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Conserved domains on  [gi|124378179|ref|YP_001029397|]
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GfV-B62-ORF1 [Ichnoviriform fumiferanae]

Protein Classification

tyrosine-protein phosphatase( domain architecture ID 10040015)

tyrosine-protein phosphatase catalyzes the dephosphorylation of O-phosphotyrosine groups in phosphoproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 102-293 1.10e-44

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: 151.28  E-value: 1.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFR-GNYIVSTKKIY 177
Cdd:cd00047    2 INASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCeryWPEEGGKPLEyGDITVTLVSEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 178 EKNYYTQYFFEIVSDATSsdRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAkmlenfFEASLVAPVIVHGNAEVGRA 257
Cdd:cd00047   82 ELSDYTIRTLELSPKGCS--ESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK------EARKPNGPIVVHCSAGVGRT 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 124378179 258 ETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSV 293
Cdd:cd00047  154 GTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMV 189
 
Name Accession Description Interval E-value
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 102-293 1.10e-44

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: 151.28  E-value: 1.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFR-GNYIVSTKKIY 177
Cdd:cd00047    2 INASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCeryWPEEGGKPLEyGDITVTLVSEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 178 EKNYYTQYFFEIVSDATSsdRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAkmlenfFEASLVAPVIVHGNAEVGRA 257
Cdd:cd00047   82 ELSDYTIRTLELSPKGCS--ESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK------EARKPNGPIVVHCSAGVGRT 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 124378179 258 ETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSV 293
Cdd:cd00047  154 GTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMV 189
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
74-298 8.09e-41

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 142.00  E-value: 8.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179   74 RYYEIPCSSQLRVTsandLPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEI 153
Cdd:pfam00102   6 RYKDVLPYDHTRVK----LTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  154 DPC---WPTTLGEQFR-GNYIVSTK--KIYEKNYYTQYFfeIVSDATsSDRPRKVNLYHYTQWPIFGNSANENKLIAFIL 227
Cdd:pfam00102  82 EKCaqyWPEEEGESLEyGDFTVTLKkeKEDEKDYTVRTL--EVSNGG-SEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124378179  228 AVNAKMLENFfeaslVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:pfam00102 159 KVRKSSLDGR-----SGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQ 224
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
74-298 3.01e-40

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 141.26  E-value: 3.01e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179    74 RYYEIPCSSQLRVTSAndlPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEI 153
Cdd:smart00194  32 RYKDVLPYDHTRVKLK---PPPGEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGR 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179   154 DPC---WPTTLGEQFR-GNYIVSTKKIYEKNYYTQYFFEIVSDATSSdrPRKVNLYHYTQWPIFGNSANENKLIAFILAV 229
Cdd:smart00194 109 EKCaqyWPDEEGEPLTyGDITVTLKSVEKVDDYTIRTLEVTNTGCSE--TRTVTHYHYTNWPDHGVPESPESILDLIRAV 186

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124378179   230 NAKMlenffeASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:smart00194 187 RKSQ------STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQ 249
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 69-302 4.48e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 123.96  E-value: 4.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  69 DEQRTRYYEIPCSSQLRVTsandLPTTS-SNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILT- 146
Cdd:PHA02747  51 NQPKNRYWDIPCWDHNRVI----LDSGGgSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTp 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 147 TEHQNEIDPCW----PTTLGEQFRGNYIVSTKKIYEKNYYTQYFFEIVSdaTSSDRPRKVNLYHYTQWPIFGNSANENKL 222
Cdd:PHA02747 127 TKGTNGEEKCYqywcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFEDETPSDHPDF 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 223 IAFILAVN---AKMLENFF-EASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:PHA02747 205 IKFIKIIDinrKKSGKLFNpKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDD 284


                 ....
gi 124378179 299 NGLI 302
Cdd:PHA02747 285 YLFI 288
 
Name Accession Description Interval E-value
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 102-293 1.10e-44

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: 151.28  E-value: 1.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFR-GNYIVSTKKIY 177
Cdd:cd00047    2 INASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCeryWPEEGGKPLEyGDITVTLVSEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 178 EKNYYTQYFFEIVSDATSsdRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAkmlenfFEASLVAPVIVHGNAEVGRA 257
Cdd:cd00047   82 ELSDYTIRTLELSPKGCS--ESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK------EARKPNGPIVVHCSAGVGRT 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 124378179 258 ETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSV 293
Cdd:cd00047  154 GTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMV 189
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
74-298 8.09e-41

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 142.00  E-value: 8.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179   74 RYYEIPCSSQLRVTsandLPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEI 153
Cdd:pfam00102   6 RYKDVLPYDHTRVK----LTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  154 DPC---WPTTLGEQFR-GNYIVSTK--KIYEKNYYTQYFfeIVSDATsSDRPRKVNLYHYTQWPIFGNSANENKLIAFIL 227
Cdd:pfam00102  82 EKCaqyWPEEEGESLEyGDFTVTLKkeKEDEKDYTVRTL--EVSNGG-SEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124378179  228 AVNAKMLENFfeaslVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:pfam00102 159 KVRKSSLDGR-----SGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQ 224
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
74-298 3.01e-40

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 141.26  E-value: 3.01e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179    74 RYYEIPCSSQLRVTSAndlPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEI 153
Cdd:smart00194  32 RYKDVLPYDHTRVKLK---PPPGEGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGR 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179   154 DPC---WPTTLGEQFR-GNYIVSTKKIYEKNYYTQYFFEIVSDATSSdrPRKVNLYHYTQWPIFGNSANENKLIAFILAV 229
Cdd:smart00194 109 EKCaqyWPDEEGEPLTyGDITVTLKSVEKVDDYTIRTLEVTNTGCSE--TRTVTHYHYTNWPDHGVPESPESILDLIRAV 186

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124378179   230 NAKMlenffeASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:smart00194 187 RKSQ------STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQ 249
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 59-298 6.14e-36

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: 130.56  E-value: 6.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  59 PKSYTFDLS---ADEQRTRYYEIPCSSQLRVTSAndLPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLW 135
Cdd:cd14543   16 PPAGTFLCSlapANQEKNRYGDVLCLDQSRVKLP--KRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVW 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 136 KNESQVVVILTTEHQNEIDPC---WPTTLGEQFR-GNYIVSTKKIYEKNYYTQYFFEIvsDATSSDRPRKVNLYHYTQWP 211
Cdd:cd14543   94 EQKVLVIVMTTRVVERGRVKCgqyWPLEEGSSLRyGDLTVTNLSVENKEHYKKTTLEI--HNTETDESRQVTHFQFTSWP 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 212 IFGNSANENKLIAFI--------LAVNAkMLENFFEASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVK 283
Cdd:cd14543  172 DFGVPSSAAALLDFLgevrqqqaLAVKA-MGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVR 250

                        250
                 ....*....|....*
gi 124378179 284 HIRSQRYGSVITANQ 298
Cdd:cd14543  251 RMRTQRAFSIQTPDQ 265
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 69-302 4.48e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 123.96  E-value: 4.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  69 DEQRTRYYEIPCSSQLRVTsandLPTTS-SNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILT- 146
Cdd:PHA02747  51 NQPKNRYWDIPCWDHNRVI----LDSGGgSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTp 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 147 TEHQNEIDPCW----PTTLGEQFRGNYIVSTKKIYEKNYYTQYFFEIVSdaTSSDRPRKVNLYHYTQWPIFGNSANENKL 222
Cdd:PHA02747 127 TKGTNGEEKCYqywcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFEDETPSDHPDF 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 223 IAFILAVN---AKMLENFF-EASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:PHA02747 205 IKFIKIIDinrKKSGKLFNpKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDD 284


                 ....
gi 124378179 299 NGLI 302
Cdd:PHA02747 285 YLFI 288
PHA02738 PHA02738
hypothetical protein; Provisional
 24-307 1.97e-31

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 119.64  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  24 YPEDCEILEVKNQERVLSTPChlelyaartsstdspkSYTFDLS-ADEQRTRYYEIPCSSQLRVTsandLPTTSSNSNPI 102
Cdd:PHA02738  19 EKSDCEEVITREHQKVISEKV----------------DGTFNAEkKNRKLNRYLDAVCFDHSRVI----LPAERNRGDYI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 103 NGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFR-GNYIVSTKKIYE 178
Cdd:PHA02738  79 NANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCfpyWSDVEQGSIRfGKFKITTTQVET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 179 KNYYTQYFFEiVSDATSSdrPRKVNLYHYTQWPIFGNSANENKLIAFILAVN-------AKMLENFFEASLVAPVIVHGN 251
Cdd:PHA02738 159 HPHYVKSTLL-LTDGTSA--TQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaQESLQIGHNRLQPPPIVVHCN 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124378179 252 AEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQNGLIIRILK 307
Cdd:PHA02738 236 AGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVK 291
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 71-307 1.40e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 114.74  E-value: 1.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  71 QRTRYYEIPCSSQLRVT-----------------SANDLPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHM 133
Cdd:PHA02746  53 KKNRFHDIPCWDHSRVVinaheslkmfdvgdsdgKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 134 LWKNESQVVVILtTEHQNEIDPC---WPTTLG-EQFRGNYIVSTKKIYEKNYYTQYFFEIVSdaTSSDRPRKVNLYHYTQ 209
Cdd:PHA02746 133 ISEHESQVIVSL-TDIDDDDEKCfelWTKEEDsELAFGRFVAKILDIIEELSFTKTRLMITD--KISDTSREIHHFWFPD 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 210 WPIFGNSANENKLIAFILAVNAKMLENFFEA----SLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHI 285
Cdd:PHA02746 210 WPDNGIPTGMAEFLELINKVNEEQAELIKQAdndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKI 289

                        250       260
                 ....*....|....*....|..
gi 124378179 286 RSQRYGSVITANQNGLIIRILK 307
Cdd:PHA02746 290 RKQRHSSVFLPEQYAFCYKALK 311
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 71-290 2.26e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 113.94  E-value: 2.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  71 QRTRYYEIPCSSQLRVTsandLPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQ 150
Cdd:PHA02742  54 KKCRYPDAPCFDRNRVI----LKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 151 NEIDPCWPTTL----GEQFRGNYIVSTKKIYEKNYYTQYFFEIVSDATSSDrpRKVNLYHYTQWPIFGNSANENKLIAFI 226
Cdd:PHA02742 130 DGKEACYPYWMpherGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGAS--LDIKHFAYEDWPHGGLPRDPNKFLDFV 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124378179 227 LAVNAKMLENFFEAS-----LVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRY 290
Cdd:PHA02742 208 LAVREADLKADVDIKgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRH 276
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 102-298 6.05e-29

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: 110.13  E-value: 6.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFrGNYIVSTKKIYE 178
Cdd:cd14549    2 INANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCdqyWPKEGTETY-GNIQVTLLSTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 179 KNYYTQYFFEI----VSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKmleNFFEAslvAPVIVHGNAEV 254
Cdd:cd14549   81 LATYTVRTFSLknlkLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAA---NPPGA---GPIVVHCSAGV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 124378179 255 GRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14549  155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQ 198
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 102-298 1.47e-28

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: 109.30  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTT---EHQNEIDPCWPTTLGEQFrGNYIVSTKKIYE 178
Cdd:cd17668    2 INANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNlveKGRRKCDQYWPADGSEEY-GNFLVTQKSVQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 179 KNYYTQYFFEI----VSDATSSDRP--RKVNLYHYTQWPIFGNSANENKLIAFILAVNAKmlenffEASLVAPVIVHGNA 252
Cdd:cd17668   81 LAYYTVRNFTLrntkIKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYA------KRHAVGPVVVHCSA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 124378179 253 EVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd17668  155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 200
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 99-298 1.91e-28

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: 109.92  E-value: 1.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  99 SNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFrGNYIVSTKK 175
Cdd:cd14554   34 SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGREKChqyWPAERSARY-QYFVVDPMA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 176 IYEKNYYTQYFFEiVSDAtSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNaKMLENFFEAslvAPVIVHGNAEVG 255
Cdd:cd14554  113 EYNMPQYILREFK-VTDA-RDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVH-KTKEQFGQE---GPITVHCSAGVG 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 124378179 256 RAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14554  187 RTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQ 229
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 69-310 4.57e-27

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: 107.04  E-value: 4.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  69 DEQRTRYYEIPCSSQLRVTSANDLPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTT- 147
Cdd:cd17667   27 NKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNl 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 148 --EHQNEIDPCWPTTLGEQFrGNYIVSTKKIYEKNYYTQYFFEIVS---------DATSSDRPRKVNLYHYTQWPIFGNS 216
Cdd:cd17667  107 veKGRRKCDQYWPTENSEEY-GNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgNPKGRQNERTVIQYHYTQWPDMGVP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 217 ANENKLIAFILAVNAKMLENffeaslVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITA 296
Cdd:cd17667  186 EYALPVLTFVRRSSAARTPE------MGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 259

                        250
                 ....*....|....
gi 124378179 297 NQNGLIIRILKELV 310
Cdd:cd17667  260 EQYIFIHDALLEAI 273
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 102-298 8.87e-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: 104.22  E-value: 8.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTlGEQFRGNYIVSTKKIYE 178
Cdd:cd14551    2 INASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCsqyWPDQ-GCWTYGNLRVRVEDTVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 179 KNYYTQYFFEI--VSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLENffeaslVAPVIVHGNAEVGR 256
Cdd:cd14551   81 LVDYTTRKFCIqkVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPR------AGPIVVHCSAGVGR 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 124378179 257 AETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14551  155 TGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQ 196
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 99-308 9.31e-27

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: 105.02  E-value: 9.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  99 SNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTlGEQFRGNYIVSTKK 175
Cdd:cd14620   23 SDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCyqyWPDQ-GCWTYGNIRVAVED 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 176 IYEKNYYTQYFFEIVSDATSSDR-PRKVNLYHYTQWPIFGNSANENKLIAFILAVNAkmlenfFEASLVAPVIVHGNAEV 254
Cdd:cd14620  102 CVVLVDYTIRKFCIQPQLPDGCKaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS------VNPVHAGPIVVHCSAGV 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124378179 255 GRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQNGLIIRILKE 308
Cdd:cd14620  176 GRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 102-298 1.77e-25

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: 100.81  E-value: 1.77e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTlGEQFRGNYIVSTKKIYE 178
Cdd:cd14552    2 INASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCaqyWPED-GSVSSGDITVELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 179 KNYYTQYFFEIVSdaTSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMlenffEASLVAPVIVHGNAEVGRAE 258
Cdd:cd14552   81 YEDYTLRDFLVTK--GKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQ-----QQSGNHPITVHCSAGAGRTG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 124378179 259 TFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14552  154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQ 193
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 98-308 2.30e-24

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: 98.58  E-value: 2.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  98 NSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTlGEQFRGNYIVSTK 174
Cdd:cd14623   23 NTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCaqyWPSD-GSVSYGDITIELK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 175 KIYEKNYYTqyFFEIVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMlenffEASLVAPVIVHGNAEV 254
Cdd:cd14623  102 KEEECESYT--VRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ-----QQSGNHPITVHCSAGA 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124378179 255 GRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQNGLIIRILKE 308
Cdd:cd14623  175 GRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 69-308 1.12e-23

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: 98.17  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  69 DEQRTRYYEI-PCS-SQLRVTSANDLPttssNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILT 146
Cdd:cd14621   52 NKEKNRYVNIlPYDhSRVHLTPVEGVP----DSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 147 TEHQNEIDPC---WPTTlGEQFRGNYIVSTKKIYEKNYYT--QYFFEIVSDATSSDRPRKVNLYHYTQWPIFGNSANENK 221
Cdd:cd14621  128 NLKERKECKCaqyWPDQ-GCWTYGNIRVSVEDVTVLVDYTvrKFCIQQVGDVTNKKPQRLITQFHFTSWPDFGVPFTPIG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 222 LIAFILAVNAkmlenfFEASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQNGL 301
Cdd:cd14621  207 MLKFLKKVKN------CNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVF 280


                 ....*..
gi 124378179 302 IIRILKE 308
Cdd:cd14621  281 IYQALLE 287
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 102-308 1.98e-22

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: 92.76  E-value: 1.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTlGEQFRGNYIVSTKKiyE 178
Cdd:cd14622    3 INASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCvqyWPSE-GSVTHGEITIEIKN--D 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 179 KNYYTQYFFEIVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMlenffEASLVAPVIVHGNAEVGRAE 258
Cdd:cd14622   80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQ-----QQTGNHPIVVHCSAGAGRTG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 124378179 259 TFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQNGLIIRILKE 308
Cdd:cd14622  155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 74-298 3.65e-22

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: 92.46  E-value: 3.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  74 RYYEIPCSSQLRVTsandLP--TTSSNSNPINGYYVDGFRMKRK-FIIIEAPSNESMDDFYHMLWKNESQVVVILT--TE 148
Cdd:cd14547    2 RYKTILPNEHSRVC----LPsvDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITnlTE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 149 HQNEIDPCWPTTLGEQFrGNYIVSTKKIYEKNYYTQYFFEIVSDATSsdrpRKVNLYHYTQWPIFGNSANENKLIAFILA 228
Cdd:cd14547   78 AKEKCAQYWPEEENETY-GDFEVTVQSVKETDGYTVRKLTLKYGGEK----RYLKHYWYTSWPDHKTPEAAQPLLSLVQE 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 229 VNakmlENFFEASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14547  153 VE----EARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQ 218
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 102-289 4.07e-22

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: 91.81  E-value: 4.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTlgEQFRGNYIVSTKKIYE 178
Cdd:cd14557    2 INASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCaqyWPSM--EEGSRAFGDVVVKINE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 179 KNYYTQYFFEIVSDATSSDR--PRKVNLYHYTQWPIFGNSANENKLIAFILAVNAkmLENFFEaslvAPVIVHGNAEVGR 256
Cdd:cd14557   80 EKICPDYIIRKLNINNKKEKgsGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA--FNNFFS----GPIVVHCSAGVGR 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 124378179 257 AETFCAIDICFEQWFTTRRLNVLNTVKHIRSQR 289
Cdd:cd14557  154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQR 186
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 99-298 5.49e-22

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: 93.64  E-value: 5.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  99 SNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFRgNYIVSTKK 175
Cdd:cd14627   81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKChqyWPAERSARYQ-YFVVDPMA 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 176 IYEKNYYTQYFFEiVSDATSSdRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNaKMLENFFEAslvAPVIVHGNAEVG 255
Cdd:cd14627  160 EYNMPQYILREFK-VTDARDG-QSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVH-KTKEQFGQD---GPISVHCSAGVG 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 124378179 256 RAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14627  234 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDE 276
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 99-304 7.50e-22

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: 93.25  E-value: 7.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  99 SNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFRgNYIVSTKK 175
Cdd:cd14629   81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKChqyWPAERSARYQ-YFVVDPMA 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 176 IYEKNYYTQYFFEiVSDATSSdRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNaKMLENFFEAslvAPVIVHGNAEVG 255
Cdd:cd14629  160 EYNMPQYILREFK-VTDARDG-QSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVH-KTKEQFGQD---GPITVHCSAGVG 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 124378179 256 RAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQNGLIIR 304
Cdd:cd14629  234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYR 282
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 102-298 1.12e-21

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: 90.77  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVD-GFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFRGNYIVSTKKIY 177
Cdd:cd18533    2 INASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCdqyWPSGEYEGEYGDLTVELVSEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 178 E--KNYYTQYFFEIVSDATSsdrPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMlenfFEASLVAPVIVHGNAEVG 255
Cdd:cd18533   82 EndDGGFIVREFELSKEDGK---VKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELN----DSASLDPPIIVHCSAGVG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 124378179 256 RAETFCAIDI---CFEQWFTTRRLN------VLNTVKHIRSQRYGSVITANQ 298
Cdd:cd18533  155 RTGTFIALDSlldELKRGLSDSQDLedsedpVYEIVNQLRKQRMSMVQTLRQ 206
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 99-298 1.64e-21

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: 92.49  E-value: 1.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  99 SNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFRgNYIVSTKK 175
Cdd:cd14628   80 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKChqyWPAERSARYQ-YFVVDPMA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 176 IYEKNYYTQYFFEiVSDATSSdRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNaKMLENFFEAslvAPVIVHGNAEVG 255
Cdd:cd14628  159 EYNMPQYILREFK-VTDARDG-QSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVH-KTKEQFGQD---GPISVHCSAGVG 232

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 124378179 256 RAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14628  233 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQ 275
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 99-298 1.92e-21

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: 90.92  E-value: 1.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  99 SNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTT-EHQNEI--DPCWPTTLGEQFrGNYIVSTKK 175
Cdd:cd14553   31 SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKlEERSRVkcDQYWPTRGTETY-GLIQVTLLD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 176 IYEKNYYTQYFFEIVSDATSSdrPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAkmlENFFEAslvAPVIVHGNAEVG 255
Cdd:cd14553  110 TVELATYTVRTFALHKNGSSE--KREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKA---CNPPDA---GPIVVHCSAGVG 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 124378179 256 RAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14553  182 RTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQ 224
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 49-308 7.96e-21

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: 90.09  E-value: 7.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  49 YAARTSSTDSPKSYTFD---LSADEQRTRYYEIPCSSQLRV--TSANDLPttssNSNPINGYYVDGFRMKRKFIIIEAPS 123
Cdd:cd14626   18 FSQEYESIDPGQQFTWEnsnLEVNKPKNRYANVIAYDHSRVilTSVDGVP----GSDYINANYIDGYRKQNAYIATQGPL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 124 NESMDDFYHMLWKNESQVVVILTT-EHQNEI--DPCWPTTlGEQFRGNYIVSTKKIYEKNYYTQYFFEIVSDATSSDrpR 200
Cdd:cd14626   94 PETLSDFWRMVWEQRTATIVMMTRlEEKSRVkcDQYWPIR-GTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEK--R 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 201 KVNLYHYTQWPIFGNSANENKLIAFILAVNAKmleNFFEAslvAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLN 280
Cdd:cd14626  171 EVRQFQFMAWPDHGVPEYPTPILAFLRRVKAC---NPPDA---GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYG 244

                        250       260
                 ....*....|....*....|....*...
gi 124378179 281 TVKHIRSQRYGSVITANQNGLIIRILKE 308
Cdd:cd14626  245 HVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 82-298 3.49e-20

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: 87.02  E-value: 3.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  82 SQLRVTSANDLPTtssnSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WP 158
Cdd:cd14548   11 SRVKLIPINEEEG----SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCdhyWP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 159 TTLGEQFRGNYIVS-TKKIYEKNYYTQYFfeivsDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLENF 237
Cdd:cd14548   87 FDQDPVYYGDITVTmLSESVLPDWTIREF-----KLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQEK 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124378179 238 feaslvAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14548  162 ------GPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQ 216
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 102-298 2.61e-19

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: 84.75  E-value: 2.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFR---GNYIVSTKK 175
Cdd:cd14545   27 INASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKCaqyWPQGEGNAMIfedTGLKVTLLS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 176 IYEKNYYTQYFFEIVSDATssDRPRKVNLYHYTQWPIFGNSANENKLIAFILAV-NAKMLEnffeaSLVAPVIVHGNAEV 254
Cdd:cd14545  107 EEDKSYYTVRTLELENLKT--QETREVLHFHYTTWPDFGVPESPAAFLNFLQKVrESGSLS-----SDVGPPVVHCSAGI 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 124378179 255 GRAETFCAIDICFEQ--WFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14545  180 GRSGTFCLVDTCLVLieKGNPSSVDVKKVLLEMRKYRMGLIQTPDQ 225
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 69-302 6.68e-19

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: 84.55  E-value: 6.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  69 DEQRTRYYEIPCSSQLRVTSANDLPTTSSnSNPINGYYVDGFRM-----KRKFIIIEAPSNESMDDFYHMLWKNESQVVV 143
Cdd:cd14606   18 NKSKNRYKNILPFDHSRVILQGRDSNIPG-SDYINANYVKNQLLgpdenAKTYIASQGCLEATVNDFWQMAWQENSRVIV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 144 ILTTE---HQNEIDPCWPTTLGEQFRGNYIVSTKKIYEKNYYTQYFFEiVSDATSSDRPRKVNLYHYTQWPIFGNSANEN 220
Cdd:cd14606   97 MTTREvekGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQ-VSPLDNGELIREIWHYQYLSWPDHGVPSEPG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 221 KLIAFILAVNAKMlENFFEAslvAPVIVHGNAEVGRAETFCAIDICFEQwFTTRRL----NVLNTVKHIRSQRYGSVITA 296
Cdd:cd14606  176 GVLSFLDQINQRQ-ESLPHA---GPIIVHCSAGIGRTGTIIVIDMLMEN-ISTKGLdcdiDIQKTIQMVRAQRSGMVQTE 250


                 ....*.
gi 124378179 297 NQNGLI 302
Cdd:cd14606  251 AQYKFI 256
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 98-298 8.33e-19

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: 83.92  E-value: 8.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  98 NSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WP-----------TTLGE 163
Cdd:cd14630   30 HSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVGRVKCvryWPddtevygdikvTLIET 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 164 QFRGNYIVSTKKIYEKNYYtqyffEIvsdatssdrpRKVNLYHYTQWPIFGNSANENKLIAFILAVnakmleNFFEASLV 243
Cdd:cd14630  110 EPLAEYVIRTFTVQKKGYH-----EI----------REIRQFHFTSWPDHGVPCYATGLLGFVRQV------KFLNPPDA 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 124378179 244 APVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14630  169 GPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQ 223
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 102-298 2.89e-18

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: 81.28  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTtlGEQFRGNYIVSTKKIYE 178
Cdd:cd14558    2 INASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCaqyWGD--EKKTYGDIEVELKDTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 179 KNYYTQYFFEIVSdaTSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLENFFEASLVAPVIVHGNAEVGRAE 258
Cdd:cd14558   80 SPTYTVRVFEITH--LKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHGRSVPIVVHCSDGSSRTG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 124378179 259 TFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14558  158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQ 197
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 106-291 3.38e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 83.09  E-value: 3.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 106 YVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVViLTTEH--QNEIDPCWPTTLGE-QFRGNYIVSTKKIYEKNYY 182
Cdd:PHA02740  83 FVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIV-LISRHadKKCFNQFWSLKEGCvITSDKFQIETLEIIIKPHF 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 183 TqyfFEIVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNA--KMLENFFEASLVAPVIVHGNAEVGRAETF 260
Cdd:PHA02740 162 N---LTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcADLEKHKADGKIAPIIIDCIDGISSSAVF 238

                        170       180       190
                 ....*....|....*....|....*....|.
gi 124378179 261 CAIDICFEQWFTTRRLNVLNTVKHIRSQRYG 291
Cdd:PHA02740 239 CVFDICATEFDKTGMLSIANALKKVRQKKYG 269
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 82-298 4.07e-18

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: 81.53  E-value: 4.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  82 SQLRVTSANDLPttssNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WP 158
Cdd:cd14618   12 SRVRLSQLGGEP----HSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRVLCdhyWP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 159 TTLGEQFRGNYIVSTKKIYEKNYYTQYFFEIVSDATSSDRprKVNLYHYTQWPIFGNSANENKLIAFILAVNakmlENFF 238
Cdd:cd14618   88 SESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKER--RVKHLHYTAWPDHGIPESTSSLMAFRELVR----EHVQ 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 239 EASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14618  162 ATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQ 221
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 81-298 5.66e-18

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: 81.12  E-value: 5.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  81 SSQLRVTSANDLPTtssnSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTT---EHQNEIDPCW 157
Cdd:cd14617   11 STRVKLSNVDDDPC----SDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQcveKGRVKCDHYW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 158 PTTLGEQFRGNYIVS--TKKIYEKnyYTQYFFEIVSDaTSSDRPRKVNLYHYTQWPIFGNSANENKLIAFIlavnaKMLE 235
Cdd:cd14617   87 PADQDSLYYGDLIVQmlSESVLPE--WTIREFKICSE-EQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFV-----RTVR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124378179 236 NFFEASLVA-PVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14617  159 DYINRTPGSgPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQ 222
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 30-310 6.40e-18

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: 82.09  E-value: 6.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  30 ILEVKNQERVLSTPCHLElYAARTSSTDSPKSYTFD---LSADEQRTRYYEIPCSSQLRV--TSANDLPttssNSNPING 104
Cdd:cd14624    6 ILELADHIERLKANDNLK-FSQEYESIDPGQQFTWEhsnLEVNKPKNRYANVIAYDHSRVllSAIEGIP----GSDYINA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 105 YYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTT-EHQNEI--DPCWPTTlGEQFRGNYIVSTKKIYEKNY 181
Cdd:cd14624   81 NYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKlEERSRVkcDQYWPSR-GTETYGLIQVTLLDTVELAT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 182 YTQYFFEIVSDATSSDrpRKVNLYHYTQWPIFGNSANENKLIAFILAVNAkmlenfFEASLVAPVIVHGNAEVGRAETFC 261
Cdd:cd14624  160 YCVRTFALYKNGSSEK--REVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT------CNPPDAGPMVVHCSAGVGRTGCFI 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 124378179 262 AIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQNGLIIRILKELV 310
Cdd:cd14624  232 VIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 55-310 7.41e-18

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: 82.06  E-value: 7.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  55 STDSPKSYTFD---LSADEQRTRYYEIPCSSQLRVTSandLPTTS-SNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDF 130
Cdd:cd14625   30 SIDPGQQFTWEhsnLEVNKPKNRYANVIAYDHSRVIL---QPIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 131 YHMLWKNESQVVVILTT-EHQNEI--DPCWPTTlGEQFRGNYIVSTKKIYEKNYYTQYFFEIVSDATSSDrpRKVNLYHY 207
Cdd:cd14625  107 WRMVWEQRSATVVMMTKlEEKSRIkcDQYWPSR-GTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEK--REVRQFQF 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 208 TQWPIFGNSANENKLIAFILAVNAkmlenfFEASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRS 287
Cdd:cd14625  184 TAWPDHGVPEYPTPFLAFLRRVKT------CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRS 257

                        250       260
                 ....*....|....*....|...
gi 124378179 288 QRYGSVITANQNGLIIRILKELV 310
Cdd:cd14625  258 QRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 84-302 1.87e-17

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: 79.58  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  84 LRVTSANDLPTTSSNSNPINGYyvdgFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTT-EHQNEidPC---WPT 159
Cdd:cd14611   18 LKPKNSNDSLSTYINANYIRGY----GGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKlKEKNE--KCvlyWPE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 160 TLGeqFRGNYIVSTKKIYEKNYYTQYFFEIVSDATSsdrpRKVNLYHYTQWPIFGNSANENKLIAFILAVNakmlENFFE 239
Cdd:cd14611   92 KRG--IYGKVEVLVNSVKECDNYTIRNLTLKQGSQS----RSVKHYWYTSWPDHKTPDSAQPLLQLMLDVE----EDRLA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124378179 240 ASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQNGLI 302
Cdd:cd14611  162 SPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 102-298 2.34e-17

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: 79.02  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVdgfRM-----KRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFR-GNYIVS 172
Cdd:cd14596    2 INASYI---TMpvgeeELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKChryWPETLQEPMElENYQLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 173 TKKIYEKNYYTQYFFEIVSDATSSDrpRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLEnffeaslvAPVIVHGNA 252
Cdd:cd14596   79 LENYQALQYFIIRIIKLVEKETGEN--RLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT--------GPIVVHCSA 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 124378179 253 EVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14596  149 GIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQ 194
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 116-298 2.55e-17

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: 78.96  E-value: 2.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 116 FIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQ--FRGNYIVSTKKIYEKNYYTQYFFEIV 190
Cdd:cd14538   18 YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKChryWPDSLNKPliCGGRLEVSLEKYQSLQDFVIRRISLR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 191 SDATSSDRPrkVNLYHYTQWPIFGNSANENKLIAFILAVnaKMLENffeaslVAPVIVHGNAEVGRAETFCAIDICFEQW 270
Cdd:cd14538   98 DKETGEVHH--ITHLNFTTWPDHGTPQSADPLLRFIRYM--RRIHN------SGPIVVHCSAGIGRTGVLITIDVALGLI 167

                        170       180
                 ....*....|....*....|....*...
gi 124378179 271 FTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14538  168 ERDLPFDIQDIVKDLREQRQGMIQTKDQ 195
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 102-298 4.79e-17

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: 78.03  E-value: 4.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WP-----------TTLGEQFRG 167
Cdd:cd14555    2 INANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCsryWPddtevygdikvTLVETEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 168 NYIVSTKKIYEKNYYtqyffEIvsdatssdrpRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKmlenffEASLVAPVI 247
Cdd:cd14555   82 EYVVRTFALERRGYH-----EI----------REVRQFHFTGWPDHGVPYHATGLLGFIRRVKAS------NPPSAGPIV 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124378179 248 VHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14555  141 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQ 191
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 98-298 6.74e-17

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: 78.14  E-value: 6.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  98 NSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTlgEQFRGNYIVSTK 174
Cdd:cd14631   12 SSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCykyWPDD--TEVYGDFKVTCV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 175 KIYEKNYYTQYFFEIvsDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNakmLENFFEAslvAPVIVHGNAEV 254
Cdd:cd14631   90 EMEPLAEYVVRTFTL--ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK---LSNPPSA---GPIVVHCSAGA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 124378179 255 GRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14631  162 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQ 205
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 91-298 2.09e-16

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: 77.12  E-value: 2.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  91 DLPTTSSNSNPINGYYV-------DGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTT 160
Cdd:cd14544   22 DRDPNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIVMTTKEVERGKNKCvryWPDE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 161 LGEQFRGNYIVSTKKIYEKNYYTQYFFEiVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMlENFFEA 240
Cdd:cd14544  102 GMQKQYGPYRVQNVSEHDTTDYTLRELQ-VSKLDQGDPIREIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQ-ESLPHA 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124378179 241 slvAPVIVHGNAEVGRAETFCAIDICFEQwftTRR------LNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14544  180 ---GPIVVHCSAGIGRTGTFIVIDMLLDQ---IKRkgldcdIDIQKTIQMVRSQRSGMVQTEAQ 237
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 201-308 2.10e-16

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: 73.55  E-value: 2.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179   201 KVNLYHYTQWPIFGNSANENKLIAFILAVNakmlENFFEASLVAPVIVHGNAEVGRAETFCAIDICFEQ-WFTTRRLNVL 279
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVK----KNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQlEAEAGEVDIF 76

                           90       100
                   ....*....|....*....|....*....
gi 124378179   280 NTVKHIRSQRYGSVITANQNGLIIRILKE 308
Cdd:smart00012  77 DTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
201-308 2.10e-16

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 73.55  E-value: 2.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179   201 KVNLYHYTQWPIFGNSANENKLIAFILAVNakmlENFFEASLVAPVIVHGNAEVGRAETFCAIDICFEQ-WFTTRRLNVL 279
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVK----KNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQlEAEAGEVDIF 76

                           90       100
                   ....*....|....*....|....*....
gi 124378179   280 NTVKHIRSQRYGSVITANQNGLIIRILKE 308
Cdd:smart00404  77 DTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 95-298 2.30e-16

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: 76.78  E-value: 2.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  95 TSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTT---EHQNEIDPCWPTTLGEQFRGNYIV 171
Cdd:cd14615   20 SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcveQGRTKCEEYWPSKQKKDYGDITVT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 172 STKKIYEKNYYTQYFfeIVSDATSSDRpRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLENFFEaslvAPVIVHGN 251
Cdd:cd14615  100 MTSEIVLPEWTIRDF--TVKNAQTNES-RTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQNPPN----SPILVHCS 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 124378179 252 AEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14615  173 AGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQ 219
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 99-298 3.31e-16

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: 76.47  E-value: 3.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  99 SNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFRGNYIVSTKK 175
Cdd:cd14619   25 SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRVKCehyWPLDYTPCTYGHLRVTVVS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 176 IYEKNYYTQYFFEIVSDATSSDrpRKVNLYHYTQWPIFGNSANENKLIAFilavnAKMLENFFEASL-VAPVIVHGNAEV 254
Cdd:cd14619  105 EEVMENWTVREFLLKQVEEQKT--LSVRHFHFTAWPDHGVPSSTDTLLAF-----RRLLRQWLDQTMsGGPTVVHCSAGV 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 124378179 255 GRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14619  178 GRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQ 221
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 59-298 5.46e-16

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: 76.44  E-value: 5.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  59 PKSYtfDLSADEQRTRYYEIPCSSQLRV----TSANDLPTTSSNSNPINGYYVDgfrmKRKFIIIEAPSNESMDDFYHML 134
Cdd:cd14613   17 PKEY--DIPGLVRKNRYKTILPNPHSRVcltsPDQDDPLSSYINANYIRGYGGE----EKVYIATQGPTVNTVGDFWRMV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 135 WKNESQVVVILTT-EHQNEidPC---WPTTLGeQFRGNYIVSTKKIYEKNYYTQYFfeivsDATSSDRPRKVNLYHYTQW 210
Cdd:cd14613   91 WQERSPIIVMITNiEEMNE--KCteyWPEEQV-TYEGIEITVKQVIHADDYRLRLI-----TLKSGGEERGLKHYWYTSW 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 211 PIFGNSANENKLIAFILAVNAKMLEnffEASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRY 290
Cdd:cd14613  163 PDQKTPDNAPPLLQLVQEVEEARQQ---AEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239


                 ....*...
gi 124378179 291 GSVITANQ 298
Cdd:cd14613  240 GMIQTCEQ 247
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 111-302 1.17e-15

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: 75.44  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 111 RMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFRGnyIVSTKKIYEKNYYTQYFF 187
Cdd:cd14605   51 KPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCvkyWPDEYALKEYG--VMRVRNVKESAAHDYILR 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 188 EI-VSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMlENFFEAslvAPVIVHGNAEVGRAETFCAIDIC 266
Cdd:cd14605  129 ELkLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQ-ESIMDA---GPVVVHCSAGIGRTGTFIVIDIL 204

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 124378179 267 FEqwfTTRR------LNVLNTVKHIRSQRYGSVITANQNGLI 302
Cdd:cd14605  205 ID---IIREkgvdcdIDVPKTIQMVRSQRSGMVQTEAQYRFI 243
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 97-298 1.94e-15

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: 75.08  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  97 SNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLW-KNESQVVVILTTEHQNEIDPC--WP-----------TTLG 162
Cdd:cd14633   66 TSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWhENTASIIMVTNLVEVGRVKCCkyWPddteiykdikvTLIE 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 163 EQFRGNYIVSTKKIYEKNYYtqyffEIvsdatssdrpRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLENffeasl 242
Cdd:cd14633  146 TELLAEYVIRTFAVEKRGVH-----EI----------REIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPN------ 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124378179 243 VAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14633  205 AGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQ 260
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 102-304 3.53e-15

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: 72.84  E-value: 3.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFR-GNYIVSTKKiy 177
Cdd:cd14542    2 INANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCeryWPEEGEEQLQfGPFKISLEK-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 178 EKNYYTQYFFEIVSdATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAkmlenfFEASLVAPVIVHGNAEVGRA 257
Cdd:cd14542   80 EKRVGPDFLIRTLK-VTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRD------YQGSEDVPICVHCSAGCGRT 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 124378179 258 ETFCAIDICFEQWFT---TRRLNVLNTVKHIRSQRYGSVITANQNGLIIR 304
Cdd:cd14542  153 GTICAIDYVWNLLKTgkiPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 116-298 3.61e-15

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: 72.86  E-value: 3.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 116 FIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTlGEQFRGNYIVS--TKKIYEKNYYTQYFF--E 188
Cdd:cd14546   17 YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCaryWPEE-GSEVYHIYEVHlvSEHIWCDDYLVRSFYlkN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 189 IVSDATssdrpRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMlenffeASLVAPVIVHGNAEVGRAETFCAIDICFE 268
Cdd:cd14546   96 LQTSET-----RTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY------RGRSCPIVVHCSDGAGRTGTYILIDMVLN 164

                        170       180       190
                 ....*....|....*....|....*....|.
gi 124378179 269 QWFT-TRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14546  165 RMAKgAKEIDIAATLEHLRDQRPGMVKTKDQ 195
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 62-298 8.74e-15

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: 72.61  E-value: 8.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  62 YTFDLSADEQRTRYYEI-PCS-SQLRVTSANDlpttSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNES 139
Cdd:cd14614    5 FAADLPVNRCKNRYTNIlPYDfSRVKLVSMHE----EEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 140 QVVVILTTEHQNEIDPC---WPTTLGEQFRGNYIVSTKKIYEKNYYTQYFFEIvsdaTSSDRPRKVNLYHYTQWPIFG-- 214
Cdd:cd14614   81 QIIVMLTQCNEKRRVKCdhyWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRV----SYADEVQDVMHFNYTAWPDHGvp 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 215 NSANENKLIAFILAVNAKMLENffeaslVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVI 294
Cdd:cd14614  157 TANAAESILQFVQMVRQQAVKS------KGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQ 230


                 ....
gi 124378179 295 TANQ 298
Cdd:cd14614  231 TEEQ 234
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 102-298 2.08e-14

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: 70.96  E-value: 2.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYV--DGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTT-EHQNEIDPC---WPTTLGE-QFRGNYIVSTK 174
Cdd:cd17658    2 INASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRlVDNYSTAKCadyFPAEENEsREFGRISVTNK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 175 KI-YEKNYYTQYFFEiVSDATSSDRPRKVNLYHYTQWPIFG---NSANENKLIAFILAVNAKMlenffeaslvAPVIVHG 250
Cdd:cd17658   82 KLkHSQHSITLRVLE-VQYIESEEPPLSVLHIQYPEWPDHGvpkDTRSVRELLKRLYGIPPSA----------GPIVVHC 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124378179 251 NAEVGRAETFCAIDicfeqwFTTRR--------LNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd17658  151 SAGIGRTGAYCTIH------NTIRRilegdmsaVDLSKTVRKFRSQRIGMVQTQDQ 200
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 52-298 2.60e-14

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: 71.98  E-value: 2.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  52 RTSSTDSPKSYTfDLSADEQRTRYYEIPCSSQLRVTsandlpTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFY 131
Cdd:cd14608    9 RHEASDFPCRVA-KLPKNKNRNRYRDVSPFDHSRIK------LHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 132 HMLWKNESQVVVILTTEHQNEIDPC---WPTTL-GEQFRGNYIVSTKKIYE--KNYYTQYFFEIvsDATSSDRPRKVNLY 205
Cdd:cd14608   82 EMVWEQKSRGVVMLNRVMEKGSLKCaqyWPQKEeKEMIFEDTNLKLTLISEdiKSYYTVRQLEL--ENLTTQETREILHF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 206 HYTQWPIFGNSANENKLIAFILavnaKMLENFFEASLVAPVIVHGNAEVGRAETFCAIDICF---EQWFTTRRLNVLNTV 282
Cdd:cd14608  160 HYTTWPDFGVPESPASFLNFLF----KVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLllmDKRKDPSSVDIKKVL 235

                        250
                 ....*....|....*.
gi 124378179 283 KHIRSQRYGSVITANQ 298
Cdd:cd14608  236 LEMRKFRMGLIQTADQ 251
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 102-298 3.59e-14

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: 70.08  E-value: 3.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WP-----------TTLGEQFRG 167
Cdd:cd14632    2 INANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCskyWPddsdtygdikiTLLKTETLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 168 NYIVSTKKIYEKNYYTQYffeivsdatssdrprKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLENffeaslVAPVI 247
Cdd:cd14632   82 EYSVRTFALERRGYSARH---------------EVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPD------AGPVV 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124378179 248 VHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14632  141 VHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQ 191
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 71-309 5.74e-14

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: 70.62  E-value: 5.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  71 QRTRYYEIPCSSQLRVTSAndLPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQ 150
Cdd:cd14603   32 KKNRYKDILPYDQTRVILS--LLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 151 NEIDPC---WPTTLGEQFRGNYIVSTKKIYEKNYYTQYFFEIVsdaTSSDRPRKVNLYHYTQWPIFGNSANENKLIAFIL 227
Cdd:cd14603  110 MGKKKCeryWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKV---TFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 228 AVNAKmlenffEASLVAPVIVHGNAEVGRAETFCAIDIcFEQWFTTRRL----NVLNTVKHIRSQRYGSVITANQNGLII 303
Cdd:cd14603  187 LARRL------QGSGPEPLCVHCSAGCGRTGVICTVDY-VRQLLLTQRIppdfSIFDVVLEMRKQRPAAVQTEEQYEFLY 259


                 ....*.
gi 124378179 304 RILKEL 309
Cdd:cd14603  260 HTVAQM 265
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 102-298 1.22e-13

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: 68.59  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILttehqNEIDPC-------WPTTLGEQFrGNYIVSTK 174
Cdd:cd14556    2 INAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-----NQLDPKdqscpqyWPDEGSGTY-GPIQVEFV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 175 KIYEKNYYTQYFFEIVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAvnakMLENFFEASLVAPVIVHGNAEV 254
Cdd:cd14556   76 STTIDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLS----EVEKWQEQSGEGPIVVHCLNGV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 124378179 255 GRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14556  152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQ 195
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 114-306 1.40e-13

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: 68.64  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 114 RKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFR---GNYIVSTKKIYEKNYYTQYFF 187
Cdd:cd14540   16 RFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCfryWPTLGGEHDAltfGEYKVSTKFSVSSGCYTTTGL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 188 EIvsDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNA---KMLENFFEASLVAPVIVHGNAEVGRAETFCAID 264
Cdd:cd14540   96 RV--KHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrHTNQDVAGHNRNPPTLVHCSAGVGRTGVVILAD 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 124378179 265 I---CFEQwftTRRLNVLNTVKHIRSQRYGSVITANQNGLIIRIL 306
Cdd:cd14540  174 LmlyCLDH---NEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVL 215
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 97-298 1.78e-13

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: 69.30  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  97 SNSNPINGYYVDGF-------RMKrKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WP---TTLGE 163
Cdd:cd14609   63 AESNPSRSDYINASpiiehdpRMP-AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCdryWPdegSSLYH 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 164 QFRGNYIvsTKKIYEKNYYTQYFFeivSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNakmlENFFEASlv 243
Cdd:cd14609  142 IYEVNLV--SEHIWCEDFLVRSFY---LKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVN----KCYRGRS-- 210

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124378179 244 APVIVHGNAEVGRAETFCAIDICFEQWFT-TRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14609  211 CPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKEIDIAATLEHVRDQRPGMVRTKDQ 266
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 65-298 2.21e-13

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: 68.71  E-value: 2.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  65 DLSADEQRTRYYEIPCSSQLRVTSANDlPTTSSNSNPINGYYVDGFRMKRK-FIIIEAPSNESMDDFYHMLWKNESQVVV 143
Cdd:cd14612   11 DIPGHASKDRYKTILPNPQSRVCLRRA-GSQEEEGSYINANYIRGYDGKEKaYIATQGPMLNTVSDFWEMVWQEECPIIV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 144 ILTT--EHQNEIDPCWPTTlgEQFRGNYIVSTKKIYEKNYYTQYFFEIVSDATSsdrpRKVNLYHYTQWPIFGNSANENK 221
Cdd:cd14612   90 MITKlkEKKEKCVHYWPEK--EGTYGRFEIRVQDMKECDGYTIRDLTIQLEEES----RSVKHYWFSSWPDHQTPESAGP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124378179 222 LIAFILAVNakmlENFFEASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14612  164 LLRLVAEVE----ESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQ 236
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 71-314 2.47e-13

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: 69.19  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  71 QRTRYYEIPCSSQLRVTSAndLPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQ 150
Cdd:cd14604   59 KKNRYKDILPFDHSRVKLT--LKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 151 NEIDPC---W------PTTLG--------EQFRGNYIVSTKKIYEKNyytqyffeivsdatssdRPRKVNLYHYTQWPIF 213
Cdd:cd14604  137 MGRKKCeryWplygeePMTFGpfrisceaEQARTDYFIRTLLLEFQN-----------------ETRRLYQFHYVNWPDH 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 214 GNSANENKLIAFIlavnakMLENFFEASLVAPVIVHGNAEVGRAETFCAIDICFEQWFTTR---RLNVLNTVKHIRSQRY 290
Cdd:cd14604  200 DVPSSFDSILDMI------SLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRH 273

                        250       260
                 ....*....|....*....|....
gi 124378179 291 GSVITANQNGLIIRILKELVKQDV 314
Cdd:cd14604  274 SAVQTKEQYELVHRAIAQLFEKQL 297
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 116-261 6.26e-13

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: 66.64  E-value: 6.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 116 FIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFR-GNYIVSTKKIYEKNYYTQYFFEIVS 191
Cdd:cd14539   17 FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVhryWPTERGQALVyGAITVSLQSVRTTPTHVERIISIQH 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 192 DATSSDrpRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLEnffEASLVAPVIVHGNAEVGRAETFC 261
Cdd:cd14539   97 KDTRLS--RSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQ---QRSLQTPIVVHCSSGVGRTGAFC 161
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 69-267 7.27e-13

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: 67.30  E-value: 7.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  69 DEQRTRYYEIPCSSQLRVTSANdlpttsSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTE 148
Cdd:cd14607   24 NRNRNRYRDVSPYDHSRVKLQN------TENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 149 HQNEIDPC---WPTTLGEQ-FRGNYIVSTKKIYE--KNYYTQYFFEIvsDATSSDRPRKVNLYHYTQWPIFGNSANENKL 222
Cdd:cd14607   98 VEKDSVKCaqyWPTDEEEVlSFKETGFSVKLLSEdvKSYYTVHLLQL--ENINSGETRTISHFHYTTWPDFGVPESPASF 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 124378179 223 IAFILavnaKMLENFFEASLVAPVIVHGNAEVGRAETFCAIDICF 267
Cdd:cd14607  176 LNFLF----KVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCL 216
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 102-263 1.73e-12

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: 65.03  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC-WPTTLGEQFRGNYIVS------TK 174
Cdd:cd14550    2 INASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIyWPTKEKPLECETFKVTlsgedhSC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 175 KIYEKNYYTQYFfeiVSDATSSDRPRKVNLYHYTQWPifGNSANENKLIAFILAVNAKMLENffeaslVAPVIVH---GN 251
Cdd:cd14550   82 LSNEIRLIVRDF---ILESTQDDYVLEVRQFQCPSWP--NPCSPIHTVFELINTVQEWAQQR------DGPIVVHdryGG 150

                        170
                 ....*....|..
gi 124378179 252 AEvgrAETFCAI 263
Cdd:cd14550  151 VQ---AATFCAL 159
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 116-298 5.12e-12

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: 65.08  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 116 FIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTlGEQFRGNYIVS--TKKIYEKNYYTQYFFeiv 190
Cdd:cd14610   90 YIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCyhyWPDE-GSNLYHIYEVNlvSEHIWCEDFLVRSFY--- 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 191 SDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMlenffeASLVAPVIVHGNAEVGRAETFCAIDICFEQW 270
Cdd:cd14610  166 LKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCY------RGRSCPIIVHCSDGAGRSGTYILIDMVLNKM 239

                        170       180
                 ....*....|....*....|....*....
gi 124378179 271 FT-TRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14610  240 AKgAKEIDIAATLEHLRDQRPGMVQTKEQ 268
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 99-289 8.59e-12

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: 63.77  E-value: 8.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  99 SNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WP--------------TTL 161
Cdd:cd14616   25 SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRChqyWPednkpvtvfgdiviTKL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 162 GEQFRGNYIVSTKKIYEKNYYTQyffeivsdatssdrprkVNLYHYTQWPIFGNSANENKLIAFILAVNAKmlenffEAS 241
Cdd:cd14616  105 MEDVQIDWTIRDLKIERHGDYMM-----------------VRQCNFTSWPEHGVPESSAPLIHFVKLVRAS------RAH 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 124378179 242 LVAPVIVHGNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQR 289
Cdd:cd14616  162 DNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSER 209
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 116-298 3.39e-11

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: 62.15  E-value: 3.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 116 FIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLG------EQFRgnyIVSTKKIYEKNYYTQYf 186
Cdd:cd14597   45 YIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGGKIKCqryWPEILGkttmvdNRLQ---LTLVRMQQLKNFVIRV- 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 187 feIVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNakmlenffEASLVAPVIVHGNAEVGRAETFCAIDIC 266
Cdd:cd14597  121 --LELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISYMR--------HIHKSGPIITHCSAGIGRSGTLICIDVV 190

                        170       180       190
                 ....*....|....*....|....*....|....
gi 124378179 267 FEqwFTTRRL--NVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14597  191 LG--LISKDLdfDISDIVRTMRLQRHGMVQTEDQ 222
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 98-298 1.21e-10

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: 60.34  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  98 NSNPINgYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFRGNYIVSTK 174
Cdd:cd14601    4 NANYIN-MEIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKChqyWPEPSGSSSYGGFQVTCH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 175 KiyEKNYYTQYFFEIVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKmlenffEASLVAPVIVHGNAEV 254
Cdd:cd14601   83 S--EEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNK------RAGKDEPVVVHCSAGI 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 124378179 255 GRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14601  155 GRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQ 198
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 102-291 2.03e-10

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: 59.24  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC--WPTT----LGEQFRGNYIVSTKK 175
Cdd:cd17669    2 INASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFvyWPNKdepiNCETFKVTLIAEEHK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 176 IY--EKNYYTQYFfeiVSDATSSDRPRKVNLYHYTQWPifgnsaNENKLIAFILAVNAKMLENffEASLVAPVIVHGNAE 253
Cdd:cd17669   82 CLsnEEKLIIQDF---ILEATQDDYVLEVRHFQCPKWP------NPDSPISKTFELISIIKEE--AANRDGPMIVHDEHG 150

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 124378179 254 VGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYG 291
Cdd:cd17669  151 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPG 188
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 72-309 2.89e-10

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: 59.47  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  72 RTRYYEIPCSSQLRVTSAndLPTTSSNSNPINGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQN 151
Cdd:cd14602    1 KNRYKDILPYDHSRVELS--LITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 152 EIDPC---WPTTLGEQFR-GNYIVSTKKIYEKNYYTQYFFEivsdATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFIL 227
Cdd:cd14602   79 GKKKCeryWAEPGEMQLEfGPFSVTCEAEKRKSDYIIRTLK----VKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 228 AVNAkmlenfFEASLVAPVIVHGNAEVGRAETFCAIDICF---EQWFTTRRLNVLNTVKHIRSQRYGSVITANQNGLIIR 304
Cdd:cd14602  155 DVRC------YQEDDSVPICIHCSAGCGRTGVICAIDYTWmllKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYN 228


                 ....*
gi 124378179 305 ILKEL 309
Cdd:cd14602  229 AVIEL 233
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 102-298 7.83e-10

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: 57.72  E-value: 7.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVD----GFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFRGNYIVSTk 174
Cdd:cd14541    3 INANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKChqyWPDLGETMQFGNLQITC- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 175 kIYEKNYYTQYFFEIVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKmlenffEASLVAPVIVHGNAEV 254
Cdd:cd14541   82 -VSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQN------RVGMVEPTVVHCSAGI 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 124378179 255 GRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14541  155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQ 198
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 98-308 2.39e-08

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: 54.09  E-value: 2.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  98 NSNPINGYYVD----GFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPTTLGEQFRGNYI 170
Cdd:cd14600   62 NEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKChqyWPDPPDVMEYGGFR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 171 VSTKKiyeKNYYTQYFF-EIVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLENffeaslvAPVIVH 249
Cdd:cd14600  142 VQCHS---EDCTIAYVFrEMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVEN-------EPVLVH 211

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124378179 250 GNAEVGRAETFCAID--ICfeqwFTTRRLNV--LNTVKHIRSQRYGSVITANQNGL----IIRILKE 308
Cdd:cd14600  212 CSAGIGRTGVLVTMEtaMC----LTERNQPVypLDIVRKMRDQRAMMVQTSSQYKFvceaILRVYEE 274
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 102-289 5.69e-07

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: 49.30  E-value: 5.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILttehqNEIDPC------WPTTlGEQFRGNYIVSTKK 175
Cdd:cd14635    2 INAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-----NDVDPAqlcpqyWPEN-GVHRHGPIQVEFVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 176 IYEKNYYTQYFFEIVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLENFFEASlvAPVIVHGNAEVG 255
Cdd:cd14635   76 ADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGE--GRTVVHCLNGGG 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 124378179 256 RAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQR 289
Cdd:cd14635  154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNK 187
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 102-291 9.14e-07

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: 48.91  E-value: 9.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC--WPT---TLGEQFRGNYIVSTKKI 176
Cdd:cd17670    2 INASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFvyWPSreeSMNCEAFTVTLISKDRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 177 YEKNYYTQYFFEIVSDATSSDRPRKVNLYHYTQWPifGNSANENKLIAFILAVNAKMLenffeaSLVAPVIVHGNAEVGR 256
Cdd:cd17670   82 CLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWP--NPDAPISSTFELINVIKEEAL------TRDGPTIVHDEFGAVS 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 124378179 257 AETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYG 291
Cdd:cd17670  154 AGTLCALTTLSQQLENENAVDVYQVAKMINLMRPG 188
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 63-311 1.58e-06

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: 48.84  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  63 TFDLSADEQRTRYYEIPCSSQLRVTSandLPTTSSNSNPINGYYVDGFRMKRK--FIIIEAPSNESMDDFYHMLWKNESQ 140
Cdd:cd14599   32 TATLPENAERNRIREVVPYEENRVEL---VPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVN 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 141 VVVILTTEHQN---EIDPCWPtTLGEQFR----GNYIVSTKKIYEKNYYTQYFFEIVSDATSSDRprkvNLYH--YTQWP 211
Cdd:cd14599  109 VIAMVTAEEEGgrsKSHRYWP-KLGSKHSsatyGKFKVTTKFRTDSGCYATTGLKVKHLLSGQER----TVWHlqYTDWP 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 212 IFGNSANENKLIAFILAVNA------KMLENffEASLVAPVIVHGNAEVGRAETFCAIDI---CFEQwftTRRLNVLNTV 282
Cdd:cd14599  184 DHGCPEEVQGFLSYLEEIQSvrrhtnSMLDS--TKNCNPPIVVHCSAGVGRTGVVILTELmigCLEH---NEKVEVPVML 258

                        250       260
                 ....*....|....*....|....*....
gi 124378179 283 KHIRSQRYGSVITANQNGLIIRILKELVK 311
Cdd:cd14599  259 RHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 102-298 4.17e-06

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: 46.94  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 102 INGYYVDGFRMKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILttehqNEIDPC------WPttlgEQFRGNY------ 169
Cdd:cd14634    2 INAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-----NEMDAAqlcmqyWP----EKTSCCYgpiqve 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 170 IVSTKkIYEKNyyTQYFFEIVSDATSSDRPRKVNLYHYTQWPIFGNSANENKLIAFILAVNAKMLENFFEASlvAPVIVH 249
Cdd:cd14634   73 FVSAD-IDEDI--ISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGRE--GRTVVH 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 124378179 250 GNAEVGRAETFCAIDICFEQWFTTRRLNVLNTVKHIRSQRYGSVITANQ 298
Cdd:cd14634  148 CLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQ 196
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 91-262 1.43e-05

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: 45.47  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179  91 DLPTTSSNSN----PINGYYVDGfrmKRKFIIIEAPSNESMDDFYHMLWKNESQVVVILTTEhqNEIdPCwpTTLGEQFR 166
Cdd:cd14559    5 NIQTRVSTPVgknlNANRVQIGN---KNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASN--KDI-QR--KGLPPYFR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 167 GNYI---VSTKKIYEKNYYT-------QYFFEIvsdaTSSDRPRKVNLYHYTQWPIFGNSANEN-KLIAFILAVNAKMLE 235
Cdd:cd14559   77 QSGTygsVTVKSKKTGKDELvdglkadMYNLKI----TDGNKTITIPVVHVTNWPDHTAISSEGlKELADLVNKSAEEKR 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 124378179 236 NFFEA---------SLVAPVIvHGNAEVGRAETFCA 262
Cdd:cd14559  153 NFYKSkgssaindkNKLLPVI-HCRAGVGRTGQLAA 187
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 116-311 1.45e-05

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: 45.35  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 116 FIIIEAPSNESMDDFYHMLWKNESQVVVILTTEHQNEIDPC---WPtTLGEQFR----GNYIVSTKKIYEKNYYTQYFFE 188
Cdd:cd14598   18 YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSfryWP-RLGSRHNtvtyGRFKITTRFRTDSGCYATTGLK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124378179 189 IVSDATSSDRprkvNLYH--YTQWPIFGNSANENKLIAF---ILAVNAKMLENFFEASLVAPVIVHGNAEVGRAETFCAI 263
Cdd:cd14598   97 IKHLLTGQER----TVWHlqYTDWPEHGCPEDLKGFLSYleeIQSVRRHTNSTIDPKSPNPPVLVHCSAGVGRTGVVILS 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124378179 264 DI---CFEQwftTRRLNVLNTVKHIRSQRYGSVITANQNGLIIRILKELVK 311
Cdd:cd14598  173 EImiaCLEH---NEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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