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Conserved domains on  [gi|767903700|ref|XP_011539523|]
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tyrosine-protein phosphatase non-receptor type 22 isoform X1 [Homo sapiens]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 57-264 3.06e-153

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


The actual alignment was detected with superfamily member cd14602:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 234  Bit Score: 445.82  E-value: 3.06e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  57 KNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 137 KKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 216
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903700 217 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDG--------------------------EQYELVYNAVLELF 264
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipenfsvfsliqemrtqrpslvqtkEQYELVYNAVIELF 234
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-264 3.06e-153

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: 445.82  E-value: 3.06e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  57 KNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 137 KKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 216
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903700 217 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDG--------------------------EQYELVYNAVLELF 264
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipenfsvfsliqemrtqrpslvqtkEQYELVYNAVIELF 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-262 5.43e-102

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 314.60  E-value: 5.43e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700    24 FANEFLKLKRQstkykADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITsDEDSSYINANFIKGVYGPKAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700   104 GPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKF--NSE 181
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700   182 TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDG----------- 250
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGkevdifeivke 235

                          250       260
                   ....*....|....*....|....
gi 767903700   251 ------------EQYELVYNAVLE 262
Cdd:smart00194 236 lrsqrpgmvqteEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-262 6.70e-94

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 292.61  E-value: 6.70e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700   54 NIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  134 MGKKKCERYWAEPGEMQLEFGPFSVSCEAEKR-KSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIW 210
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903700  211 DVR-CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDG-----------------------EQYELVYNAVLE 262
Cdd:pfam00102 159 KVRkSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEgevdifqivkelrsqrpgmvqtlEQYIFLYDAILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 33-241 1.15e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 152.00  E-value: 1.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  33 RQSTKYKADKTYPTTVAEKpKNIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLD 112
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEK-KNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 113 FWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE-TRTIYQFHYK 191
Cdd:PHA02738 106 FYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFT 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903700 192 NWPDHDVPSSIDPILELIWDVRCYQED-------------DSVPICIHCSAGCGRTGVICAID 241
Cdd:PHA02738 186 AWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVD 248
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
13-240 3.77e-36

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 137.92  E-value: 3.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  13 EAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNikknRYKDILPYDYSRVElslitsdEDSSYINANFIKg 92
Cdd:COG5599    5 NPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLN----RFRDIQPYKETALR-------ANLGYLNANYIQ- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  93 VYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK--KKCERYWAEPGEMqlefgpFSVSCEAEKRKSDYI 170
Cdd:COG5599   73 VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDGEY------GKYEVSSELTESIQL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 171 -----IRTLKVKFNS---ETRTIYQFHYKNWPDHDVPSSiDPILELIWDVRCYQEDDSV---PICIHCSAGCGRTGVICA 239
Cdd:COG5599  147 rdgieARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIA 225


                 .
gi 767903700 240 I 240
Cdd:COG5599  226 C 226
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-264 3.06e-153

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: 445.82  E-value: 3.06e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  57 KNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 137 KKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 216
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903700 217 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDG--------------------------EQYELVYNAVLELF 264
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipenfsvfsliqemrtqrpslvqtkEQYELVYNAVIELF 234
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2-268 1.87e-145

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: 428.58  E-value: 1.87e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700   2 DQREILQKFLDEAQSKKIT----KEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLIT 77
Cdd:cd14604    1 EQVEILKKFIERVQAMKSTdhngEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  78 SDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFS 157
Cdd:cd14604   81 SSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 158 VSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVI 237
Cdd:cd14604  161 ISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767903700 238 CAIDYTWMLLKDG--------------------------EQYELVYNAVLELFKRQM 268
Cdd:cd14604  241 CAIDYTWNLLKAGkipeefnvfnliqemrtqrhsavqtkEQYELVHRAIAQLFEKQL 297
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 84-258 9.89e-119

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: 355.96  E-value: 9.89e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAE 163
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKS-DYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDY 242
Cdd:cd14542   81 KRVGpDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767903700 243 TWMLLKDG--------------------------EQYELVYN 258
Cdd:cd14542  161 VWNLLKTGkipeefslfdlvremrkqrpamvqtkEQYELVYR 202
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 25-264 1.13e-107

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: 329.86  E-value: 1.13e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14603    1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 105 PLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEmQLEFGPFSVSCEAEKR-KSDYIIRTLKVKFNSETR 183
Cdd:cd14603   81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQE-PLQTGPFTITLVKEKRlNEEVILRTLKVTFQKESR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 184 TIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLL---------------- 247
Cdd:cd14603  160 SVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLltqrippdfsifdvvl 239

                        250       260
                 ....*....|....*....|....*..
gi 767903700 248 ----------KDGEQYELVYNAVLELF 264
Cdd:cd14603  240 emrkqrpaavQTEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-262 5.43e-102

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 314.60  E-value: 5.43e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700    24 FANEFLKLKRQstkykADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITsDEDSSYINANFIKGVYGPKAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700   104 GPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKF--NSE 181
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700   182 TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDG----------- 250
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGkevdifeivke 235

                          250       260
                   ....*....|....*....|....
gi 767903700   251 ------------EQYELVYNAVLE 262
Cdd:smart00194 236 lrsqrpgmvqteEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-262 6.70e-94

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 292.61  E-value: 6.70e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700   54 NIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  134 MGKKKCERYWAEPGEMQLEFGPFSVSCEAEKR-KSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIW 210
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903700  211 DVR-CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDG-----------------------EQYELVYNAVLE 262
Cdd:pfam00102 159 KVRkSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEgevdifqivkelrsqrpgmvqtlEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 84-263 2.07e-80

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: 256.06  E-value: 2.07e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAE 163
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd00047   81 EELSDYTIRTLELSPkgCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                        170       180
                 ....*....|....*....|..
gi 767903700 242 YTWMLLKDGEQYElVYNAVLEL 263
Cdd:cd00047  161 ILLERLEAEGEVD-VFEIVKAL 181
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 51-241 6.51e-66

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: 219.93  E-value: 6.51e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  51 KPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACM 130
Cdd:cd14543   26 APANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 131 EYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVkFNSET---RTIYQFHYKNWPDHDVPSSIDPILE 207
Cdd:cd14543  106 VVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEI-HNTETdesRQVTHFQFTSWPDFGVPSSAAALLD 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767903700 208 LIWDVRCYQEdDSV--------------PICIHCSAGCGRTGVICAID 241
Cdd:cd14543  185 FLGEVRQQQA-LAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLD 231
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 59-281 9.44e-65

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: 215.30  E-value: 9.44e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  59 RYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKK 138
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 139 CERYWAEpGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQED 218
Cdd:cd14548   81 CDHYWPF-DQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903700 219 DSVPICIHCSAGCGRTGVICAIDYTWMLLKDgEQYELVYNAVLELFKRQMDVIRdkhsgTESQ 281
Cdd:cd14548  160 EKGPTIVHCSAGVGRTGTFIALDRLLQQIES-EDYVDIFGIVYDLRKHRPLMVQ-----TEAQ 216
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 54-283 1.61e-59

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: 201.92  E-value: 1.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  54 NIKKNRYKDILPYDYSRVELSLITSDED-SSYINANFIK------GVYGP-KAYIATQGPLSTTLLDFWRMIWEYSVLII 125
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIRnenegpTTDENaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 126 VMACMEYEMGKKKCERYWAEPGeMQLEFGPFSVSCEAEKRKSDYIIRTL---KVKFNSETRTIYQFHYKNWPDHDVPSSI 202
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEG-MQKQYGPYRVQNVSEHDTTDYTLRELqvsKLDQGDPIREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 203 DPILELIWDVRCYQE--DDSVPICIHCSAGCGRTGVICAIDytwmllkdgeqyelvynAVLELFKRQ-----MDV----- 270
Cdd:cd14544  160 GGVLNFLEDVNQRQEslPHAGPIVVHCSAGIGRTGTFIVID-----------------MLLDQIKRKgldcdIDIqktiq 222

                        250
                 ....*....|....*..
gi 767903700 271 -IRDKHSG---TESQAK 283
Cdd:cd14544  223 mVRSQRSGmvqTEAQYK 239
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 58-240 2.36e-58

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: 198.00  E-value: 2.36e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMgK 136
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 137 KKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCY 215
Cdd:cd14547   80 EKCAQYW--PEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVeEAR 157

                        170       180
                 ....*....|....*....|....*.
gi 767903700 216 QEDDSV-PICIHCSAGCGRTGVICAI 240
Cdd:cd14547  158 QTEPHRgPIVVHCSAGIGRTGCFIAT 183
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 54-241 6.94e-55

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: 189.14  E-value: 6.94e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  54 NIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYE 133
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 134 MGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWD 211
Cdd:cd14553   83 RSRVKCDQYW--PTRGTETYGLIQVTLLDTVELATYTVRTFALHKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 767903700 212 VRCYQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14553  161 VKACNPPDAGPIVVHCSAGVGRTGCFIVID 190
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 84-268 3.46e-54

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: 185.92  E-value: 3.46e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIK-GVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEpGEMQLEFGPFSVSC-- 160
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-GEYEGEYGDLTVELvs 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 161 EAEKRKSDYIIRTLKVKF-NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR--CYQEDDSVPICIHCSAGCGRTGVI 237
Cdd:cd18533   80 EEENDDGGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRelNDSASLDPPIIVHCSAGVGRTGTF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767903700 238 CAIDyTWM-LLKDG--------EQYELVYNAVLELFKRQM 268
Cdd:cd18533  160 IALD-SLLdELKRGlsdsqdleDSEDPVYEIVNQLRKQRM 198
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 58-281 9.03e-53

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: 183.17  E-value: 9.03e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA--CMeyEMG 135
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLtnCM--EAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 136 KKKCERYWaePGEMQ-LEFGPFSVSCEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELiWD- 211
Cdd:cd14619   79 RVKCEHYW--PLDYTpCTYGHLRVTVVSEEVMENWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAF-RRl 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903700 212 VRCY--QEDDSVPICIHCSAGCGRTGVICAIDYtwmLLKDGEQYELVYNAVlelFKRQMDVIRDKHSGTESQ 281
Cdd:cd14619  156 LRQWldQTMSGGPTVVHCSAGVGRTGTLIALDV---LLQQLQSEGLLGPFS---FVQKMRENRPLMVQTESQ 221
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 84-241 1.87e-52

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: 181.01  E-value: 1.87e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAE 163
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYW--PKEGTETYGNIQVTLLST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTL--------KVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTG 235
Cdd:cd14549   79 EVLATYTVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158


                 ....*.
gi 767903700 236 VICAID 241
Cdd:cd14549  159 TYIVID 164
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 58-241 1.96e-52

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: 181.94  E-value: 1.96e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  58 NRYKDILPYDYSRVELSLITSDEDSsYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKK 137
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTDD-YINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 138 KCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY 215
Cdd:cd14615   80 KCEEYW--PSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNaqTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                        170       180
                 ....*....|....*....|....*...
gi 767903700 216 --QEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14615  158 mkQNPPNSPILVHCSAGVGRTGTFIAID 185
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 53-281 1.99e-52

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: 182.15  E-value: 1.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  53 KNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEY 132
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 133 EMGKKKCERYWAEPGEMqleFGPFSVSCEAEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 210
Cdd:cd14630   82 EVGRVKCVRYWPDDTEV---YGDIKVTLIETEPLAEYVIRTFTVqkKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767903700 211 DVRCYQEDDSVPICIHCSAGCGRTGVICAIDyTWMLLKDGEQYELVYNAVLELFKRQMDVIRdkhsgTESQ 281
Cdd:cd14630  159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAID-IMLDMAENEGVVDIFNCVRELRAQRVNMVQ-----TEEQ 223
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 49-240 8.42e-52

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: 180.41  E-value: 8.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 129 CMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14554   81 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767903700 207 ELIWDV-RCY-QEDDSVPICIHCSAGCGRTGVICAI 240
Cdd:cd14554  159 DFIGQVhKTKeQFGQEGPITVHCSAGVGRTGVFITL 194
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 50-283 1.19e-50

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: 178.15  E-value: 1.19e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  50 EKPKNIKKNRYKDILPYDYSRVELSLITSD-EDSSYINANFIKG-VYG----PKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:cd14606   14 QRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNqLLGpdenAKTYIASQGCLEATVNDFWQMAWQENSR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 124 IIVMACMEYEMGKKKCERYWAEPGeMQLEFGPFSVSCEAEKRKSDYIIRTLKVKF---NSETRTIYQFHYKNWPDHDVPS 200
Cdd:cd14606   94 VIVMTTREVEKGRNKCVPYWPEVG-MQRAYGPYSVTNCGEHDTTEYKLRTLQVSPldnGELIREIWHYQYLSWPDHGVPS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 201 SIDPILELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDytwMLLkdgeqyELVYNAVLEL---FKRQMDVIRDKH 275
Cdd:cd14606  173 EPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVID---MLM------ENISTKGLDCdidIQKTIQMVRAQR 243

                        250
                 ....*....|.
gi 767903700 276 SG---TESQAK 283
Cdd:cd14606  244 SGmvqTEAQYK 254
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 45-251 1.23e-50

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: 177.39  E-value: 1.23e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  45 PTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLI 124
Cdd:cd14614    3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 125 IVMACMEYEMGKKKCERYW---AEPgemqLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPS- 200
Cdd:cd14614   83 IVMLTQCNEKRRVKCDHYWpftEEP----VAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTa 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767903700 201 -SIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGE 251
Cdd:cd14614  159 nAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHE 210
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 57-271 3.32e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 175.66  E-value: 3.32e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  57 KNRYKDILPYDYSRVELSLitSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKL--KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 137 KKCERYW-AEPGEMQ-LEFGPFSVSCEAEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 212
Cdd:cd14545   79 IKCAQYWpQGEGNAMiFEDTGLKVTLLSEEDKSYYTVRTLELenLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903700 213 RCYQ--EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGEQYEL-VYNAVLELFKRQMDVI 271
Cdd:cd14545  159 RESGslSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSSVdVKKVLLEMRKYRMGLI 220
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 58-268 8.06e-50

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: 174.71  E-value: 8.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKK 137
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 138 KCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQE 217
Cdd:cd14616   81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767903700 218 DDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGEQYElVYNAVLELFKRQM 268
Cdd:cd14616  161 HDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVD-IYGLVAELRSERM 210
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 24-262 1.00e-49

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: 175.99  E-value: 1.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  24 FANEFLKLKRQStkykADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDED--SSYINANFIKGVYGPKAYIA 101
Cdd:cd17667    1 FSEDFEEVQRCT----ADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 102 TQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKV----- 176
Cdd:cd17667   77 TQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYW--PTENSEEYGNIIVTLKSTKIHACYTVRRFSIrntkv 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 177 --------KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK 248
Cdd:cd17667  155 kkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIK 234

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 767903700 249 DG-----------------------EQYELVYNAVLE 262
Cdd:cd17667  235 DKstvnvlgflkhirtqrnylvqteEQYIFIHDALLE 271
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 53-241 2.58e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 174.05  E-value: 2.58e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  53 KNIKKNRYKDILPYDYSRVELSLITSDED-SSYINANFIKGVYG--------PKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPvSDYINANIIMPEFEtkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 124 IIVMACMEYEMGKKKCERYWaePGEMQL-EFGPFSVSCEAEKRKSDYIIRTLKV----KFNSEtRTIYQFHYKNWPDHDV 198
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYW--PDEYALkEYGVMRVRNVKESAAHDYILRELKLskvgQGNTE-RTVWQYHFRTWPDHGV 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767903700 199 PSSIDPILELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14605  158 PSDPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVID 202
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 52-249 4.60e-49

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 173.10  E-value: 4.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  52 PKNIKKNRYKDILPYDYSRVEL-SLITSDEDSSYINANFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMAC 129
Cdd:cd14612   13 PGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDGkEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 130 MEYEmGKKKCERYWAEPgemQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELI 209
Cdd:cd14612   93 KLKE-KKEKCVHYWPEK---EGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRLV 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767903700 210 WDVRCYQEDDSV--PICIHCSAGCGRTGVICAIDYTWMLLKD 249
Cdd:cd14612  169 AEVEESRQTAASpgPIVVHCSAGIGRTGCFIATSIGCQQLKD 210
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 31-272 5.53e-48

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: 171.38  E-value: 5.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  31 LKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTL 110
Cdd:cd14633   17 FKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 111 LDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMqleFGPFSVSCEAEKRKSDYIIRTLKVKFNS--ETRTIYQF 188
Cdd:cd14633   97 YDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI---YKDIKVTLIETELLAEYVIRTFAVEKRGvhEIREIRQF 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 189 HYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDytwMLLKDGEQYELV--YNAVLELFKR 266
Cdd:cd14633  174 HFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVID---IMLDMAEREGVVdiYNCVRELRSR 250


                 ....*.
gi 767903700 267 QMDVIR 272
Cdd:cd14633  251 RVNMVQ 256
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 47-265 5.66e-48

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: 171.19  E-value: 5.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  47 TVAEKPKNIKKNRYKDILPYDYSRVELslitsDEDSSYINANFIK----GVYGPKAYIATQGPLSTTLLDFWRMIWEYSV 122
Cdd:cd14600   33 TCAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 123 LIIVMACMEYEMGKKKCERYWAEPGEMqLEFGPFSVSCEAEKRKSDYIIRTLKVKfNSET---RTIYQFHYKNWPDHDVP 199
Cdd:cd14600  108 SLIVMLTTLTERGRTKCHQYWPDPPDV-MEYGGFRVQCHSEDCTIAYVFREMLLT-NTQTgeeRTVTHLQYVAWPDHGVP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 200 SSIDPILELIWDVRCYQEdDSVPICIHCSAGCGRTGVICAI-----------------------DYTWMLLKDGEQYELV 256
Cdd:cd14600  186 DDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTMetamclternqpvypldivrkmrDQRAMMVQTSSQYKFV 264


                 ....*....
gi 767903700 257 YNAVLELFK 265
Cdd:cd14600  265 CEAILRVYE 273
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 58-263 5.89e-47

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: 166.63  E-value: 5.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKK 137
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 138 KCERYWAEPGEmQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE---TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 214
Cdd:cd14617   81 KCDHYWPADQD-SLYYGDLIVQMLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767903700 215 Y--QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGEQYElVYNAVLEL 263
Cdd:cd14617  160 YinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVD-IYGAVHDL 209
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 58-268 3.57e-46

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: 164.73  E-value: 3.57e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKK 137
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 138 KCERYWaePGEMQ-LEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 214
Cdd:cd14618   81 LCDHYW--PSESTpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLrkERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767903700 215 YQE--DDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgEQYELVYNAV--LELFKRQM 268
Cdd:cd14618  159 HVQatKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKE-EKVVDVFNTVyiLRMHRYLM 215
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 44-272 6.41e-46

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: 165.58  E-value: 6.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  44 YPTTVAEKPKNIKKNRYKDILPYDYSRVELSLitsdEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:cd14608   15 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 124 IIVMACMEYEMGKKKCERYWA--EPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVP 199
Cdd:cd14608   91 GVVMLNRVMEKGSLKCAQYWPqkEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 200 SSIDPILELIWDVRcyqEDDSV-----PICIHCSAGCGRTGVICAIDYTWMLL---KDGEQYElVYNAVLELFKRQMDVI 271
Cdd:cd14608  171 ESPASFLNFLFKVR---ESGSLspehgPVVVHCSAGIGRSGTFCLADTCLLLMdkrKDPSSVD-IKKVLLEMRKFRMGLI 246


                 .
gi 767903700 272 R 272
Cdd:cd14608  247 Q 247
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 53-269 8.34e-46

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 163.85  E-value: 8.34e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  53 KNIKKNRYKDILPYDYSRVELSlitsdEDSSYINANFIKGVYGPK--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACM 130
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 131 EYEMGKKKCERYWAE-PGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILE 207
Cdd:cd14597   77 EVEGGKIKCQRYWPEiLGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903700 208 LIWDVRCYQEddSVPICIHCSAGCGRTGVICAIDytwmllkdgeqyelvynAVLELFKRQMD 269
Cdd:cd14597  157 FISYMRHIHK--SGPIITHCSAGIGRSGTLICID-----------------VVLGLISKDLD 199
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 38-267 1.01e-45

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: 165.21  E-value: 1.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  38 YKADktyPTT--VAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGvYGPK--AYIATQGPLSTTLLDF 113
Cdd:cd14609   27 YQAE---PNTcsTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSHTIADF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 114 WRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEK-RKSDYIIRTLKVKF--NSETRTIYQFHY 190
Cdd:cd14609  103 WQMVWENGCTVIVMLTPLVEDGVKQCDRYW--PDEGSSLYHIYEVNLVSEHiWCEDFLVRSFYLKNvqTQETRTLTQFHF 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767903700 191 KNWPDHDVPSSIDPILELIWDV-RCYQeDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGEQyELVYNAVLELFKRQ 267
Cdd:cd14609  181 LSWPAEGIPSSTRPLLDFRRKVnKCYR-GRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVK-EIDIAATLEHVRDQ 256
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-273 5.37e-45

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: 160.57  E-value: 5.37e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANF----IKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEmQLEFGPFSVS 159
Cdd:cd14541    2 YINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE-TMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 160 CEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVI 237
Cdd:cd14541   81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767903700 238 CAIDyTWMLLKdgEQYELVYnaVLELFkRQMdviRD 273
Cdd:cd14541  161 ITME-TAMCLI--EANEPVY--PLDIV-RTM---RD 187
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 52-264 7.96e-45

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: 161.95  E-value: 7.96e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  52 PKNIKKNRYKDILPYDYSRVelSLITSDED---SSYINANFIKGvYG--PKAYIATQGPLSTTLLDFWRMIWEYSVLIIV 126
Cdd:cd14613   23 PGLVRKNRYKTILPNPHSRV--CLTSPDQDdplSSYINANYIRG-YGgeEKVYIATQGPTVNTVGDFWRMVWQERSPIIV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 127 MACMEYEMgKKKCERYWAEPgemQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14613  100 MITNIEEM-NEKCTEYWPEE---QVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 207 ELIWDV---RCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDG-----------------------EQYELVYNaV 260
Cdd:cd14613  176 QLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEgvvdilrttcqlrldrggmiqtcEQYQFVHH-V 254


                 ....
gi 767903700 261 LELF 264
Cdd:cd14613  255 LSLY 258
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 14-281 1.52e-44

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: 162.21  E-value: 1.52e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  14 AQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTV--AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIK 91
Cdd:cd14628   10 AYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFisANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  92 GVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYII 171
Cdd:cd14628   90 GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYIL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 172 RTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLL 247
Cdd:cd14628  168 REFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERM 247

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767903700 248 KdgeqyelvYNAVLELFK--RQMDVIRDKHSGTESQ 281
Cdd:cd14628  248 R--------YEGVVDIFQtvKMLRTQRPAMVQTEDQ 275
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 25-241 1.55e-44

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: 161.74  E-value: 1.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14626   12 ANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 105 PLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFN--SET 182
Cdd:cd14626   92 PLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYW--PIRGTETYGMIQVTLLDTVELATYSVRTFALYKNgsSEK 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767903700 183 RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14626  170 REVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVID 228
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 49-285 2.16e-44

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: 161.82  E-value: 2.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14629   48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 129 CMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14629  128 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTIRQFQFTDWPEQGVPKTGEGFI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 207 ELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLKdgeqyelvYNAVLELFK--RQMDVIRDKHSGTESQA 282
Cdd:cd14629  206 DFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMR--------YEGVVDMFQtvKTLRTQRPAMVQTEDQY 277


                 ...
gi 767903700 283 KHC 285
Cdd:cd14629  278 QLC 280
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 49-285 3.25e-44

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: 161.05  E-value: 3.25e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14627   48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 129 CMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14627  128 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 207 ELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLKdgeqyelvYNAVLELFK--RQMDVIRDKHSGTESQA 282
Cdd:cd14627  206 DFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMR--------YEGVVDIFQtvKMLRTQRPAMVQTEDEY 277


                 ...
gi 767903700 283 KHC 285
Cdd:cd14627  278 QFC 280
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 84-241 9.62e-44

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: 156.77  E-value: 9.62e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAE-PGEMQLEFGPFSVSC 160
Cdd:cd14538    1 YINASHIRIPVGGDTyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDsLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 161 EAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQedDSVPICIHCSAGCGRTGVIC 238
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKetGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGVLI 158


                 ...
gi 767903700 239 AID 241
Cdd:cd14538  159 TID 161
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 84-262 2.63e-43

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: 155.68  E-value: 2.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGvYGPK--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQleFGPFSVSCE 161
Cdd:cd14546    1 YINASTIYD-HDPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV--YHIYEVHLV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 162 AEKRKS-DYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCYQeDDSVPICIHCSAGCGRTGVI 237
Cdd:cd14546   78 SEHIWCdDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYR-GRSCPIVVHCSDGAGRTGTY 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767903700 238 CAIDYTWM------------------------LLKDGEQYELVYNAVLE 262
Cdd:cd14546  157 ILIDMVLNrmakgakeidiaatlehlrdqrpgMVKTKDQFEFVLTAVAE 205
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 84-281 7.02e-43

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: 154.30  E-value: 7.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMqleFGPFSVSCEAE 163
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLVET 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14555   78 EPLAEYVVRTFALerRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767903700 242 yTWMLLKDGEQYELVYNAVLELFKRQMDVIRdkhsgTESQ 281
Cdd:cd14555  158 -IMLDMAEREGVVDIYNCVKELRSRRVNMVQ-----TEEQ 191
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 26-272 7.09e-43

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 156.28  E-value: 7.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  26 NEFLKLKRQSTKYkadktyPTTVAEKPKNIKKNRYKDILPYDYSRVELSlitsDEDSSYINANFIKGVYGPKAYIATQGP 105
Cdd:cd14607    2 PLYLEIRNESHDY------PHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 106 LSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGP--FSVSCEAEKRKSDYIIRTLKVK-FNS-E 181
Cdd:cd14607   72 LPNTCCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLEnINSgE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 182 TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRcyqEDDSV-----PICIHCSAGCGRTGVICAIDYTWMLLKDGEQYEL- 255
Cdd:cd14607  152 TRTISHFHYTTWPDFGVPESPASFLNFLFKVR---ESGSLspehgPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDSVd 228

                        250
                 ....*....|....*..
gi 767903700 256 VYNAVLELFKRQMDVIR 272
Cdd:cd14607  229 IKQVLLDMRKYRMGLIQ 245
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 70-281 8.17e-43

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: 154.79  E-value: 8.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  70 RVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEM 149
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 150 qleFGPFSVSCEAEKRKSDYIIRTLKVK---FNsETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIH 226
Cdd:cd14631   81 ---YGDFKVTCVEMEPLAEYVVRTFTLErrgYN-EIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767903700 227 CSAGCGRTGVICAIDytwMLLKDGEQYELV--YNAVLELFKRQMDVIRdkhsgTESQ 281
Cdd:cd14631  157 CSAGAGRTGCYIVID---IMLDMAEREGVVdiYNCVKALRSRRINMVQ-----TEEQ 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 38-267 2.70e-42

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: 155.60  E-value: 2.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  38 YKADKTyPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGvYGPK--AYIATQGPLSTTLLDFWR 115
Cdd:cd14610   29 YQAEPN-ATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 116 MIWEYSVLIIVMACMEYEMGKKKCERYWAEPGE-----MQLEFGPFSVSCEaekrksDYIIRTLKVKF--NSETRTIYQF 188
Cdd:cd14610  107 MVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSnlyhiYEVNLVSEHIWCE------DFLVRSFYLKNlqTNETRTVTQF 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 189 HYKNWPDHDVPSSIDPILELIWDV-RCYQeDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGEQyELVYNAVLELFKRQ 267
Cdd:cd14610  181 HFLSWNDQGVPASTRSLLDFRRKVnKCYR-GRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAK-EIDIAATLEHLRDQ 258
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 84-241 4.32e-42

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: 152.44  E-value: 4.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAE 163
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYW--PADGSEEYGNFLVTQKSV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKV----------KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGR 233
Cdd:cd17668   79 QVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158


                 ....*...
gi 767903700 234 TGVICAID 241
Cdd:cd17668  159 TGTYIVLD 166
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 57-239 4.88e-42

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 152.76  E-value: 4.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  57 KNRYKDILPYDYSRVELSLITSDED-SSYINANFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEM 134
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 135 gKKKCERYWAEPGEMqleFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVrc 214
Cdd:cd14611   82 -NEKCVLYWPEKRGI---YGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV-- 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 767903700 215 yQED-----DSVPICIHCSAGCGRTGVICA 239
Cdd:cd14611  156 -EEDrlaspGRGPVVVHCSAGIGRTGCFIA 184
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 34-255 2.85e-41

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: 152.84  E-value: 2.85e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  34 QSTKYKADKTYptTVAEKPKNIKKNRYKDILPYDYSRVELsLITSDEDSSYINANFIKGVYGPKA--YIATQGPLSTTLL 111
Cdd:cd14599   20 QIPKKKADGVF--TTATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCH 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 112 DFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQ--LEFGPFSVSCEAEKRKSDYIIRTLKVK--FNSETRTIYQ 187
Cdd:cd14599   97 DFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHssATYGKFKVTTKFRTDSGCYATTGLKVKhlLSGQERTVWH 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767903700 188 FHYKNWPDHDVPSSID---PILELIWDVRCY-------QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGEQYEL 255
Cdd:cd14599  177 LQYTDWPDHGCPEEVQgflSYLEEIQSVRRHtnsmldsTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEV 254
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-285 3.13e-41

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 150.30  E-value: 3.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYW--AEPGEMQLEFGPFSVS 159
Cdd:cd14540    1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptLGGEHDALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 160 CEAEKRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-----RCYQEDD----SVPICIHCS 228
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSgqSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrHTNQDVAghnrNPPTLVHCS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767903700 229 AGCGRTGVICAIDYTWMLLKDGEQYELvyNAVLELFKRQmdviRDKHSGTESQAKHC 285
Cdd:cd14540  161 AGVGRTGVVILADLMLYCLDHNEELDI--PRVLALLRHQ----RMLLVQTLAQYKFV 211
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 25-241 3.70e-41

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: 152.17  E-value: 3.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14625   18 ANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 105 PLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFN--SET 182
Cdd:cd14625   98 PLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYW--PSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNgsSEK 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767903700 183 RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14625  176 REVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID 234
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 84-240 7.77e-41

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: 148.57  E-value: 7.77e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAE 163
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYW--PEDGSVSSGDITVELKDQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCYQEDDSVPICIHCSAGCGRTGVICAI 240
Cdd:cd14552   79 TDYEDYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCAL 158
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 84-291 8.41e-41

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: 148.69  E-value: 8.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGV--YGPKaYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCE 161
Cdd:cd14539    1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 162 AEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY---QEDDSVPICIHCSAGCGRTGV 236
Cdd:cd14539   80 SVRTTPTHVERIISIQHKdtRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHylqQRSLQTPIVVHCSSGVGRTGA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903700 237 ICaidytwmllkdgeqyeLVYNAVLEL-----------FKRQMdvirdkhsgtESQAKHCIPEKNH 291
Cdd:cd14539  160 FC----------------LLYAAVQEIeagngipdlpqLVRKM----------RQQRKYMLQEKEH 199
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 59-240 8.63e-41

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: 149.42  E-value: 8.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  59 RYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKK 138
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 139 CERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCY 215
Cdd:cd14623   81 CAQYW--PSDGSVSYGDITIELKKEEECESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVqKQQ 158

                        170       180
                 ....*....|....*....|....*
gi 767903700 216 QEDDSVPICIHCSAGCGRTGVICAI 240
Cdd:cd14623  159 QQSGNHPITVHCSAGAGRTGTFCAL 183
PHA02738 PHA02738
hypothetical protein; Provisional
 33-241 1.15e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 152.00  E-value: 1.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  33 RQSTKYKADKTYPTTVAEKpKNIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLD 112
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEK-KNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 113 FWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE-TRTIYQFHYK 191
Cdd:PHA02738 106 FYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFT 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903700 192 NWPDHDVPSSIDPILELIWDVRCYQED-------------DSVPICIHCSAGCGRTGVICAID 241
Cdd:PHA02738 186 AWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVD 248
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 84-267 9.78e-40

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: 145.35  E-value: 9.78e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAE 163
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKVKFNSET---RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAI 240
Cdd:cd14557   81 KICPDYIIRKLNINNKKEKgsgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                        170       180
                 ....*....|....*....|....*..
gi 767903700 241 DYTWMLLkDGEQYELVYNAVLELfKRQ 267
Cdd:cd14557  161 DAMLEGL-EAEGRVDVYGYVVKL-RRQ 185
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 25-241 1.10e-39

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: 148.34  E-value: 1.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14624   18 ANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 105 PLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFN--SET 182
Cdd:cd14624   98 ALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYW--PSRGTETYGLIQVTLLDTVELATYCVRTFALYKNgsSEK 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767903700 183 RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14624  176 REVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID 234
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 84-256 3.52e-38

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: 140.99  E-value: 3.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEmqlEFGPFSVSCEAE 163
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK---TYGDIEVELKDT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDD------SVPICIHCSAGCGRTG 235
Cdd:cd14558   78 EKSPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKnskhgrSVPIVVHCSDGSSRTG 157

                        170       180
                 ....*....|....*....|.
gi 767903700 236 VICAIdytWMLLKDGEQYELV 256
Cdd:cd14558  158 IFCAL---WNLLESAETEKVV 175
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 49-241 1.24e-37

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: 142.86  E-value: 1.24e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14621   47 ASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 129 CMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAEKRKSDYIIRTL------KVKFNSETRTIYQFHYKNWPDHDVPSSI 202
Cdd:cd14621  127 TNLKERKECKCAQYW--PDQGCWTYGNIRVSVEDVTVLVDYTVRKFciqqvgDVTNKKPQRLITQFHFTSWPDFGVPFTP 204

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767903700 203 DPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14621  205 IGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVID 243
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 84-252 1.72e-37

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 139.31  E-value: 1.72e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKA----YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQlEFGPFSVS 159
Cdd:cd14601    2 YINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-SYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 160 CEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVI 237
Cdd:cd14601   81 CHSEEGNPAYVFRemTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                        170
                 ....*....|....*
gi 767903700 238 CAIDyTWMLLKDGEQ 252
Cdd:cd14601  161 ITME-TAMCLIECNQ 174
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 84-281 3.65e-37

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: 138.26  E-value: 3.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMqleFGPFSVSCEAE 163
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT---YGDIKITLLKT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGviCAID 241
Cdd:cd14632   78 ETLAEYSVRTFALERRgySARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTG--CYIV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767903700 242 YTWML-LKDGEQYELVYNAVLELFKRQMDVIRdkhsgTESQ 281
Cdd:cd14632  156 LDVMLdMAECEGVVDIYNCVKTLCSRRINMIQ-----TEEQ 191
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
13-240 3.77e-36

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 137.92  E-value: 3.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  13 EAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNikknRYKDILPYDYSRVElslitsdEDSSYINANFIKg 92
Cdd:COG5599    5 NPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLN----RFRDIQPYKETALR-------ANLGYLNANYIQ- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  93 VYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK--KKCERYWAEPGEMqlefgpFSVSCEAEKRKSDYI 170
Cdd:COG5599   73 VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDGEY------GKYEVSSELTESIQL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 171 -----IRTLKVKFNS---ETRTIYQFHYKNWPDHDVPSSiDPILELIWDVRCYQEDDSV---PICIHCSAGCGRTGVICA 239
Cdd:COG5599  147 rdgieARTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIA 225


                 .
gi 767903700 240 I 240
Cdd:COG5599  226 C 226
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 84-265 4.82e-36

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: 135.26  E-value: 4.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCE 161
Cdd:cd14596    1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 162 AEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIwdvrCYQED--DSVPICIHCSAGCGRTGVI 237
Cdd:cd14596   81 NYQALQYFIIRIIKLveKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFI----CYMRKvhNTGPIVVHCSAGIGRAGVL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767903700 238 CAIDYTWMLLKDG-----------------------EQYELVYNAVLELFK 265
Cdd:cd14596  157 ICVDVLLSLIEKDlsfnikdivremrqqrygmiqtkDQYLFCYKVVLEVLQ 207
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 60-241 1.10e-35

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: 135.07  E-value: 1.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  60 YKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKC 139
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 140 ERYWAEPGemQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSE-----TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 214
Cdd:cd14620   81 YQYWPDQG--CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPdgckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                        170       180
                 ....*....|....*....|....*..
gi 767903700 215 YQEDDSVPICIHCSAGCGRTGVICAID 241
Cdd:cd14620  159 VNPVHAGPIVVHCSAGVGRTGTFIVID 185
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 84-241 4.53e-35

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: 132.15  E-value: 4.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMaCMEYEMGKKKCERYWAEPGemQLEFGPFSVSCEAE 163
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVM-LNQLDPKDQSCPQYWPDEG--SGTYGPIQVEFVST 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKV----KFNSETRTIYQFHYKNWPDH-DVPSSIDPILELIWDVRCYQED-DSVPICIHCSAGCGRTGVI 237
Cdd:cd14556   78 TIDEDVISRIFRLqnttRPQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRSGVF 157


                 ....
gi 767903700 238 CAID 241
Cdd:cd14556  158 CAIS 161
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 44-241 4.65e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 132.43  E-value: 4.65e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  44 YPTTVAEKPKNIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:PHA02742  42 FSCNESLELKNMKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 124 IIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKfNSETRT---IYQFHYKNWPDHDVPS 200
Cdd:PHA02742 120 VIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLT-DTNTGAsldIKHFAYEDWPHGGLPR 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767903700 201 SIDPILELIWDVRCYQEDDSV-----------PICIHCSAGCGRTGVICAID 241
Cdd:PHA02742 199 DPNKFLDFVLAVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAID 250
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 50-241 1.92e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 130.89  E-value: 1.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  50 EKPKNIKKNRYKDILPYDYSRVELSlITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMAC 129
Cdd:PHA02747  47 EKPENQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 130 -MEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:PHA02747 126 pTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEItdKILKDSRKISHFQCSEWFEDETPSDHPDFI 205

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767903700 207 ELIWDV--------RCYQEDDSV--PICIHCSAGCGRTGVICAID 241
Cdd:PHA02747 206 KFIKIIdinrkksgKLFNPKDALlcPIVVHCSDGVGKTGIFCAVD 250
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 84-240 3.61e-33

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: 127.04  E-value: 3.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWaePGEMQLEFGPFSVSCEAE 163
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYW--PSEGSVTHGEITIEIKND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCYQEDDSVPICIHCSAGCGRTGVICAI 240
Cdd:cd14622   80 TLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 84-267 6.99e-33

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 126.63  E-value: 6.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQ--LEFGPFSVS 159
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 160 CEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSID---PILELIWDVRCYQEDDS------VPICIHCS 228
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKhlLTGQERTVWHLQYTDWPEHGCPEDLKgflSYLEEIQSVRRHTNSTIdpkspnPPVLVHCS 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767903700 229 AGCGRTGVICAIDYTWMLLKDGEQYELvyNAVLELFKRQ 267
Cdd:cd14598  161 AGVGRTGVVILSEIMIACLEHNEMLDI--PRVLDMLRQQ 197
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 51-241 1.01e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 129.38  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  51 KPKNIKKNRYKDILPYDYSRVELS------------------LITS-DEDSSYINANFIKGVYGPKAYIATQGPLSTTLL 111
Cdd:PHA02746  48 KKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkiEVTSeDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 112 DFWRMIWEYSVLIIVmACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKV--KFNSETRTIYQFH 189
Cdd:PHA02746 128 DFFKLISEHESQVIV-SLTDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMItdKISDTSREIHHFW 206

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903700 190 YKNWPDHDVPSSIDPILELIWDVRCYQ-------EDDSV---PICIHCSAGCGRTGVICAID 241
Cdd:PHA02746 207 FPDWPDNGIPTGMAEFLELINKVNEEQaelikqaDNDPQtlgPIVVHCSAGIGRAGTFCAID 268
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 84-241 4.19e-31

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: 120.79  E-value: 4.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQleFGPFSVSCEAE 163
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWT--YGNLRVRVEDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKV-KFNSET-----RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVI 237
Cdd:cd14551   79 VVLVDYTTRKFCIqKVNRGIgekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158


                 ....
gi 767903700 238 CAID 241
Cdd:cd14551  159 IVID 162
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 84-243 6.70e-30

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 117.57  E-value: 6.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKG---VYGPKaYIATQGPLSTTLLDFWRMIWEYSVLIIVMAC-MEYEMGKKKCERYWAEPGEMQLEFGPFSVS 159
Cdd:cd17658    1 YINASLVETpasESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrLVDNYSTAKCADYFPAEENESREFGRISVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 160 CEAEKRKSDYI-IRTLKVKFNS---ETRTIYQFHYKNWPDHDVPSSIDPILELIwdVRCYQEDDSV-PICIHCSAGCGRT 234
Cdd:cd17658   80 NKKLKHSQHSItLRVLEVQYIEseePPLSVLHIQYPEWPDHGVPKDTRSVRELL--KRLYGIPPSAgPIVVHCSAGIGRT 157


                 ....*....
gi 767903700 235 GVICAIDYT 243
Cdd:cd17658  158 GAYCTIHNT 166
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
184-262 3.28e-24

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 97.81  E-value: 3.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700   184 TIYQFHYKNWPDHDVPSSIDPILELIWDVR--CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDG----------- 250
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifdtvk 80

                           90       100
                   ....*....|....*....|....*
gi 767903700   251 -------------EQYELVYNAVLE 262
Cdd:smart00404  81 elrsqrpgmvqteEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 184-262 3.28e-24

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: 97.81  E-value: 3.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700   184 TIYQFHYKNWPDHDVPSSIDPILELIWDVR--CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDG----------- 250
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEagevdifdtvk 80

                           90       100
                   ....*....|....*....|....*
gi 767903700   251 -------------EQYELVYNAVLE 262
Cdd:smart00012  81 elrsqrpgmvqteEQYLFLYRALLE 105
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 84-248 3.59e-23

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 98.17  E-value: 3.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMaCMEYEMgKKKCERYWAEPGemQLEFGPFSVSCEAE 163
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-LNEVDL-AQGCPQYWPEEG--MLRYGPIQVECMSC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKVKFNSETRTIY----QFHYKNWPDH-DVPSSIDPILELIWDVRCYQED----DSVPIcIHCSAGCGRT 234
Cdd:cd14636   77 SMDCDVISRIFRICNLTRPQEGYlmvqQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdegEGRTI-IHCLNGGGRS 155

                        170
                 ....*....|....
gi 767903700 235 GVICAIDYTWMLLK 248
Cdd:cd14636  156 GMFCAISIVCEMIK 169
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 84-240 1.66e-19

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 87.38  E-value: 1.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMaCMEYEMGKKKCErYWAEPGEmQLEFGPFSVSCEAE 163
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVM-LTDNELNEDEPI-YWPTKEK-PLECETFKVTLSGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKS----------DYIIRTLKVKFNSETRtiyQFHYKNWPDHDVPssIDPILELIWDVRCYQEDDSVPICIHCSAGCGR 233
Cdd:cd14550   78 DHSClsneirlivrDFILESTQDDYVLEVR---QFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQ 152


                 ....*..
gi 767903700 234 TGVICAI 240
Cdd:cd14550  153 AATFCAL 159
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 84-240 3.32e-18

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: 83.92  E-value: 3.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMAcmeYEMGKKK-CERYWaePGEMQLEFGPFSVSCEA 162
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML---NEMDAAQlCMQYW--PEKTSCCYGPIQVEFVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 163 EKRKSDYIIRTLKV----KFNSETRTIYQFHYKNWPDH-DVPSSIDPILELIWDVRCYQED---DSVPICIHCSAGCGRT 234
Cdd:cd14634   76 ADIDEDIISRIFRIcnmaRPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGGGRS 155


                 ....*.
gi 767903700 235 GVICAI 240
Cdd:cd14634  156 GTFCAI 161
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 84-263 8.74e-18

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 82.43  E-value: 8.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMacMEYEMGKKKCERYWAEPGEMQleFGPFSVSCEAE 163
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVM--LNDVDPAQLCPQYWPENGVHR--HGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 164 KRKSDYIIRTLKVkFNSET-----RTIYQFHYKNWPDH-DVPSSIDPILELIWDVRCYQED---DSVPICIHCSAGCGRT 234
Cdd:cd14635   77 DLEEDIISRIFRI-YNAARpqdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGGRS 155

                        170       180
                 ....*....|....*....|....*....
gi 767903700 235 GVICAIDYTWMLLKDGEQYElVYNAVLEL 263
Cdd:cd14635  156 GTFCAISIVCEMLRHQRAVD-VFHAVKTL 183
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 84-261 3.00e-17

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: 80.81  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCErYWAEPGE-MQLEfgPFSVSCEA 162
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpINCE--TFKVTLIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 163 EKRK----------SDYIIRTLKVKFNSETRtiyQFHYKNWPDHDVPssIDPILELIWDVRCYQEDDSVPICIHCSAGCG 232
Cdd:cd17669   78 EEHKclsneekliiQDFILEATQDDYVLEVR---HFQCPKWPNPDSP--ISKTFELISIIKEEAANRDGPMIVHDEHGGV 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767903700 233 RTGVICAIdYTWM------------------------LLKDGEQYELVYNAVL 261
Cdd:cd17669  153 TAGTFCAL-TTLMhqlekensvdvyqvakminlmrpgVFTDIEQYQFLYKAIL 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 84-239 4.49e-17

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 80.72  E-value: 4.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMAC-MEYEMGKKKCERYWAEPGEMQleFGPFSVSCEA 162
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqLNQSNSAWPCLQYWPEPGLQQ--YGPMEVEFVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 163 EKRKSDYIIRTLKVK----FNSETRTIYQFHYKNW-PDHDVPSSIDPILELIWDVRCYQEDDSV-PICIHCSAGCGRTGV 236
Cdd:cd14637   79 GSADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEgRTVVHCLNGGGRSGT 158


                 ...
gi 767903700 237 ICA 239
Cdd:cd14637  159 YCA 161
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 84-240 2.57e-15

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: 75.49  E-value: 2.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMacMEYEMGKKKCER-YWAEPGE-MQLEfgPFSVSCE 161
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM--LPDNQGLAEDEFvYWPSREEsMNCE--AFTVTLI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 162 AEKRK----------SDYIIRTLKVKFNSETRtiyQFHYKNWPDHDVPssIDPILELIWDVRCYQEDDSVPICIHCSAGC 231
Cdd:cd17670   77 SKDRLclsneeqiiiHDFILEATQDDYVLEVR---HFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEFGA 151


                 ....*....
gi 767903700 232 GRTGVICAI 240
Cdd:cd17670  152 VSAGTLCAL 160
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 58-239 1.25e-09

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 59.34  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  58 NRYKDIlpydYSRVELSlitsdeDSSYINANFIKgVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKK 137
Cdd:cd14559    1 NRFTNI----QTRVSTP------VGKNLNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 138 KCERYWAEPGEmqleFGpfSVSCEAEKRKSDYIIR-------TLKVKFNSETRTIYQFHYKNWPDHDVPSSID------- 203
Cdd:cd14559   70 GLPPYFRQSGT----YG--SVTVKSKKTGKDELVDglkadmyNLKITDGNKTITIPVVHVTNWPDHTAISSEGlkeladl 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767903700 204 ---------PILELIWDVRCYQEDDSVPIcIHCSAGCGRTGVICA 239
Cdd:cd14559  144 vnksaeekrNFYKSKGSSAINDKNKLLPV-IHCRAGVGRTGQLAA 187
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 49-241 8.77e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 51.51  E-value: 8.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700  49 AEKPKNIKKNRYKD------ILPYDYSRVELSlitsdEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSV 122
Cdd:PHA02740  42 ANKACAQAENKAKDenlalhITRLLHRRIKLF-----NDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 123 LIIVMACMEYEmgKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKV--KFNSEtRTIYQFHYKNWP----DH 196
Cdd:PHA02740 117 QIIVLISRHAD--KKCFNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLtdKFGQA-QKISHFQYTAWPadgfSH 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767903700 197 DVPSSID---PILELIWDVRCYQEDDSV-PICIHCSAGCGRTGVICAID 241
Cdd:PHA02740 194 DPDAFIDffcNIDDLCADLEKHKADGKIaPIIIDCIDGISSSAVFCVFD 242
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 187-267 1.65e-05

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 45.65  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903700 187 QFHYKNWPDHDVPSsidpiLELIWDVrCY------QEDDSVPICIHCSAGCGRTG-VICAidytwMLLKDGeQYELVYNA 259
Cdd:cd14497   62 RVLHYGFPDHHPPP-----LGLLLEI-VDdidswlSEDPNNVAVVHCKAGKGRTGtVICA-----YLLYYG-QYSTADEA 129


                 ....*...
gi 767903700 260 vLELFKRQ 267
Cdd:cd14497  130 -LEYFAKK 136
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
193-239 1.43e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 42.65  E-value: 1.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767903700 193 WPDHDVPS--SIDPILELIWdvRCYQEDDSVpiCIHCSAGCGRTGVICA 239
Cdd:COG2453   55 IPDFGAPDdeQLQEAVDFID--EALREGKKV--LVHCRGGIGRTGTVAA 99
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 203-252 3.78e-04

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 40.80  E-value: 3.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767903700 203 DPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGEQ 252
Cdd:cd14494   39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEE 88
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 194-254 4.18e-03

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 38.88  E-value: 4.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903700 194 PDHDVPSsIDPILELIWDVRCY-QEDDSVPICIHCSAGCGRTG-VICAidytWMLlkDGEQYE 254
Cdd:cd14510   82 DDHNVPT-LDEMLSFTAEVREWmAADPKNVVAIHCKGGKGRTGtMVCA----WLI--YSGQFE 137
PFA-DSP_Oca2 cd17661
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2; ...
 179-240 4.76e-03

atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2; Oxidant-induced cell-cycle arrest protein 2 (Oca2) is an atypical dual specificity phosphatase of unknown function. It has been identified as a putative negative regulator acting on cell wall integrity and mating MAPK pathways in yeast. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca2 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif.


Pssm-ID: 350499 [Multi-domain]  Cd Length: 146  Bit Score: 38.15  E-value: 4.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767903700 179 NSETRTIYQFHYKNWPDHDVP---SSIDPILELIWDVRCYqeddsvPICIHCSAGCGRTGVICAI 240
Cdd:cd17661   53 QSQGIELYYFDFSSSSEPFTEedqERMEQALKLLLDKRNY------PILVHSNKGKHRVGVLVGI 111
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 188-239 7.53e-03

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 37.95  E-value: 7.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767903700 188 FHYK--NWP--DHDVPSsIDPILELIWDVRCY-QEDDSVPICIHCSAGCGRTGV-ICA 239
Cdd:cd14509   58 FNGRvaEYPfdDHNPPP-LELIKPFCEDVDEWlKEDEKNVAAVHCKAGKGRTGVmICC 114
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
189-240 9.32e-03

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 38.79  E-value: 9.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767903700 189 HYKNWPDHDVPSSIDPILELIwdvrcyQEDDSVPICIHCSAGCGRTGVICAI 240
Cdd:COG2365  108 LYRAFVDPDAADAYRAAFRAL------ADAENGPVLFHCTAGKDRTGVAAAL 153
 
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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