NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157824150|ref|NP_001099930|]
View 

tyrosine-protein phosphatase non-receptor type 22 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 3.59e-174

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: 500.14  E-value: 3.59e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  57 KNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 137 KKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQ 216
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157824150 217 EDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELF 290
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 539-800 2.32e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.91  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  539 SSSPPNSAGSKMSFDLPEKQDGATSP--GAQLPASSAASSSYSNPRDSLMESTLTS--FPPPINQETAIEATSARTDDEI 614
Cdd:pfam05109 491 SPSPRDNGTESKAPDMTSPTSAVTTPtpNATSPTPAVTTPTPNATSPTLGKTSPTSavTTPTPNATSPTPAVTTPTPNAT 570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  615 PPPLPERTPESFIVAEAAGEPSPSITESLPLAGKSGVTLecGGTSESQshdlvAFTSSKNVELGSPKSDQHQDGSppppl 694
Cdd:pfam05109 571 IPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTL--GGTSSTP-----VVTSPPKNATSAVTTGQHNITS----- 638

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  695 pertlesffladeDCIQAQPMKPSSIS---YPETTEISTSSKQTLK----TPGKSFTRSKSLKIFRNMKKSVCNSPSPSK 767
Cdd:pfam05109 639 -------------SSTSSMSLRPSSISetlSPSTSDNSTSHMPLLTsahpTGGENITQVTPASTSTHHVSTSSPAPRPGT 705

                         250       260       270
                  ....*....|....*....|....*....|...
gi 157824150  768 PTECVQPKNSSSFLNFGfGTRFSKPKGPRNPPS 800
Cdd:pfam05109 706 TSQASGPGNSSTSTKPG-EVNVTKGTPPKNATS 737
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 3.59e-174

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: 500.14  E-value: 3.59e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  57 KNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 137 KKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQ 216
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157824150 217 EDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELF 290
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-288 4.60e-114

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 346.57  E-value: 4.60e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150    24 FANEFLKLKRQstkykADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTsDEDSSYINASFIKGVYGPRAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150   104 GPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKAKF--NSE 181
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150   182 TRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGiipKNFSVFNL 261
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 157824150   262 IQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-288 1.77e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.42  E-value: 1.77e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150   54 NIKKNRYKDILPYDHSLVELSllTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  134 MGKKKCERYWAEPGETQLQFGPFSISCETEKK-KSDYKIRTL--KAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIW 210
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEdEKDYTVRTLevSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157824150  211 DMRCYQEDDCV-PLCIHCSAGCGRTGVICAVDYTWMLLKDGIIpknFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:pfam00102 159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
12-297 3.27e-44

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 161.03  E-value: 3.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  12 KEAQKKKINREEFANEFLKLKRQSTKYKADKIYPTTVAQRPKNikknRYKDILPYDHSLVElslltsdEDSSYINASFIK 91
Cdd:COG5599    4 KNPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLN----RFRDIQPYKETALR-------ANLGYLNANYIQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  92 gVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVM--ACMEFEMGKKKCERYWAEPGETqlqfgpFSISCETEKKKSDY 169
Cdd:COG5599   73 -VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGEY------GKYEVSSELTESIQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 170 -------KIRTLKAKFNS-ETRIVYQFHYKNWPDHDVPSS--IDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICA 239
Cdd:COG5599  146 lrdgieaRTYVLTIKGTGqKKIEIPVLHVKNWPDHGAISAeaLKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIA 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 240 VDYTWMLLKDGIIpKNFSVFNLIQEMRTQR-PSLVQTQEQY-ELVysavlELFKRHVDII 297
Cdd:COG5599  226 CLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQLdVLV-----KLAEQQIRPL 279
PHA02738 PHA02738
hypothetical protein; Provisional
 33-296 1.41e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 143.14  E-value: 1.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  33 RQSTKYKADKIYPTTVAQRpKNIKKNRYKDILPYDHSLVELSllTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLD 112
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEK-KNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 113 FWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSE-TRIVYQFHYK 191
Cdd:PHA02738 106 FYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFT 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 192 NWPDHDVPSSIDPILQLIWDMRCYQED-------------DCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGiipKNFSV 258
Cdd:PHA02738 186 AWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDAC---ATVSI 262

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 157824150 259 FNLIQEMRTQRPSLVQTQEQYELVYSAVlelfKRHVDI 296
Cdd:PHA02738 263 PSIVSSIRNQRYYSLFIPFQYFFCYRAV----KRYVNL 296
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 539-800 2.32e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.91  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  539 SSSPPNSAGSKMSFDLPEKQDGATSP--GAQLPASSAASSSYSNPRDSLMESTLTS--FPPPINQETAIEATSARTDDEI 614
Cdd:pfam05109 491 SPSPRDNGTESKAPDMTSPTSAVTTPtpNATSPTPAVTTPTPNATSPTLGKTSPTSavTTPTPNATSPTPAVTTPTPNAT 570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  615 PPPLPERTPESFIVAEAAGEPSPSITESLPLAGKSGVTLecGGTSESQshdlvAFTSSKNVELGSPKSDQHQDGSppppl 694
Cdd:pfam05109 571 IPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTL--GGTSSTP-----VVTSPPKNATSAVTTGQHNITS----- 638

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  695 pertlesffladeDCIQAQPMKPSSIS---YPETTEISTSSKQTLK----TPGKSFTRSKSLKIFRNMKKSVCNSPSPSK 767
Cdd:pfam05109 639 -------------SSTSSMSLRPSSISetlSPSTSDNSTSHMPLLTsahpTGGENITQVTPASTSTHHVSTSSPAPRPGT 705

                         250       260       270
                  ....*....|....*....|....*....|...
gi 157824150  768 PTECVQPKNSSSFLNFGfGTRFSKPKGPRNPPS 800
Cdd:pfam05109 706 TSQASGPGNSSTSTKPG-EVNVTKGTPPKNATS 737
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 3.59e-174

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: 500.14  E-value: 3.59e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  57 KNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 137 KKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQ 216
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157824150 217 EDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELF 290
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2-294 1.89e-162

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: 472.88  E-value: 1.89e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150   2 DQREILQQLLKEAQKKKI---NREE-FANEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLT 77
Cdd:cd14604    1 EQVEILKKFIERVQAMKStdhNGEDnFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  78 SDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFS 157
Cdd:cd14604   81 SSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 158 ISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVI 237
Cdd:cd14604  161 ISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157824150 238 CAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELFKRHV 294
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; ...
 84-283 6.69e-137

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: 403.34  E-value: 6.69e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCETE 163
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKS-DYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDY 242
Cdd:cd14542   81 KRVGpDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 157824150 243 TWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14542  161 VWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 25-290 1.40e-127

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: 381.87  E-value: 1.40e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  25 ANEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQG 104
Cdd:cd14603    1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 105 PLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETqLQFGPFSIS-CETEKKKSDYKIRTLKAKFNSETR 183
Cdd:cd14603   81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEP-LQTGPFTITlVKEKRLNEEVILRTLKVTFQKESR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 184 IVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQ 263
Cdd:cd14603  160 SVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVL 239

                        250       260
                 ....*....|....*....|....*..
gi 157824150 264 EMRTQRPSLVQTQEQYELVYSAVLELF 290
Cdd:cd14603  240 EMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-288 4.60e-114

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 346.57  E-value: 4.60e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150    24 FANEFLKLKRQstkykADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTsDEDSSYINASFIKGVYGPRAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150   104 GPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKAKF--NSE 181
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150   182 TRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGiipKNFSVFNL 261
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 157824150   262 IQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-288 1.77e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.42  E-value: 1.77e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150   54 NIKKNRYKDILPYDHSLVELSllTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  134 MGKKKCERYWAEPGETQLQFGPFSISCETEKK-KSDYKIRTL--KAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIW 210
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEdEKDYTVRTLevSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157824150  211 DMRCYQEDDCV-PLCIHCSAGCGRTGVICAVDYTWMLLKDGIIpknFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:pfam00102 159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 84-283 1.22e-88

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: 278.01  E-value: 1.22e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCETE 163
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTLKAKF--NSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVD 241
Cdd:cd00047   81 EELSDYTIRTLELSPkgCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 157824150 242 YTWMLLKDGiipKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd00047  161 ILLERLEAE---GEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 59-279 4.35e-70

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 229.93  E-value: 4.35e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  59 RYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKK 138
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 139 CERYWAEpGETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQED 218
Cdd:cd14548   81 CDHYWPF-DQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157824150 219 DCVPLCIHCSAGCGRTGVICAVDYtwmlLKDGIIPKNF-SVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:cd14548  160 EKGPTIVHCSAGVGRTGTFIALDR----LLQQIESEDYvDIFGIVYDLRKHRPLMVQTEAQY 217
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 52-284 1.45e-69

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: 230.33  E-value: 1.45e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  52 PKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACME 131
Cdd:cd14543   27 PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 132 FEMGKKKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKAkFNSET---RIVYQFHYKNWPDHDVPSSIDPILQL 208
Cdd:cd14543  107 VERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEI-HNTETdesRQVTHFQFTSWPDFGVPSSAAALLDF 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 209 IWDMRCYQEDDCV-------------PLCIHCSAGCGRTGVICAVDYTWMLLKD-GIIpknfSVFNLIQEMRTQRPSLVQ 274
Cdd:cd14543  186 LGEVRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDvGTL----NVMQTVRRMRTQRAFSIQ 261

                        250
                 ....*....|
gi 157824150 275 TQEQYELVYS 284
Cdd:cd14543  262 TPDQYYFCYK 271
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 84-283 1.15e-65

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: 217.50  E-value: 1.15e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIK-GVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEpGETQLQFGPFSISC-- 160
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-GEYEGEYGDLTVELvs 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 161 ETEKKKSDYKIRTLK-AKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIwdmRC-----YQEDDCVPLCIHCSAGCGRT 234
Cdd:cd18533   80 EEENDDGGFIVREFElSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLI---KLkrelnDSASLDPPIIVHCSAGVGRT 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157824150 235 GVICAVDyTWM-LLKDGIIPKNFS------VFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd18533  157 GTFIALD-SLLdELKRGLSDSQDLedsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 54-286 4.08e-64

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: 215.02  E-value: 4.08e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  54 NIKKNRYKDILPYDHSLVELSLLTSDED-SSYINASFIKGVY-GPRA------YIATQGPLSTTLLDFWRMIWEYRVLVI 125
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIRNENeGPTTdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 126 VMACMEFEMGKKKCERYWAEPGETQlQFGPFSISCETEKKKSDYKIRTL---KAKFNSETRIVYQFHYKNWPDHDVPSSI 202
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELqvsKLDQGDPIREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 203 DPILQLIWDMRCYQE--DDCVPLCIHCSAGCGRTGVICAVDytwMLLKdgIIPKN-----FSVFNLIQEMRTQRPSLVQT 275
Cdd:cd14544  160 GGVLNFLEDVNQRQEslPHAGPIVVHCSAGIGRTGTFIVID---MLLD--QIKRKgldcdIDIQKTIQMVRSQRSGMVQT 234

                        250
                 ....*....|.
gi 157824150 276 QEQYELVYSAV 286
Cdd:cd14544  235 EAQYKFIYVAV 245
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 58-283 4.33e-61

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: 205.71  E-value: 4.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  58 NRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYG-PRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMgK 136
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 137 KKCERYWaePGETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCY- 215
Cdd:cd14547   80 EKCAQYW--PEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEAr 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 216 -QEDDCVPLCIHCSAGCGRTGVICAVDY-TWMLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14547  158 qTEPHRGPIVVHCSAGIGRTGCFIATSIgCQQLREEGVV----DVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 54-288 6.39e-61

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: 205.71  E-value: 6.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  54 NIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFE 133
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 134 MGKKKCERYWaePGETQLQFGPFSISCETEKKKSDYKIRTLKAKFN--SETRIVYQFHYKNWPDHDVPSSIDPILQLIWD 211
Cdd:cd14553   83 RSRVKCDQYW--PTRGTETYGLIQVTLLDTVELATYTVRTFALHKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157824150 212 MRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGiipKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14553  161 VKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHE---KTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 58-289 6.08e-60

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: 202.81  E-value: 6.08e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  58 NRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKK 137
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 138 KCERYWaePGETQ-LQFGPFSISCETEKKKSDYKIR--TLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLiWDM-R 213
Cdd:cd14619   81 KCEHYW--PLDYTpCTYGHLRVTVVSEEVMENWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAF-RRLlR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157824150 214 CY--QEDDCVPLCIHCSAGCGRTGVICAVDYtwmLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLEL 289
Cdd:cd14619  158 QWldQTMSGGPTVVHCSAGVGRTGTLIALDV---LLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 53-288 1.60e-59

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: 201.79  E-value: 1.60e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  53 KNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEF 132
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 133 EMGKKKCERYWaePGETQLqFGPFSISCETEKKKSDYKIR--TLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIW 210
Cdd:cd14630   82 EVGRVKCVRYW--PDDTEV-YGDIKVTLIETEPLAEYVIRtfTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157824150 211 DMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTW-MLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14630  159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLdMAENEGVV----DIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 84-279 1.64e-57

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: 195.26  E-value: 1.64e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCETE 163
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYW--PKEGTETYGNIQVTLLST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTL--------KAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTG 235
Cdd:cd14549   79 EVLATYTVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 157824150 236 VICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:cd14549  159 TYIVIDSMLQQIQD---KGTVNVFGFLKHIRTQRNYLVQTEEQY 199
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 49-287 6.31e-57

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 194.67  E-value: 6.31e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  49 AQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMA 128
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 129 CMEFEMGKKKCERYWaePGETQLQFGPFSISCETEKKKSDYKIRTLKAK--FNSETRIVYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14554   81 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 207 QLIWDM-RCYQEDDCV-PLCIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14554  159 DFIGQVhKTKEQFGQEgPITVHCSAGVGRTGVFITLSIVLERMRyEGVV----DVFQTVKLLRTQRPAMVQTEDQYQFCY 234


                 ....
gi 157824150 284 SAVL 287
Cdd:cd14554  235 RAAL 238
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 84-288 7.11e-57

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: 193.36  E-value: 7.11e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYG--PRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAE-PGETQLQFGPFSISC 160
Cdd:cd14538    1 YINASHIRIPVGgdTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDsLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 161 ETEKKKSDYKIR--TLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDdcVPLCIHCSAGCGRTGVIC 238
Cdd:cd14538   81 EKYQSLQDFVIRriSLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS--GPIVVHCSAGIGRTGVLI 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157824150 239 AVDYTWMLLKDGIipkNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14538  159 TIDVALGLIERDL---PFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 58-279 2.70e-56

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: 192.72  E-value: 2.70e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  58 NRYKDILPYDHSLVELSLLTSDEDSsYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKK 137
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTDD-YINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 138 KCERYWaePGETQLQFGPFSISCETEKKKSDYKIR--TLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPIL---QLIWD- 211
Cdd:cd14615   80 KCEEYW--PSKQKKDYGDITVTMTSEIVLPEWTIRdfTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLInfrHLVREy 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157824150 212 MRCYQEDDcvPLCIHCSAGCGRTGVICAVDY-TWMLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:cd14615  158 MKQNPPNS--PILVHCSAGVGRTGTFIAIDRlIYQIENENVV----DVYGIVYDLRMHRPLMVQTEDQY 220
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 24-288 2.72e-56

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: 194.48  E-value: 2.72e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  24 FANEFLKLKRQStkykADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDED--SSYINASFIKGVYGPRAYIA 101
Cdd:cd17667    1 FSEDFEEVQRCT----ADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 102 TQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCETEKKKSDYKIRTL------- 174
Cdd:cd17667   77 TQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYW--PTENSEEYGNIIVTLKSTKIHACYTVRRFsirntkv 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 175 ------KAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLK 248
Cdd:cd17667  155 kkgqkgNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIK 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 157824150 249 DgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd17667  235 D---KSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 20-288 4.30e-56

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: 194.10  E-value: 4.30e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  20 NREEFANEFLKLkrqsTKYKADkiyPTT--VAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGvYGPR 97
Cdd:cd14609   13 NRDRLAKEWQAL----CAYQAE---PNTcsTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  98 --AYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGET-----QLQFGPFSISCEtekkksDYK 170
Cdd:cd14609   85 mpAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSlyhiyEVNLVSEHIWCE------DFL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 171 IRT--LKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDM-RCYQEDDCvPLCIHCSAGCGRTGVICAVDYTWMLL 247
Cdd:cd14609  159 VRSfyLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVnKCYRGRSC-PIIVHCSDGAGRTGTYILIDMVLNRM 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 157824150 248 KDGIipKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14609  238 AKGV--KEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 50-288 2.20e-55

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: 191.63  E-value: 2.20e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  50 QRPKNIKKNRYKDILPYDHSLVELSLLTSD-EDSSYINASFIKG-VYG----PRAYIATQGPLSTTLLDFWRMIWEYRVL 123
Cdd:cd14606   14 QRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNqLLGpdenAKTYIASQGCLEATVNDFWQMAWQENSR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 124 VIVMACMEFEMGKKKCERYWAEPGeTQLQFGPFSISCETEKKKSDYKIRTLKAKF---NSETRIVYQFHYKNWPDHDVPS 200
Cdd:cd14606   94 VIVMTTREVEKGRNKCVPYWPEVG-MQRAYGPYSVTNCGEHDTTEYKLRTLQVSPldnGELIREIWHYQYLSWPDHGVPS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 201 SIDPILQLIWDMRCYQED--DCVPLCIHCSAGCGRTGVICAVDytwMLLkDGIIPK----NFSVFNLIQEMRTQRPSLVQ 274
Cdd:cd14606  173 EPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVID---MLM-ENISTKgldcDIDIQKTIQMVRAQRSGMVQ 248

                        250
                 ....*....|....
gi 157824150 275 TQEQYELVYSAVLE 288
Cdd:cd14606  249 TEAQYKFIYVAIAQ 262
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 45-287 5.45e-54

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: 187.02  E-value: 5.45e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  45 PTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLV 124
Cdd:cd14614    3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 125 IVMACMEFEMGKKKCERYW---AEPgetqLQFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPS- 200
Cdd:cd14614   83 IVMLTQCNEKRRVKCDHYWpftEEP----VAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTa 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 201 -SIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGiipKNFSVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:cd14614  159 nAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH---EFVDILGLVSEMRSYRMSMVQTEEQY 235


                 ....*...
gi 157824150 280 ELVYSAVL 287
Cdd:cd14614  236 IFIHQCVQ 243
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 53-287 8.06e-54

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: 186.19  E-value: 8.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  53 KNIKKNRYKDILPYDHSLVELSlltsdEDSSYINASFIKGVYGPR--AYIATQGPLSTTLLDFWRMIWEYRVLVIVMACM 130
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 131 EFEMGKKKCERYWAE-PGETQLQFGPFSISCETEKKKSDYKIRTLKAK--FNSETRIVYQFHYKNWPDHDVPSSIDPILQ 207
Cdd:cd14597   77 EVEGGKIKCQRYWPEiLGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 208 LIWDMRCYQEDDcvPLCIHCSAGCGRTGVICAVDYtwMLlkdGIIPKN--FSVFNLIQEMRTQRPSLVQTQEQYELVYSA 285
Cdd:cd14597  157 FISYMRHIHKSG--PIITHCSAGIGRSGTLICIDV--VL---GLISKDldFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                 ..
gi 157824150 286 VL 287
Cdd:cd14597  230 IL 231
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 44-288 2.97e-53

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: 186.00  E-value: 2.97e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  44 YPTTVAQRPKNIKKNRYKDILPYDHSLVELSLltsdEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVL 123
Cdd:cd14608   15 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 124 VIVMACMEFEMGKKKCERYWAEPGETQLQF--GPFSISCETEKKKSDYKIRTLKAK--FNSETRIVYQFHYKNWPDHDVP 199
Cdd:cd14608   91 GVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 200 SSIDPILQLIWDMRcyqEDDCV-----PLCIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQ 274
Cdd:cd14608  171 ESPASFLNFLFKVR---ESGSLspehgPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQ 247

                        250
                 ....*....|....
gi 157824150 275 TQEQYELVYSAVLE 288
Cdd:cd14608  248 TADQLRFSYLAVIE 261
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 57-283 7.06e-53

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: 183.36  E-value: 7.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  57 KNRYKDILPYDHSLVELSLltSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGK 136
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKL--KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 137 KKCERYWAePGETQ---LQFGPFSISCETEKKKSDYKIRTLK--AKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWD 211
Cdd:cd14545   79 IKCAQYWP-QGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLEleNLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157824150 212 MRCYQ--EDDCVPLCIHCSAGCGRTGVICAVDyTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14545  158 VRESGslSSDVGPPVVHCSAGIGRSGTFCLVD-TCLVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 53-286 9.92e-53

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: 184.07  E-value: 9.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  53 KNIKKNRYKDILPYDHSLVELSLLTSDED-SSYINASFIKGVYG--------PRAYIATQGPLSTTLLDFWRMIWEYRVL 123
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPvSDYINANIIMPEFEtkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 124 VIVMACMEFEMGKKKCERYWaePGETQL-QFGPFSISCETEKKKSDYKIRTLK----AKFNSEtRIVYQFHYKNWPDHDV 198
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYW--PDEYALkEYGVMRVRNVKESAAHDYILRELKlskvGQGNTE-RTVWQYHFRTWPDHGV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 199 PSSIDPILQLIWDMRCYQED--DCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQ 276
Cdd:cd14605  158 PSDPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTE 237

                        250
                 ....*....|
gi 157824150 277 EQYELVYSAV 286
Cdd:cd14605  238 AQYRFIYMAV 247
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 47-291 2.08e-52

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: 183.51  E-value: 2.08e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  47 TVAQRPKNIKKNRYKDILPYDHSLVelsLLTSDEDssYINASFIK----GVYGPRAYIATQGPLSTTLLDFWRMIWEYRV 122
Cdd:cd14600   33 TCAKLPQNMDKNRYKDVLPYDATRV---VLQGNED--YINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 123 LVIVMACMEFEMGKKKCERYWAEPGETqLQFGPFSISCETEKKKSDYKIR--TLKAKFNSETRIVYQFHYKNWPDHDVPS 200
Cdd:cd14600  108 SLIVMLTTLTERGRTKCHQYWPDPPDV-MEYGGFRVQCHSEDCTIAYVFRemLLTNTQTGEERTVTHLQYVAWPDHGVPD 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 201 SIDPILQLIWDMRCYQEDDcVPLCIHCSAGCGRTGVICAVDyTWMLLkdgiIPKNFSVFNL--IQEMRTQRPSLVQTQEQ 278
Cdd:cd14600  187 DSSDFLEFVNYVRSKRVEN-EPVLVHCSAGIGRTGVLVTME-TAMCL----TERNQPVYPLdiVRKMRDQRAMMVQTSSQ 260

                        250
                 ....*....|...
gi 157824150 279 YELVYSAVLELFK 291
Cdd:cd14600  261 YKFVCEAILRVYE 273
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 58-279 2.14e-52

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: 182.03  E-value: 2.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  58 NRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKK 137
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 138 KCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQE 217
Cdd:cd14616   81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157824150 218 DDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDgiipKNF-SVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:cd14616  161 HDNTPMIVHCSAGVGRTGVFIALDHLTQHIND----HDFvDIYGLVAELRSERMCMVQNLAQY 219
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 84-288 2.99e-52

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: 180.72  E-value: 2.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGvYGPR--AYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETqlQFGPFSISCE 161
Cdd:cd14546    1 YINASTIYD-HDPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE--VYHIYEVHLV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 162 TEKKKS-DYKIRT--LKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDM-RCYQEDDCvPLCIHCSAGCGRTGVI 237
Cdd:cd14546   78 SEHIWCdDYLVRSfyLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRSC-PIVVHCSDGAGRTGTY 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157824150 238 CAVDYTWMLLKDGIipKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14546  157 ILIDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 45-288 4.23e-52

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: 182.93  E-value: 4.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  45 PTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLV 124
Cdd:cd14633   31 PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 125 IVMACMEFEMGKKKCERYWaePGETQLqFGPFSISCETEKKKSDYKIRT--LKAKFNSETRIVYQFHYKNWPDHDVPSSI 202
Cdd:cd14633  111 IIMVTNLVEVGRVKCCKYW--PDDTEI-YKDIKVTLIETELLAEYVIRTfaVEKRGVHEIREIRQFHFTGWPDHGVPYHA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 203 DPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTW-MLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYEL 281
Cdd:cd14633  188 TGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLdMAEREGVV----DIYNCVRELRSRRVNMVQTEEQYVF 263


                 ....*..
gi 157824150 282 VYSAVLE 288
Cdd:cd14633  264 IHDAILE 270
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-291 1.01e-51

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: 179.45  E-value: 1.01e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASF----IKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQlQFGPFSIS 159
Cdd:cd14541    2 YINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETM-QFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 160 CETEKKKSDYKIR--TLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVI 237
Cdd:cd14541   81 CVSEEVTPSFAFRefILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157824150 238 CAVDyTWMLLkdgiIPKNFSVFNL--IQEMRTQRPSLVQTQEQYELVYSAVLELFK 291
Cdd:cd14541  161 ITME-TAMCL----IEANEPVYPLdiVRTMRDQRAMLIQTPSQYRFVCEAILRVYE 211
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 52-284 2.77e-51

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: 179.65  E-value: 2.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  52 PKNIKKNRYKDILPYDHSLVEL-SLLTSDEDSSYINASFIKGVYG-PRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMaC 129
Cdd:cd14612   13 PGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDGkEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM-I 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 130 MEFEMGKKKCERYWAEPGETqlqFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLI 209
Cdd:cd14612   92 TKLKEKKEKCVHYWPEKEGT---YGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRLV 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157824150 210 WDMRCYQEDDCV--PLCIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYS 284
Cdd:cd14612  169 AEVEESRQTAASpgPIVVHCSAGIGRTGCFIATSIGCQQLKD---TGKVDILGIVCQLRLDRGGMIQTSEQYQFLHH 242
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 46-288 3.65e-51

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: 180.64  E-value: 3.65e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  46 TTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGvYGPR--AYIATQGPLSTTLLDFWRMIWEYRVL 123
Cdd:cd14610   36 TNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 124 VIVMACMEFEMGKKKCERYWAEPGET-----QLQFGPFSISCEtekkksDYKIRT--LKAKFNSETRIVYQFHYKNWPDH 196
Cdd:cd14610  115 VIVMLTPLAENGVKQCYHYWPDEGSNlyhiyEVNLVSEHIWCE------DFLVRSfyLKNLQTNETRTVTQFHFLSWNDQ 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 197 DVPSSIDPILQLIWDM-RCYQEDDCvPLCIHCSAGCGRTGVICAVDYTWMLLKDGiiPKNFSVFNLIQEMRTQRPSLVQT 275
Cdd:cd14610  189 GVPASTRSLLDFRRKVnKCYRGRSC-PIIVHCSDGAGRSGTYILIDMVLNKMAKG--AKEIDIAATLEHLRDQRPGMVQT 265

                        250
                 ....*....|...
gi 157824150 276 QEQYELVYSAVLE 288
Cdd:cd14610  266 KEQFEFALTAVAE 278
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 58-287 4.94e-51

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 178.21  E-value: 4.94e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  58 NRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKK 137
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 138 KCERYWaePGE-TQLQFGPFSISCETEKKKSDYKIRTLKAKFNSE--TRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRC 214
Cdd:cd14618   81 LCDHYW--PSEsTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLrkERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157824150 215 YQE--DDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVL 287
Cdd:cd14618  159 HVQatKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKE---EKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 25-288 5.97e-51

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: 179.85  E-value: 5.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  25 ANEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQG 104
Cdd:cd14626   12 ANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 105 PLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCETEKKKSDYKIRTLKAKFN--SET 182
Cdd:cd14626   92 PLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYW--PIRGTETYGMIQVTLLDTVELATYSVRTFALYKNgsSEK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 183 RIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDytwMLLKDGIIPKNFSVFNLI 262
Cdd:cd14626  170 REVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERMKHEKTVDIYGHV 246

                        250       260
                 ....*....|....*....|....*.
gi 157824150 263 QEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14626  247 TCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 49-288 1.44e-49

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: 176.46  E-value: 1.44e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  49 AQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMA 128
Cdd:cd14628   47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 129 CMEFEMGKKKCERYWaePGETQLQFGPFSISCETEKKKSDYKIRTLKAK--FNSETRIVYQFHYKNWPDHDVPSS----I 202
Cdd:cd14628  127 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSgegfI 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 203 DPILQLIWDMRCYQEDDcvPLCIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYEL 281
Cdd:cd14628  205 DFIGQVHKTKEQFGQDG--PISVHCSAGVGRTGVFITLSIVLERMRyEGVV----DIFQTVKMLRTQRPAMVQTEDQYQF 278


                 ....*..
gi 157824150 282 VYSAVLE 288
Cdd:cd14628  279 CYRAALE 285
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 84-286 2.93e-49

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 172.45  E-value: 2.93e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCETE 163
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYW--PEDGSVSSGDITVELKDQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTLKAKFNSE--TRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCV-PLCIHCSAGCGRTGVICAV 240
Cdd:cd14552   79 TDYEDYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNhPITVHCSAGAGRTGTFCAL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157824150 241 DYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAV 286
Cdd:cd14552  159 STVLERVKaEGVL----DVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 26-286 5.48e-49

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: 173.61  E-value: 5.48e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  26 NEFLKLKRQSTKYkadkiyPTTVAQRPKNIKKNRYKDILPYDHSLVELSlltsDEDSSYINASFIKGVYGPRAYIATQGP 105
Cdd:cd14607    2 PLYLEIRNESHDY------PHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 106 LSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGP--FSISCETEKKKSDYKIRTLKAK-FNS-E 181
Cdd:cd14607   72 LPNTCCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLEnINSgE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 182 TRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRcyqEDDCV-----PLCIHCSAGCGRTGVICAVDyTWMLLKDGIIPKNF 256
Cdd:cd14607  152 TRTISHFHYTTWPDFGVPESPASFLNFLFKVR---ESGSLspehgPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSV 227

                        250       260       270
                 ....*....|....*....|....*....|
gi 157824150 257 SVFNLIQEMRTQRPSLVQTQEQYELVYSAV 286
Cdd:cd14607  228 DIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 58-283 5.78e-49

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: 172.41  E-value: 5.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  58 NRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKK 137
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 138 KCERYWAEPGETqLQFGPFSISCETEKKKSDYKIRTLKAKFNSE---TRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRC 214
Cdd:cd14617   81 KCDHYWPADQDS-LYYGDLIVQMLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157824150 215 Y--QEDDCVPLCIHCSAGCGRTGVICAVDYTWMLL--KDGIipknfSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14617  160 YinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLdsKDSV-----DIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 59-288 7.89e-49

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: 172.15  E-value: 7.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  59 RYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKK 138
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 139 CERYWaePGETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSE--TRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQ 216
Cdd:cd14623   81 CAQYW--PSDGSVSYGDITIELKKEEECESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157824150 217 EDDCV-PLCIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14623  159 QQSGNhPITVHCSAGAGRTGTFCALSTVLERVKaEGIL----DVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 84-287 1.11e-48

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: 170.93  E-value: 1.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCETE 163
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYW--PADGSEEYGNFLVTQKSV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTL----------KAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGR 233
Cdd:cd17668   79 QVLAYYTVRNFtlrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157824150 234 TGVICAVDytwMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVL 287
Cdd:cd17668  159 TGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 84-288 1.53e-48

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: 170.48  E-value: 1.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETqlqFGPFSISCETE 163
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLVET 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRT--LKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVD 241
Cdd:cd14555   78 EPLAEYVVRTfaLERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157824150 242 YTW-MLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14555  158 IMLdMAEREGVV----DIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 49-288 1.64e-48

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 173.38  E-value: 1.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  49 AQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMA 128
Cdd:cd14627   48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 129 CMEFEMGKKKCERYWaePGETQLQFGPFSISCETEKKKSDYKIRTLKAK--FNSETRIVYQFHYKNWPDHDVPSS----I 202
Cdd:cd14627  128 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSgegfI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 203 DPILQLIWDMRCYQEDDcvPLCIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYEL 281
Cdd:cd14627  206 DFIGQVHKTKEQFGQDG--PISVHCSAGVGRTGVFITLSIVLERMRyEGVV----DIFQTVKMLRTQRPAMVQTEDEYQF 279


                 ....*..
gi 157824150 282 VYSAVLE 288
Cdd:cd14627  280 CYQAALE 286
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 49-288 3.13e-48

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: 172.60  E-value: 3.13e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  49 AQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMA 128
Cdd:cd14629   48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 129 CMEFEMGKKKCERYWaePGETQLQFGPFSISCETEKKKSDYKIRTLKAK--FNSETRIVYQFHYKNWPDHDVPSS----I 202
Cdd:cd14629  128 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTIRQFQFTDWPEQGVPKTgegfI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 203 DPILQLIWDMRCYQEDDcvPLCIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYEL 281
Cdd:cd14629  206 DFIGQVHKTKEQFGQDG--PITVHCSAGVGRTGVFITLSIVLERMRyEGVV----DMFQTVKTLRTQRPAMVQTEDQYQL 279


                 ....*..
gi 157824150 282 VYSAVLE 288
Cdd:cd14629  280 CYRAALE 286
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 52-290 4.15e-48

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: 171.20  E-value: 4.15e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  52 PKNIKKNRYKDILPYDHSLVelSLLTSDED---SSYINASFIKGvYG--PRAYIATQGPLSTTLLDFWRMIWEYRVLVIV 126
Cdd:cd14613   23 PGLVRKNRYKTILPNPHSRV--CLTSPDQDdplSSYINANYIRG-YGgeEKVYIATQGPTVNTVGDFWRMVWQERSPIIV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 127 MACMEFEMgKKKCERYWAepgETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14613  100 MITNIEEM-NEKCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 207 QLIWDM---RCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGIIpknFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14613  176 QLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVH 252


                 ....*..
gi 157824150 284 SaVLELF 290
Cdd:cd14613  253 H-VLSLY 258
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 84-291 1.38e-47

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: 168.00  E-value: 1.38e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYG--PRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCE 161
Cdd:cd14596    1 YINASYITMPVGeeELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 162 TEKKKSDYKIRTLKA--KFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDcvPLCIHCSAGCGRTGVICA 239
Cdd:cd14596   81 NYQALQYFIIRIIKLveKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTG--PIVVHCSAGIGRAGVLIC 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157824150 240 VDYTWMLLKDGIipkNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELFK 291
Cdd:cd14596  159 VDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-288 2.18e-47

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: 167.63  E-value: 2.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYG--PRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYW--AEPGETQLQFGPFSIS 159
Cdd:cd14540    1 YINASHITATVGgkQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptLGGEHDALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 160 CETEKKKSDYKIRTLKAKFNSE--TRIVYQFHYKNWPDHDVPSSIDPILQLIWDM-----RCYQEDDC----VPLCIHCS 228
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSgqSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrHTNQDVAGhnrnPPTLVHCS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157824150 229 AGCGRTGVICAVDYTWMLLKDGI---IPKnfsvfnLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14540  161 AGVGRTGVVILADLMLYCLDHNEeldIPR------VLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 71-288 8.16e-47

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: 166.35  E-value: 8.16e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  71 VELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWaePGETQ 150
Cdd:cd14631    2 VILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW--PDDTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 151 LqFGPFSISCETEKKKSDYKIR--TLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCS 228
Cdd:cd14631   80 V-YGDFKVTCVEMEPLAEYVVRtfTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157824150 229 AGCGRTGVICAVDYTW-MLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14631  159 AGAGRTGCYIVIDIMLdMAEREGVV----DIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 25-288 8.25e-47

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: 168.35  E-value: 8.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  25 ANEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQG 104
Cdd:cd14625   18 ANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 105 PLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCETEKKKSDYKIRTLKAKFN--SET 182
Cdd:cd14625   98 PLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYW--PSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNgsSEK 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 183 RIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNLI 262
Cdd:cd14625  176 REVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKH---EKTVDIYGHV 252

                        250       260
                 ....*....|....*....|....*.
gi 157824150 263 QEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14625  253 TLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 57-283 5.85e-46

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


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 163.94  E-value: 5.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  57 KNRYKDILPYDHSLVELSLLTSDED-SSYINASFIKGVYG-PRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMaCMEFEM 134
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM-ITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 135 GKKKCERYWAEpgeTQLQFGPFSISCETEKKKSDYKIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMrc 214
Cdd:cd14611   81 KNEKCVLYWPE---KRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV-- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157824150 215 yQEDDCV-----PLCIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14611  156 -EEDRLAspgrgPVVVHCSAGIGRTGCFIATTIGCQQLKeEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 25-288 2.34e-45

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: 164.52  E-value: 2.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  25 ANEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQG 104
Cdd:cd14624   18 ANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 105 PLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPG-ETQlqfGPFSISCETEKKKSDYKIRTLKAKFN--SE 181
Cdd:cd14624   98 ALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGtETY---GLIQVTLLDTVELATYCVRTFALYKNgsSE 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 182 TRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNL 261
Cdd:cd14624  175 KREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKH---EKTVDIYGH 251

                        250       260
                 ....*....|....*....|....*..
gi 157824150 262 IQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14624  252 VTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 16-291 2.93e-45

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: 164.01  E-value: 2.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  16 KKKINREEFANEFlklkRQSTKYKADKIYptTVAQRPKNIKKNRYKDILPYDHSLVELsLLTSDEDSSYINASFIKGVYG 95
Cdd:cd14599    6 ERKLEEGMVFTEY----EQIPKKKADGVF--TTATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  96 PRA--YIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPG--ETQLQFGPFSISCETEKKKSDYKI 171
Cdd:cd14599   79 GEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGskHSSATYGKFKVTTKFRTDSGCYAT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 172 RTLKAK--FNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQE---------DDCV-PLCIHCSAGCGRTGVICA 239
Cdd:cd14599  159 TGLKVKhlLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRhtnsmldstKNCNpPIVVHCSAGVGRTGVVIL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157824150 240 VDYTWMLLKDGiipKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELFK 291
Cdd:cd14599  239 TELMIGCLEHN---EKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 84-283 5.13e-45

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


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 160.64  E-value: 5.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETqlqFGPFSISCETE 163
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT---YGDIEVELKDT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTLKAKF--NSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDC------VPLCIHCSAGCGRTG 235
Cdd:cd14558   78 EKSPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNskhgrsVPIVVHCSDGSSRTG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157824150 236 VICAVdytWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14558  158 IFCAL---WNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 60-288 1.58e-44

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: 160.11  E-value: 1.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  60 YKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKC 139
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 140 ERYWAEPGetQLQFGPFSISCETEKKKSDYKIRTLKAKFNSE-----TRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRC 214
Cdd:cd14620   81 YQYWPDQG--CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPdgckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157824150 215 YQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14620  159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHA---EQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
12-297 3.27e-44

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 161.03  E-value: 3.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  12 KEAQKKKINREEFANEFLKLKRQSTKYKADKIYPTTVAQRPKNikknRYKDILPYDHSLVElslltsdEDSSYINASFIK 91
Cdd:COG5599    4 KNPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLN----RFRDIQPYKETALR-------ANLGYLNANYIQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  92 gVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVM--ACMEFEMGKKKCERYWAEPGETqlqfgpFSISCETEKKKSDY 169
Cdd:COG5599   73 -VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVlaSDDEISKPKVKMPVYFRQDGEY------GKYEVSSELTESIQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 170 -------KIRTLKAKFNS-ETRIVYQFHYKNWPDHDVPSS--IDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICA 239
Cdd:COG5599  146 lrdgieaRTYVLTIKGTGqKKIEIPVLHVKNWPDHGAISAeaLKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIA 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 240 VDYTWMLLKDGIIpKNFSVFNLIQEMRTQR-PSLVQTQEQY-ELVysavlELFKRHVDII 297
Cdd:COG5599  226 CLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQLdVLV-----KLAEQQIRPL 279
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 14-288 1.09e-43

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: 160.19  E-value: 1.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  14 AQKKKINREEFaNEFLKLKRQSTkykadkiypTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGV 93
Cdd:cd14621   22 ADDNKLFREEF-NALPACPIQAT---------CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGY 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  94 YGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCETEKKKSDYKIRT 173
Cdd:cd14621   92 QEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYW--PDQGCWTYGNIRVSVEDVTVLVDYTVRK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 174 L------KAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLL 247
Cdd:cd14621  170 FciqqvgDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMM 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 157824150 248 KDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14621  250 HA---ERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 84-286 8.79e-43

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: 154.39  E-value: 8.79e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCETE 163
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYW--PSEGSVTHGEITIEIKND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTLKAKFNSE--TRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCV-PLCIHCSAGCGRTGVICAV 240
Cdd:cd14622   80 TLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTGTFIAL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 157824150 241 DYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAV 286
Cdd:cd14622  160 SNILERVKaEGLL----DVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 84-283 9.33e-43

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: 154.08  E-value: 9.33e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGV--YGPRaYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCE 161
Cdd:cd14539    1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 162 TEKKKSDY--KIRTLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCY---QEDDCVPLCIHCSAGCGRTGV 236
Cdd:cd14539   80 SVRTTPTHveRIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHylqQRSLQTPIVVHCSSGVGRTGA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157824150 237 ICAVdYTWML---LKDGI--IPKnfsvfnLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14539  160 FCLL-YAAVQeieAGNGIpdLPQ------LVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 84-283 8.26e-42

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: 151.52  E-value: 8.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCETE 163
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTL---KAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAV 240
Cdd:cd14557   81 KICPDYIIRKLninNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 157824150 241 DytwmLLKDGIIPKN-FSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14557  161 D----AMLEGLEAEGrVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 84-288 3.96e-41

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: 149.82  E-value: 3.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETqlqFGPFSISCETE 163
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT---YGDIKITLLKT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRT--LKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVICAVD 241
Cdd:cd14632   78 ETLAEYSVRTfaLERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157824150 242 YTW-MLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14632  158 VMLdMAECEGVV----DIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 84-291 2.84e-40

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: 147.40  E-value: 2.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFI------KGVYgpRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQlQFGPFS 157
Cdd:cd14601    2 YINANYInmeipsSSII--NRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-SYGGFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 158 ISCETEKKKSDYKIR--TLKAKFNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTG 235
Cdd:cd14601   79 VTCHSEEGNPAYVFRemTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157824150 236 VICAVDyTWMLLKDGiipkNFSVFNL--IQEMRTQRPSLVQTQEQYELVYSAVLELFK 291
Cdd:cd14601  159 VLITME-TAMCLIEC----NQPVYPLdiVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 84-283 1.67e-39

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: 144.86  E-value: 1.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMaCMEFEMGKKKCERYWAEPGetQLQFGPFSISCETE 163
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVM-LNQLDPKDQSCPQYWPDEG--SGTYGPIQVEFVST 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTLK----AKFNSETRIVYQFHYKNWPDH-DVPSSIDPILQLIWDMRCYQED-DCVPLCIHCSAGCGRTGVI 237
Cdd:cd14556   78 TIDEDVISRIFRlqntTRPQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRSGVF 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157824150 238 CAVDYTWMLLKdgiIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14556  158 CAISSVCERIK---VENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 84-283 1.15e-37

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: 139.66  E-value: 1.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETqlQFGPFSISCETE 163
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVEDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTL-KAKFNSET-----RIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGVI 237
Cdd:cd14551   79 VVLVDYTTRKFcIQKVNRGIgekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 157824150 238 CAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14551  159 IVIDAMLDMMHA---EGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PHA02738 PHA02738
hypothetical protein; Provisional
 33-296 1.41e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 143.14  E-value: 1.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  33 RQSTKYKADKIYPTTVAQRpKNIKKNRYKDILPYDHSLVELSllTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLD 112
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEK-KNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 113 FWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKAKFNSE-TRIVYQFHYK 191
Cdd:PHA02738 106 FYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSaTQTVTHFNFT 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 192 NWPDHDVPSSIDPILQLIWDMRCYQED-------------DCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGiipKNFSV 258
Cdd:PHA02738 186 AWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDAC---ATVSI 262

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 157824150 259 FNLIQEMRTQRPSLVQTQEQYELVYSAVlelfKRHVDI 296
Cdd:PHA02738 263 PSIVSSIRNQRYYSLFIPFQYFFCYRAV----KRYVNL 296
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 53-291 1.56e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 139.75  E-value: 1.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  53 KNIKKNRYKDILPYDHSLVELSllTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEF 132
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 133 EMGKKKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLK-AKFNSETRI-VYQFHYKNWPDHDVPSSIDPILQLIW 210
Cdd:PHA02742 129 EDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLClTDTNTGASLdIKHFAYEDWPHGGLPRDPNKFLDFVL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 211 DMRCYQEDDCV-----------PLCIHCSAGCGRTGVICAVDYTWMLLKDGIIpknFSVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:PHA02742 209 AVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIVRDLRKQRHNCLSLPQQY 285

                        250
                 ....*....|..
gi 157824150 280 ELVYSAVLELFK 291
Cdd:PHA02742 286 IFCYFIVLIFAK 297
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 47-286 4.65e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 139.01  E-value: 4.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  47 TVAQ--RPKNIKKNRYKDILPYDHSLVELS------------------LLTS-DEDSSYINASFIKGVYGPRAYIATQGP 105
Cdd:PHA02746  42 TTNHflKKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkiEVTSeDNAENYIHANFVDGFKEANKFICAQGP 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 106 LSTTLLDFWRMIWEYRVLVIVmACMEFEMGKKKCERYWAEPGETQLQFGPFSI-SCETEKKKSDYKIRTLKAKFNSET-R 183
Cdd:PHA02746 122 KEDTSEDFFKLISEHESQVIV-SLTDIDDDDEKCFELWTKEEDSELAFGRFVAkILDIIEELSFTKTRLMITDKISDTsR 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 184 IVYQFHYKNWPDHDVPSSIDPILQLI-------WDMRCYQEDDCV---PLCIHCSAGCGRTGVICAVDYTWMLLKDgiiP 253
Cdd:PHA02746 201 EIHHFWFPDWPDNGIPTGMAEFLELInkvneeqAELIKQADNDPQtlgPIVVHCSAGIGRAGTFCAIDNALEQLEK---E 277

                        250       260       270
                 ....*....|....*....|....*....|...
gi 157824150 254 KNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAV 286
Cdd:PHA02746 278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 84-291 2.06e-35

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: 133.95  E-value: 2.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRA--YIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPG--ETQLQFGPFSIS 159
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGsrHNTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 160 CETEKKKSDYKIRTLKAK--FNSETRIVYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQ---------EDDCVPLCIHCS 228
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKhlLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRrhtnstidpKSPNPPVLVHCS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157824150 229 AGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLiqeMRTQRPSLVQTQEQYELVYSAVLELFK 291
Cdd:cd14598  161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDM---LRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 50-297 1.05e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 134.74  E-value: 1.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  50 QRPKNIKKNRYKDILPYDHSLVELSLlTSDEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMAC 129
Cdd:PHA02747  47 EKPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 130 -MEFEMGKKKCERYWAEPGETQLQFGPFSISCETEKKKSDYKIRTLKA--KFNSETRIVYQFHYKNWPDHDVPSSIDPIL 206
Cdd:PHA02747 126 pTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEItdKILKDSRKISHFQCSEWFEDETPSDHPDFI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 207 QLI--------WDMRCYQEDDCV--PLCIHCSAGCGRTGVICAVDytwMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQ 276
Cdd:PHA02747 206 KFIkiidinrkKSGKLFNPKDALlcPIVVHCSDGVGKTGIFCAVD---ICLNQLVKRKAICLAKTAEKIREQRHAGIMNF 282

                        250       260
                 ....*....|....*....|....
gi 157824150 277 EQYELV---YSAVLELFKRHVDII 297
Cdd:PHA02747 283 DDYLFIqpgYEVLHYFLSKIKAID 306
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
184-288 1.37e-34

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 127.48  E-value: 1.37e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150   184 IVYQFHYKNWPDHDVPSSIDPILQLIWDMR--CYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGIipKNFSVFNL 261
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 157824150   262 IQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 184-288 1.37e-34

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: 127.48  E-value: 1.37e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150   184 IVYQFHYKNWPDHDVPSSIDPILQLIWDMR--CYQEDDCVPLCIHCSAGCGRTGVICAVDYTWMLLKDGIipKNFSVFNL 261
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 157824150   262 IQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 84-284 2.78e-33

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: 127.20  E-value: 2.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKG---VYGPRaYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKK-KCERYWAEPGETQLQFGPFSIS 159
Cdd:cd17658    1 YINASLVETpasESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 160 cETEKKKSDYKI--RTLKAKFNS---ETRIVYQFHYKNWPDHDVPSSIDPILQLIwdMRCYQ-EDDCVPLCIHCSAGCGR 233
Cdd:cd17658   80 -NKKLKHSQHSItlRVLEVQYIEseePPLSVLHIQYPEWPDHGVPKDTRSVRELL--KRLYGiPPSAGPIVVHCSAGIGR 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157824150 234 TGVICAVDYTWmllkDGIIPKNFSVFNL---IQEMRTQRPSLVQTQEQYELVYS 284
Cdd:cd17658  157 TGAYCTIHNTI----RRILEGDMSAVDLsktVRKFRSQRIGMVQTQDQYIFCYA 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 84-288 3.89e-28

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: 112.43  E-value: 3.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMaCMEFEMgKKKCERYWaePGETQLQFGPFSISCETE 163
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-LNEVDL-AQGCPQYW--PEEGMLRYGPIQVECMSC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTLK----AKFNSETRIVYQFHYKNWPDH-DVPSSIDPILQLIWDMRCYQEdDCVP----LCIHCSAGCGRT 234
Cdd:cd14636   77 SMDCDVISRIFRicnlTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQE-ECDEgegrTIIHCLNGGGRS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157824150 235 GVICAVDYTWMLLKDGIIpknFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14636  156 GMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 84-288 1.22e-26

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 108.18  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACmefEMGKKK-CERYWaePGETQLQFGPFSISCET 162
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYW--PEKTSCCYGPIQVEFVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 163 EKKKSDYKIRTLK----AKFNSETRIVYQFHYKNWPDH-DVPSSIDPILQLIWDMRCYQED-DCVP--LCIHCSAGCGRT 234
Cdd:cd14634   76 ADIDEDIISRIFRicnmARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQyDGREgrTVVHCLNGGGRS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157824150 235 GVICAV-DYTWMLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14634  156 GTFCAIcSVCEMIQQQNII----DVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 84-288 1.27e-22

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 96.68  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMacMEFEMGKKKCERYWAEPGETqlQFGPFSISCETE 163
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVM--LNDVDPAQLCPQYWPENGVH--RHGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKSDYKIRTLK----AKFNSETRIVYQFHYKNWPDH-DVPSSIDPILQLIWDMRCYQED---DCVPLCIHCSAGCGRTG 235
Cdd:cd14635   77 DLEEDIISRIFRiynaARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGGRSG 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157824150 236 VICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14635  157 TFCAISIVCEMLRH---QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 84-288 5.67e-22

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 94.59  E-value: 5.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKK-KCERYWAEPGETqlQFGPFSISCET 162
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQ--QYGPMEVEFVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 163 EKKKSDYKIRTLK----AKFNSETRIVYQFHYKNW-PDHDVPSSIDPILQLIWDMRCYQEDDCV-PLCIHCSAGCGRTGV 236
Cdd:cd14637   79 GSADEDIVTRLFRvqniTRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEgRTVVHCLNGGGRSGT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157824150 237 ICAVDytwmLLKDGIIPKNF-SVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14637  159 YCASA----MILEMIRCHNIvDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 84-283 5.79e-18

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: 82.75  E-value: 5.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMaCMEFEMGKKKCErYWAEPGETqLQFGPFSISCETE 163
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVM-LTDNELNEDEPI-YWPTKEKP-LECETFKVTLSGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKKS-----DYKIR--TLKAKFNSETRIVYQFHYKNWPDHDVPssIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGRTGV 236
Cdd:cd14550   78 DHSClsneiRLIVRdfILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAAT 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157824150 237 ICAvdytWMLLKDGIIPKN----FSVFNLIQEMrtqRPSLVQTQEQYELVY 283
Cdd:cd14550  156 FCA----LTTLHQQLEHESsvdvYQVAKLYHLM---RPGVFTSKEDYQFLY 199
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 84-287 1.08e-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: 82.35  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCErYWAEPGETqLQFGPFSISCETE 163
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEP-INCETFKVTLIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 164 KKK----------SDYKIRTLKAKFNSETRivyQFHYKNWPDHDVPssIDPILQLIWDMRCYQEDDCVPLCIHCSAGCGR 233
Cdd:cd17669   79 EHKclsneekliiQDFILEATQDDYVLEVR---HFQCPKWPNPDSP--ISKTFELISIIKEEAANRDGPMIVHDEHGGVT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157824150 234 TGVICAVdYTWM--LLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVL 287
Cdd:cd17669  154 AGTFCAL-TTLMhqLEKENSV----DVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 84-287 6.32e-17

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: 80.11  E-value: 6.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  84 YINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMacMEFEMGKKKCER-YWAEPGE---------TQLQF 153
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM--LPDNQGLAEDEFvYWPSREEsmnceaftvTLISK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 154 GPFSISCETEKKKSDYKIRTLKAKFNSETRivyQFHYKNWPDHDVP-SSIDPILQLIWDMRCYQEDdcvPLCIHCSAGCG 232
Cdd:cd17670   79 DRLCLSNEEQIIIHDFILEATQDDYVLEVR---HFQCPKWPNPDAPiSSTFELINVIKEEALTRDG---PTIVHDEFGAV 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157824150 233 RTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMrtqRPSLVQTQEQYELVYSAVL 287
Cdd:cd17670  153 SAGTLCALTTLSQQLENENAVDVYQVAKMINLM---RPGVFTDIEQYQFLYKAML 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 85-281 1.23e-14

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: 73.97  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  85 INASFIKgVYGPRAYIATQGPLSTTLLDFWRMIWEYRVLVIVMACMEFEMGKKKCERYWAEPGetqlQFGpfSISCETEK 164
Cdd:cd14559   18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSG----TYG--SVTVKSKK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 165 KKSDYKIRTLKAK-FNSETR------IVYQFHYKNWPDHDVPSSID----------------PILQLIWDMRCYQEDDCV 221
Cdd:cd14559   91 TGKDELVDGLKADmYNLKITdgnktiTIPVVHVTNWPDHTAISSEGlkeladlvnksaeekrNFYKSKGSSAINDKNKLL 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157824150 222 PLcIHCSAGCGRTGVICAVdytwMLLKDGiiPKNFSVFNLIQEMRTQRPS-LVQTQEQYEL 281
Cdd:cd14559  171 PV-IHCRAGVGRTGQLAAA----MELNKS--PNNLSVEDIVSDMRTSRNGkMVQKDEQLDT 224
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 49-297 3.81e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 55.74  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  49 AQRPKNIKKNRYKD------ILPYDHSLVELSlltsdEDSSYINASFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYRV 122
Cdd:PHA02740  42 ANKACAQAENKAKDenlalhITRLLHRRIKLF-----NDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 123 LVIVMACmefEMGKKKC-ERYWAEPGETQLQFGPFSISCETEKKKSDYKIR--TLKAKFNSETRIVYqFHYKNWP----D 195
Cdd:PHA02740 117 QIIVLIS---RHADKKCfNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTllSLTDKFGQAQKISH-FQYTAWPadgfS 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 196 HDVPSSID---PILQLIWDMRCYQEDDCV-PLCIHCSAGCGRTGVICAVDYTWMLL-KDGIIpknfSVFNLIQEMRTQRP 270
Cdd:PHA02740 193 HDPDAFIDffcNIDDLCADLEKHKADGKIaPIIIDCIDGISSSAVFCVFDICATEFdKTGML----SIANALKKVRQKKY 268

                        250       260
                 ....*....|....*....|....*..
gi 157824150 271 SLVQTQEQYELVYSAVLELFKRHVDII 297
Cdd:PHA02740 269 GCMNCLDDYVFCYHLIAAYLKEKFDIL 295
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 222-283 4.52e-08

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: 51.97  E-value: 4.52e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157824150 222 PLCIHCSAGCGRTGVICAVdytWMLLKDGiipknFSVFNLIQEMRTQRPS-LVQTQEQYELVY 283
Cdd:cd14494   58 PVLVHCKAGVGRTGTLVAC---YLVLLGG-----MSAEEAVRIVRLIRPGgIPQTIEQLDFLI 112
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
193-283 1.98e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 48.04  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 193 WPDHDVPS--SIDPILQLIWdmRCYQEDDcvPLCIHCSAGCGRTGVICAvdyTWMLLKDgiipknFSVFNLIQEMRTQRP 270
Cdd:COG2453   55 IPDFGAPDdeQLQEAVDFID--EALREGK--KVLVHCRGGIGRTGTVAA---AYLVLLG------LSAEEALARVRAARP 121

                         90
                 ....*....|...
gi 157824150 271 SLVQTQEQYELVY 283
Cdd:COG2453  122 GAVETPAQRAFLE 134
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 194-283 6.36e-06

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 46.87  E-value: 6.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 194 PDHDVPSSIDPILQLIWDMR-CYQEDDCVplCIHCSAGCGRTGVICAVdyTWMLLKDGIIPKnfsvfNLIQEMRTQRPSL 272
Cdd:cd14505   81 PDGGVPSDIAQWQELLEELLsALENGKKV--LIHCKGGLGRTGLIAAC--LLLELGDTLDPE-----QAIAAVRALRPGA 151

                         90
                 ....*....|.
gi 157824150 273 VQTQEQYELVY 283
Cdd:cd14505  152 IQTPKQENFLH 162
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 162-239 7.78e-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: 43.72  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 162 TEKKKSDYKIRTLKA-------KFNSetrivyQFHYKNWPDHDVPSsIDPILQLIWDMRCY-QEDDCVPLCIHCSAGCGR 233
Cdd:cd14497   36 NTHHPDHYMIFNLSEeeydddsKFEG------RVLHYGFPDHHPPP-LGLLLEIVDDIDSWlSEDPNNVAVVHCKAGKGR 108


                 ....*.
gi 157824150 234 TGVICA 239
Cdd:cd14497  109 TGTVIC 114
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 539-800 2.32e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.91  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  539 SSSPPNSAGSKMSFDLPEKQDGATSP--GAQLPASSAASSSYSNPRDSLMESTLTS--FPPPINQETAIEATSARTDDEI 614
Cdd:pfam05109 491 SPSPRDNGTESKAPDMTSPTSAVTTPtpNATSPTPAVTTPTPNATSPTLGKTSPTSavTTPTPNATSPTPAVTTPTPNAT 570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  615 PPPLPERTPESFIVAEAAGEPSPSITESLPLAGKSGVTLecGGTSESQshdlvAFTSSKNVELGSPKSDQHQDGSppppl 694
Cdd:pfam05109 571 IPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTL--GGTSSTP-----VVTSPPKNATSAVTTGQHNITS----- 638

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150  695 pertlesffladeDCIQAQPMKPSSIS---YPETTEISTSSKQTLK----TPGKSFTRSKSLKIFRNMKKSVCNSPSPSK 767
Cdd:pfam05109 639 -------------SSTSSMSLRPSSISetlSPSTSDNSTSHMPLLTsahpTGGENITQVTPASTSTHHVSTSSPAPRPGT 705

                         250       260       270
                  ....*....|....*....|....*....|...
gi 157824150  768 PTECVQPKNSSSFLNFGfGTRFSKPKGPRNPPS 800
Cdd:pfam05109 706 TSQASGPGNSSTSTKPG-EVNVTKGTPPKNATS 737
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 222-282 3.81e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 41.49  E-value: 3.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157824150 222 PLCIHCSAGCGRTGVICAVdYtwmLLKDGiipkNFSVFNLIQEMRTQRPSLVQTQEQYELV 282
Cdd:cd14504   84 AVLVHCLAGKGRTGTMLAC-Y---LVKTG----KISAVDAINEIRRIRPGSIETSEQEKFV 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 185-282 4.07e-04

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 42.34  E-value: 4.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157824150 185 VYQFhykNWPDHDVPSsidpiLQLIWDM-----RCYQEDDCVplCIHCSAGCGRTGVICAvdyTWMLLKDGIIPKnfsvf 259
Cdd:cd14506   79 FYNF---GWKDYGVPS-----LTTILDIvkvmaFALQEGGKV--AVHCHAGLGRTGVLIA---CYLVYALRMSAD----- 140

                         90       100
                 ....*....|....*....|...
gi 157824150 260 NLIQEMRTQRPSLVQTQEQYELV 282
Cdd:cd14506  141 QAIRLVRSKRPNSIQTRGQVLCV 163
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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