAKYWPDEQITRYGDIIVEPASFS 923
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVM---LNEMDAAQlCMQYWPEKTSCCYGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  924 FHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfANNSRRILQY-HFTNWNDYK-APECSTGLLRFMYRL--- 998
Cdd:cd14634   78 IDEDIISRIFRICNMAR------------------------PQDGYRIVQHlQYIGWPAYRdTPPSKRSILKVVRRLekw 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990705  999 RELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14634  134 QEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1190-1397 3.41e-26

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: 107.85  E-value: 3.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPIDGSgtechfgSERNSVNVT 1267
Cdd:cd14635    1 YINAALMDSYKqpSAFIVTQHPLPN-TVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGV-------HRHGPIQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1268 CVSEEHHQDFIIRNLSYSmkdNESMPAN--QEVVQYSYTGWPSDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVHCR 1345
Cdd:cd14635   73 FVSADLEEDIISRIFRIY---NAARPQDgyRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCL 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 71990705 1346 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd14635  150 NGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1190-1397 8.69e-26

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: 106.65  E-value: 8.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPIDGSgteCHFGSernsVNVT 1267
Cdd:cd14636    1 YINAALMDSYRqpAAFIVTQHPLPN-TVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGM---LRYGP----IQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1268 CVSEEHHQDFIIRNLSYSmkdNESMPanQE----VVQYSYTGWPSDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVH 1343
Cdd:cd14636   73 CMSCSMDCDVISRIFRIC---NLTRP--QEgylmVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIH 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71990705 1344 CRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd14636  148 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1190-1409 1.33e-25

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: 106.18  E-value: 1.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHI------KGYFFDYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWP-IDGSGTECHFgse 1260
Cdd:cd14601    2 YINANYInmeipsSSIINRYIACQGPLP-NTCSDFWQMTWEQGSSMVVMLTTQVERGRVKchQYWPePSGSSSYGGF--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1261 rnsvNVTCVSEEHHQDFIIRNLSYS-MKDNESMPanqeVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSslmGSQAP 1339
Cdd:cd14601   78 ----QVTCHSEEGNPAYVFREMTLTnLEKNESRP----LTQIQYIAWP-DHGVPDDSSDFLDFVCLVRNKRA---GKDEP 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1340 IVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAladyISKTYR 1409
Cdd:cd14601  146 VVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEA----ILKVYE 211
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1190-1397 3.19e-25

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: 105.10  E-value: 3.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINA----SHIKGYFFdyIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPidgSGTECHFGSernsVN 1265
Cdd:cd14634    1 YINAalmdSHKQPAAF--IVTQHPLPN-TVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWP---EKTSCCYGP----IQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHHQDFIIRNLSYSmkdNESMPAN--QEVVQYSYTGWPSDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVH 1343
Cdd:cd14634   71 VEFVSADIDEDIISRIFRIC---NMARPQDgyRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVH 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71990705 1344 CRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd14634  148 CLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVY 201
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1138-1400 4.26e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 107.81  E-value: 4.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1138 EFKKLERN--LTTPLS--SNFAAKDENLLKNRYEAAVPFDKYRVILPP-------------------TIGHADSSYINAS 1194
Cdd:PHA02746   25 EFVLLEHAevMDIPIRgtTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHAN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1195 HIKGY--FFDYIAAQDPVsEGTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPIDGSGTECHFGseRNSVNVTCVSEE 1272
Cdd:PHA02746  105 FVDGFkeANKFICAQGPK-EDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKEEDSELAFG--RFVAKILDIIEE 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1273 hhqdfiirnLSYS----MKDNESMPANQEVVQYSYTGWPSDSIvPKSANSLMNLIEMVLQRQSSLM-------GSQAPIV 1341
Cdd:PHA02746  182 ---------LSFTktrlMITDKISDTSREIHHFWFPDWPDNGI-PTGMAEFLELINKVNEEQAELIkqadndpQTLGPIV 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990705  1342 VHCRNGSSESGIFICI--SLLWLRQkaEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:PHA02746  252 VHCSAGIGRAGTFCAIdnALEQLEK--EKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1190-1400 5.02e-25

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 104.38  E-value: 5.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYFF--DYIAAQDPVSEGTAfDFWRMIADQNVTTVVMLSDETDWSDVEK-YWPIDGSGTECH-FGSERNSVN 1265
Cdd:cd17670    1 YINASYIMGYYRsnEFIITQHPLPHTTK-DFWRMIWDHNAQIIVMLPDNQGLAEDEFvYWPSREESMNCEaFTVTLISKD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1266 VTCVSEEHH---QDFIIRnlsySMKDNESMpanqEVVQYSYTGWPSDSIVPKSANSLMNLIemvlqrQSSLMGSQAPIVV 1342
Cdd:cd17670   80 RLCLSNEEQiiiHDFILE----ATQDDYVL----EVRHFQCPKWPNPDAPISSTFELINVI------KEEALTRDGPTIV 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 71990705 1343 HCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd17670  146 HDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1163-1397 2.51e-24

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: 103.07  E-value: 2.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1163 KNRYEAAVPFDKYRVIL-PPTIGHADSSYINASHIKGYFFD---YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETD 1238
Cdd:cd14611    2 KNRYKTILPNPHSRVCLkPKNSNDSLSTYINANYIRGYGGKekaFIATQGPMIN-TVNDFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1239 WSdvEK---YWPiDGSGTechFGseRNSVNVTCVSEEHHqdFIIRNLSysMKDNESmpaNQEVVQYSYTGWPsDSIVPKS 1315
Cdd:cd14611   81 KN--EKcvlYWP-EKRGI---YG--KVEVLVNSVKECDN--YTIRNLT--LKQGSQ---SRSVKHYWYTSWP-DHKTPDS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1316 ANSLMNLIEMVLQ-RQSSLmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1394
Cdd:cd14611  145 AQPLLQLMLDVEEdRLASP--GRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYE 222


                 ...
gi 71990705 1395 FCY 1397
Cdd:cd14611  223 FVH 225
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1144-1404 3.19e-24

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: 104.34  E-value: 3.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1144 RNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILpptiGHADSSYINASHIK--GYFFDYIAAQDPVSEgTAFDFWRM 1221
Cdd:cd14608    9 RHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKmeEAQRSYILTQGPLPN-TCGHFWEM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1222 IADQNVTTVVMLSDETDWSDVE--KYWPiDGSGTECHFgsERNSVNVTCVSEEHHQDFIIRNLsysMKDNESMPANQEVV 1299
Cdd:cd14608   84 VWEQKSRGVVMLNRVMEKGSLKcaQYWP-QKEEKEMIF--EDTNLKLTLISEDIKSYYTVRQL---ELENLTTQETREIL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1300 QYSYTGWPsDSIVPKSANSLMNLIEMVlqRQS-SLMGSQAPIVVHCRNGSSESGIF----ICIsLLWLRQKAEQRIDVFQ 1374
Cdd:cd14608  158 HFHYTTWP-DFGVPESPASFLNFLFKV--RESgSLSPEHGPVVVHCSAGIGRSGTFcladTCL-LLMDKRKDPSSVDIKK 233

                        250       260       270
                 ....*....|....*....|....*....|...
gi 71990705 1375 TVKGLQSHRPMMFTRFEQYSFCYRAL---ADYI 1404
Cdd:cd14608  234 VLLEMRKFRMGLIQTADQLRFSYLAViegAKFI 266
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1190-1395 3.38e-24

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: 102.02  E-value: 3.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIK------GYFFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPiDGSGTECHFGSEr 1261
Cdd:cd14541    2 YINANYVNmeipgsGIVNRYIAAQGPLPN-TCADFWQMVWEQKSTLIVMLTTLVERGRVKchQYWP-DLGETMQFGNLQ- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1262 nsvnVTCVSEEHHQDFIIRNLS-YSMKDNESmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqRQSSlMGSQAPI 1340
Cdd:cd14541   79 ----ITCVSEEVTPSFAFREFIlTNTNTGEE----RHITQMQYLAWP-DHGVPDDSSDFLDFVKRV--RQNR-VGMVEPT 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1341 VVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSF 1395
Cdd:cd14541  147 VVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1132-1400 8.72e-24

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: 102.62  E-value: 8.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1132 ETGLEE-----EFKKLERNlTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILpptigHADSSYINASHIK------GYF 1200
Cdd:cd14600    8 KKGLESgtvliQFEQLYRK-KPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipsaNIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1201 FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPidGSGTECHFGSERnsvnVTCVSEEHHQDFI 1278
Cdd:cd14600   82 NKYIATQGPLPH-TCAQFWQVVWEQKLSLIVMLTTLTERGRTKchQYWP--DPPDVMEYGGFR----VQCHSEDCTIAYV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1279 IRNLsysMKDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQsslMGSQaPIVVHCRNGSSESGIFICIS 1358
Cdd:cd14600  155 FREM---LLTNTQTGEERTVTHLQYVAWP-DHGVPDDSSDFLEFVNYVRSKR---VENE-PVLVHCSAGIGRTGVLVTME 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 71990705 1359 LLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd14600  227 TAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAI 268
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1140-1404 8.96e-24

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: 103.15  E-value: 8.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1140 KKLERNLTTplssnfAAKDENLLKNRYEAAVPFDKYRVILPPTiGHADSSYINASHIK----GYFFDYIAAQDPVSEgTA 1215
Cdd:cd14599   24 KKADGVFTT------ATLPENAERNRIREVVPYEENRVELVPT-KENNTGYINASHIKvtvgGEEWHYIATQGPLPH-TC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1216 FDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGtecHFGSERNSVNVTcvseehhQDFIIRNLSYS---MKDNE 1290
Cdd:cd14599   96 HDFWQMVWEQGVNVIAMVTaeEEGGRSKSHRYWPKLGSK---HSSATYGKFKVT-------TKFRTDSGCYAttgLKVKH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1291 SMPANQEVVQY-SYTGWPsDSIVPKSANSLMNLIEMV--LQRQSSLM-----GSQAPIVVHCRNGSSESGIFICISLLWL 1362
Cdd:cd14599  166 LLSGQERTVWHlQYTDWP-DHGCPEEVQGFLSYLEEIqsVRRHTNSMldstkNCNPPIVVHCSAGVGRTGVVILTELMIG 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 71990705 1363 RQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1404
Cdd:cd14599  245 CLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1149-1397 9.48e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 100.46  E-value: 9.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1149 PLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADssYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQN 1226
Cdd:PHA02742   41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDGGDD--FINASYVDGHNAKgrFICTQAPLEE-TALDFWQAIFQDQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1227 VTTVVMLSD--ETDWSDVEKYWPIDGSGTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSmkdNESMPANQEVVQYSYT 1304
Cdd:PHA02742  118 VRVIVMITKimEDGKEACYPYWMPHERGKATH-----GEFKIKTKKIKSFRNYAVTNLCLT---DTNTGASLDIKHFAYE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1305 GWPSDSiVPKSANSLMNLIEMVLQRQSSL--------MGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTV 1376
Cdd:PHA02742  190 DWPHGG-LPRDPNKFLDFVLAVREADLKAdvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIV 268

                         250       260
                  ....*....|....*....|.
gi 71990705  1377 KGLQSHRPMMFTRFEQYSFCY 1397
Cdd:PHA02742  269 RDLRKQRHNCLSLPQQYIFCY 289
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 845-1071 1.25e-22

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: 97.40  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKnrQQCAKYWPDEQITRYGDIIVEPASFSF 924
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWPEEGMLRYGPIQVECMSCSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFDIAHIG--ECGPDVIPNGNGVEYAN---VPIVKGQFAnnsRRILQyhFTNWNDykapECSTGLLRfmyrlr 999
Cdd:cd14636   79 DCDVISRIFRICNLTrpQEGYLMVQQFQYLGWAShreVPGSKRSFL---KLILQ--VEKWQE----ECDEGEGR------ 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71990705 1000 elpqfnnspVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14636  144 ---------TIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1190-1400 5.31e-22

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: 95.58  E-value: 5.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHI------KGYFfdYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSDETDWSDV--EKYWPIDGSGTechfgSER 1261
Cdd:cd14596    1 YINASYItmpvgeEELF--YIATQGPLP-STIDDFWQMVWENRSDVIAMMTREVERGKVkcHRYWPETLQEP-----MEL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1262 NSVNVTCVSEEHHQDFIIRnlSYSMKDNESmPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqRQSSLMGsqaPIV 1341
Cdd:cd14596   73 ENYQLRLENYQALQYFIIR--IIKLVEKET-GENRLIKHLQFTTWP-DHGTPQSSDQLVKFICYM--RKVHNTG---PIV 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1342 VHCRNGSSESGIFICIS-LLWLRQKAEQrIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd14596  144 VHCSAGIGRAGVLICVDvLLSLIEKDLS-FNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 845-1071 5.46e-22

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: 95.52  E-value: 5.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKnrQQCAKYWPDEQITRYGDIIVEPASFSF 924
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPENGVHRHGPIQVEFVSADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFDIAHigecgpdvipngngveyANVPivkgqfANNSRRILQYHFTNWNDYKAPECST----GLLRFMYRLRE 1000
Cdd:cd14635   79 EEDIISRIFRIYN-----------------AARP------QDGYRMVQQFQFLGWPMYRDTPVSKrsflKLIRQVDKWQE 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990705 1001 LPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14635  136 EYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 845-1071 6.21e-22

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: 95.36  E-value: 6.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ-QCAKYWPDEQITRYGDIIVEPASFS 923
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  924 FHSDYAIRAFDIAHIGEcgpdvipngngveyanvpIVKGQFAnnsrrILQYHFTNWNDYK-APECSTGLLRFMYRLRELP 1002
Cdd:cd14637   81 ADEDIVTRLFRVQNITR------------------LQEGHLM-----VRHFQFLRWSAYRdTPDSKKAFLHLLASVEKWQ 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1003 QFN-NSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1071
Cdd:cd14637  138 RESgEGRTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 845-1067 8.46e-21

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: 92.00  E-value: 8.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKnrQQCAKYWPDEQitrygdiivEPASFSf 924
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELN--EDEPIYWPTKE---------KPLECE- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 hsdyairAFDIAHIGEcgpDVIPNGNGVEYanvpIVKgQF---ANNSRRIL---QYHFTNWNDYKAPECSTglLRFMYRL 998
Cdd:cd14550   69 -------TFKVTLSGE---DHSCLSNEIRL----IVR-DFileSTQDDYVLevrQFQCPSWPNPCSPIHTV--FELINTV 131

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990705  999 RELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFV--CNLRRQRnlMVQSLEQYVFIYK 1067
Cdd:cd14550  132 QEWAQQRDGPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAklYHLMRPG--VFTSKEDYQFLYK 200
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1144-1400 1.04e-20

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: 93.49  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1144 RNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPptigHADSSYINAS--HIKGYFFDYIAAQDPVSEgTAFDFWRM 1221
Cdd:cd14607    8 RNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASlvVIEEAQRSYILTQGPLPN-TCCHFWLM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1222 IADQNVTTVVMLSD--ETDWSDVEKYWPIDGSgtECHFGSErNSVNVTCVSEEHHQDFIIRNLSYsmkDNESMPANQEVV 1299
Cdd:cd14607   83 VWQQKTKAVVMLNRivEKDSVKCAQYWPTDEE--EVLSFKE-TGFSVKLLSEDVKSYYTVHLLQL---ENINSGETRTIS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1300 QYSYTGWPsDSIVPKSANSLMNLIEMVlqRQS-SLMGSQAPIVVHCRNGSSESGIFICIS--LLWLRQKAEQRIDVFQTV 1376
Cdd:cd14607  157 HFHYTTWP-DFGVPESPASFLNFLFKV--RESgSLSPEHGPAVVHCSAGIGRSGTFSLVDtcLVLMEKKDPDSVDIKQVL 233

                        250       260
                 ....*....|....*....|....
gi 71990705 1377 KGLQSHRPMMFTRFEQYSFCYRAL 1400
Cdd:cd14607  234 LDMRKYRMGLIQTPDQLRFSYMAV 257
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1146-1395 1.38e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 91.22  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1146 LTTPLSSNFAA--KDENLLKNRYEAAVPFDKYRVILPpTIGHADSSYINASHIKGYFFD--YIAAQDPVSEGTAfDFWRM 1221
Cdd:PHA02747   35 ILKPFDGLIANfeKPENQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWIDGFEDDkkFIATQGPFAETCA-DFWKA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1222 IADQNVTTVVMLSDETDWSDVEK---YWPIdgsgtechfgSERNSVNVtcvseehhQDFIIRNLSYSMK----------D 1288
Cdd:PHA02747  113 VWQEHCSIIVMLTPTKGTNGEEKcyqYWCL----------NEDGNIDM--------EDFRIETLKTSVRakyiltlieiT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1289 NESMPANQEVVQYSYTGWPSDSIVPKSAN--SLMNLIEMVLQRQSSLMGSQ----APIVVHCRNGSSESGIF----ICIS 1358
Cdd:PHA02747  175 DKILKDSRKISHFQCSEWFEDETPSDHPDfiKFIKIIDINRKKSGKLFNPKdallCPIVVHCSDGVGKTGIFcavdICLN 254

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 71990705  1359 LLWLRQKaeqrIDVFQTVKGLQSHRPMMFTRFEQYSF 1395
Cdd:PHA02747  255 QLVKRKA----ICLAKTAEKIREQRHAGIMNFDDYLF 287
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1190-1397 2.40e-19

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: 87.91  E-value: 2.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIK----GYFFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVEK---YWPiDGSGTECHFGSern 1262
Cdd:cd17658    1 YINASLVEtpasESLPKFIATQGPLPH-TFEDFWEMVIQQRCPVIIMLTRLVDNYSTAKcadYFP-AEENESREFGR--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1263 sVNVTCVSEEHHQDFI-IRNLSysMKDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLiemvLQRQSSLMGSQAPIV 1341
Cdd:cd17658   76 -ISVTNKKLKHSQHSItLRVLE--VQYIESEEPPLSVLHIQYPEWP-DHGVPKDTRSVREL----LKRLYGIPPSAGPIV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990705 1342 VHCRNGSSESGIFICISllwlrqKAEQRI--------DVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd17658  148 VHCSAGIGRTGAYCTIH------NTIRRIlegdmsavDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1190-1397 2.94e-19

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: 87.66  E-value: 2.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIKGYF--FDYIAAQDPVsEGTAFDFWRMIADQNVTTVVMLS----DETDWSDVEkYWPIDGSgteCHFGSerns 1263
Cdd:cd14637    1 YINAALTDSYTrsAAFIVTLHPL-QNTTTDFWRLVYDYGCTSVVMLNqlnqSNSAWPCLQ-YWPEPGL---QQYGP---- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1264 VNVTCVSEEHHQDFIIRnlSYSMKDNESMPANQEVV-QYSYTGWPSDSIVPKSANSLMNLIEMVLQRQSSlmGSQAPIVV 1342
Cdd:cd14637   72 MEVEFVSGSADEDIVTR--LFRVQNITRLQEGHLMVrHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRE--SGEGRTVV 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71990705 1343 HCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1397
Cdd:cd14637  148 HCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCY 202
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1190-1404 2.85e-17

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: 82.33  E-value: 2.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1190 YINASHIK----GYFFDYIAAQDPVsEGTAFDFWRMIADQNVTTVVMLSDETDwSDVEK---YWPidgsgtecHFGSERN 1262
Cdd:cd14598    1 YINASHIKvtvgGKEWDYIATQGPL-QNTCQDFWQMVWEQGVAIIAMVTAEEE-GGREKsfrYWP--------RLGSRHN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705 1263 SVN-----VTCvseehhqDFIIRNLSYS---MKDNESMPANQEVVQY-SYTGWPsDSIVP---KSANSLMNLIEMVLQRQ 1330
Cdd:cd14598   71 TVTygrfkITT-------RFRTDSGCYAttgLKIKHLLTGQERTVWHlQYTDWP-EHGCPedlKGFLSYLEEIQSVRRHT 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705 1331 SSLM---GSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1404
Cdd:cd14598  143 NSTIdpkSPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 845-1069 9.63e-16

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: 77.34  E-value: 9.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAkYWPDEQitrygdiivEPASfsf 924
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKD---------EPIN--- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 hsdyaIRAFDIAHIGE---CgpdvIPNGNGVEYANVpIVKGQFANNSRRILQYHFTNWNDYKAPECSTglLRFMYRLREL 1001
Cdd:cd17669   68 -----CETFKVTLIAEehkC----LSNEEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEE 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71990705 1002 PQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1069
Cdd:cd17669  136 AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 845-1069 2.53e-13

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: 70.48  E-value: 2.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVAN---LTEKNrqqcAKYWPDEQitrygdiivEPAS 921
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAEDE----FVYWPSRE---------ESMN 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  922 fsfhsdyaIRAFDIAHIGEcgpDVIPNGNGVEyanvpIVKGQF---ANNSRRILQY-HFT--NWNDYKAPECSTglLRFM 995
Cdd:cd17670   68 --------CEAFTVTLISK---DRLCLSNEEQ-----IIIHDFileATQDDYVLEVrHFQcpKWPNPDAPISST--FELI 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990705  996 YRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1069
Cdd:cd17670  130 NVIKEEALTRDGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1156-1408 6.29e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 71.15  E-value: 6.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1156 AKDENLlknryeaAVPFDKY---RVILpptigHADSSYINASHIKGYFFD--YIAAQDpVSEGTAFDFWRMIADQNVTTV 1230
Cdd:PHA02740   53 AKDENL-------ALHITRLlhrRIKL-----FNDEKVLDARFVDGYDFEqkFICIIN-LCEDACDKFLQALSDNKVQII 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1231 VMLSDETDWSDVEKYWpidGSGTECHFGSERNSVNVTCVSEEHHqdFIIRNLSYSMKDNESmpanQEVVQYSYTGWPSD- 1309
Cdd:PHA02740  120 VLISRHADKKCFNQFW---SLKEGCVITSDKFQIETLEIIIKPH--FNLTLLSLTDKFGQA----QKISHFQYTAWPADg 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  1310 -SIVPKS-ANSLMNLIEMVLQ-RQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMM 1386
Cdd:PHA02740  191 fSHDPDAfIDFFCNIDDLCADlEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGC 270

                         250       260
                  ....*....|....*....|..
gi 71990705  1387 FTRFEQYSFCYRALADYISKTY 1408
Cdd:PHA02740  271 MNCLDDYVFCYHLIAAYLKEKF 292
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 846-1063 3.07e-12

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 67.81  E-value: 3.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  846 INANFIKsWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYW-PDEQitrYGDIIVEpaSFSF 924
Cdd:cd14559   18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFrQSGT---YGSVTVK--SKKT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  925 HSDYAIRAFDIAHIgecgpDVIPNGNGVEYaNVPIvkgqfannsrrilqYHFTNWNDYKApeCSTGLLRFMYRL------ 998
Cdd:cd14559   92 GKDELVDGLKADMY-----NLKITDGNKTI-TIPV--------------VHVTNWPDHTA--ISSEGLKELADLvnksae 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990705  999 ---RELPQFNNSPV--------VIHCSAGVGRTGTFISIDSMLDQclaEDKANIFEFVCNLRRQRN-LMVQSLEQYV 1063
Cdd:cd14559  150 ekrNFYKSKGSSAIndknkllpVIHCRAGVGRTGQLAAAMELNKS---PNNLSVEDIVSDMRTSRNgKMVQKDEQLD 223
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 368-488 1.24e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 50.96  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  368 PFPPkeEDVRVLNSGSAlSCEVEWKSPAEPNGRITKYFVSVRgamrksdgsltPDDLPAAVEVDKRCANwdgdentskhn 447
Cdd:cd00063    1 PSPP--TNLRVTDVTST-SVTLSWTPPEDDGGPITGYVVEYR-----------EKGSGDWKEVEVTPGS----------- 55

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 71990705  448 ginpidfaneFYSCKFGPLKPNRNYTVTVWAENSAGRSLPA 488
Cdd:cd00063   56 ----------ETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 991-1067 2.78e-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: 50.43  E-value: 2.78e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71990705  991 LLRFMYRLRELPQfNNSPVVIHCSAGVGRTGTFISIDsmldqCLAEDKANIFEFVCNLRRQR-NLMVQSLEQYVFIYK 1067
Cdd:cd14494   42 VDRFLEVLDQAEK-PGEPVLVHCKAGVGRTGTLVACY-----LVLLGGMSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
972-1072 1.96e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 45.73  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  972 LQYHFTNWNDYKAPEcSTGLLRFMYRLRELPQfNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDkanIFEFVCNLRRQ 1051
Cdd:COG2453   48 LEYLHLPIPDFGAPD-DEQLQEAVDFIDEALR-EGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAEE---ALARVRAARPG 122

                         90       100
                 ....*....|....*....|.
gi 71990705 1052 RnlmVQSLEQYVFIYKALAEW 1072
Cdd:COG2453  123 A---VETPAQRAFLERFAKRL 140
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 778-1072 2.77e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 47.65  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   778 LPTEYVVRHRDTDFL-----------FAQEYESLPHFQLD--TVASNRKENAIKNRYNdirAFDDTRVKLKKINGDDYSD 844
Cdd:PHA02740    1 MAIEDAVDINGMDFInfinkpdllscIIKEYRAIVPEHEDeaNKACAQAENKAKDENL---ALHITRLLHRRIKLFNDEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   845 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQcaKYWPDEQitryGDIIVepasfsf 924
Cdd:PHA02740   78 VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFN--QFWSLKE----GCVIT------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705   925 HSDYAIRAFDIAhigecgpdVIPNGNgVEYANVPIVKGQfannSRRILQYHFTNWNDYKAPECSTGLLRFMYRLREL--- 1001
Cdd:PHA02740  145 SDKFQIETLEII--------IKPHFN-LTLLSLTDKFGQ----AQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcad 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71990705  1002 -----PQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1072
Cdd:PHA02740  212 lekhkADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAY 287
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 972-1065 9.27e-05

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: 43.81  E-value: 9.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990705  972 LQYHFTNWNDYKAPECSTgLLRFMyRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKAnIFEfvcnLRRQ 1051
Cdd:cd14504   50 LRYHHIPIEDYTPPTLEQ-IDEFL-DIVEEANAKNEAVLVHCLAGKGRTGTMLACYLVKTGKISAVDA-INE----IRRI 122

                         90
                 ....*....|....
gi 71990705 1052 RNLMVQSLEQYVFI 1065
Cdd:cd14504  123 RPGSIETSEQEKFV 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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