NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|7504409|gb|T30111|]
View 

hypothetical protein F56D1.4 - 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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
790-1084 6.59e-90

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 292.26  E-value: 6.59e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      790 LFAQEYESLPHFQLD---TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDySDYINANFIKSWKEKKLFIAAQAPVD 866
Cdd:smart00194    1 GLEEEFEKLDRLKPDdesCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      867 ATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQIT--RYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvi 944
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGC------ 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      945 pngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqliv 1024
Cdd:smart00194  154 -------------------SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHC------------- 201

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1025 nlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:smart00194  202 --SAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1147-1415 2.60e-83

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 273.38  E-value: 2.60e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1147 GLEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPtIGHADSSYINASHIKGY--FFDYIAAQDPVs 1224
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPngPKAYIATQGPL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1225 EGTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDN 1302
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTelVEKGREKCAQYWPDEEGEPLTY-----GDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1303 ESmpaNQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQR 1382
Cdd:smart00194  154 SE---TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQST---STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE 226

                           250       260       270
                    ....*....|....*....|....*....|...
gi 7504409     1383 IDVFQTVKGLQSHRPMMFTRFEQYSFCYRALAD 1415
Cdd:smart00194  227 VDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 366-486 1.25e-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: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   366 PFPPkeEDVRVLNSGSAlSCEVEWKSPAEPNGRITKYFVSVRgamrksdgsltPDDLPAAVEVDKRCANwdgdentskhn 445
Cdd:cd00063    1 PSPP--TNLRVTDVTST-SVTLSWTPPEDDGGPITGYVVEYR-----------EKGSGDWKEVEVTPGS----------- 55

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 7504409   446 ginpidfaneFYSCKFGPLKPNRNYTVTVWAENSAGRSLPA 486
Cdd:cd00063   56 ----------ETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
790-1084 6.59e-90

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 292.26  E-value: 6.59e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      790 LFAQEYESLPHFQLD---TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDySDYINANFIKSWKEKKLFIAAQAPVD 866
Cdd:smart00194    1 GLEEEFEKLDRLKPDdesCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      867 ATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQIT--RYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvi 944
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGC------ 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      945 pngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqliv 1024
Cdd:smart00194  154 -------------------SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHC------------- 201

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1025 nlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:smart00194  202 --SAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
813-1084 2.44e-83

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 272.58  E-value: 2.44e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     813 NAIKNRYNDIRAFDDTRVKLKKINGDdySDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTE 892
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     893 KNRQQCAKYWPD--EQITRYGDIIVEPASFSFH-SDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRI 969
Cdd:pfam00102   79 KGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDeKDYTVRTLEVSNGGS-------------------------EETRTV 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     970 LQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFN-NSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLA 1048
Cdd:pfam00102  134 KHFHYTGWPDHGVPESPNSLLDLLRKVRKSSLDGrSGPIVVHC---------------SAGIGRTGTFIAIDIALQQLEA 198

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 7504409    1049 EDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:pfam00102  199 EGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1147-1415 2.60e-83

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 273.38  E-value: 2.60e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1147 GLEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPtIGHADSSYINASHIKGY--FFDYIAAQDPVs 1224
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPngPKAYIATQGPL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1225 EGTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDN 1302
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTelVEKGREKCAQYWPDEEGEPLTY-----GDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1303 ESmpaNQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQR 1382
Cdd:smart00194  154 SE---TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQST---STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE 226

                           250       260       270
                    ....*....|....*....|....*....|...
gi 7504409     1383 IDVFQTVKGLQSHRPMMFTRFEQYSFCYRALAD 1415
Cdd:smart00194  227 VDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 843-1080 1.05e-79

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: 260.68  E-value: 1.05e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDE--QITRYGDIIVEPASF 920
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEggKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   921 SFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP 1000
Cdd:cd00047   81 EELSDYTIRTLELSPKGC-------------------------SESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEA 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1001 QFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd00047  136 RKPNGPIVVHC---------------SAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1173-1415 1.00e-74

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 247.93  E-value: 1.00e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    1173 NLLKNRYEAAVPFDKYRVILPPTIGHADssYINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDET 1250
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD--YINASYIDGYKkpKKYIATQGPLPN-TVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    1251 DWSDV--EKYWPIDgSGTECHFGSernsVNVTCVSEE-HHQDFIIRNLSYSMKDNEsmpANQEVVQYSYTGWPsDSIVPK 1327
Cdd:pfam00102   78 EKGREkcAQYWPEE-EGESLEYGD----FTVTLKKEKeDEKDYTVRTLEVSNGGSE---ETRTVKHFHYTGWP-DHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    1328 SANSLMNLIEMVlqRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1407
Cdd:pfam00102  149 SPNSLLDLLRKV--RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                   ....*...
gi 7504409    1408 FCYRALAD 1415
Cdd:pfam00102  227 FLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1203-1411 1.93e-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: 211.38  E-value: 1.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVML--SDETDWSDVEKYWPIDGsGTECHFGSernsVN 1278
Cdd:cd00047    1 YINASYIDGYRGPkeYIATQGPLPN-TVEDFWRMVWEQKVSVIVMLtnLVEKGREKCERYWPEEG-GKPLEYGD----IT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIRNLSYSMKDNESmpaNQEVVQYSYTGWPSDSIVPksanSLMNLIEMVLQRQSSLMGSQAPIVVHCR 1358
Cdd:cd00047   75 VTLVSEEELSDYTIRTLELSPKGCSE---SREVTHLHYTGWPDHGVPS----SPEDLLALVRRVRKEARKPNGPIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 7504409  1359 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1411
Cdd:cd00047  148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 805-1078 2.49e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 131.66  E-value: 2.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    805 TVASNRK-ENAIKNRYNDIRAFDDTRVKLKKINGDDySDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYL 883
Cdd:PHA02747   42 LIANFEKpENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    884 IVMVANLTEKN-RQQCAKYW-PDEQitryGDIIVEpasfsfhsDYAIRAFDIAhigecgpdVIPngngvEYANVPI-VKG 960
Cdd:PHA02747  121 IVMLTPTKGTNgEEKCYQYWcLNED----GNIDME--------DFRIETLKTS--------VRA-----KYILTLIeITD 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    961 QFANNSRRILQYHFTNWNDYKAPECSTGLLRFM-----YRLRELPQFNN-----SPVVIHCrylyfskihqlivnlSAGV 1030
Cdd:PHA02747  176 KILKDSRKISHFQCSEWFEDETPSDHPDFIKFIkiidiNRKKSGKLFNPkdallCPIVVHC---------------SDGV 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 7504409   1031 GRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFI 1078
Cdd:PHA02747  241 GKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFI 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
796-1086 5.45e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 129.83  E-value: 5.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   796 ESLPHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKlkkINGDdysdYINANFIKSwKEKKLFIAAQAPVDATIGDFWRM 875
Cdd:COG5599   25 NELAPSHNDPQYLQNINGSPLNRFRDIQPYKETALR---ANLG----YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   876 VWEQESYLIVMVANLTE--KNRQQCAKYWPdeQITRYGDIIVEpasfsfhsdyairafdIAHIgecgpDVIPNGNGVEYA 953
Cdd:COG5599   97 LFDNNTPVLVVLASDDEisKPKVKMPVYFR--QDGEYGKYEVS----------------SELT-----ESIQLRDGIEAR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   954 NVPIVKGQFANNSRRILQYHFTNWNDYKAPEcSTGLLRFMYRLRE---LPQFNNSPVVIHCRylyfskihqlivnlsAGV 1030
Cdd:COG5599  154 TYVLTIKGTGQKKIEIPVLHVKNWPDHGAIS-AEALKNLADLIDKkekIKDPDKLLPVVHCR---------------AGV 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 7504409  1031 GRTGTFISIDSMLD--QCLAEDKANIFEFVCNLRRQRN-LMVQSLEQYVFIyKALAEWH 1086
Cdd:COG5599  218 GRTGTLIACLALSKsiNALVQITLSVEEIVIDMRTSRNgGMVQTSEQLDVL-VKLAEQQ 275
PHA02738 PHA02738
hypothetical protein; Provisional
 1139-1420 3.13e-27

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 114.25  E-value: 3.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1139 MTTSNGETGLEEEFKKLernLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADssYINASHIKGYFFD--Y 1216
Cdd:PHA02738   18 MEKSDCEEVITREHQKV---ISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVILPAERNRGD--YINANYVDGFEYKkkF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1217 IAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETD---------WSDVEkywpidgsGTECHFGSERnsvnVTCVSEEHH 1287
Cdd:PHA02738   93 ICGQAPTRQ-TCYDFYRMLWMEHVQIIVMLCKKKEngrekcfpyWSDVE--------QGSIRFGKFK----ITTTQVETH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1288 QDFIIRNLSYSmkdnESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSL------MGSQA----PIVVHC 1357
Cdd:PHA02738  160 PHYVKSTLLLT----DGTSATQTVTHFNFTAWP-DHDVPKNTSEFLNFVLEVRQCQKELaqeslqIGHNRlqppPIVVHC 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7504409   1358 RNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYISKT 1420
Cdd:PHA02738  235 NAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLT 297
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 366-486 1.25e-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: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   366 PFPPkeEDVRVLNSGSAlSCEVEWKSPAEPNGRITKYFVSVRgamrksdgsltPDDLPAAVEVDKRCANwdgdentskhn 445
Cdd:cd00063    1 PSPP--TNLRVTDVTST-SVTLSWTPPEDDGGPITGYVVEYR-----------EKGSGDWKEVEVTPGS----------- 55

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 7504409   446 ginpidfaneFYSCKFGPLKPNRNYTVTVWAENSAGRSLPA 486
Cdd:cd00063   56 ----------ETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
790-1084 6.59e-90

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 292.26  E-value: 6.59e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      790 LFAQEYESLPHFQLD---TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDySDYINANFIKSWKEKKLFIAAQAPVD 866
Cdd:smart00194    1 GLEEEFEKLDRLKPDdesCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      867 ATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQIT--RYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvi 944
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGC------ 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      945 pngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqliv 1024
Cdd:smart00194  154 -------------------SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHC------------- 201

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1025 nlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:smart00194  202 --SAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
813-1084 2.44e-83

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 272.58  E-value: 2.44e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     813 NAIKNRYNDIRAFDDTRVKLKKINGDdySDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTE 892
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     893 KNRQQCAKYWPD--EQITRYGDIIVEPASFSFH-SDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRI 969
Cdd:pfam00102   79 KGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDeKDYTVRTLEVSNGGS-------------------------EETRTV 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     970 LQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFN-NSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLA 1048
Cdd:pfam00102  134 KHFHYTGWPDHGVPESPNSLLDLLRKVRKSSLDGrSGPIVVHC---------------SAGIGRTGTFIAIDIALQQLEA 198

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 7504409    1049 EDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:pfam00102  199 EGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1147-1415 2.60e-83

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 273.38  E-value: 2.60e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1147 GLEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPtIGHADSSYINASHIKGY--FFDYIAAQDPVs 1224
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPngPKAYIATQGPL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1225 EGTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDN 1302
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTelVEKGREKCAQYWPDEEGEPLTY-----GDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1303 ESmpaNQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQR 1382
Cdd:smart00194  154 SE---TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQST---STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE 226

                           250       260       270
                    ....*....|....*....|....*....|...
gi 7504409     1383 IDVFQTVKGLQSHRPMMFTRFEQYSFCYRALAD 1415
Cdd:smart00194  227 VDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 843-1080 1.05e-79

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: 260.68  E-value: 1.05e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDE--QITRYGDIIVEPASF 920
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEggKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   921 SFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP 1000
Cdd:cd00047   81 EELSDYTIRTLELSPKGC-------------------------SESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEA 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1001 QFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd00047  136 RKPNGPIVVHC---------------SAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1173-1415 1.00e-74

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 247.93  E-value: 1.00e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    1173 NLLKNRYEAAVPFDKYRVILPPTIGHADssYINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDET 1250
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD--YINASYIDGYKkpKKYIATQGPLPN-TVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    1251 DWSDV--EKYWPIDgSGTECHFGSernsVNVTCVSEE-HHQDFIIRNLSYSMKDNEsmpANQEVVQYSYTGWPsDSIVPK 1327
Cdd:pfam00102   78 EKGREkcAQYWPEE-EGESLEYGD----FTVTLKKEKeDEKDYTVRTLEVSNGGSE---ETRTVKHFHYTGWP-DHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    1328 SANSLMNLIEMVlqRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1407
Cdd:pfam00102  149 SPNSLLDLLRKV--RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                   ....*...
gi 7504409    1408 FCYRALAD 1415
Cdd:pfam00102  227 FLYDAILE 234
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 771-1092 2.90e-71

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: 240.70  E-value: 2.90e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   771 IPVDDLPTEYVVRHRDTDFLFAQEYESLPH--FQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANF 848
Cdd:cd14621    8 LPVDKLEEEINRRMADDNKLFREEFNALPAcpIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   849 IKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAI 928
Cdd:cd14621   88 INGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   929 RAFDIAHIGEcgpdvipngngveyanvpiVKGQfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLREL-PQFnNSPV 1007
Cdd:cd14621  168 RKFCIQQVGD-------------------VTNK--KPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCnPQY-AGAI 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1008 VIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEWHM 1087
Cdd:cd14621  226 VVHC---------------SAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYL 290


                 ....*
gi 7504409  1088 YGDTD 1092
Cdd:cd14621  291 YGDTE 295
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 791-1084 4.93e-70

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: 236.47  E-value: 4.93e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   791 FAQEYESLPHFQLD----TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDD--YSDYINANFIKSWKEKKLFIAAQAP 864
Cdd:cd17667    1 FSEDFEEVQRCTADmnitAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDskHSDYINANYVDGYNKAKAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   865 VDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIahigecgpdvi 944
Cdd:cd17667   81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSI----------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   945 pngngveyANVPIVKGQFAN-----NSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfski 1019
Cdd:cd17667  150 --------RNTKVKKGQKGNpkgrqNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHC-------- 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1020 hqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd17667  214 -------SAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 818-1080 6.76e-70

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: 233.79  E-value: 6.76e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   818 RYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQ 897
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   898 CAKYWP-DEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGECgpdvipngngveyanvpivkgqfannsRRILQYHFTN 976
Cdd:cd14548   81 CDHYWPfDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEV---------------------------RSVRQFHFTA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   977 WNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFE 1056
Cdd:cd14548  134 WPDHGVPEAPDSLLRFVRLVRDYIKQEKGPTIVHC---------------SAGVGRTGTFIALDRLLQQIESEDYVDIFG 198

                        250       260
                 ....*....|....*....|....
gi 7504409  1057 FVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd14548  199 IVYDLRKHRPLMVQTEAQYIFLHQ 222
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 843-1079 5.21e-69

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: 230.70  E-value: 5.21e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSF 922
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFDIAHIGecgpdvipngngveyanvpIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFmyrLRELPQF 1002
Cdd:cd14549   81 LATYTVRTFSLKNLK-------------------LKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAA 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1003 NN---SPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIY 1079
Cdd:cd14549  139 NPpgaGPIVVHC---------------SAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 813-1084 6.27e-68

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: 228.82  E-value: 6.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   813 NAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTE 892
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   893 KNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQY 972
Cdd:cd14553   83 RSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNG-------------------------SSEKREVRQF 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   973 HFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKA 1052
Cdd:cd14553  138 QFTAWPDHGVPEHPTPFLAFLRRVKACNPPDAGPIVVHC---------------SAGVGRTGCFIVIDSMLERIKHEKTV 202

                        250       260       270
                 ....*....|....*....|....*....|..
gi 7504409  1053 NIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14553  203 DIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 819-1084 1.47e-64

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: 218.66  E-value: 1.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   819 YNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQC 898
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   899 AKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIA--HIGECGPdvipngngveyanvpivkgqfannSRRILQYHFTN 976
Cdd:cd14620   81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpqLPDGCKA------------------------PRLVTQLHFTS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   977 WNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFE 1056
Cdd:cd14620  137 WPDFGVPFTPIGMLKFLKKVKSVNPVHAGPIVVHC---------------SAGVGRTGTFIVIDAMIDMMHAEQKVDVFE 201

                        250       260
                 ....*....|....*....|....*...
gi 7504409  1057 FVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14620  202 FVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 807-1080 1.44e-63

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: 217.62  E-value: 1.44e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   807 ASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVM 886
Cdd:cd14543   23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   887 VANLTEKNRQQCAKYWPDEQ--ITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaN 964
Cdd:cd14543  103 TTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTET-------------------------D 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   965 NSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNS-------------PVVIHCrylyfskihqlivnlSAGVG 1031
Cdd:cd14543  158 ESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKamgdrwkghppgpPIVVHC---------------SAGIG 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 7504409  1032 RTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd14543  223 RTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1203-1411 1.93e-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: 211.38  E-value: 1.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVML--SDETDWSDVEKYWPIDGsGTECHFGSernsVN 1278
Cdd:cd00047    1 YINASYIDGYRGPkeYIATQGPLPN-TVEDFWRMVWEQKVSVIVMLtnLVEKGREKCERYWPEEG-GKPLEYGD----IT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIRNLSYSMKDNESmpaNQEVVQYSYTGWPSDSIVPksanSLMNLIEMVLQRQSSLMGSQAPIVVHCR 1358
Cdd:cd00047   75 VTLVSEEELSDYTIRTLELSPKGCSE---SREVTHLHYTGWPDHGVPS----SPEDLLALVRRVRKEARKPNGPIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 7504409  1359 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1411
Cdd:cd00047  148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 791-1084 3.95e-60

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: 207.97  E-value: 3.95e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   791 FAQEYESL-PHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATI 869
Cdd:cd14626   18 FSQEYESIdPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   870 GDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngng 949
Cdd:cd14626   98 SDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNG------------ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   950 veyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAG 1029
Cdd:cd14626  166 -------------SSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHC---------------SAG 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1030 VGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14626  218 VGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 817-1078 6.95e-60

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: 205.44  E-value: 6.95e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   817 NRYNDIRAFDDTRVKLKkINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ 896
Cdd:cd14615    1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   897 QCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTN 976
Cdd:cd14615   80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQT-------------------------NESRTVRHFHFTS 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   977 WNDYKAPECSTGLLRFMYRLRELPQFN--NSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANI 1054
Cdd:cd14615  135 WPDHGVPETTDLLINFRHLVREYMKQNppNSPILVHC---------------SAGVGRTGTFIAIDRLIYQIENENVVDV 199

                        250       260
                 ....*....|....*....|....
gi 7504409  1055 FEFVCNLRRQRNLMVQSLEQYVFI 1078
Cdd:cd14615  200 YGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 817-1079 3.00e-59

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: 203.40  E-value: 3.00e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   817 NRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWK-EKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNr 895
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   896 QQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfannSRRILQYHFT 975
Cdd:cd14547   80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGE---------------------------KRYLKHYWYT 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   976 NWNDYKAPECSTGLLRFMYRLRELPQFNNS--PVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKAN 1053
Cdd:cd14547  133 SWPDHKTPEAAQPLLSLVQEVEEARQTEPHrgPIVVHC---------------SAGIGRTGCFIATSIGCQQLREEGVVD 197

                        250       260
                 ....*....|....*....|....*.
gi 7504409  1054 IFEFVCNLRRQRNLMVQSLEQYVFIY 1079
Cdd:cd14547  198 VLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 843-1080 2.75e-58

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: 199.75  E-value: 2.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSF 922
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFDIAhigecgpdvipngngveyanvPIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQF 1002
Cdd:cd14551   81 LVDYTTRKFCIQ---------------------KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPP 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7504409  1003 NNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd14551  140 RAGPIVVHC---------------SAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 812-1084 5.97e-58

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: 200.25  E-value: 5.97e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   812 ENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLT 891
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   892 EKNRQQCAKYWPDEQITrYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQ 971
Cdd:cd14630   82 EVGRVKCVRYWPDDTEV-YGDIKVTLIETEPLAEYVIRTFTVQKKG-------------------------YHEIREIRQ 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   972 YHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDK 1051
Cdd:cd14630  136 FHFTSWPDHGVPCYATGLLGFVRQVKFLNPPDAGPIVVHC---------------SAGAGRTGCFIAIDIMLDMAENEGV 200

                        250       260       270
                 ....*....|....*....|....*....|...
gi 7504409  1052 ANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14630  201 VDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 771-1084 3.82e-57

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: 199.55  E-value: 3.82e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   771 IPVDDLpTEYVVRHRDTDFL-FAQEYESL-PHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANF 848
Cdd:cd14625    4 IPISEL-AEHTERLKANDNLkLSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   849 IKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAI 928
Cdd:cd14625   83 IDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFCV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   929 RAFDIahigecgpdvipNGNGveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVV 1008
Cdd:cd14625  163 RTFSL------------HKNG-------------SSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIV 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7504409  1009 IHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14625  218 VHC---------------SAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 843-1082 2.00e-56

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: 194.81  E-value: 2.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSF 922
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFDIahigecgpdvipngngveyANVPIVKG--QFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP 1000
Cdd:cd17668   81 LAYYTVRNFTL-------------------RNTKIKKGsqKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAK 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1001 QFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd17668  142 RHAVGPVVVHC---------------SAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206


                 ..
gi 7504409  1081 AL 1082
Cdd:cd17668  207 AL 208
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 791-1084 4.84e-56

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 196.03  E-value: 4.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   791 FAQEYESLPHFQLDTVASNRK-ENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATI 869
Cdd:cd14633   17 FKEEYESFFEGQSAPWDSAKKdENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   870 GDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQiTRYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngng 949
Cdd:cd14633   97 YDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDT-EIYKDIKVTLIETELLAEYVIRTFAVEKRG------------ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   950 veyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAG 1029
Cdd:cd14633  164 -------------VHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHC---------------SAG 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1030 VGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14633  216 AGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 813-1081 6.71e-56

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: 194.28  E-value: 6.71e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   813 NAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTE 892
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   893 KNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkGQfannSRRILQY 972
Cdd:cd14554   86 MGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD---------------------GQ----SRTVRQF 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   973 HFTNWNDYKAPECSTGLLRFMYRL-RELPQFN-NSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAED 1050
Cdd:cd14554  141 QFTDWPEQGVPKSGEGFIDFIGQVhKTKEQFGqEGPITVHC---------------SAGVGRTGVFITLSIVLERMRYEG 205

                        250       260       270
                 ....*....|....*....|....*....|.
gi 7504409  1051 KANIFEFVCNLRRQRNLMVQSLEQYVFIYKA 1081
Cdd:cd14554  206 VVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 843-1079 1.16e-55

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: 192.46  E-value: 1.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIK-SWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQIT-RYGDIIVEPASF 920
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   921 SFHSDYA--IRAFDIAHigecgpdvipngNGVEyanvpivkgqfannSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRE 998
Cdd:cd18533   81 EENDDGGfiVREFELSK------------EDGK--------------VKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRE 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   999 LPQ--FNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLD---------QCLAEDKANIFEFVCNLRRQRNL 1067
Cdd:cd18533  135 LNDsaSLDPPIIVHC---------------SAGVGRTGTFIALDSLLDelkrglsdsQDLEDSEDPVYEIVNQLRKQRMS 199

                        250
                 ....*....|..
gi 7504409  1068 MVQSLEQYVFIY 1079
Cdd:cd18533  200 MVQTLRQYIFLY 211
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 771-1084 5.21e-55

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: 193.41  E-value: 5.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   771 IPVDDLpTEYVVRHRDTDFL-FAQEYESL-PHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANF 848
Cdd:cd14624    4 IPILEL-ADHIERLKANDNLkFSQEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   849 IKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAI 928
Cdd:cd14624   83 IDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   929 RAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVV 1008
Cdd:cd14624  163 RTFALYKNG-------------------------SSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMV 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7504409  1009 IHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14624  218 VHC---------------SAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 817-1080 7.66e-55

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: 190.90  E-value: 7.66e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   817 NRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ 896
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   897 QCAKYWP-DEQITRYGDIIVEPASFSFHSDYAIRAFDIahigeCGPDVIpngngveyanvpivkgqfaNNSRRILQYHFT 975
Cdd:cd14617   81 KCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKI-----CSEEQL-------------------DAPRLVRHFHYT 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   976 NWNDYKAPECSTGLLRFMYRLRELPQFNNS--PVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKAN 1053
Cdd:cd14617  137 VWPDHGVPETTQSLIQFVRTVRDYINRTPGsgPTVVHC---------------SAGVGRTGTFIALDRILQQLDSKDSVD 201

                        250       260
                 ....*....|....*....|....*..
gi 7504409  1054 IFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd14617  202 IYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 817-1082 2.10e-54

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: 189.71  E-value: 2.10e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   817 NRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ 896
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   897 QCAKYWP-DEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGECGpdvipngngveyanvpivkgqfannSRRILQYHFT 975
Cdd:cd14619   81 KCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQK-------------------------TLSVRHFHFT 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   976 NWNDYKAPECSTGLLRFMYRLREL--PQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKAN 1053
Cdd:cd14619  136 AWPDHGVPSSTDTLLAFRRLLRQWldQTMSGGPTVVHC---------------SAGVGRTGTLIALDVLLQQLQSEGLLG 200

                        250       260
                 ....*....|....*....|....*....
gi 7504409  1054 IFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1082
Cdd:cd14619  201 PFSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 843-1080 7.44e-54

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: 186.96  E-value: 7.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWP--DEQITRYGDIIVEPASF 920
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   921 SFHSDYAIRAFDIAHIGECGpdvipngngveyanvpivkgqfanNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP 1000
Cdd:cd14557   81 KICPDYIIRKLNINNKKEKG------------------------SGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFN 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1001 QFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd14557  137 NFFSGPIVVHC---------------SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 813-1085 2.46e-52

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: 184.59  E-value: 2.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   813 NAIKNRYNDIRAFDDTRVKLKKINGD-DYSDYINANFIKS-------WKEKKLFIAAQAPVDATIGDFWRMVWEQESYLI 884
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIRNenegpttDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   885 VMVANLTEKNRQQCAKYWPDEQITR-YGDIIVEPASFSFHSDYAIRAFDIAHIGECGPdvipngngveyanvpivkgqfa 963
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQKqYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDP---------------------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   964 nnSRRILQYHFTNWNDYKAPECSTGLLRFMYRL-RELPQFNNS-PVVIHCrylyfskihqlivnlSAGVGRTGTFISIDS 1041
Cdd:cd14544  139 --IREIWHYQYLSWPDHGVPSDPGGVLNFLEDVnQRQESLPHAgPIVVHC---------------SAGIGRTGTFIVIDM 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 7504409  1042 MLDQC----LAEDkANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1085
Cdd:cd14544  202 LLDQIkrkgLDCD-IDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQY 248
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 798-1080 4.45e-52

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: 183.55  E-value: 4.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   798 LPHFqldtvASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVW 877
Cdd:cd14614    2 IPHF-----AADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   878 EQESYLIVMVANLTEKNRQQCAKYWP-DEQITRYGDIIVEPASFSFHSDYAIRAFDIAhigecgpdvipngngveyanvp 956
Cdd:cd14614   77 QQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVS---------------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   957 ivkgqFANNSRRILQYHFTNWNDYKAPECSTG--LLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTG 1034
Cdd:cd14614  135 -----YADEVQDVMHFNYTAWPDHGVPTANAAesILQFVQMVRQQAVKSKGPMIIHC---------------SAGVGRTG 194

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 7504409  1035 TFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd14614  195 TFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 817-1082 4.80e-51

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: 180.14  E-value: 4.80e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   817 NRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ 896
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   897 QCAKYWPDEQI-TRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFT 975
Cdd:cd14618   81 LCDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKLWHEDL-------------------------RKERRVKHLHYT 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   976 NWNDYKAPECSTGLLRFMYRLRELPQF--NNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKAN 1053
Cdd:cd14618  136 AWPDHGIPESTSSLMAFRELVREHVQAtkGKGPTLVHC---------------SAGVGRSGTFIALDRLLRQLKEEKVVD 200

                        250       260
                 ....*....|....*....|....*....
gi 7504409  1054 IFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1082
Cdd:cd14618  201 VFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 803-1084 3.11e-50

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: 179.25  E-value: 3.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   803 LDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESY 882
Cdd:cd14603   20 CSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   883 LIVMVANLTEKNRQQCAKYWPDEQitrygdiivEPASFSfhsdyairAFDIAHIGE--CGPDVIpngngveyanVPIVKG 960
Cdd:cd14603  100 VILMACREIEMGKKKCERYWAQEQ---------EPLQTG--------PFTITLVKEkrLNEEVI----------LRTLKV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   961 QFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISID 1040
Cdd:cd14603  153 TFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHC---------------SAGCGRTGVICTVD 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 7504409  1041 SMLDQCLAE---DKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14603  218 YVRQLLLTQripPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 843-1082 2.93e-49

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: 173.99  E-value: 2.93e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSF 922
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFdiahigecgpdVIPNGNGveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRL-RELPQ 1001
Cdd:cd14552   81 YEDYTLRDF-----------LVTKGKG--------------GSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQ 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1002 FNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKA 1081
Cdd:cd14552  136 SGNHPITVHC---------------SAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200


                 .
gi 7504409  1082 L 1082
Cdd:cd14552  201 V 201
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 814-1083 4.69e-49

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: 175.02  E-value: 4.69e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   814 AIKNRYNDIRAFDDTRVKLKKI-NGDDYSDYINANFIKSWK-EKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLT 891
Cdd:cd14612   16 ASKDRYKTILPNPQSRVCLRRAgSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   892 EKNrQQCAKYWPDEQITrYGDIIVEPASFSFHSDYAIRAFDIAHIGECgpdvipngngveyanvpivkgqfannsRRILQ 971
Cdd:cd14612   96 EKK-EKCVHYWPEKEGT-YGRFEIRVQDMKECDGYTIRDLTIQLEEES---------------------------RSVKH 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   972 YHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNS--PVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAE 1049
Cdd:cd14612  147 YWFSSWPDHQTPESAGPLLRLVAEVEESRQTAASpgPIVVHC---------------SAGIGRTGCFIATSIGCQQLKDT 211

                        250       260       270
                 ....*....|....*....|....*....|....
gi 7504409  1050 DKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALA 1083
Cdd:cd14612  212 GKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLA 245
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 843-1084 7.16e-49

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: 172.79  E-value: 7.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITrYGDIIVEPASFSF 922
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV-YGDIKVTLVETEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQF 1002
Cdd:cd14555   80 LAEYVVRTFALERRG-------------------------YHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPP 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1003 NNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1082
Cdd:cd14555  135 SAGPIVVHC---------------SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199


                 ..
gi 7504409  1083 AE 1084
Cdd:cd14555  200 LE 201
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1173-1412 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 7504409  1173 NLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLS--D 1248
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRgaYIATQGPLAE-TTEDFWRMLWEHNSTIIVMLTklR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1249 ETDWSDVEKYWPIDGSGTECHFgsernsvNVTCVSEEHHQDFIIRNLSYS-MKDNESmpanQEVVQYSYTGWPsDSIVPK 1327
Cdd:cd14554   85 EMGREKCHQYWPAERSARYQYF-------VVDPMAEYNMPQYILREFKVTdARDGQS----RTVRQFQFTDWP-EQGVPK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1328 SANSLMNLIEMVlQRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1407
Cdd:cd14554  153 SGEGFIDFIGQV-HKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQ 231


                 ....*
gi 7504409  1408 FCYRA 1412
Cdd:cd14554  232 FCYRA 236
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 805-1084 1.45e-48

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: 175.51  E-value: 1.45e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   805 TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLI 884
Cdd:cd14604   49 TATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAII 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   885 VMVANLTEKNRQQCAKYWP--DEQITRYGDIIVEPASFSFHSDYAIRAFDIahigecgpdvipngngveyanvpivkgQF 962
Cdd:cd14604  129 VMACREFEMGRKKCERYWPlyGEEPMTFGPFRISCEAEQARTDYFIRTLLL---------------------------EF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   963 ANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISID-- 1040
Cdd:cd14604  182 QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHC---------------SAGCGRTGAICAIDyt 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 7504409  1041 -SMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14604  247 wNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 829-1084 2.18e-48

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: 172.13  E-value: 2.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   829 RVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQiT 908
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDT-E 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   909 RYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTG 988
Cdd:cd14631   80 VYGDFKVTCVEMEPLAEYVVRTFTLERRG-------------------------YNEIREVKQFHFTGWPDHGVPYHATG 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   989 LLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLM 1068
Cdd:cd14631  135 LLSFIRRVKLSNPPSAGPIVVHC---------------SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINM 199

                        250
                 ....*....|....*.
gi 7504409  1069 VQSLEQYVFIYKALAE 1084
Cdd:cd14631  200 VQTEEQYIFIHDAILE 215
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 806-1085 2.49e-48

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: 174.53  E-value: 2.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   806 VASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIV 885
Cdd:cd14628   45 ISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   886 MVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkGQfann 965
Cdd:cd14628  125 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD---------------------GQ---- 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   966 SRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP-QF-NNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSML 1043
Cdd:cd14628  180 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKeQFgQDGPISVHC---------------SAGVGRTGVFITLSIVL 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 7504409  1044 DQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1085
Cdd:cd14628  245 ERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 806-1085 7.17e-48

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: 173.00  E-value: 7.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   806 VASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIV 885
Cdd:cd14627   46 ISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   886 MVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkGQfann 965
Cdd:cd14627  126 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD---------------------GQ---- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   966 SRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP-QF-NNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSML 1043
Cdd:cd14627  181 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKeQFgQDGPISVHC---------------SAGVGRTGVFITLSIVL 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 7504409  1044 DQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1085
Cdd:cd14627  246 ERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 817-1080 1.94e-47

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: 169.32  E-value: 1.94e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   817 NRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ 896
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   897 QCAKYWPDEQ--ITRYGDIIVEPASFSFHSDYAIRAFDIAHIGECgpdvipngngveyanvpivkgqfannsRRILQYHF 974
Cdd:cd14616   81 RCHQYWPEDNkpVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDY---------------------------MMVRQCNF 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   975 TNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANI 1054
Cdd:cd14616  134 TSWPEHGVPESSAPLIHFVKLVRASRAHDNTPMIVHC---------------SAGVGRTGVFIALDHLTQHINDHDFVDI 198

                        250       260
                 ....*....|....*....|....*.
gi 7504409  1055 FEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd14616  199 YGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 806-1085 6.07e-47

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: 170.68  E-value: 6.07e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   806 VASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIV 885
Cdd:cd14629   46 ISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   886 MVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkGQfann 965
Cdd:cd14629  126 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARD---------------------GQ---- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   966 SRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP-QF-NNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSML 1043
Cdd:cd14629  181 SRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKeQFgQDGPITVHC---------------SAGVGRTGVFITLSIVL 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 7504409  1044 DQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1085
Cdd:cd14629  246 ERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 816-1080 7.40e-47

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: 167.95  E-value: 7.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   816 KNRYNDIRAFDDTRVKLKKINGDdySDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNR 895
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   896 QQCAKYWPDEQITrygDIIVEPASFSF-------HSDYAIRAFDIAHIgecgpdvipngngveyanvpivKGQFannSRR 968
Cdd:cd14545   79 IKCAQYWPQGEGN---AMIFEDTGLKVtllseedKSYYTVRTLELENL----------------------KTQE---TRE 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   969 ILQYHFTNWNDYKAPECSTGLLRFMYRLRE--LPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFisidSMLDQC 1046
Cdd:cd14545  131 VLHFHYTTWPDFGVPESPAAFLNFLQKVREsgSLSSDVGPPVVHC---------------SAGIGRSGTF----CLVDTC 191

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 7504409  1047 LAE------DKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd14545  192 LVLiekgnpSSVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 818-1084 1.81e-46

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: 166.76  E-value: 1.81e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   818 RYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQ 897
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   898 CAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNW 977
Cdd:cd14623   81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRE-------------------------NKSRQIRQFHFHGW 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   978 NDYKAPECSTGLLRFMYRL-RELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFE 1056
Cdd:cd14623  136 PEVGIPSDGKGMINIIAAVqKQQQQSGNHPITVHC---------------SAGAGRTGTFCALSTVLERVKAEGILDVFQ 200

                        250       260
                 ....*....|....*....|....*...
gi 7504409  1057 FVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14623  201 TVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 812-1085 5.22e-46

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: 166.35  E-value: 5.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   812 ENAIKNRYNDIRAFDDTRVKLKkiNGD---DYSDYINANFI--------KSWKEKKLFIAAQAPVDATIGDFWRMVWEQE 880
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLH--DGDpnePVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQEN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   881 SYLIVMVANLTEKNRQQCAKYWPDE-QITRYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivk 959
Cdd:cd14605   79 SRVIVMTTKEVERGKSKCVKYWPDEyALKEYGVMRVRNVKESAAHDYILRELKLSKVGQ--------------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   960 gqfANNSRRILQYHFTNWNDYKAPECSTGLLRFM--YRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFI 1037
Cdd:cd14605  138 ---GNTERTVWQYHFRTWPDHGVPSDPGGVLDFLeeVHHKQESIMDAGPVVVHC---------------SAGIGRTGTFI 199

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 7504409  1038 SIDSMLDqcLAEDKA-----NIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1085
Cdd:cd14605  200 VIDILID--IIREKGvdcdiDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHY 250
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 842-1085 7.88e-46

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: 164.02  E-value: 7.88e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   842 DYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFS 921
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   922 FHSDYAIRAFdiahigecgpdvipngngveyanvpIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRL-RELP 1000
Cdd:cd14622   81 LLETISIRDF-------------------------LVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQ 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1001 QFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd14622  136 QTGNHPIVVHC---------------SAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYR 200


                 ....*
gi 7504409  1081 ALAEW 1085
Cdd:cd14622  201 VVQDF 205
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 816-1083 7.99e-46

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: 166.19  E-value: 7.99e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   816 KNRYNDIRAFDDTRVKLKKINGDDY-SDYINANFIKSW-KEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEK 893
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   894 NrQQCAKYWPDEQITrYGDIIVEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfannSRRILQYH 973
Cdd:cd14613  108 N-EKCTEYWPEEQVT-YEGIEITVKQVIHADDYRLRLITLKSGGE---------------------------ERGLKHYW 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   974 FTNWNDYKAPECSTGLLRFMYRLRELPQ---FNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAED 1050
Cdd:cd14613  159 YTSWPDQKTPDNAPPLLQLVQEVEEARQqaePNCGPVIVHC---------------SAGIGRTGCFIATSICCKQLRNEG 223

                        250       260       270
                 ....*....|....*....|....*....|...
gi 7504409  1051 KANIFEFVCNLRRQRNLMVQSLEQYVFIYKALA 1083
Cdd:cd14613  224 VVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 780-1084 3.51e-45

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: 165.23  E-value: 3.51e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   780 YVVRHRDTDFLFAQEYESLPHFQLDTVASN---RKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKK 856
Cdd:cd14610    8 YMEDHLKNKNRLEKEWEALCAYQAEPNATNvaqREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   857 -LFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGdiIVEPASFSFH---SDYAIRAFd 932
Cdd:cd14610   88 pAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYH--IYEVNLVSEHiwcEDFLVRSF- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   933 iahigecgpdvipngngveyanvpIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCr 1012
Cdd:cd14610  165 ------------------------YLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHC- 219

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7504409  1013 ylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKA-NIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14610  220 --------------SDGAGRSGTYILIDMVLNKMAKGAKEiDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 843-1084 2.37e-44

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: 159.83  E-value: 2.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITrYGDIIVEPASFSF 922
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT-YGDIKITLLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQF 1002
Cdd:cd14632   80 LAEYSVRTFALERRG-------------------------YSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPP 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1003 NNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1082
Cdd:cd14632  135 DAGPVVVHC---------------SAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199


                 ..
gi 7504409  1083 AE 1084
Cdd:cd14632  200 LE 201
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1178-1408 8.18e-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: 8.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1178 RYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVsEGTAFDFWRMIADQNVTTVVMLSD--ETDWS 1253
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSprEFIATQGPL-PGTKDDFWRMVWEQNSHTIVMLTQcmEKGRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1254 DVEKYWPIDGsgTECHFGSernsVNVTCVSEEHHQDFIIRNLSYSMKDnESMPanqeVVQYSYTGWPsDSIVPKSANSLM 1333
Cdd:cd14548   80 KCDHYWPFDQ--DPVYYGD----ITVTMLSESVLPDWTIREFKLERGD-EVRS----VRQFHFTAWP-DHGVPEAPDSLL 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7504409  1334 NLIEMVLQRqssLMGSQAPIVVHCRNGSSESGIFicISLLWLRQK--AEQRIDVFQTVKGLQSHRPMMFTRFEQYSF 1408
Cdd:cd14548  148 RFVRLVRDY---IKQEKGPTIVHCSAGVGRTGTF--IALDRLLQQieSEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 816-1084 4.34e-43

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: 157.31  E-value: 4.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   816 KNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNR 895
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   896 QQCAKYW--PDEQITRYGDIIVEPASFSFHSDYAIRafdiahigecgpdvipngngveyanvpIVKGQFANNSRRILQYH 973
Cdd:cd14602   81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIR---------------------------TLKVKFNSETRTIYQFH 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   974 FTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISID---SMLDQCLAED 1050
Cdd:cd14602  134 YKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHC---------------SAGCGRTGVICAIDytwMLLKDGIIPE 198

                        250       260       270
                 ....*....|....*....|....*....|....
gi 7504409  1051 KANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14602  199 NFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 810-1085 8.39e-43

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: 157.73  E-value: 8.39e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   810 RKENAIKNRYNDIRAFDDTRVKLKkiNGDDY---SDYINANFIKS--W---KEKKLFIAAQAPVDATIGDFWRMVWEQES 881
Cdd:cd14606   15 RPENKSKNRYKNILPFDHSRVILQ--GRDSNipgSDYINANYVKNqlLgpdENAKTYIASQGCLEATVNDFWQMAWQENS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   882 YLIVMVANLTEKNRQQCAKYWPDEQITR-YGDIIVEPASFSFHSDYAIRafdiaHIGECGPDvipNGNGVeyanvpivkg 960
Cdd:cd14606   93 RVIVMTTREVEKGRNKCVPYWPEVGMQRaYGPYSVTNCGEHDTTEYKLR-----TLQVSPLD---NGELI---------- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   961 qfannsRRILQYHFTNWNDYKAPECSTGLLRFM----YRLRELPqfNNSPVVIHCrylyfskihqlivnlSAGVGRTGTF 1036
Cdd:cd14606  155 ------REIWHYQYLSWPDHGVPSEPGGVLSFLdqinQRQESLP--HAGPIIVHC---------------SAGIGRTGTI 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 7504409  1037 ISIDSMLDQCLAED---KANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1085
Cdd:cd14606  212 IVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQF 263
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1131-1417 1.12e-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: 158.36  E-value: 1.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1131 AIVSSRESMTTSNGETGLEEEFKKL---ERNLTTPLSSNFAAkdeNLLKNRYEAAVPFDKYRVILPPTIGHADSSYINAS 1207
Cdd:cd14628   10 AYIQKLTQIETGENVTGMELEFKRLassKAHTSRFISANLPC---NKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINAS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1208 HIKGYFFD--YIAAQDPVSEGTAfDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTECHFgsernsvNVTCVS 1283
Cdd:cd14628   87 FIDGYRQQkaYIATQGPLAETTE-DFWRMLWEHNSTIVVMLTKlrEMGREKCHQYWPAERSARYQYF-------VVDPMA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1284 EEHHQDFIIRNLSYS-MKDNESmpanQEVVQYSYTGWPSDSiVPKSANSLMNLIEMVlQRQSSLMGSQAPIVVHCRNGSS 1362
Cdd:cd14628  159 EYNMPQYILREFKVTdARDGQS----RTVRQFQFTDWPEQG-VPKSGEGFIDFIGQV-HKTKEQFGQDGPISVHCSAGVG 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1363 ESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1417
Cdd:cd14628  233 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1146-1417 1.78e-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: 1.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1146 TGLEEEFKKL---ERNLTTPLSSNFAAkdeNLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQ 1220
Cdd:cd14627   26 TGMELEFKRLansKAHTSRFISANLPC---NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQkaYIATQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1221 DPVSEGTAfDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTECHFgsernsvNVTCVSEEHHQDFIIRNLSYS 1298
Cdd:cd14627  103 GPLAETTE-DFWRMLWENNSTIVVMLTKlrEMGREKCHQYWPAERSARYQYF-------VVDPMAEYNMPQYILREFKVT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1299 -MKDNESmpanQEVVQYSYTGWPSDSiVPKSANSLMNLIEMVlQRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQ 1377
Cdd:cd14627  175 dARDGQS----RTVRQFQFTDWPEQG-VPKSGEGFIDFIGQV-HKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERM 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 7504409  1378 KAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1417
Cdd:cd14627  249 RYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 811-1082 1.87e-42

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: 155.37  E-value: 1.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   811 KENAIKNRYNDIRAFDDTRVKLkkinGDDySDYINANFIK--SWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVA 888
Cdd:cd14597    1 KENRKKNRYKNILPYDTTRVPL----GDE-GGYINASFIKmpVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   889 NLTEKNRQQCAKYWPDEqiTRYGDIIVEPASFSFHSDYAIRAFDIAHIgecgpdvipngngvEYANVPivkgqfANNSRR 968
Cdd:cd14597   76 QEVEGGKIKCQRYWPEI--LGKTTMVDNRLQLTLVRMQQLKNFVIRVL--------------ELEDIQ------TREVRH 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   969 ILQYHFTNWNDYKAPECSTGLLRFMYRLRELpqFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLA 1048
Cdd:cd14597  134 ITHLNFTAWPDHDTPSQPEQLLTFISYMRHI--HKSGPIITHC---------------SAGIGRSGTLICIDVVLGLISK 196

                        250       260       270
                 ....*....|....*....|....*....|....
gi 7504409  1049 EDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1082
Cdd:cd14597  197 DLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1144-1410 2.45e-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: 2.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1144 GETGLEEEFKKLeRNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQD 1221
Cdd:cd14543    1 QKRGIYEEYEDI-RREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKnaYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1222 PVsEGTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGTEcHFGsernSVNVTCVSEEHHQDFIIRNLS-YS 1298
Cdd:cd14543   80 PL-PKTYSDFWRMVWEQKVLVIVMTTrvVERGRVKCGQYWPLEEGSSL-RYG----DLTVTNLSVENKEHYKKTTLEiHN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1299 MKDNESmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSL---MGSQ-------APIVVHCRNGSSESGIF- 1367
Cdd:cd14543  154 TETDES----RQVTHFQFTSWP-DFGVPSSAAALLDFLGEVRQQQALAvkaMGDRwkghppgPPIVVHCSAGIGRTGTFc 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 7504409  1368 ---ICISllwlRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd14543  229 tldICLS----QLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 843-1079 5.45e-42

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: 152.93  E-value: 5.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITrYGDIIVEPASFSF 922
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT-YGDIEVELKDTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRE-LPQ 1001
Cdd:cd14558   80 SPTYTVRVFEITHLKR-------------------------KDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQkLPY 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1002 FN-----NSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYV 1076
Cdd:cd14558  135 KNskhgrSVPIVVHC---------------SDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQ 199


                 ...
gi 7504409  1077 FIY 1079
Cdd:cd14558  200 FLY 202
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 843-1084 5.82e-42

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: 152.91  E-value: 5.82e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIK--SWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPD---EQITRYGDIIVEP 917
Cdd:cd14538    1 YINASHIRipVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   918 ASFSFHSDYAIRAFDIAHI--GEcgpdvipngngveyanvpivkgqfannSRRILQYHFTNWNDYKAPECSTGLLRFMYR 995
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKetGE---------------------------VHHITHLNFTTWPDHGTPQSADPLLRFIRY 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   996 LRELpqFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQY 1075
Cdd:cd14538  134 MRRI--HNSGPIVVHC---------------SAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQY 196


                 ....*....
gi 7504409  1076 VFIYKALAE 1084
Cdd:cd14538  197 IFCYKACLE 205
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 816-1079 8.20e-42

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: 153.54  E-value: 8.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   816 KNRYNDIRAFDDTRVKLKKINGDDY-SDYINANFIKSWK-EKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEK 893
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   894 NrQQCAKYWPdEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGECgpdvipngngveyanvpivkgqfannsRRILQYH 973
Cdd:cd14611   82 N-EKCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQS---------------------------RSVKHYW 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   974 FTNWNDYKAPECSTGLLRFMYRLRE--LPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDK 1051
Cdd:cd14611  133 YTSWPDHKTPDSAQPLLQLMLDVEEdrLASPGRGPVVVHC---------------SAGIGRTGCFIATTIGCQQLKEEGV 197

                        250       260
                 ....*....|....*....|....*...
gi 7504409  1052 ANIFEFVCNLRRQRNLMVQSLEQYVFIY 1079
Cdd:cd14611  198 VDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1203-1410 1.23e-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: 1.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTEchfgsernSVN 1278
Cdd:cd14558    1 YINASFIDGYWGpkSLIATQGPLPD-TIADFWQMIFQKKVKVIVMLTElkEGDQEQCAQYWGDEKKTYG--------DIE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIRNLS-YSMKDNESmpanQEVVQYSYTGWpSDSIVPKSANSLMNLIEMVLQRQ---SSLMGSQAPIV 1354
Cdd:cd14558   72 VELKDTEKSPTYTVRVFEiTHLKRKDS----RTVYQYQYHKW-KGEELPEKPKDLVDMIKSIKQKLpykNSKHGRSVPIV 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 7504409  1355 VHCRNGSSESGIFICislLW-LRQKA--EQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd14558  147 VHCSDGSSRTGIFCA---LWnLLESAetEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 843-1080 1.53e-41

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: 151.81  E-value: 1.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQ--ITRYGDIIVEPASF 920
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeeQLQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   921 SFHS-DYAIRAfdiahigecgpdvipngngveyanvpiVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLREL 999
Cdd:cd14542   81 KRVGpDFLIRT---------------------------LKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1000 PQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISID----SMLDQCLAEDkANIFEFVCNLRRQRNLMVQSLEQY 1075
Cdd:cd14542  134 QGSEDVPICVHC---------------SAGCGRTGTICAIDyvwnLLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQY 197


                 ....*
gi 7504409  1076 VFIYK 1080
Cdd:cd14542  198 ELVYR 202
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 812-1097 1.56e-41

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: 154.41  E-value: 1.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   812 ENAIKNRYNDIRAFDDTRVKLKKinGDDysDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLT 891
Cdd:cd14608   24 KNKNRNRYRDVSPFDHSRIKLHQ--EDN--DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVM 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   892 EKNRQQCAKYWP----DEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngngveyanvpivkgqfANNSR 967
Cdd:cd14608  100 EKGSLKCAQYWPqkeeKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLT-------------------------TQETR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   968 RILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFN--NSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDS---M 1042
Cdd:cd14608  155 EILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSpeHGPVVVHC---------------SAGIGRSGTFCLADTcllL 219

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1043 LDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEWHMYGDTDEDVRD 1097
Cdd:cd14608  220 MDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQD 274
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1139-1419 4.01e-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: 4.01e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1139 MTTSNGETGLEEEFKKLERnLTTPLSS------NFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGY 1212
Cdd:cd14604   18 STDHNGEDNFASDFMRLRR-LSTKYRTekiyptATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1213 F--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDW--SDVEKYWPIDGSGTeCHFGSERnsvnVTCVSEEHHQ 1288
Cdd:cd14604   97 YgpKAYIATQGPLAN-TVIDFWRMIWEYNVAIIVMACREFEMgrKKCERYWPLYGEEP-MTFGPFR----ISCEAEQART 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1289 DFIIRNLSYSMkDNESmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFI 1368
Cdd:cd14604  171 DYFIRTLLLEF-QNET----RRLYQFHYVNWP-DHDVPSSFDSILDMISLMRKYQEH---EDVPICIHCSAGCGRTGAIC 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 7504409  1369 CISLLWLRQKA---EQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYISK 1419
Cdd:cd14604  242 AIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEK 295
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1146-1417 2.87e-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: 2.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1146 TGLEEEFKKL---ERNLTTPLSSNFAAkdeNLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQ 1220
Cdd:cd14629   26 TAMELEFKLLansKAHTSRFISANLPC---NKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQkaYIATQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1221 DPVSEGTAfDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTECHFgsernsvNVTCVSEEHHQDFIIRNLSYS 1298
Cdd:cd14629  103 GPLAETTE-DFWRMLWEHNSTIVVMLTKlrEMGREKCHQYWPAERSARYQYF-------VVDPMAEYNMPQYILREFKVT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1299 -MKDNESmpanQEVVQYSYTGWPSDSiVPKSANSLMNLIEMVlQRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQ 1377
Cdd:cd14629  175 dARDGQS----RTIRQFQFTDWPEQG-VPKTGEGFIDFIGQV-HKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERM 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 7504409  1378 KAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1417
Cdd:cd14629  249 RYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1173-1418 2.04e-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: 2.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1173 NLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDET 1250
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQnaYIATQGPLPE-TFGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1251 DWSDV--EKYWPIDGSGTechFGSernsVNVTCVSEEHHQDFIIRNLSYSMkdnESMPANQEVVQYSYTGWPsDSIVPKS 1328
Cdd:cd14553   82 ERSRVkcDQYWPTRGTET---YGL----IQVTLLDTVELATYTVRTFALHK---NGSSEKREVRQFQFTAWP-DHGVPEH 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1329 ANSLMnlieMVLQRQSSLMGSQA-PIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1407
Cdd:cd14553  151 PTPFL----AFLRRVKACNPPDAgPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYI 226

                        250
                 ....*....|.
gi 7504409  1408 FCYRALADYIS 1418
Cdd:cd14553  227 FIHDALLEAVT 237
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1173-1417 4.08e-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: 4.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1173 NLLKNRYEAAVPFDKYRVIL---PPTIGHADssYINASHIK---------GYFFDYIAAQDPVsEGTAFDFWRMIADQNV 1240
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILkdrDPNVPGSD--YINANYIRnenegpttdENAKTYIATQGCL-ENTVSDFWSMVWQENS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1241 TTVVMLSDETDW--SDVEKYWPIDGSGTEchFGSERnsvnVTCVSEEHHQDFIIRNLSYSMKDNESMPanQEVVQYSYTG 1318
Cdd:cd14544   78 RVIVMTTKEVERgkNKCVRYWPDEGMQKQ--YGPYR----VQNVSEHDTTDYTLRELQVSKLDQGDPI--REIWHYQYLS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1319 WPsDSIVPKSANSLMNLIEMVLQRQSSLMgSQAPIVVHCRNGSSESGIFICISLLwLRQKAEQ----RIDVFQTVKGLQS 1394
Cdd:cd14544  150 WP-DHGVPSDPGGVLNFLEDVNQRQESLP-HAGPIVVHCSAGIGRTGTFIVIDML-LDQIKRKgldcDIDIQKTIQMVRS 226

                        250       260
                 ....*....|....*....|...
gi 7504409  1395 HRPMMFTRFEQYSFCYRALADYI 1417
Cdd:cd14544  227 QRSGMVQTEAQYKFIYVAVAQYI 249
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1183-1415 4.43e-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: 4.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1183 VPFDKYRVILPPTIGHADSSYINASHIKGY--FFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKY 1258
Cdd:cd14623    6 IPYEFNRVIIPVKRGEENTDYVNASFIDGYrqKDSYIASQGPLQH-TIEDFWRMIWEWKSCSIVMLTEleERGQEKCAQY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1259 WPIDGSGTechFGSernsVNVTCVSEEHHQDFIIRNLSYS-MKDNESmpanQEVVQYSYTGWPSDSIvPKSANSLMNLIE 1337
Cdd:cd14623   85 WPSDGSVS---YGD----ITIELKKEEECESYTVRDLLVTnTRENKS----RQIRQFHFHGWPEVGI-PSDGKGMINIIA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7504409  1338 MVlQRQSSLMGSQaPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALAD 1415
Cdd:cd14623  153 AV-QKQQQQSGNH-PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 794-1082 6.54e-39

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: 146.26  E-value: 6.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   794 EYESLPHfqldTVASNrKENAIKNRYNDIRAFDDTRVKLKKINgddySDYINANFIKSWKEKKLFIAAQAPVDATIGDFW 873
Cdd:cd14607   10 ESHDYPH----RVAKY-PENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   874 RMVWEQESYLIVMVANLTEKNRQQCAKYWP--DEQITRYGD--IIVEPASFSFHSDYAIRAFDIAHIGecgpdvipngng 949
Cdd:cd14607   81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPtdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENIN------------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   950 veyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFN--NSPVVIHCrylyfskihqlivnlS 1027
Cdd:cd14607  149 -------------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSpeHGPAVVHC---------------S 200

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7504409  1028 AGVGRTGTFisidSMLDQCLA------EDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1082
Cdd:cd14607  201 AGIGRSGTF----SLVDTCLVlmekkdPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1203-1413 8.14e-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: 8.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTEchfgserNSVN 1278
Cdd:cd14552    1 YINASFIDGYRQKdaYIATQGPLDH-TVEDFWRMIWEWKSCSIVMLTEikERSQNKCAQYWPEDGSVSS-------GDIT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIRNLSYSMKDNESMpanQEVVQYSYTGWPSDSIvPKSANSLMNLIEMVlQRQSSLMGSQaPIVVHCR 1358
Cdd:cd14552   73 VELKDQTDYEDYTLRDFLVTKGKGGST---RTVRQFHFHGWPEVGI-PDNGKGMIDLIAAV-QKQQQQSGNH-PITVHCS 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1359 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd14552  147 AGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 842-1081 1.08e-38

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: 144.01  E-value: 1.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   842 DYINANFIK------SWKEKklFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPD-EQITRYGDII 914
Cdd:cd14541    1 DYINANYVNmeipgsGIVNR--YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   915 VEPASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMY 994
Cdd:cd14541   79 ITCVSEEVTPSFAFREFILTNTNT-------------------------GEERHITQMQYLAWPDHGVPDDSSDFLDFVK 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   995 RLRELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQ 1074
Cdd:cd14541  134 RVRQNRVGMVEPTVVHC---------------SAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQ 198


                 ....*..
gi 7504409  1075 YVFIYKA 1081
Cdd:cd14541  199 YRFVCEA 205
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 812-1082 1.73e-38

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: 145.38  E-value: 1.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   812 ENAIKNRYNDIRAFDDTRVKLkkiNGDDysDYINANFIK----SWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMV 887
Cdd:cd14600   39 QNMDKNRYKDVLPYDATRVVL---QGNE--DYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   888 ANLTEKNRQQCAKYWPDEQ-ITRYGDIIVEPASFSFHSDYAIRAFDIAHIgECGpdvipngngveyanvpivkgqfanNS 966
Cdd:cd14600  114 TTLTERGRTKCHQYWPDPPdVMEYGGFRVQCHSEDCTIAYVFREMLLTNT-QTG------------------------EE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   967 RRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQfNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLdqC 1046
Cdd:cd14600  169 RTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHC---------------SAGIGRTGVLVTMETAM--C 230

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 7504409  1047 LAEDKANIF--EFVCNLRRQRNLMVQSLEQYVFIYKAL 1082
Cdd:cd14600  231 LTERNQPVYplDIVRKMRDQRAMMVQTSSQYKFVCEAI 268
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1203-1410 3.99e-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: 3.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFFD--YIAAQDPVsEGTAFDFWRMIADQNVTTVVMLS--DETDWSdVEKYWPIDGSGTechFGSernsVN 1278
Cdd:cd14556    1 YINAALLDSYKQPaaFIVTQHPL-PNTVTDFWRLVYDYGCTSIVMLNqlDPKDQS-CPQYWPDEGSGT---YGP----IQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIR--NLSYSMKDNEsmpANQEVVQYSYTGWPSDSIVPKSANSLMNLIEMV--LQRQSSlmgsQAPIV 1354
Cdd:cd14556   72 VEFVSTTIDEDVISRifRLQNTTRPQE---GYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVekWQEQSG----EGPIV 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 7504409  1355 VHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd14556  145 VHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 843-1085 6.85e-38

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: 141.82  E-value: 6.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIK-SWKEKKLF-IAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQI----TRYGDIIVE 916
Cdd:cd14540    1 YINASHITaTVGGKQRFyIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGehdaLTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   917 PASFSFHSDYAIRAFDIAHIGECgpdvipngngveyanvpivkgqfanNSRRILQYHFTNWNDYKAPECSTGLLRFMYRL 996
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSG-------------------------QSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEI 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   997 REL---------PQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLdQCLAED-KANIFEFVCNLRRQRN 1066
Cdd:cd14540  136 NSVrrhtnqdvaGHNRNPPTLVHC---------------SAGVGRTGVVILADLML-YCLDHNeELDIPRVLALLRHQRM 199

                        250
                 ....*....|....*....
gi 7504409  1067 LMVQSLEQYVFIYKALAEW 1085
Cdd:cd14540  200 LLVQTLAQYKFVYNVLIQY 218
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 782-1084 9.41e-38

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: 143.64  E-value: 9.41e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   782 VRHRDTdflFAQEYESLPHFQLD---TVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINAN-FIKSWKEKKL 857
Cdd:cd14609   11 LRNRDR---LAKEWQALCAYQAEpntCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   858 FIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGdiIVEPASFSFH---SDYAIRAFDIA 934
Cdd:cd14609   88 YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYH--IYEVNLVSEHiwcEDFLVRSFYLK 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   935 HIGecgpdvipngngveyanvpivkgqfANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCryl 1014
Cdd:cd14609  166 NVQ-------------------------TQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHC--- 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1015 yfskihqlivnlSAGVGRTGTFISIDSMLDQcLAE-----DKANIFEFVcnlRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:cd14609  218 ------------SDGAGRTGTYILIDMVLNR-MAKgvkeiDIAATLEHV---RDQRPGMVRTKDQFEFALTAVAE 276
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1177-1417 1.56e-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: 1.56e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1177 NRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSD 1254
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSsqEFIATQGPLPQ-TVGDFWRMIWEQQSSTIVMLTNCMEAGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1255 V--EKYWPIDGsgTECHFGSERnsvnVTCVSEEHHQDFIIRNLSYSMKDNESmpaNQEVVQYSYTGWPsDSIVPKSANSL 1332
Cdd:cd14619   80 VkcEHYWPLDY--TPCTYGHLR----VTVVSEEVMENWTVREFLLKQVEEQK---TLSVRHFHFTAWP-DHGVPSSTDTL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1333 MNLIEMVLQRQSSLMgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRA 1412
Cdd:cd14619  150 LAFRRLLRQWLDQTM-SGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQC 228


                 ....*
gi 7504409  1413 LADYI 1417
Cdd:cd14619  229 ILDFL 233
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1147-1413 3.52e-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: 3.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1147 GLEEEFKKLERNLTTPLSSnfAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVS 1224
Cdd:cd14633   16 GFKEEYESFFEGQSAPWDS--AKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRpnHYIATQGPMQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1225 EgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPIDgsgTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDN 1302
Cdd:cd14633   94 E-TIYDFWRMVWHENTASIIMVTNLVEVGRVKccKYWPDD---TEIY-----KDIKVTLIETELLAEYVIRTFAVEKRGV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1303 ESMpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQR 1382
Cdd:cd14633  165 HEI---REIRQFHFTGWP-DHGVPYHATGLLGFVRQV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV 237

                        250       260       270
                 ....*....|....*....|....*....|.
gi 7504409  1383 IDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd14633  238 VDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1163-1415 1.23e-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: 1.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1163 LSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNV 1240
Cdd:cd14603   20 CSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSraYIATQGPLSH-TVLDFWRMIWQYGV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1241 TTVVMLSDETDWS--DVEKYWPIDGSGTEchFGsernSVNVTCVSEEH-HQDFIIRNLSYSMKDNEsmpanQEVVQYSYT 1317
Cdd:cd14603   99 KVILMACREIEMGkkKCERYWAQEQEPLQ--TG----PFTITLVKEKRlNEEVILRTLKVTFQKES-----RSVSHFQYM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1318 GWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIfIC----ISLLWLRQKAEQRIDVFQTVKGLQ 1393
Cdd:cd14603  168 AWP-DHGIPDSPDCMLAMIELARRLQGS---GPEPLCVHCSAGCGRTGV-ICtvdyVRQLLLTQRIPPDFSIFDVVLEMR 242

                        250       260
                 ....*....|....*....|..
gi 7504409  1394 SHRPMMFTRFEQYSFCYRALAD 1415
Cdd:cd14603  243 KQRPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1203-1416 1.11e-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: 1.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYF-FDY-IAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTechFGSernsVN 1278
Cdd:cd14622    2 YINASFIDGYRqKDYfIATQGPLAH-TVEDFWRMVWEWKCHTIVMLTElqEREQEKCVQYWPSEGSVT---HGE----IT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIRNLSYSMKDNESmpaNQEVVQYSYTGWPSDSIvPKSANSLMNLIEMVlQRQSSLMGSQaPIVVHCR 1358
Cdd:cd14622   74 IEIKNDTLLETISIRDFLVTYNQEKQ---TRLVRQFHFHGWPEIGI-PAEGKGMIDLIAAV-QKQQQQTGNH-PIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 7504409  1359 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADY 1416
Cdd:cd14622  148 AGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1177-1415 2.19e-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: 2.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1177 NRYEAAVPFDKYRVILPpTIGHADSSYINASHIKGYFF--DYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSD--ETDW 1252
Cdd:cd14615    1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSkkEFIAAQGPLP-NTVKDFWRMVWEKNVYAIVMLTKcvEQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1253 SDVEKYWPIDGSGTechfgseRNSVNVTCVSEEHHQDFIIRNLSY-SMKDNESMPanqeVVQYSYTGWPsDSIVPKSANS 1331
Cdd:cd14615   79 TKCEEYWPSKQKKD-------YGDITVTMTSEIVLPEWTIRDFTVkNAQTNESRT----VRHFHFTSWP-DHGVPETTDL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1332 LMNLIEMVLQ--RQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFC 1409
Cdd:cd14615  147 LINFRHLVREymKQNP---PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223


                 ....*.
gi 7504409  1410 YRALAD 1415
Cdd:cd14615  224 NQCALD 229
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 843-1084 3.87e-35

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: 133.33  E-value: 3.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFI--KSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEqitrygdiIVEPASF 920
Cdd:cd14596    1 YINASYItmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPET--------LQEPMEL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   921 SfhsDYAIRafdiahigecgpdvIPNGNGVEYANVPIVK--GQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRE 998
Cdd:cd14596   73 E---NYQLR--------------LENYQALQYFIIRIIKlvEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRK 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   999 LpqFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFI 1078
Cdd:cd14596  136 V--HNTGPIVVHC---------------SAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFC 198


                 ....*.
gi 7504409  1079 YKALAE 1084
Cdd:cd14596  199 YKVVLE 204
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1203-1410 6.42e-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: 6.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIK---GYFFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDwSDVEK---YWPidgsgtECHFGSERNS 1276
Cdd:cd18533    1 YINASYITlpgTSSKRYIATQGPLPA-TIGDFWKMIWQNNVGVIVMLTPLVE-NGREKcdqYWP------SGEYEGEYGD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1277 VNVTCVSEEHHQD--FIIRNLSYSMKDNESmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMV--LQRQSSLMGsqaP 1352
Cdd:cd18533   73 LTVELVSEEENDDggFIVREFELSKEDGKV----KKVYHIQYKSWP-DFGVPDSPEDLLTLIKLKreLNDSASLDP---P 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7504409  1353 IVVHCRNGSSESGIFICI--------SLLWLRQKAEQRID-VFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd18533  145 IIVHCSAGVGRTGTFIALdslldelkRGLSDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 843-1084 9.45e-35

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: 132.57  E-value: 9.45e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKK-LFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPAS-F 920
Cdd:cd14546    1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSeH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   921 SFHSDYAIRAFdiahigecgpdvipngngveyanvpIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELP 1000
Cdd:cd14546   81 IWCDDYLVRSF-------------------------YLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1001 QFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKA-NIFEFVCNLRRQRNLMVQSLEQYVFIY 1079
Cdd:cd14546  136 RGRSCPIVVHC---------------SDGAGRTGTYILIDMVLNRMAKGAKEiDIAATLEHLRDQRPGMVKTKDQFEFVL 200


                 ....*
gi 7504409  1080 KALAE 1084
Cdd:cd14546  201 TAVAE 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1148-1418 9.77e-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: 9.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1148 LEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYffD-----YIAAQDP 1222
Cdd:cd14610   19 LEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDH--DprnpaYIATQGP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1223 VSeGTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTECHFGSERNSVNVTCvseehhQDFIIRnlSYSMK 1300
Cdd:cd14610   97 LP-ATVADFWQMVWESGCVVIVMLTPlaENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWC------EDFLVR--SFYLK 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1301 dNESMPANQEVVQYSYTGWpSDSIVPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQ-KA 1379
Cdd:cd14610  168 -NLQTNETRTVTQFHFLSW-NDQGVPASTRSLLDFRRKV---NKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKG 242

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 7504409  1380 EQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYIS 1418
Cdd:cd14610  243 AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVN 281
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1177-1413 2.64e-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: 2.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1177 NRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSD 1254
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSpqEFIATQGPLKK-TIEDFWRLVWEQQVCNIIMLTVGMENGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1255 V--EKYWPIDGsgTECHFGSernsVNVTCVSEEHHQDFIIRNLSYSmkdNESMPANQEVVQYSYTGWPsDSIVPKSANSL 1332
Cdd:cd14618   80 VlcDHYWPSES--TPVSYGH----ITVHLLAQSSEDEWTRREFKLW---HEDLRKERRVKHLHYTAWP-DHGIPESTSSL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1333 MNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRA 1412
Cdd:cd14618  150 MAFRELVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                 .
gi 7504409  1413 L 1413
Cdd:cd14618  229 I 229
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1179-1413 4.94e-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: 4.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1179 YEAAVPFDKYRVILPPTIGHADSSYINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSD 1254
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKekNKFIAAQGPKQE-TVNDFWRMVWEQKSATIVMLTNlkERKEEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1255 VEKYWPIDGSGTechFGSERNSVNVTCVSeehhQDFIIRNLSYSMKDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMN 1334
Cdd:cd14620   80 CYQYWPDQGCWT---YGNIRVAVEDCVVL----VDYTIRKFCIQPQLPDGCKAPRLVTQLHFTSWP-DFGVPFTPIGMLK 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7504409  1335 LIEMVLQRQSSLMGsqaPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd14620  152 FLKKVKSVNPVHAG---PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 794-1085 5.09e-34

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: 132.81  E-value: 5.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   794 EYESLPHFQLDTVASNRK--ENAIKNRYNDIRAFDDTRVKLKKiNGDDYSDYINANFIK------SWKekklFIAAQAPV 865
Cdd:cd14599   17 EYEQIPKKKADGVFTTATlpENAERNRIREVVPYEENRVELVP-TKENNTGYINASHIKvtvggeEWH----YIATQGPL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   866 DATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWP----DEQITRYGDIIVepaSFSFHSD---YAIRAFDIAHige 938
Cdd:cd14599   92 PHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgsKHSSATYGKFKV---TTKFRTDsgcYATTGLKVKH--- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   939 cgpdvipngngveyanvpIVKGQfannSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNS----------PVV 1008
Cdd:cd14599  166 ------------------LLSGQ----ERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIV 223

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7504409  1009 IHCrylyfskihqlivnlSAGVGRTGTFISIDSMLdQCLAE-DKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEW 1085
Cdd:cd14599  224 VHC---------------SAGVGRTGVVILTELMI-GCLEHnEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1203-1410 7.23e-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: 7.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPIDGSGTEChfgserNSVNVT 1280
Cdd:cd14550    1 YINASYLQGYRRsnEFIITQHPLEH-TIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEKPLEC------ETFKVT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1281 CVSEEH----------HQDFIIRnlsySMKDNESMpanqEVVQYSYTGWPsDSIVPKSanSLMNLIEMVLQRQSSlmgSQ 1350
Cdd:cd14550   74 LSGEDHsclsneirliVRDFILE----STQDDYVL----EVRQFQCPSWP-NPCSPIH--TVFELINTVQEWAQQ---RD 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1351 APIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd14550  140 GPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1148-1416 7.68e-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: 132.84  E-value: 7.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1148 LEEEFKKLErnlTTPL--SSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGY--FFDYIAAQDPv 1223
Cdd:cd14621   28 FREEFNALP---ACPIqaTCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYqeKNKFIAAQGP- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1224 SEGTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTechFGSERNSVNVTCVSeehhQDFIIRNLSYSMKD 1301
Cdd:cd14621  104 KEETVNDFWRMIWEQNTATIVMVTNlkERKECKCAQYWPDQGCWT---YGNIRVSVEDVTVL----VDYTVRKFCIQQVG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1302 NESMPANQEVV-QYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGsqaPIVVHCRNGSSESGIFICISLLWLRQKAE 1380
Cdd:cd14621  177 DVTNKKPQRLItQFHFTSWP-DFGVPFTPIGMLKFLKKVKNCNPQYAG---AIVVHCSAGVGRTGTFIVIDAMLDMMHAE 252

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 7504409  1381 QRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADY 1416
Cdd:cd14621  253 RKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1165-1411 9.30e-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: 9.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1165 SNFAAK-DENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVT 1241
Cdd:cd14614    3 PHFAADlPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSpqEYIATQGPLPE-TRNDFWKMVLQQKSQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1242 TVVMLS--DETDWSDVEKYWPidgsgtechFGSE---RNSVNVTCVSEEHHQDFIIRNLSYSMKDnesmpANQEVVQYSY 1316
Cdd:cd14614   82 IIVMLTqcNEKRRVKCDHYWP---------FTEEpvaYGDITVEMLSEEEQPDWAIREFRVSYAD-----EVQDVMHFNY 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1317 TGWPsDSIVP--KSANSLMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQS 1394
Cdd:cd14614  148 TAWP-DHGVPtaNAAESILQFVQMVRQQAVK---SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRS 223

                        250
                 ....*....|....*..
gi 7504409  1395 HRPMMFTRFEQYSFCYR 1411
Cdd:cd14614  224 YRMSMVQTEEQYIFIHQ 240
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 842-1082 1.39e-33

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: 129.29  E-value: 1.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   842 DYINANFIK----SWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQIT-RYGDIIVE 916
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSsSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   917 PASFSFHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfaNNSRRILQYHFTNWNDYKAPECSTGLLRFMYRL 996
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNLEK-------------------------NESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLV 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   997 RELPQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLdqCLAEDKANIF--EFVCNLRRQRNLMVQSLEQ 1074
Cdd:cd14601  136 RNKRAGKDEPVVVHC---------------SAGIGRTGVLITMETAM--CLIECNQPVYplDIVRTMRDQRAMMIQTPSQ 198


                 ....*...
gi 7504409  1075 YVFIYKAL 1082
Cdd:cd14601  199 YRFVCEAI 206
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1203-1413 1.67e-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: 1.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIK----GYFFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDV--EKYWPiDGSGTECHFGserNS 1276
Cdd:cd14538    1 YINASHIRipvgGDTYHYIACQGPLPN-TTGDFWQMVWEQKSEVIAMVTQDVEGGKVkcHRYWP-DSLNKPLICG---GR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1277 VNVTCVSEEHHQDFIIRNLSysMKDNESmPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqRQSSLMGsqaPIVVH 1356
Cdd:cd14538   76 LEVSLEKYQSLQDFVIRRIS--LRDKET-GEVHHITHLNFTTWP-DHGTPQSADPLLRFIRYM--RRIHNSG---PIVVH 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 7504409  1357 CRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd14538  147 CSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 843-1079 2.19e-33

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: 128.29  E-value: 2.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVaNLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSF 922
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFDIAHIgecgpdvipngngveyanvpivkGQFANNSRRILQYHFTNWNDYKapECSTGLLRFMYRLREL--- 999
Cdd:cd14556   80 DEDVISRIFRLQNT-----------------------TRPQEGYRMVQQFQFLGWPRDR--DTPPSKRALLKLLSEVekw 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1000 -PQFNNSPVVIHCRylyfskihqlivnlsAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFI 1078
Cdd:cd14556  135 qEQSGEGPIVVHCL---------------NGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFC 199


                 .
gi 7504409  1079 Y 1079
Cdd:cd14556  200 Y 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 805-1078 2.49e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 131.66  E-value: 2.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    805 TVASNRK-ENAIKNRYNDIRAFDDTRVKLKKINGDDySDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYL 883
Cdd:PHA02747   42 LIANFEKpENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    884 IVMVANLTEKN-RQQCAKYW-PDEQitryGDIIVEpasfsfhsDYAIRAFDIAhigecgpdVIPngngvEYANVPI-VKG 960
Cdd:PHA02747  121 IVMLTPTKGTNgEEKCYQYWcLNED----GNIDME--------DFRIETLKTS--------VRA-----KYILTLIeITD 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    961 QFANNSRRILQYHFTNWNDYKAPECSTGLLRFM-----YRLRELPQFNN-----SPVVIHCrylyfskihqlivnlSAGV 1030
Cdd:PHA02747  176 KILKDSRKISHFQCSEWFEDETPSDHPDFIKFIkiidiNRKKSGKLFNPkdallCPIVVHC---------------SDGV 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 7504409   1031 GRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFI 1078
Cdd:PHA02747  241 GKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFI 288
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
969-1084 3.74e-33

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 124.01  E-value: 3.74e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      969 ILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQF--NNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQC 1046
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHC---------------SAGVGRTGTFVAIDILLQQL 66

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 7504409     1047 LAE-DKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:smart00404   67 EAEaGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 969-1084 3.74e-33

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: 124.01  E-value: 3.74e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409      969 ILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQF--NNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQC 1046
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQseSSGPVVVHC---------------SAGVGRTGTFVAIDILLQQL 66

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 7504409     1047 LAE-DKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAE 1084
Cdd:smart00012   67 EAEaGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1189-1413 4.33e-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: 4.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1189 RVILPPTIGHADSSYINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPIDgs 1264
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQrpSHYIATQGPVHE-TVYDFWRMIWQEQSACIVMVTNLVEVGRVKcyKYWPDD-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1265 gTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDNESMpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqrQS 1344
Cdd:cd14631   78 -TEVY-----GDFKVTCVEMEPLAEYVVRTFTLERRGYNEI---REVKQFHFTGWP-DHGVPYHATGLLSFIRRV---KL 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7504409  1345 SLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd14631  145 SNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
796-1086 5.45e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 129.83  E-value: 5.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   796 ESLPHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKlkkINGDdysdYINANFIKSwKEKKLFIAAQAPVDATIGDFWRM 875
Cdd:COG5599   25 NELAPSHNDPQYLQNINGSPLNRFRDIQPYKETALR---ANLG----YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   876 VWEQESYLIVMVANLTE--KNRQQCAKYWPdeQITRYGDIIVEpasfsfhsdyairafdIAHIgecgpDVIPNGNGVEYA 953
Cdd:COG5599   97 LFDNNTPVLVVLASDDEisKPKVKMPVYFR--QDGEYGKYEVS----------------SELT-----ESIQLRDGIEAR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   954 NVPIVKGQFANNSRRILQYHFTNWNDYKAPEcSTGLLRFMYRLRE---LPQFNNSPVVIHCRylyfskihqlivnlsAGV 1030
Cdd:COG5599  154 TYVLTIKGTGQKKIEIPVLHVKNWPDHGAIS-AEALKNLADLIDKkekIKDPDKLLPVVHCR---------------AGV 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 7504409  1031 GRTGTFISIDSMLD--QCLAEDKANIFEFVCNLRRQRN-LMVQSLEQYVFIyKALAEWH 1086
Cdd:COG5599  218 GRTGTLIACLALSKsiNALVQITLSVEEIVIDMRTSRNgGMVQTSEQLDVL-VKLAEQQ 275
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1176-1413 7.83e-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: 127.65  E-value: 7.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1176 KNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDW- 1252
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPraYIATQGPLST-TLLDFWRMIWEYSVLIIVMACMEFEMg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1253 -SDVEKYWPIDGSgTECHFGsernSVNVTCVSEEHHQDFIIRNLSYSMKDnesmpANQEVVQYSYTGWPsDSIVPKSANS 1331
Cdd:cd14602   80 kKKCERYWAEPGE-MQLEFG----PFSVTCEAEKRKSDYIIRTLKVKFNS-----ETRTIYQFHYKNWP-DHDVPSSIDP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1332 LMNLIEMVLQRQSSlmgSQAPIVVHCRNGSSESGIFICISLLWLRQK---AEQRIDVFQTVKGLQSHRPMMFTRFEQYSF 1408
Cdd:cd14602  149 ILELIWDVRCYQED---DSVPICIHCSAGCGRTGVICAIDYTWMLLKdgiIPENFSVFSLIQEMRTQRPSLVQTKEQYEL 225


                 ....*
gi 7504409  1409 CYRAL 1413
Cdd:cd14602  226 VYNAV 230
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1203-1410 1.53e-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: 1.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTechFGSernsVN 1278
Cdd:cd14549    1 YINANYVDGYNKAraYIATQGPLPS-TFDDFWRMVWEQNSAIIVMITNlvERGRRKCDQYWPKEGTET---YGN----IQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIRNLSYSM---KDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIemvlqRQSSL--MGSQAPI 1353
Cdd:cd14549   73 VTLLSTEVLATYTVRTFSLKNlklKKVKGRSSERVVYQYHYTQWP-DHGVPDYTLPVLSFV-----RKSSAanPPGAGPI 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 7504409  1354 VVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd14549  147 VVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 810-1082 1.58e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 129.76  E-value: 1.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    810 RKENAIKNRYNDIRAFDDTRVKL----------------KKI---NGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIG 870
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgKKIevtSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    871 DFWRMVWEQESYLIVMVANlTEKNRQQCAKYW--PDEQITRYGDIIVEPASFSFHSDYAIRAFDIAhigecgpDVIpngn 948
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFTKTRLMIT-------DKI---- 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    949 gveyanvpivkgqfANNSRRILQYHFTNWNDYKAPecsTGLLRFM--------YRLRELPQFNNS-----PVVIHCryly 1015
Cdd:PHA02746  196 --------------SDTSREIHHFWFPDWPDNGIP---TGMAEFLelinkvneEQAELIKQADNDpqtlgPIVVHC---- 254

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7504409   1016 fskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1082
Cdd:PHA02746  255 -----------SAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1148-1418 1.95e-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: 1.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1148 LEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGY---FFDYIAAQDPVS 1224
Cdd:cd14609   17 LAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHdprMPAYIATQGPLS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1225 EGTAfDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSgtechfgSERNSVNVTCVSEehH---QDFIIRnlSYSM 1299
Cdd:cd14609   97 HTIA-DFWQMVWENGCTVIVMLTPlvEDGVKQCDRYWPDEGS-------SLYHIYEVNLVSE--HiwcEDFLVR--SFYL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1300 KDNESMpANQEVVQYSYTGWPSDSIvPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQ-K 1378
Cdd:cd14609  165 KNVQTQ-ETRTLTQFHFLSWPAEGI-PSSTRPLLDFRRKV---NKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 7504409  1379 AEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYIS 1418
Cdd:cd14609  240 GVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVN 279
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1172-1417 2.90e-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: 2.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1172 ENLLKNRYEAAVPFDKYRVILPP-TIGHADSSYINASHIKGYF----------FDYIAAQDPVsEGTAFDFWRMIADQNV 1240
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDgDPNEPVSDYINANIIMPEFetkcnnskpkKSYIATQGCL-QNTVNDFWRMVFQENS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1241 TTVVMLSDETDW--SDVEKYWPIDGSGTEchFGSERnsvnVTCVSEEHHQDFIIRNLSYSMKDNESMpaNQEVVQYSYTG 1318
Cdd:cd14605   80 RVIVMTTKEVERgkSKCVKYWPDEYALKE--YGVMR----VRNVKESAAHDYILRELKLSKVGQGNT--ERTVWQYHFRT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1319 WPsDSIVPKSANSLMNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLW--LRQKA-EQRIDVFQTVKGLQSH 1395
Cdd:cd14605  152 WP-DHGVPSDPGGVLDFLEEVHHKQESIMDA-GPVVVHCSAGIGRTGTFIVIDILIdiIREKGvDCDIDVPKTIQMVRSQ 229

                        250       260
                 ....*....|....*....|..
gi 7504409  1396 RPMMFTRFEQYSFCYRALADYI 1417
Cdd:cd14605  230 RSGMVQTEAQYRFIYMAVQHYI 251
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1148-1418 4.16e-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: 4.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1148 LEEEFKKLERNLTTPLSSNFAAKDE-------------NLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF 1214
Cdd:cd14625    9 LAEHTERLKANDNLKLSQEYESIDPgqqftwehsnlevNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1215 D--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPidGSGTECHfgserNSVNVTCVSEEHHQDF 1290
Cdd:cd14625   89 QnaYIATQGPLPE-TFGDFWRMVWEQRSATVVMMTklEEKSRIKCDQYWP--SRGTETY-----GMIQVTLLDTIELATF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1291 IIRnlSYSMKDNESmPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGsqaPIVVHCRNGSSESGIFICI 1370
Cdd:cd14625  161 CVR--TFSLHKNGS-SEKREVRQFQFTAWP-DHGVPEYPTPFLAFLRRVKTCNPPDAG---PIVVHCSAGVGRTGCFIVI 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 7504409  1371 SLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYIS 1418
Cdd:cd14625  234 DAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1171-1413 5.45e-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: 5.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1171 DENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD 1248
Cdd:cd14630    1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPrhYIATQGPMQE-TVKDFWRMIWQENSASVVMVTN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1249 ETDWSDVE--KYWPIDgsgTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSMKDNESMpanQEVVQYSYTGWPsDSIVP 1326
Cdd:cd14630   80 LVEVGRVKcvRYWPDD---TEVY-----GDIKVTLIETEPLAEYVIRTFTVQKKGYHEI---REIRQFHFTSWP-DHGVP 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1327 KSANSLMNLIemvlqRQSSLMG--SQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFE 1404
Cdd:cd14630  148 CYATGLLGFV-----RQVKFLNppDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEE 222


                 ....*....
gi 7504409  1405 QYSFCYRAL 1413
Cdd:cd14630  223 QYVFVHDAI 231
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1177-1411 5.70e-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: 5.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1177 NRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD---YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWS 1253
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEekaYIATQGPLPN-TVADFWRMVWQEKTPIIVMITNLTEAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1254 D-VEKYWPIDgsgtechFGSERNSVNVTCVSEEHHQDFIIRNLSYsmkdnESMPANQEVVQYSYTGWPsDSIVPKSANSL 1332
Cdd:cd14547   80 EkCAQYWPEE-------ENETYGDFEVTVQSVKETDGYTVRKLTL-----KYGGEKRYLKHYWYTSWP-DHKTPEAAQPL 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7504409  1333 MNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1411
Cdd:cd14547  147 LSLVQEVEEARQTEPHR-GPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1173-1413 2.94e-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: 2.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1173 NLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDET 1250
Cdd:cd14626   41 NKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQnaYIATQGPLPE-TLSDFWRMVWEQRTATIVMMTRLE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1251 DWSDV--EKYWPIDGSGTechFGsernSVNVTCVSEEHHQDFIIRNLS-YSMKDNEsmpaNQEVVQYSYTGWPsDSIVPK 1327
Cdd:cd14626  120 EKSRVkcDQYWPIRGTET---YG----MIQVTLLDTVELATYSVRTFAlYKNGSSE----KREVRQFQFMAWP-DHGVPE 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1328 SANSLMNLIEMVLQRQSSLMGsqaPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1407
Cdd:cd14626  188 YPTPILAFLRRVKACNPPDAG---PMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYI 264


                 ....*.
gi 7504409  1408 FCYRAL 1413
Cdd:cd14626  265 FIHEAL 270
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 843-1079 1.20e-30

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: 120.65  E-value: 1.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKL--FIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ-QCAKYWPDE--QITRYGDIIVEP 917
Cdd:cd17658    1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   918 ASFSfHSDYAI--RAFDIAHIgecgpdvipngngvEYANVPivkgqfannsRRILQYHFTNWNDYKAPECSTGLLRFMYR 995
Cdd:cd17658   81 KKLK-HSQHSItlRVLEVQYI--------------ESEEPP----------LSVLHIQYPEWPDHGVPKDTRSVRELLKR 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   996 LRELPQfNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKA--NIFEFVCNLRRQRNLMVQSLE 1073
Cdd:cd17658  136 LYGIPP-SAGPIVVHC---------------SAGIGRTGAYCTIHNTIRRILEGDMSavDLSKTVRKFRSQRIGMVQTQD 199


                 ....*.
gi 7504409  1074 QYVFIY 1079
Cdd:cd17658  200 QYIFCY 205
PHA02738 PHA02738
hypothetical protein; Provisional
 786-1082 6.53e-30

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 121.96  E-value: 6.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    786 DTDFLFAQEYESLPHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKinGDDYSDYINANFIKSWKEKKLFIAAQAPV 865
Cdd:PHA02738   22 DCEEVITREHQKVISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVILPA--ERNRGDYINANYVDGFEYKKKFICGQAPT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    866 DATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDeqitrygdiiVEPASFSFhSDYAIRAFDIAHIgecgpdvip 945
Cdd:PHA02738  100 RQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSD----------VEQGSIRF-GKFKITTTQVETH--------- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    946 ngngVEYANVPIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLR----ELPQ--FNNS-------PVVIHCr 1012
Cdd:PHA02738  160 ----PHYVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkELAQesLQIGhnrlqppPIVVHC- 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1013 ylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKAL 1082
Cdd:PHA02738  235 --------------NAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1203-1413 9.33e-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: 9.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPIDgsgTECHfgserNSVN 1278
Cdd:cd14555    1 YINANYIDGYHRPnhYIATQGPMQE-TVYDFWRMVWQENSASIVMVTNLVEVGRVKcsRYWPDD---TEVY-----GDIK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIRNLSYSMKdneSMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHCR 1358
Cdd:cd14555   72 VTLVETEPLAEYVVRTFALERR---GYHEIREVRQFHFTGWP-DHGVPYHATGLLGFIRRV---KASNPPSAGPIVVHCS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1359 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd14555  145 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1172-1413 1.45e-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: 1.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1172 ENLLKNRYEAAVPFDKYRVILpptigHADSSYINASHIK----GYFFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLS 1247
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFIKmpvgDEEFVYIACQGPLPT-TVADFWQMVWEQKSTVIAMMT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1248 DETDWSDV--EKYWP-IDGSGTEChfgSERnsVNVTCVSEEHHQDFIIRNLsySMKDNESMPAnQEVVQYSYTGWPsDSI 1324
Cdd:cd14597   76 QEVEGGKIkcQRYWPeILGKTTMV---DNR--LQLTLVRMQQLKNFVIRVL--ELEDIQTREV-RHITHLNFTAWP-DHD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1325 VPKSANSLMNLIEMVLQRQSSlmgsqAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFE 1404
Cdd:cd14597  147 TPSQPEQLLTFISYMRHIHKS-----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221


                 ....*....
gi 7504409  1405 QYSFCYRAL 1413
Cdd:cd14597  222 QYIFCYQVI 230
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 843-1085 1.96e-29

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: 117.38  E-value: 1.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIK------SWKekklFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWP----DEQITRYGD 912
Cdd:cd14598    1 YINASHIKvtvggkEWD----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   913 IIVepaSFSFHSD---YAIRAFDIAHigecgpdvipngngveyanvpIVKGQfannSRRILQYHFTNWNDYKAPECSTGL 989
Cdd:cd14598   77 FKI---TTRFRTDsgcYATTGLKIKH---------------------LLTGQ----ERTVWHLQYTDWPEHGCPEDLKGF 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   990 LRFMYRLREL---------PQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLdQCLAEDKANIFEFVCN 1060
Cdd:cd14598  129 LSYLEEIQSVrrhtnstidPKSPNPPVLVHC---------------SAGVGRTGVVILSEIMI-ACLEHNEMLDIPRVLD 192

                        250       260
                 ....*....|....*....|....*.
gi 7504409  1061 -LRRQRNLMVQSLEQYVFIYKALAEW 1085
Cdd:cd14598  193 mLRQQRMMMVQTLSQYTFVYKVLIQF 218
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1203-1411 2.26e-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: 2.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWS--DVEKYWPIDGSGTEChFGsernSVN 1278
Cdd:cd14542    1 YINANFIKGVSGSkaYIATQGPLPN-TVLDFWRMIWEYNVQVIVMACREFEMGkkKCERYWPEEGEEQLQ-FG----PFK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEH-HQDFIIRNLSYSMkDNESmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlmgSQAPIVVHC 1357
Cdd:cd14542   75 ISLEKEKRvGPDFLIRTLKVTF-QKES----RTVYQFHYTAWP-DHGVPSSVDPILDLVRLVRDYQGS---EDVPICVHC 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 7504409  1358 RNGSSESGIFICISLLW---LRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1411
Cdd:cd14542  146 SAGCGRTGTICAIDYVWnllKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1150-1417 2.28e-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: 2.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1150 EEFKKLER-----NLTTPLSSNfaakDENLLKNRYEAAVPFDKYRVILPPTIG----HADssYINASHIKGY--FFDYIA 1218
Cdd:cd17667    3 EDFEEVQRctadmNITAEHSNH----PDNKHKNRYINILAYDHSRVKLRPLPGkdskHSD--YINANYVDGYnkAKAYIA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1219 AQDPVsEGTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSgtechfgSERNSVNVTCVSEEHHQDFIIRNLS 1296
Cdd:cd17667   77 TQGPL-KSTFEDFWRMIWEQNTGIIVMITNlvEKGRRKCDQYWPTENS-------EEYGNIIVTLKSTKIHACYTVRRFS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1297 Y-SMKDNESMPAN-------QEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGsqaPIVVHCRNGSSESGIFI 1368
Cdd:cd17667  149 IrNTKVKKGQKGNpkgrqneRTVIQYHYTQWP-DMGVPEYALPVLTFVRRSSAARTPEMG---PVLVHCSAGVGRTGTYI 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 7504409  1369 CISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1417
Cdd:cd17667  225 VIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 843-1080 2.54e-29

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: 116.71  E-value: 2.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKL-FIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDE--QITRYGDIIVEPAS 919
Cdd:cd14539    1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   920 FSFHSDYAIRAFDIAHIGECGpdvipngngveyanvpivkgqfannSRRILQYHFTNWNDYKAPECSTGLLRFMYRLREL 999
Cdd:cd14539   81 VRTTPTHVERIISIQHKDTRL-------------------------SRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSH 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1000 PQFNNS---PVVIHCrylyfskihqlivnlSAGVGRTGTFISIDSMLDQCLAEDK-ANIFEFVCNLRRQRNLMVQSLEQY 1075
Cdd:cd14539  136 YLQQRSlqtPIVVHC---------------SSGVGRTGAFCLLYAAVQEIEAGNGiPDLPQLVRKMRQQRKYMLQEKEHL 200


                 ....*
gi 7504409  1076 VFIYK 1080
Cdd:cd14539  201 KFCYE 205
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1177-1408 3.22e-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: 3.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1177 NRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSD--ETDW 1252
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCpnEFIATQGPLP-GTVGDFWRMVWETRAKTIVMLTQcfEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1253 SDVEKYWPIDGSGTEChFGsernSVNVTCVSEEHHQDFIIRNLSYSMKDNESMpanqeVVQYSYTGWPSDSiVPKSANSL 1332
Cdd:cd14616   80 IRCHQYWPEDNKPVTV-FG----DIVITKLMEDVQIDWTIRDLKIERHGDYMM-----VRQCNFTSWPEHG-VPESSAPL 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7504409  1333 MNLIEMVlqrQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSF 1408
Cdd:cd14616  149 IHFVKLV---RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1203-1413 4.26e-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: 4.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFFD--YIAAQDPVsEGTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTECHFGSERNSVN 1278
Cdd:cd17668    1 YINANYVDGYNKPkaYIAAQGPL-KSTAEDFWRMIWEHNVEVIVMITNlvEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHqdFIIRNLSYSMKDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGsqaPIVVHCR 1358
Cdd:cd17668   80 VLAYYTVRN--FTLRNTKIKKGSQKGRPSGRVVTQYHYTQWP-DMGVPEYTLPVLTFVRKASYAKRHAVG---PVVVHCS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1359 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd17668  154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1310-1415 5.49e-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: 112.07  E-value: 5.49e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1310 EVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLWLRQKAEQR-IDVFQT 1388
Cdd:smart00012    1 TVKHYHYTGWP-DHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 7504409     1389 VKGLQSHRPMMFTRFEQYSFCYRALAD 1415
Cdd:smart00012   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1310-1415 5.49e-29

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 112.07  E-value: 5.49e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409     1310 EVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLWLRQKAEQR-IDVFQT 1388
Cdd:smart00404    1 TVKHYHYTGWP-DHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 7504409     1389 VKGLQSHRPMMFTRFEQYSFCYRALAD 1415
Cdd:smart00404   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1172-1417 5.82e-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: 5.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1172 ENLLKNRYEAAVPFDKYRVIL----PPTIGhadSSYINASHIKGYFF-------DYIAAQDPVsEGTAFDFWRMIADQNV 1240
Cdd:cd14606   17 ENKSKNRYKNILPFDHSRVILqgrdSNIPG---SDYINANYVKNQLLgpdenakTYIASQGCL-EATVNDFWQMAWQENS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1241 TTVVMLSDEtdwsdVEK-------YWPidGSGTECHFGsernSVNVTCVSEEHHQDFIIRNLSYSMKDNESMPanQEVVQ 1313
Cdd:cd14606   93 RVIVMTTRE-----VEKgrnkcvpYWP--EVGMQRAYG----PYSVTNCGEHDTTEYKLRTLQVSPLDNGELI--REIWH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1314 YSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlMGSQAPIVVHCRNGSSESGIFICISLLW--LRQKA-EQRIDVFQTVK 1390
Cdd:cd14606  160 YQYLSWP-DHGVPSEPGGVLSFLDQINQRQES-LPHAGPIIVHCSAGIGRTGTIIVIDMLMenISTKGlDCDIDIQKTIQ 237

                        250       260
                 ....*....|....*....|....*..
gi 7504409  1391 GLQSHRPMMFTRFEQYSFCYRALADYI 1417
Cdd:cd14606  238 MVRAQRSGMVQTEAQYKFIYVAIAQFI 264
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1165-1416 1.27e-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: 1.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1165 SNFAAKDE-----NLLKNRYEAAVPFDKYRVILP-PTIGHADSSYINASHIKGYFFD---YIAAQDPVSEgTAFDFWRMI 1235
Cdd:cd14612    2 PNFVSPEEldipgHASKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIRGYDGKekaYIATQGPMLN-TVSDFWEMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1236 ADQNVTTVVMLSDETDWSD-VEKYWPiDGSGTECHFGsernsVNVTCVSEehHQDFIIRNLSYSMKDnesmpANQEVVQY 1314
Cdd:cd14612   81 WQEECPIIVMITKLKEKKEkCVHYWP-EKEGTYGRFE-----IRVQDMKE--CDGYTIRDLTIQLEE-----ESRSVKHY 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1315 SYTGWPsDSIVPKSANSLMNLIEMVLQRQSSlMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQS 1394
Cdd:cd14612  148 WFSSWP-DHQTPESAGPLLRLVAEVEESRQT-AASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRL 225

                        250       260
                 ....*....|....*....|..
gi 7504409  1395 HRPMMFTRFEQYSFCYRALADY 1416
Cdd:cd14612  226 DRGGMIQTSEQYQFLHHTLALY 247
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1203-1410 1.27e-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: 1.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKG---YFFDYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSDETDWSD--VEKYWPIDgSGTECHFGSernsV 1277
Cdd:cd14539    1 YINASLIEDltpYCPRFIATQAPLP-GTAADFWLMVYEQQVSVIVMLVSEQENEKqkVHRYWPTE-RGQALVYGA----I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1278 NVTCVSEEHHQDFIIRNLSYSMKDNESMpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVHC 1357
Cdd:cd14539   75 TVSLQSVRTTPTHVERIISIQHKDTRLS---RSVVHLQFTTWP-ELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHC 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1358 RNGSSESGIFiCISLLWLRQKAEQR--IDVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd14539  151 SSGVGRTGAF-CLLYAAVQEIEAGNgiPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1148-1416 1.78e-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: 1.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1148 LEEEFKKLERNLTTPLSSNFAAKdenLLKNRYEAAVPFDKYRVIL-PPTIGHADSSYINASHIKGYFFD---YIAAQDPV 1223
Cdd:cd14613    3 LQAEFFEIPMNFVDPKEYDIPGL---VRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYGGEekvYIATQGPT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1224 SEgTAFDFWRMIADQNVTTVVMLSD-ETDWSDVEKYWPIDGSGTEchfgsernSVNVTCVSEEHHQDFIIRNLSYSMKDN 1302
Cdd:cd14613   80 VN-TVGDFWRMVWQERSPIIVMITNiEEMNEKCTEYWPEEQVTYE--------GIEITVKQVIHADDYRLRLITLKSGGE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1303 EsmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQR 1382
Cdd:cd14613  151 E-----RGLKHYWYTSWP-DQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV 224

                        250       260       270
                 ....*....|....*....|....*....|....
gi 7504409  1383 IDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADY 1416
Cdd:cd14613  225 VDILRTTCQLRLDRGGMIQTCEQYQFVHHVLSLY 258
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1203-1413 2.12e-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: 2.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFF--DYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE-KYWPIDGSGTEChfgserNSVNV 1279
Cdd:cd17669    1 YINASYIMGYYQsnEFIITQHPLLH-TIKDFWRMIWDHNAQLIVMLPDGQNMAEDEfVYWPNKDEPINC------ETFKV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1280 TCVSEEHH----------QDFIIRnlsySMKDNESMpanqEVVQYSYTGWPS-DSIVPKSanslMNLIEMVLQRQSSLMG 1348
Cdd:cd17669   74 TLIAEEHKclsneekliiQDFILE----ATQDDYVL----EVRHFQCPKWPNpDSPISKT----FELISIIKEEAANRDG 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1349 sqaPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd17669  142 ---PMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1203-1417 2.87e-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: 2.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIK----GYFFDYIAAQDPVsEGTAFDFWRMIADQNVTTVVMLSDETDWS--DVEKYWPIDGSGTECHFGSERNS 1276
Cdd:cd14540    1 YINASHITatvgGKQRFYIAAQGPL-QNTVGDFWQMVWEQGVYLVVMVTAEEEGGreKCFRYWPTLGGEHDALTFGEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1277 VNVTCVSEEHhqdFIIRNLSYsmkdnESMPANQE--VVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSLMGSQA--- 1351
Cdd:cd14540   80 STKFSVSSGC---YTTTGLRV-----KHTLSGQSrtVWHLQYTDWP-DHGCPEDVSGFLDFLEEINSVRRHTNQDVAghn 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7504409  1352 ---PIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1417
Cdd:cd14540  151 rnpPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1203-1411 5.70e-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: 5.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGTECHfgserNSVN 1278
Cdd:cd14557    1 YINASYIDGFKepRKYIAAQGPKDE-TVDDFWRMIWEQKSTVIVMVTrcEEGNRNKCAQYWPSMEEGSRAF-----GDVV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIRNLSYSMKDNESmpANQEVVQYSYTGWPsDSIVPKSANSLMNLiemvLQRQSSLMGS-QAPIVVHC 1357
Cdd:cd14557   75 VKINEEKICPDYIIRKLNINNKKEKG--SGREVTHIQFTSWP-DHGVPEDPHLLLKL----RRRVNAFNNFfSGPIVVHC 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 7504409  1358 RNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1411
Cdd:cd14557  148 SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1177-1411 6.26e-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: 6.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1177 NRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFF--DYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSDETDWSD 1254
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFrrEYIATQGPLP-GTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1255 V--EKYWPIDGSGTecHFGsernSVNVTCVSEEHHQDFIIRNlsYSMKDNESMPANQEVVQYSYTGWPsDSIVPKSANSL 1332
Cdd:cd14617   80 VkcDHYWPADQDSL--YYG----DLIVQMLSESVLPEWTIRE--FKICSEEQLDAPRLVRHFHYTVWP-DHGVPETTQSL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7504409  1333 MNLIEMVLQRQSSLMGSqAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1411
Cdd:cd14617  151 IQFVRTVRDYINRTPGS-GPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1173-1418 7.53e-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: 7.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1173 NLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDET 1250
Cdd:cd14624   47 NKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQnaYIATQGALPE-TFGDFWRMIWEQRSATVVMMTKLE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1251 DWSDV--EKYWPidGSGTECHfgserNSVNVTCVSEEHHQDFIIRnlSYSMKDNESmPANQEVVQYSYTGWPsDSIVPKS 1328
Cdd:cd14624  126 ERSRVkcDQYWP--SRGTETY-----GLIQVTLLDTVELATYCVR--TFALYKNGS-SEKREVRQFQFTAWP-DHGVPEH 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1329 ANSLMNLIEMVlqrQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSF 1408
Cdd:cd14624  195 PTPFLAFLRRV---KTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIF 271

                        250
                 ....*....|
gi 7504409  1409 CYRALADYIS 1418
Cdd:cd14624  272 IHDALLEAVT 281
PHA02738 PHA02738
hypothetical protein; Provisional
 1139-1420 3.13e-27

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 114.25  E-value: 3.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1139 MTTSNGETGLEEEFKKLernLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADssYINASHIKGYFFD--Y 1216
Cdd:PHA02738   18 MEKSDCEEVITREHQKV---ISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVILPAERNRGD--YINANYVDGFEYKkkF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1217 IAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETD---------WSDVEkywpidgsGTECHFGSERnsvnVTCVSEEHH 1287
Cdd:PHA02738   93 ICGQAPTRQ-TCYDFYRMLWMEHVQIIVMLCKKKEngrekcfpyWSDVE--------QGSIRFGKFK----ITTTQVETH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1288 QDFIIRNLSYSmkdnESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSSL------MGSQA----PIVVHC 1357
Cdd:PHA02738  160 PHYVKSTLLLT----DGTSATQTVTHFNFTAWP-DHDVPKNTSEFLNFVLEVRQCQKELaqeslqIGHNRlqppPIVVHC 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7504409   1358 RNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYISKT 1420
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 ...
 1203-1415 3.58e-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: 3.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIkgYFFD-----YIAAQDPVSEGTAfDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSgtECHFGSErn 1275
Cdd:cd14546    1 YINASTI--YDHDprnpaYIATQGPLPHTIA-DFWQMIWEQGCVVIVMLTrlQENGVKQCARYWPEEGS--EVYHIYE-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1276 svnVTCVSEehH---QDFIIRNLsY--SMKDNESmpanQEVVQYSYTGWPSDSIvPKSANSLMNLIEMVlqrQSSLMGSQ 1350
Cdd:cd14546   74 ---VHLVSE--HiwcDDYLVRSF-YlkNLQTSET----RTVTQFHFLSWPDEGI-PASAKPLLEFRRKV---NKSYRGRS 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7504409  1351 APIVVHCRNGSSESGIFICISLLWLR-QKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALAD 1415
Cdd:cd14546  140 CPIVVHCSDGAGRTGTYILIDMVLNRmAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1203-1411 6.80e-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: 6.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGY--FFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETDWSDVEKYWPIDGSGTechFGSERNSVN 1278
Cdd:cd14551    1 YINASYIDGYqeKNKFIAAQGPKDE-TVNDFWRMIWEQGSATIVMVTNlkERKEKKCSQYWPDQGCWT---YGNLRVRVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHH-QDFIIRNLSysmkDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHC 1357
Cdd:cd14551   77 DTVVLVDYTtRKFCIQKVN----RGIGEKRVRLVTQFHFTSWP-DFGVPFTPIGMLKFLKKV---KSANPPRAGPIVVHC 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 7504409  1358 RNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYR 1411
Cdd:cd14551  149 SAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1203-1413 8.52e-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: 8.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPiDGSGTechFGSernsVN 1278
Cdd:cd14632    1 YINANYIDGYHRSnhFIATQGPKQE-MVYDFWRMVWQEHCSSIVMITKLVEVGRVKcsKYWP-DDSDT---YGD----IK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIRNLSYsmkDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqrQSSLMGSQAPIVVHCR 1358
Cdd:cd14632   72 ITLLKTETLAEYSVRTFAL---ERRGYSARHEVKQFHFTSWP-EHGVPYHATGLLAFIRRV---KASTPPDAGPVVVHCS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1359 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd14632  145 AGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1176-1410 1.20e-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: 1.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1176 KNRYEAAVPFDKYRVILPPTIGhaDSSYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSD--ETD 1251
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINASLVEVEEAKrsYILTQGPLPN-TSGHFWQMVWEQNSKAVIMLNKlmEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1252 WSDVEKYWPIDGSGTEChfgSERNSVNVTCVSEEHHQDFIIRNLSY-SMKDNESmpanQEVVQYSYTGWPsDSIVPKSAN 1330
Cdd:cd14545   78 QIKCAQYWPQGEGNAMI---FEDTGLKVTLLSEEDKSYYTVRTLELeNLKTQET----REVLHFHYTTWP-DFGVPESPA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1331 SLMNLIEMVlqRQS-SLMGSQAPIVVHCRNGSSESGIFICI--SLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1407
Cdd:cd14545  150 AFLNFLQKV--RESgSLSSDVGPPVVHCSAGIGRSGTFCLVdtCLVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLR 227


                 ...
gi 7504409  1408 FCY 1410
Cdd:cd14545  228 FSY 230
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1203-1410 3.61e-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: 3.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPIDGSgtechfgSERNSVNVT 1280
Cdd:cd14635    1 YINAALMDSYKqpSAFIVTQHPLPN-TVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGV-------HRHGPIQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1281 CVSEEHHQDFIIRNLSYSmkdNESMPAN--QEVVQYSYTGWPSDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVHCR 1358
Cdd:cd14635   73 FVSADLEEDIISRIFRIY---NAARPQDgyRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCL 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 7504409  1359 NGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd14635  150 NGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1203-1410 8.61e-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: 8.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYF--FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPIDGSgteCHFGSernsVNVT 1280
Cdd:cd14636    1 YINAALMDSYRqpAAFIVTQHPLPN-TVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGM---LRYGP----IQVE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1281 CVSEEHHQDFIIRNLSYSmkdNESMPanQE----VVQYSYTGWPSDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVH 1356
Cdd:cd14636   73 CMSCSMDCDVISRIFRIC---NLTRP--QEgylmVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIH 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 7504409  1357 CRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd14636  148 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1203-1422 1.29e-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: 1.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHI------KGYFFDYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWP-IDGSGTECHFgse 1273
Cdd:cd14601    2 YINANYInmeipsSSIINRYIACQGPLP-NTCSDFWQMTWEQGSSMVVMLTTQVERGRVKchQYWPePSGSSSYGGF--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1274 rnsvNVTCVSEEHHQDFIIRNLSYS-MKDNESMPanqeVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQSslmGSQAP 1352
Cdd:cd14601   78 ----QVTCHSEEGNPAYVFREMTLTnLEKNESRP----LTQIQYIAWP-DHGVPDDSSDFLDFVCLVRNKRA---GKDEP 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1353 IVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAladyISKTYR 1422
Cdd:cd14601  146 VVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEA----ILKVYE 211
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1203-1410 3.22e-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: 3.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINA----SHIKGYFFdyIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPidgSGTECHFGSernsVN 1278
Cdd:cd14634    1 YINAalmdSHKQPAAF--IVTQHPLPN-TVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWP---EKTSCCYGP----IQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHHQDFIIRNLSYSmkdNESMPAN--QEVVQYSYTGWPSDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVH 1356
Cdd:cd14634   71 VEFVSADIDEDIISRIFRIC---NMARPQDgyRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVH 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 7504409  1357 CRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd14634  148 CLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVY 201
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1151-1413 3.99e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 108.19  E-value: 3.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1151 EFKKLERN--LTTPLS--SNFAAKDENLLKNRYEAAVPFDKYRVILPP-------------------TIGHADSSYINAS 1207
Cdd:PHA02746   25 EFVLLEHAevMDIPIRgtTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHAN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1208 HIKGY--FFDYIAAQDPVsEGTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPIDGSGTECHFGseRNSVNVTCVSEE 1285
Cdd:PHA02746  105 FVDGFkeANKFICAQGPK-EDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKEEDSELAFG--RFVAKILDIIEE 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1286 hhqdfiirnLSYS----MKDNESMPANQEVVQYSYTGWPSDSIvPKSANSLMNLIEMVLQRQSSLM-------GSQAPIV 1354
Cdd:PHA02746  182 ---------LSFTktrlMITDKISDTSREIHHFWFPDWPDNGI-PTGMAEFLELINKVNEEQAELIkqadndpQTLGPIV 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7504409   1355 VHCRNGSSESGIFICI--SLLWLRQkaEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
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 ...
 1203-1413 5.08e-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: 5.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYFF--DYIAAQDPVSEGTAfDFWRMIADQNVTTVVMLSDETDWSDVEK-YWPIDGSGTECH-FGSERNSVN 1278
Cdd:cd17670    1 YINASYIMGYYRsnEFIITQHPLPHTTK-DFWRMIWDHNAQIIVMLPDNQGLAEDEFvYWPSREESMNCEaFTVTLISKD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1279 VTCVSEEHH---QDFIIRnlsySMKDNESMpanqEVVQYSYTGWPSDSIVPKSANSLMNLIemvlqrQSSLMGSQAPIVV 1355
Cdd:cd17670   80 RLCLSNEEQiiiHDFILE----ATQDDYVL----EVRHFQCPKWPNPDAPISSTFELINVI------KEEALTRDGPTIV 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 7504409  1356 HCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd17670  146 HDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 812-1079 6.55e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 107.01  E-value: 6.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    812 ENAIKNRYNDIRAFDDTRVKLKKINGDDysDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLT 891
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILKIEDGGD--DFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    892 EKNRQQCAKYW-PDEQIT-RYGDIIVEPASFSFHSDYAIRAFDIAhigecgpdvipNGNgveyanvpivkgqfANNSRRI 969
Cdd:PHA02742  129 EDGKEACYPYWmPHERGKaTHGEFKIKTKKIKSFRNYAVTNLCLT-----------DTN--------------TGASLDI 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    970 LQYHFTNWNDYKAPECSTGLLRFMYRLREL-----------PQFNNSPVVIHCrylyfskihqlivnlSAGVGRTGTFIS 1038
Cdd:PHA02742  184 KHFAYEDWPHGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHC---------------SAGLDRAGAFCA 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 7504409   1039 IDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIY 1079
Cdd:PHA02742  249 IDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1176-1410 2.77e-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: 102.69  E-value: 2.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1176 KNRYEAAVPFDKYRVIL-PPTIGHADSSYINASHIKGYFFD---YIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETD 1251
Cdd:cd14611    2 KNRYKTILPNPHSRVCLkPKNSNDSLSTYINANYIRGYGGKekaFIATQGPMIN-TVNDFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1252 WSdvEK---YWPiDGSGTechFGseRNSVNVTCVSEEHHqdFIIRNLSysMKDNESmpaNQEVVQYSYTGWPsDSIVPKS 1328
Cdd:cd14611   81 KN--EKcvlYWP-EKRGI---YG--KVEVLVNSVKECDN--YTIRNLT--LKQGSQ---SRSVKHYWYTSWP-DHKTPDS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1329 ANSLMNLIEMVLQ-RQSSLmgSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYS 1407
Cdd:cd14611  145 AQPLLQLMLDVEEdRLASP--GRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYE 222


                 ...
gi 7504409  1408 FCY 1410
Cdd:cd14611  223 FVH 225
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1157-1417 3.22e-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: 3.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1157 RNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILpptiGHADSSYINASHIK--GYFFDYIAAQDPVSEgTAFDFWRM 1234
Cdd:cd14608    9 RHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKmeEAQRSYILTQGPLPN-TCGHFWEM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1235 IADQNVTTVVMLSDETDWSDVE--KYWPiDGSGTECHFgsERNSVNVTCVSEEHHQDFIIRNLsysMKDNESMPANQEVV 1312
Cdd:cd14608   84 VWEQKSRGVVMLNRVMEKGSLKcaQYWP-QKEEKEMIF--EDTNLKLTLISEDIKSYYTVRQL---ELENLTTQETREIL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1313 QYSYTGWPsDSIVPKSANSLMNLIEMVlqRQS-SLMGSQAPIVVHCRNGSSESGIF----ICIsLLWLRQKAEQRIDVFQ 1387
Cdd:cd14608  158 HFHYTTWP-DFGVPESPASFLNFLFKV--RESgSLSPEHGPVVVHCSAGIGRSGTFcladTCL-LLMDKRKDPSSVDIKK 233

                        250       260       270
                 ....*....|....*....|....*....|...
gi 7504409  1388 TVKGLQSHRPMMFTRFEQYSFCYRAL---ADYI 1417
Cdd:cd14608  234 VLLEMRKFRMGLIQTADQLRFSYLAViegAKFI 266
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1203-1408 3.45e-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: 3.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIK------GYFFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPiDGSGTECHFGSEr 1274
Cdd:cd14541    2 YINANYVNmeipgsGIVNRYIAAQGPLPN-TCADFWQMVWEQKSTLIVMLTTLVERGRVKchQYWP-DLGETMQFGNLQ- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1275 nsvnVTCVSEEHHQDFIIRNLS-YSMKDNESmpanQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqRQSSlMGSQAPI 1353
Cdd:cd14541   79 ----ITCVSEEVTPSFAFREFIlTNTNTGEE----RHITQMQYLAWP-DHGVPDDSSDFLDFVKRV--RQNR-VGMVEPT 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1354 VVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSF 1408
Cdd:cd14541  147 VVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1145-1413 8.81e-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: 8.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1145 ETGLEE-----EFKKLERNlTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILpptigHADSSYINASHIK------GYF 1213
Cdd:cd14600    8 KKGLESgtvliQFEQLYRK-KPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipsaNIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1214 FDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVE--KYWPidGSGTECHFGSERnsvnVTCVSEEHHQDFI 1291
Cdd:cd14600   82 NKYIATQGPLPH-TCAQFWQVVWEQKLSLIVMLTTLTERGRTKchQYWP--DPPDVMEYGGFR----VQCHSEDCTIAYV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1292 IRNLsysMKDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVLQRQsslMGSQaPIVVHCRNGSSESGIFICIS 1371
Cdd:cd14600  155 FREM---LLTNTQTGEERTVTHLQYVAWP-DHGVPDDSSDFLEFVNYVRSKR---VENE-PVLVHCSAGIGRTGVLVTME 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 7504409  1372 LLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd14600  227 TAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAI 268
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1153-1417 9.06e-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: 9.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1153 KKLERNLTTplssnfAAKDENLLKNRYEAAVPFDKYRVILPPTiGHADSSYINASHIK----GYFFDYIAAQDPVSEgTA 1228
Cdd:cd14599   24 KKADGVFTT------ATLPENAERNRIREVVPYEENRVELVPT-KENNTGYINASHIKvtvgGEEWHYIATQGPLPH-TC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1229 FDFWRMIADQNVTTVVMLS--DETDWSDVEKYWPIDGSGtecHFGSERNSVNVTcvseehhQDFIIRNLSYS---MKDNE 1303
Cdd:cd14599   96 HDFWQMVWEQGVNVIAMVTaeEEGGRSKSHRYWPKLGSK---HSSATYGKFKVT-------TKFRTDSGCYAttgLKVKH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1304 SMPANQEVVQY-SYTGWPsDSIVPKSANSLMNLIEMV--LQRQSSLM-----GSQAPIVVHCRNGSSESGIFICISLLWL 1375
Cdd:cd14599  166 LLSGQERTVWHlQYTDWP-DHGCPEEVQGFLSYLEEIqsVRRHTNSMldstkNCNPPIVVHCSAGVGRTGVVILTELMIG 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 7504409  1376 RQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1417
Cdd:cd14599  245 CLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 843-1084 4.08e-23

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: 98.94  E-value: 4.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMvanLTEKNRQQ-CAKYWPDEQITRYGDIIVEPASFS 921
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVM---LNEMDAAQlCMQYWPEKTSCCYGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   922 FHSDYAIRAFDIAHIGEcgpdvipngngveyanvpivkgqfANNSRRILQY-HFTNWNDYK-APECSTGLLRFMYRL--- 996
Cdd:cd14634   78 IDEDIISRIFRICNMAR------------------------PQDGYRIVQHlQYIGWPAYRdTPPSKRSILKVVRRLekw 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   997 RELPQFNNSPVVIHCrylyfskihqlivnLSAGvGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYV 1076
Cdd:cd14634  134 QEQYDGREGRTVVHC--------------LNGG-GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYK 198


                 ....*...
gi 7504409  1077 FIYKALAE 1084
Cdd:cd14634  199 FVYEVALE 206
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1162-1410 1.00e-22

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 100.46  E-value: 1.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1162 PLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADssYINASHIKGYFFD--YIAAQDPVSEgTAFDFWRMIADQN 1239
Cdd:PHA02742   41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDGGDD--FINASYVDGHNAKgrFICTQAPLEE-TALDFWQAIFQDQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1240 VTTVVMLSD--ETDWSDVEKYWPIDGSGTECHfgserNSVNVTCVSEEHHQDFIIRNLSYSmkdNESMPANQEVVQYSYT 1317
Cdd:PHA02742  118 VRVIVMITKimEDGKEACYPYWMPHERGKATH-----GEFKIKTKKIKSFRNYAVTNLCLT---DTNTGASLDIKHFAYE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1318 GWPSDSiVPKSANSLMNLIEMVLQRQSSL--------MGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTV 1389
Cdd:PHA02742  190 DWPHGG-LPRDPNKFLDFVLAVREADLKAdvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIV 268

                         250       260
                  ....*....|....*....|.
gi 7504409   1390 KGLQSHRPMMFTRFEQYSFCY 1410
Cdd:PHA02742  269 RDLRKQRHNCLSLPQQYIFCY 289
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1203-1413 6.69e-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: 95.20  E-value: 6.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHI------KGYFfdYIAAQDPVSeGTAFDFWRMIADQNVTTVVMLSDETDWSDV--EKYWPIDGSGTechfgSER 1274
Cdd:cd14596    1 YINASYItmpvgeEELF--YIATQGPLP-STIDDFWQMVWENRSDVIAMMTREVERGKVkcHRYWPETLQEP-----MEL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1275 NSVNVTCVSEEHHQDFIIRnlSYSMKDNESmPANQEVVQYSYTGWPsDSIVPKSANSLMNLIEMVlqRQSSLMGsqaPIV 1354
Cdd:cd14596   73 ENYQLRLENYQALQYFIIR--IIKLVEKET-GENRLIKHLQFTTWP-DHGTPQSSDQLVKFICYM--RKVHNTG---PIV 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1355 VHCRNGSSESGIFICIS-LLWLRQKAEQrIDVFQTVKGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd14596  144 VHCSAGIGRAGVLICVDvLLSLIEKDLS-FNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1157-1413 1.08e-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: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1157 RNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPptigHADSSYINAS--HIKGYFFDYIAAQDPVSEgTAFDFWRM 1234
Cdd:cd14607    8 RNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASlvVIEEAQRSYILTQGPLPN-TCCHFWLM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1235 IADQNVTTVVMLSD--ETDWSDVEKYWPIDGSgtECHFGSErNSVNVTCVSEEHHQDFIIRNLSYsmkDNESMPANQEVV 1312
Cdd:cd14607   83 VWQQKTKAVVMLNRivEKDSVKCAQYWPTDEE--EVLSFKE-TGFSVKLLSEDVKSYYTVHLLQL---ENINSGETRTIS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1313 QYSYTGWPsDSIVPKSANSLMNLIEMVlqRQS-SLMGSQAPIVVHCRNGSSESGIFICIS--LLWLRQKAEQRIDVFQTV 1389
Cdd:cd14607  157 HFHYTTWP-DFGVPESPASFLNFLFKV--RESgSLSPEHGPAVVHCSAGIGRSGTFSLVDtcLVLMEKKDPDSVDIKQVL 233

                        250       260
                 ....*....|....*....|....
gi 7504409  1390 KGLQSHRPMMFTRFEQYSFCYRAL 1413
Cdd:cd14607  234 LDMRKYRMGLIQTPDQLRFSYMAV 257
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 843-1080 1.13e-19

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: 88.53  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKnrQQCAKYWPDEQitrygdiivEPASFSf 922
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELN--EDEPIYWPTKE---------KPLECE- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 hsdyairAFDIAHIGEcgpDVIPNGNGVEYanvpIVKgQF---ANNSRRIL---QYHFTNWNDYKAPECSTglLRFMYRL 996
Cdd:cd14550   69 -------TFKVTLSGE---DHSCLSNEIRL----IVR-DFileSTQDDYVLevrQFQCPSWPNPCSPIHTV--FELINTV 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   997 RELPQFNNSPVVIHCRYlyfskihqlivnlsaGVGRTGTFISIDSMLDQCLAEDKANIFEFV--CNLRRQRnlMVQSLEQ 1074
Cdd:cd14550  132 QEWAQQRDGPIVVHDRY---------------GGVQAATFCALTTLHQQLEHESSVDVYQVAklYHLMRPG--VFTSKED 194


                 ....*.
gi 7504409  1075 YVFIYK 1080
Cdd:cd14550  195 YQFLYK 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1159-1408 1.41e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 91.22  E-value: 1.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1159 LTTPLSSNFAA--KDENLLKNRYEAAVPFDKYRVILPpTIGHADSSYINASHIKGYFFD--YIAAQDPVSEGTAfDFWRM 1234
Cdd:PHA02747   35 ILKPFDGLIANfeKPENQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWIDGFEDDkkFIATQGPFAETCA-DFWKA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1235 IADQNVTTVVMLSDETDWSDVEK---YWPIdgsgtechfgSERNSVNVtcvseehhQDFIIRNLSYSMK----------D 1301
Cdd:PHA02747  113 VWQEHCSIIVMLTPTKGTNGEEKcyqYWCL----------NEDGNIDM--------EDFRIETLKTSVRakyiltlieiT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1302 NESMPANQEVVQYSYTGWPSDSIVPKSAN--SLMNLIEMVLQRQSSLMGSQ----APIVVHCRNGSSESGIF----ICIS 1371
Cdd:PHA02747  175 DKILKDSRKISHFQCSEWFEDETPSDHPDfiKFIKIIDINRKKSGKLFNPKdallCPIVVHCSDGVGKTGIFcavdICLN 254

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 7504409   1372 LLWLRQKaeqrIDVFQTVKGLQSHRPMMFTRFEQYSF 1408
Cdd:PHA02747  255 QLVKRKA----ICLAKTAEKIREQRHAGIMNFDDYLF 287
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 843-1084 1.81e-19

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: 88.16  E-value: 1.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKnrQQCAKYWPDEQITRYGDIIVEPASFSF 922
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWPEEGMLRYGPIQVECMSCSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFDIAHIG--ECGPDVIPNGNGVEYAN---VPIVKGQFAnnsRRILQyhFTNWNDykapECSTGLLRfmyrlr 997
Cdd:cd14636   79 DCDVISRIFRICNLTrpQEGYLMVQQFQYLGWAShreVPGSKRSFL---KLILQ--VEKWQE----ECDEGEGR------ 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   998 elpqfnnspVVIHCrylyfskihqlivnLSAGvGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVF 1077
Cdd:cd14636  144 ---------TIIHC--------------LNGG-GRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199


                 ....*..
gi 7504409  1078 IYKALAE 1084
Cdd:cd14636  200 CYDVALE 206
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1203-1410 2.51e-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: 2.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIK----GYFFDYIAAQDPVSEgTAFDFWRMIADQNVTTVVMLSDETDWSDVEK---YWPiDGSGTECHFGSern 1275
Cdd:cd17658    1 YINASLVEtpasESLPKFIATQGPLPH-TFEDFWEMVIQQRCPVIIMLTRLVDNYSTAKcadYFP-AEENESREFGR--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1276 sVNVTCVSEEHHQDFI-IRNLSysMKDNESMPANQEVVQYSYTGWPsDSIVPKSANSLMNLiemvLQRQSSLMGSQAPIV 1354
Cdd:cd17658   76 -ISVTNKKLKHSQHSItLRVLE--VQYIESEEPPLSVLHIQYPEWP-DHGVPKDTRSVREL----LKRLYGIPPSAGPIV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7504409  1355 VHCRNGSSESGIFICISllwlrqKAEQRI--------DVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd17658  148 VHCSAGIGRTGAYCTIH------NTIRRIlegdmsavDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1203-1410 3.15e-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: 3.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIKGYF--FDYIAAQDPVsEGTAFDFWRMIADQNVTTVVMLS----DETDWSDVEkYWPIDGSgteCHFGSerns 1276
Cdd:cd14637    1 YINAALTDSYTrsAAFIVTLHPL-QNTTTDFWRLVYDYGCTSVVMLNqlnqSNSAWPCLQ-YWPEPGL---QQYGP---- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1277 VNVTCVSEEHHQDFIIRnlSYSMKDNESMPANQEVV-QYSYTGWPSDSIVPKSANSLMNLIEMVLQRQSSlmGSQAPIVV 1355
Cdd:cd14637   72 MEVEFVSGSADEDIVTR--LFRVQNITRLQEGHLMVrHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRE--SGEGRTVV 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7504409  1356 HCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCY 1410
Cdd:cd14637  148 HCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCY 202
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 843-1084 7.31e-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: 86.50  E-value: 7.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQ-QCAKYWPDEQITRYGDIIVEPASFS 921
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   922 FHSDYAIRAFDIAHIGEcgpdvipngngveyanvpIVKGQFAnnsrrILQYHFTNWNDYK-APECSTGllrFMYRLRELP 1000
Cdd:cd14637   81 ADEDIVTRLFRVQNITR------------------LQEGHLM-----VRHFQFLRWSAYRdTPDSKKA---FLHLLASVE 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1001 QFNNSpvvihcrylyfSKIHQLIVNLSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYK 1080
Cdd:cd14637  135 KWQRE-----------SGEGRTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYE 203


                 ....
gi 7504409  1081 ALAE 1084
Cdd:cd14637  204 IALE 207
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 843-1084 1.00e-18

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: 86.28  E-value: 1.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKnrQQCAKYWPDEQITRYGDIIVEPASFSF 922
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPENGVHRHGPIQVEFVSADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFDIAHigecgpdvipngngveyANVPivkgqfANNSRRILQYHFTNWNDYKAPECST----GLLRFMYRLRE 998
Cdd:cd14635   79 EEDIISRIFRIYN-----------------AARP------QDGYRMVQQFQFLGWPMYRDTPVSKrsflKLIRQVDKWQE 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   999 LPQFNNSPVVIHCrylyfskihqlivnLSAGvGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFI 1078
Cdd:cd14635  136 EYNGGEGRTVVHC--------------LNGG-GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFC 200


                 ....*.
gi 7504409  1079 YKALAE 1084
Cdd:cd14635  201 YEVALE 206
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1203-1417 2.88e-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: 2.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1203 YINASHIK----GYFFDYIAAQDPVsEGTAFDFWRMIADQNVTTVVMLSDETDwSDVEK---YWPidgsgtecHFGSERN 1275
Cdd:cd14598    1 YINASHIKvtvgGKEWDYIATQGPL-QNTCQDFWQMVWEQGVAIIAMVTAEEE-GGREKsfrYWP--------RLGSRHN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1276 SVN-----VTCvseehhqDFIIRNLSYS---MKDNESMPANQEVVQY-SYTGWPsDSIVP---KSANSLMNLIEMVLQRQ 1343
Cdd:cd14598   71 TVTygrfkITT-------RFRTDSGCYAttgLKIKHLLTGQERTVWHlQYTDWP-EHGCPedlKGFLSYLEEIQSVRRHT 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7504409  1344 SSLM---GSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYI 1417
Cdd:cd14598  143 NSTIdpkSPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 843-1082 2.30e-13

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: 70.41  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAkYWPDEQitrygdiivEPASfsf 922
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKD---------EPIN--- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 hsdyaIRAFDIAHIGE---CgpdvIPNGNGVEYANVpIVKGQFANNSRRILQYHFTNWNDYKAPECSTglLRFMYRLREL 999
Cdd:cd17669   68 -----CETFKVTLIAEehkC----LSNEEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEE 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409  1000 PQFNNSPVVIHCRYlyfskihqlivnlsAGVgRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIY 1079
Cdd:cd17669  136 AANRDGPMIVHDEH--------------GGV-TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLY 200


                 ...
gi 7504409  1080 KAL 1082
Cdd:cd17669  201 KAI 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1169-1421 6.24e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 71.15  E-value: 6.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1169 AKDENLlknryeaAVPFDKY---RVILpptigHADSSYINASHIKGYFFD--YIAAQDpVSEGTAFDFWRMIADQNVTTV 1243
Cdd:PHA02740   53 AKDENL-------ALHITRLlhrRIKL-----FNDEKVLDARFVDGYDFEqkFICIIN-LCEDACDKFLQALSDNKVQII 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1244 VMLSDETDWSDVEKYWpidGSGTECHFGSERNSVNVTCVSEEHHqdFIIRNLSYSMKDNESmpanQEVVQYSYTGWPSD- 1322
Cdd:PHA02740  120 VLISRHADKKCFNQFW---SLKEGCVITSDKFQIETLEIIIKPH--FNLTLLSLTDKFGQA----QKISHFQYTAWPADg 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   1323 -SIVPKS-ANSLMNLIEMVLQ-RQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMM 1399
Cdd:PHA02740  191 fSHDPDAfIDFFCNIDDLCADlEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGC 270

                         250       260
                  ....*....|....*....|..
gi 7504409   1400 FTRFEQYSFCYRALADYISKTY 1421
Cdd:PHA02740  271 MNCLDDYVFCYHLIAAYLKEKF 292
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 843-1082 6.88e-11

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: 63.16  E-value: 6.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVAN---LTEKNrqqcAKYWPDEQitrygdiivEPAS 919
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAEDE----FVYWPSRE---------ESMN 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   920 fsfhsdyaIRAFDIAHIGEcgpDVIPNGNGVEyanvpIVKGQF---ANNSRRILQY-HFT--NWNDYKAPECSTglLRFM 993
Cdd:cd17670   68 --------CEAFTVTLISK---DRLCLSNEEQ-----IIIHDFileATQDDYVLEVrHFQcpKWPNPDAPISST--FELI 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   994 YRLRELPQFNNSPVVIHCRYlyfskihqlivnlsaGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLE 1073
Cdd:cd17670  130 NVIKEEALTRDGPTIVHDEF---------------GAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIE 194


                 ....*....
gi 7504409  1074 QYVFIYKAL 1082
Cdd:cd17670  195 QYQFLYKAM 203
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 844-1076 1.27e-09

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: 60.11  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   844 INANFIKsWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYW-PDEQitrYGDIIVEpaSFSF 922
Cdd:cd14559   18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFrQSGT---YGSVTVK--SKKT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   923 HSDYAIRAFDIAHIgecgpDVIPNGNGVEYaNVPIvkgqfannsrrilqYHFTNWNDYKApeCSTGLLRFMYRL------ 996
Cdd:cd14559   92 GKDELVDGLKADMY-----NLKITDGNKTI-TIPV--------------VHVTNWPDHTA--ISSEGLKELADLvnksae 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   997 ---RELPQFNNSPV--------VIHCRylyfskihqlivnlsAGVGRTGTFISIDSMLDQclaEDKANIFEFVCNLRRQR 1065
Cdd:cd14559  150 ekrNFYKSKGSSAIndknkllpVIHCR---------------AGVGRTGQLAAAMELNKS---PNNLSVEDIVSDMRTSR 211

                        250
                 ....*....|..
gi 7504409  1066 N-LMVQSLEQYV 1076
Cdd:cd14559  212 NgKMVQKDEQLD 223
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 366-486 1.25e-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: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   366 PFPPkeEDVRVLNSGSAlSCEVEWKSPAEPNGRITKYFVSVRgamrksdgsltPDDLPAAVEVDKRCANwdgdentskhn 445
Cdd:cd00063    1 PSPP--TNLRVTDVTST-SVTLSWTPPEDDGGPITGYVVEYR-----------EKGSGDWKEVEVTPGS----------- 55

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 7504409   446 ginpidfaneFYSCKFGPLKPNRNYTVTVWAENSAGRSLPA 486
Cdd:cd00063   56 ----------ETSYTLTGLKPGTEYEFRVRAVNGGGESPPS 86
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 989-1080 6.39e-04

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: 40.80  E-value: 6.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409   989 LLRFMYRLRELPQfNNSPVVIHCRylyfskihqlivnlsAGVGRTGTFISIDsmldqCLAEDKANIFEFVCNLRRQR-NL 1067
Cdd:cd14494   42 VDRFLEVLDQAEK-PGEPVLVHCK---------------AGVGRTGTLVACY-----LVLLGGMSAEEAVRIVRLIRpGG 100

                         90
                 ....*....|...
gi 7504409  1068 MVQSLEQYVFIYK 1080
Cdd:cd14494  101 IPQTIEQLDFLIK 113
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 776-902 2.72e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 41.49  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    776 LPTEYVVRHRDTDFL-----------FAQEYESLPHFQLD--TVASNRKENAIKNRYNdirAFDDTRVKLKKINGDDYSD 842
Cdd:PHA02740    1 MAIEDAVDINGMDFInfinkpdllscIIKEYRAIVPEHEDeaNKACAQAENKAKDENL---ALHITRLLHRRIKLFNDEK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7504409    843 YINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQcaKYW 902
Cdd:PHA02740   78 VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFN--QFW 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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