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Conserved domains on  [gi|2018536931|ref|NP_001380953|]
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receptor-type tyrosine-protein phosphatase T isoform 3 precursor [Homo sapiens]

Protein Classification

R-PTPc-T-1 and R-PTPc-T-2 domain-containing protein( domain architecture ID 13891670)

protein containing domains MAM, FN3, R-PTPc-T-1, and R-PTPc-T-2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 909-1165 1.91e-170

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: 509.18  E-value: 1.91e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  909 DENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNL 988
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  989 VEVGRhpaehtvgnatlgraaspgmVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTS 1068
Cdd:cd14630     81 VEVGR--------------------VKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTS 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1069 WPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQT 1148
Cdd:cd14630    141 WPDHGVPCYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQT 220

                          250
                   ....*....|....*..
gi 2018536931 1149 EEQYVFVHDAILEACLC 1165
Cdd:cd14630    221 EEQYVFVHDAILEACLC 237
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1250-1455 3.74e-162

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: 486.07  E-value: 3.74e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQFCMQYWPEKTSGCYGPIQVEFVSADIDE 1329
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1330 DIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 1409
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2018536931 1410 ICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 29-189 1.67e-56

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 192.94  E-value: 1.67e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931    29 AGGCSFDEHySNCGYSVALgTNGFTWEQINTWEK---PMLDQAVPTGSFMMVNSSGRASGQKAHLLLPTLKEN-DTHCID 104
Cdd:smart00137    3 PGNCDFEEG-STCGWHQDS-NDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   105 FHYYFSsrdRSSPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTfWPHFYQVIFESVSLKGHPGYIAVDEVRV 184
Cdd:smart00137   81 FWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 2018536931   185 LAHPC 189
Cdd:smart00137  157 SNGPC 161
fn3 pfam00041
Fibronectin type III domain;
502-577 7.50e-12

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 7.50e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931  502 IYIQWKPPNETNGVITLYEINYKAVGSLDPSADLSSqrgkvfkLRNETHHLFVGLYPGTTYSFTIKASTAKGFGPP 577
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 390-480 7.60e-08

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.34  E-value: 7.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  390 PQNVEIVDIRARQLTLQWEPFGYAVTRCHSYnlTVQYQYVFNQQQYEAEEVIQTSSHYTLRGLRPFMTIRLRLLLSNPEG 469
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGY--VVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 2018536931  470 RME-SEELVVQT 480
Cdd:cd00063     82 ESPpSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
294-360 2.16e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 2.16e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931  294 PPELL---AVGATYL---WIKPNAnsiiGDGPIILKEVEYRTTTGTWAETHIVDSPN---YKLWHLDPDVEYEIRV 360
Cdd:pfam00041    2 APSNLtvtDVTSTSLtvsWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV 73
 
Name Accession Description Interval E-value
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 909-1165 1.91e-170

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: 509.18  E-value: 1.91e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  909 DENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNL 988
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  989 VEVGRhpaehtvgnatlgraaspgmVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTS 1068
Cdd:cd14630     81 VEVGR--------------------VKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTS 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1069 WPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQT 1148
Cdd:cd14630    141 WPDHGVPCYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQT 220

                          250
                   ....*....|....*..
gi 2018536931 1149 EEQYVFVHDAILEACLC 1165
Cdd:cd14630    221 EEQYVFVHDAILEACLC 237
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1250-1455 3.74e-162

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: 486.07  E-value: 3.74e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQFCMQYWPEKTSGCYGPIQVEFVSADIDE 1329
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1330 DIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 1409
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2018536931 1410 ICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
887-1161 2.61e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 365.44  E-value: 2.61e-116
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   887 GFKEEYEALPEGQTA--SWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPhSDYINANYIDGYHRPRHYIATQGPMQ 964
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   965 ETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWPDD---TEVYGDIKVTLIETEPLA 1041
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGR--------------------EKCAQYWPDEegePLTYGDITVTLKSVEKVD 139

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1042 EYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLD 1121
Cdd:smart00194  140 DYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQ 219

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|
gi 2018536931  1122 MAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:smart00194  220 QLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
911-1161 5.31e-109

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 344.23  E-value: 5.31e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  911 NRNKNRYGNIISYDHSRVRLLvlDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVE 990
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  991 VGRhpaehtvgnatlgraaspgmVKCVRYWP---DDTEVYGDIKVTLIETEP-LAEYVIRTFTVQKKGYHEIRELRLFHF 1066
Cdd:pfam00102   79 KGR--------------------EKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHY 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1067 TSWPDHGVPCYATGLLGFVRQV-KFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNL 1145
Cdd:pfam00102  139 TGWPDHGVPESPNSLLDLLRKVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGM 218

                          250
                   ....*....|....*.
gi 2018536931 1146 VQTEEQYVFVHDAILE 1161
Cdd:pfam00102  219 VQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1193-1455 1.03e-88

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 288.79  E-value: 1.03e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1193 QIKDEFQTLNIVTPRvrPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPL 1272
Cdd:smart00194    1 GLEEEFEKLDRLKPD--DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1273 PNTVADFWRLVFDYNCSSVVMLNEMDTAQF--CMQYWPEKTSG--CYGPIQVEFVSADIDEDIIHRIFRICNMARPQDgy 1348
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGRekCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-- 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1349 RIVQHLQYIGWPaYRDTPPSKRSLLKVVRRLEKWQEQYDgreGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHI 1428
Cdd:smart00194  157 RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQSTST---GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232

                           250       260
                    ....*....|....*....|....*..
gi 2018536931  1429 VKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1221-1455 6.37e-85

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.20  E-value: 6.37e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1221 NHDKNRSMDVLPLDRCLPFLISVDGeSSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD-- 1298
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEek 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1299 TAQFCMQYWPEKTSG--CYGPIQVEFVSADIDE-DIIHRIFRICNMARPQdgYRIVQHLQYIGWPAyRDTPPSKRSLLKV 1375
Cdd:pfam00102   80 GREKCAQYWPEEEGEslEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEE--TRTVKHFHYTGWPD-HGVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1376 VRRLEKWQEqyDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:pfam00102  157 LRKVRKSSL--DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 29-189 1.67e-56

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 192.94  E-value: 1.67e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931    29 AGGCSFDEHySNCGYSVALgTNGFTWEQINTWEK---PMLDQAVPTGSFMMVNSSGRASGQKAHLLLPTLKEN-DTHCID 104
Cdd:smart00137    3 PGNCDFEEG-STCGWHQDS-NDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   105 FHYYFSsrdRSSPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTfWPHFYQVIFESVSLKGHPGYIAVDEVRV 184
Cdd:smart00137   81 FWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 2018536931   185 LAHPC 189
Cdd:smart00137  157 SNGPC 161
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
910-1152 5.22e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.58  E-value: 5.22e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  910 ENRNKNRYGNIISYDHSRVRllvldgdPHSDYINANYIDGYhRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLV 989
Cdd:COG5599     41 NGSPLNRFRDIQPYKETALR-------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  990 EVgrhpaehtvgnatlgraaSPGMVKCVRYWPDDTEvYG--DIKVTLIETEPLAEYV-IRTFTVQKKGY-HEIRELRLFH 1065
Cdd:COG5599    113 EI------------------SKPKVKMPVYFRQDGE-YGkyEVSSELTESIQLRDGIeARTYVLTIKGTgQKKIEIPVLH 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1066 FTSWPDHGVPCYAT--GLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDM--AENEGVVDIFNCVRELRAQ 1141
Cdd:COG5599    174 VKNWPDHGAISAEAlkNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRTS 253

                          250
                   ....*....|..
gi 2018536931 1142 RVN-LVQTEEQY 1152
Cdd:COG5599    254 RNGgMVQTSEQL 265
PHA02738 PHA02738
hypothetical protein; Provisional
 908-1159 2.36e-45

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 167.02  E-value: 2.36e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  908 EDENRNKNRYGNIISYDHSRVRLLVLDGdpHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTN 987
Cdd:PHA02738    46 EKKNRKLNRYLDAVCFDHSRVILPAERN--RGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  988 LVEVGRHpaehtvgnatlgraaspgmvKCVRYWPD---DTEVYGDIKVTLIETEPLAEYVIRTFTVqKKGYHEIRELRLF 1064
Cdd:PHA02738   124 KKENGRE--------------------KCFPYWSDveqGSIRFGKFKITTTQVETHPHYVKSTLLL-TDGTSATQTVTHF 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1065 HFTSWPDHGVPCYATGLLGFVRQVK----------------FLNPPeagPIVVHCSAGAGRTGCFIAIDTMLDMAENEGV 1128
Cdd:PHA02738   183 NFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighnRLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACAT 259

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2018536931 1129 VDIFNCVRELRAQRVNLVQTEEQYVFVHDAI 1159
Cdd:PHA02738   260 VSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 32-189 4.04e-41

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 148.68  E-value: 4.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   32 CSFDEHYsnCGYSVALgTNGFTWEQINTWEK-----PMLDQAVPTGSFMMVNSSGRASGQKAHLLLPTLKEN-DTHCIDF 105
Cdd:cd06263      1 CDFEDGL--CGWTQDS-TDDFDWTRVSGSTPspgtpPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  106 HYYFSSRDrssPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTFWPHFyQVIFESVSLKGHPGYIAVDEVRVL 185
Cdd:cd06263     78 WYHMYGSG---VGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPF-QVVFEGVRGSGSRGDIALDDISLS 153


                   ....
gi 2018536931  186 AHPC 189
Cdd:cd06263    154 PGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 32-190 1.16e-37

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 139.03  E-value: 1.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   32 CSFDEHYSnCGYSVALGTnGFTWEQINTWE---KPMLD--QAVPTGSFMMVNSSGRASGQKAHLLLPTLKENDT-HCIDF 105
Cdd:pfam00629    1 CDFEDGNL-CGWTQDSSD-DFDWERVSGPSvktGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  106 HYYFSSrdrSSPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTFwPHFYQVIFESVSLKGHPGYIAVDEVRVL 185
Cdd:pfam00629   79 WYHMSG---SGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLS 154


                   ....*
gi 2018536931  186 AHPCR 190
Cdd:pfam00629  155 SGPCP 159
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1219-1458 6.62e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 118.95  E-value: 6.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1219 PRNHDKNRSMDVLPLDRCLPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN--- 1295
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1296 EMDTAQFCMQYW--PEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNmaRPQDGYRIVQHLQYIGWPAYrDTPPSKRSLL 1373
Cdd:PHA02747   129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1374 KVVRRLEKWQEQY-------DGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQY 1446
Cdd:PHA02747   206 KFIKIIDINRKKSgklfnpkDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                          250
                   ....*....|....*
gi 2018536931 1447 KFV---YEVALEYLS 1458
Cdd:PHA02747   286 LFIqpgYEVLHYFLS 300
fn3 pfam00041
Fibronectin type III domain;
502-577 7.50e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 7.50e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931  502 IYIQWKPPNETNGVITLYEINYKAVGSLDPSADLSSqrgkvfkLRNETHHLFVGLYPGTTYSFTIKASTAKGFGPP 577
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 502-584 3.27e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.97  E-value: 3.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  502 IYIQWKPPNETNGVITLYEINYKAVGSlDPSADLSSQRGkvfklrNETHHLFVGLYPGTTYSFTIKASTAKGFGPPVTTR 581
Cdd:cd00063     17 VTLSWTPPEDDGGPITGYVVEYREKGS-GDWKEVEVTPG------SETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESV 89


                   ...
gi 2018536931  582 IAT 584
Cdd:cd00063     90 TVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 390-480 7.60e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.34  E-value: 7.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  390 PQNVEIVDIRARQLTLQWEPFGYAVTRCHSYnlTVQYQYVFNQQQYEAEEVIQTSSHYTLRGLRPFMTIRLRLLLSNPEG 469
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGY--VVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 2018536931  470 RME-SEELVVQT 480
Cdd:cd00063     82 ESPpSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 502-575 6.76e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.38  E-value: 6.76e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018536931   502 IYIQWKPPNETNGviTLYEINYKAVGSldpsaDLSSQRGKVFKLRNETHHLFVGLYPGTTYSFTIKASTAKGFG 575
Cdd:smart00060   17 VTLSWEPPPDDGI--TGYIVGYRVEYR-----EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 390-470 1.55e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.53  E-value: 1.55e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   390 PQNVEIVDIRARQLTLQWEPFGYAVTRchSYNLTVQYQYVFNQQQYEAEEVIQTSSHYTLRGLRPFMTIRLRLLLSNPEG 469
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    .
gi 2018536931   470 R 470
Cdd:smart00060   82 E 82
fn3 pfam00041
Fibronectin type III domain;
294-360 2.16e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 2.16e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931  294 PPELL---AVGATYL---WIKPNAnsiiGDGPIILKEVEYRTTTGTWAETHIVDSPN---YKLWHLDPDVEYEIRV 360
Cdd:pfam00041    2 APSNLtvtDVTSTSLtvsWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV 73
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 289-360 1.01e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 42.22  E-value: 1.01e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931   289 PTPIAPPELLAVGATYL---WIKPNANSiiGDGPIILKEVEYRTTTGTWAETHIVDSPN-YKLWHLDPDVEYEIRV 360
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVtlsWEPPPDDG--ITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1333-1453 5.14e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 41.88  E-value: 5.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1333 HRIFRICNMARPQDGYRIVQ---HLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQydgrEGRTVVHCLNGGGRSGTFCA 1409
Cdd:COG2453     24 EGIDAVVSLTEEEELLLGLLeeaGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALRE----GKKVLVHCRGGIGRTGTVAA 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2018536931 1410 icsvCEMIQQQniIDVFHIVKTLRNNKSNMVETLEQYKFVYEVA 1453
Cdd:COG2453    100 ----AYLVLLG--LSAEEALARVRAARPGAVETPAQRAFLERFA 137
 
Name Accession Description Interval E-value
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 909-1165 1.91e-170

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: 509.18  E-value: 1.91e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  909 DENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNL 988
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  989 VEVGRhpaehtvgnatlgraaspgmVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTS 1068
Cdd:cd14630     81 VEVGR--------------------VKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTS 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1069 WPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQT 1148
Cdd:cd14630    141 WPDHGVPCYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQT 220

                          250
                   ....*....|....*..
gi 2018536931 1149 EEQYVFVHDAILEACLC 1165
Cdd:cd14630    221 EEQYVFVHDAILEACLC 237
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1250-1455 3.74e-162

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: 486.07  E-value: 3.74e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQFCMQYWPEKTSGCYGPIQVEFVSADIDE 1329
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1330 DIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 1409
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2018536931 1410 ICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 872-1164 3.67e-157

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: 475.69  E-value: 3.67e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  872 DLLQHITQMKRGQGYGFKEEYEALPEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYH 951
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  952 RPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWPDDTEVYGDIK 1031
Cdd:cd14633     81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGR--------------------VKCCKYWPDDTEIYKDIK 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1032 VTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTG 1111
Cdd:cd14633    141 VTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTG 220

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2018536931 1112 CFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACL 1164
Cdd:cd14633    221 CFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 941-1164 2.20e-143

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: 436.27  E-value: 2.20e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYW 1020
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGR--------------------VKCSRYW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIV 1100
Cdd:cd14555     61 PDDTEVYGDIKVTLVETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIV 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018536931 1101 VHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACL 1164
Cdd:cd14555    141 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1250-1451 1.34e-125

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: 388.30  E-value: 1.34e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDT-AQFCMQYWPEKTSGCYGPIQVEFVSADID 1328
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPkDQSCPQYWPDEGSGTYGPIQVEFVSTTID 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1329 EDIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQYDgrEGRTVVHCLNGGGRSGTFC 1408
Cdd:cd14556     81 EDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSG--EGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2018536931 1409 AICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 927-1164 2.24e-121

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: 377.44  E-value: 2.24e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  927 RVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlg 1006
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGR------------- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1007 raaspgmVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVR 1086
Cdd:cd14631     68 -------VKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIR 140

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018536931 1087 QVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACL 1164
Cdd:cd14631    141 RVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 911-1165 2.35e-120

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: 375.58  E-value: 2.35e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  911 NRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVE 990
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  991 VGRhpaehtvgnatlgraaspgmVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSW 1069
Cdd:cd14553     83 RSR--------------------VKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAW 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1070 PDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTE 1149
Cdd:cd14553    143 PDHGVPEHPTPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTE 222

                          250
                   ....*....|....*.
gi 2018536931 1150 EQYVFVHDAILEACLC 1165
Cdd:cd14553    223 DQYIFIHDALLEAVTC 238
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
887-1161 2.61e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 365.44  E-value: 2.61e-116
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   887 GFKEEYEALPEGQTA--SWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPhSDYINANYIDGYHRPRHYIATQGPMQ 964
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   965 ETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWPDD---TEVYGDIKVTLIETEPLA 1041
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGR--------------------EKCAQYWPDEegePLTYGDITVTLKSVEKVD 139

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1042 EYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLD 1121
Cdd:smart00194  140 DYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQ 219

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|
gi 2018536931  1122 MAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:smart00194  220 QLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 941-1165 1.98e-115

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: 360.91  E-value: 1.98e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYW 1020
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGR--------------------VKCSKYW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIV 1100
Cdd:cd14632     61 PDDSDTYGDIKITLLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVV 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018536931 1101 VHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACLC 1165
Cdd:cd14632    141 VHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1250-1455 3.43e-111

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: 349.37  E-value: 3.43e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQFCMQYWPEKTSGCYGPIQVEFVSADIDE 1329
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1330 DIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 1409
Cdd:cd14635     81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2018536931 1410 ICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14635    161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
911-1161 5.31e-109

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 344.23  E-value: 5.31e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  911 NRNKNRYGNIISYDHSRVRLLvlDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVE 990
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  991 VGRhpaehtvgnatlgraaspgmVKCVRYWP---DDTEVYGDIKVTLIETEP-LAEYVIRTFTVQKKGYHEIRELRLFHF 1066
Cdd:pfam00102   79 KGR--------------------EKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHY 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1067 TSWPDHGVPCYATGLLGFVRQV-KFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNL 1145
Cdd:pfam00102  139 TGWPDHGVPESPNSLLDLLRKVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGM 218

                          250
                   ....*....|....*.
gi 2018536931 1146 VQTEEQYVFVHDAILE 1161
Cdd:pfam00102  219 VQTLEQYIFLYDAILE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 871-1165 1.09e-108

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: 345.48  E-value: 1.09e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  871 ADLLQHITQMKRGQGYGFKEEYEALPEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGY 950
Cdd:cd14626      1 SDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  951 HRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWP-DDTEVYGD 1029
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSR--------------------VKCDQYWPiRGTETYGM 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1030 IKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGR 1109
Cdd:cd14626    141 IQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGR 220

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931 1110 TGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACLC 1165
Cdd:cd14626    221 TGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1250-1455 4.41e-106

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: 335.46  E-value: 4.41e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQFCMQYWPEKTSGCYGPIQVEFVSADIDE 1329
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1330 DIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 1409
Cdd:cd14636     81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2018536931 1410 ICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14636    161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 865-1167 9.58e-102

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: 326.69  E-value: 9.58e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  865 QPAIRVADLLQHITQMKRGQGYGFKEEYEALPEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINA 944
Cdd:cd14624      1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  945 NYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWPD-D 1023
Cdd:cd14624     81 NYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSR--------------------VKCDQYWPSrG 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1024 TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHC 1103
Cdd:cd14624    141 TETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHC 220

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018536931 1104 SAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACLCGN 1167
Cdd:cd14624    221 SAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGN 284
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 865-1165 1.58e-100

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: 323.20  E-value: 1.58e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  865 QPAIRVADLLQHITQMKRGQGYGFKEEYEALPEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINA 944
Cdd:cd14625      1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  945 NYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWPD-D 1023
Cdd:cd14625     81 NYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSR--------------------IKCDQYWPSrG 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1024 TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHC 1103
Cdd:cd14625    141 TETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHC 220

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018536931 1104 SAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACLC 1165
Cdd:cd14625    221 SAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 941-1157 1.06e-95

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: 306.13  E-value: 1.06e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYW 1020
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGR--------------------EKCERYW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTE---VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAG 1097
Cdd:cd00047     61 PEEGGkplEYGDITVTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1098 PIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHD 1157
Cdd:cd00047    141 PIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 941-1157 1.77e-95

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: 305.81  E-value: 1.77e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYW 1020
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRR--------------------KCDQYW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQ------KKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNP 1093
Cdd:cd14549     61 PKEgTETYGNIQVTLLSTEVLATYTVRTFSLKnlklkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANP 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018536931 1094 PEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHD 1157
Cdd:cd14549    141 PGAGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1250-1455 5.53e-95

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: 304.52  E-value: 5.53e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD---TAQFCMQYWPEKTSGCYGPIQVEFVSAD 1326
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNqsnSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1327 IDEDIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQydGREGRTVVHCLNGGGRSGT 1406
Cdd:cd14637     81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRE--SGEGRTVVHCLNGGGRSGT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2018536931 1407 FCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14637    159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 916-1156 2.51e-94

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: 303.12  E-value: 2.51e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  916 RYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhp 995
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  996 aehtvgnatlgraaspgmVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGyhEIRELRLFHFTSWPDHG 1073
Cdd:cd14548     79 ------------------VKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHG 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1074 VPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYV 1153
Cdd:cd14548    139 VPEAPDSLLRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYI 218


                   ...
gi 2018536931 1154 FVH 1156
Cdd:cd14548    219 FLH 221
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1193-1455 1.03e-88

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 288.79  E-value: 1.03e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1193 QIKDEFQTLNIVTPRvrPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPL 1272
Cdd:smart00194    1 GLEEEFEKLDRLKPD--DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1273 PNTVADFWRLVFDYNCSSVVMLNEMDTAQF--CMQYWPEKTSG--CYGPIQVEFVSADIDEDIIHRIFRICNMARPQDgy 1348
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGRekCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-- 156

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1349 RIVQHLQYIGWPaYRDTPPSKRSLLKVVRRLEKWQEQYDgreGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHI 1428
Cdd:smart00194  157 RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQSTST---GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232

                           250       260
                    ....*....|....*....|....*..
gi 2018536931  1429 VKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 888-1164 2.15e-87

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: 285.78  E-value: 2.15e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  888 FKEEYEalpEGQTASWD---TAKED---ENRNKNRYGNIISYDHSRVRLLVLDG--DPHSDYINANYIDGYHRPRHYIAT 959
Cdd:cd17667      1 FSEDFE---EVQRCTADmniTAEHSnhpDNKHKNRYINILAYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIAT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  960 QGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYWP-DDTEVYGDIKVTLIETE 1038
Cdd:cd17667     78 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRR--------------------KCDQYWPtENSEEYGNIIVTLKSTK 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1039 PLAEYVIRTFTVQK-----------KGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGA 1107
Cdd:cd17667    138 IHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGV 217

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2018536931 1108 GRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACL 1164
Cdd:cd17667    218 GRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1221-1455 6.37e-85

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.20  E-value: 6.37e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1221 NHDKNRSMDVLPLDRCLPFLISVDGeSSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD-- 1298
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEek 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1299 TAQFCMQYWPEKTSG--CYGPIQVEFVSADIDE-DIIHRIFRICNMARPQdgYRIVQHLQYIGWPAyRDTPPSKRSLLKV 1375
Cdd:pfam00102   80 GREKCAQYWPEEEGEslEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEE--TRTVKHFHYTGWPD-HGVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1376 VRRLEKWQEqyDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:pfam00102  157 LRKVRKSSL--DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 866-1170 1.32e-84

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: 278.83  E-value: 1.32e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  866 PAIRVADLLQHITQMKRGQGYGFKEEYEALPEGQ-TASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINA 944
Cdd:cd14621      6 PPLPVDKLEEEINRRMADDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  945 NYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWPDD- 1023
Cdd:cd14621     86 SFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKE--------------------CKCAQYWPDQg 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1024 TEVYGDIKVTLIETEPLAEYVIRTFTVQKKG----YHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPI 1099
Cdd:cd14621    146 CWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAI 225

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1100 VVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACLCGNTAI 1170
Cdd:cd14621    226 VVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 887-1156 1.26e-83

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: 275.01  E-value: 1.26e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  887 GFKEEYEAL----PEGqtaSWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGP 962
Cdd:cd14543      4 GIYEEYEDIrrepPAG---TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  963 MQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWPDD---TEVYGDIKVTLIETEP 1039
Cdd:cd14543     81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGR--------------------VKCGQYWPLEegsSLRYGDLTVTNLSVEN 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1040 LAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGF---VRQ-----VKFLNPPEAG-----PIVVHCSAG 1106
Cdd:cd14543    141 KEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAAALLDFlgeVRQqqalaVKAMGDRWKGhppgpPIVVHCSAG 220

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1107 AGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVH 1156
Cdd:cd14543    221 IGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 915-1161 4.54e-83

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: 271.69  E-value: 4.54e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  915 NRYGNIISYDHSRVRLLVLdGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRh 994
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQ-SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  995 paehtvgnatlgraaspgmVKCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHG 1073
Cdd:cd14615     79 -------------------TKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHG 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1074 VPCYATGLLGF---VRQVKFLNPPEaGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEE 1150
Cdd:cd14615    140 VPETTDLLINFrhlVREYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTED 218

                          250
                   ....*....|.
gi 2018536931 1151 QYVFVHDAILE 1161
Cdd:cd14615    219 QYVFLNQCALD 229
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 917-1161 1.31e-79

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: 261.80  E-value: 1.31e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  917 YGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpa 996
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  997 ehtvgnatlgraaspgmvKCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRL---FHFTSWPDH 1072
Cdd:cd14620     79 ------------------KCYQYWPDQgCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRLvtqLHFTSWPDF 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1073 GVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQY 1152
Cdd:cd14620    141 GVPFTPIGMLKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQY 220


                   ....*....
gi 2018536931 1153 VFVHDAILE 1161
Cdd:cd14620    221 SFIYQALLE 229
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 915-1156 6.19e-76

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: 251.16  E-value: 6.19e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  915 NRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGY-HRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEvgr 993
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  994 hpaehtvgnatlgraaspGMVKCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGyhEIRELRLFHFTSWPDH 1072
Cdd:cd14547     78 ------------------AKEKCAQYWPEEeNETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDH 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1073 GVPCYATGLLGFVRQVKFL--NPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEE 1150
Cdd:cd14547    138 KTPEAAQPLLSLVQEVEEArqTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAE 217


                   ....*.
gi 2018536931 1151 QYVFVH 1156
Cdd:cd14547    218 QYEFVH 223
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 915-1161 5.52e-75

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: 249.04  E-value: 5.52e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  915 NRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRh 994
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  995 paehtvgnatlgraaspgmVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDH 1072
Cdd:cd14619     80 -------------------VKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDH 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1073 GVPCYATGLLGFVRQVK--FLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEE 1150
Cdd:cd14619    141 GVPSSTDTLLAFRRLLRqwLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTES 220

                          250
                   ....*....|.
gi 2018536931 1151 QYVFVHDAILE 1161
Cdd:cd14619    221 QYVFLHQCILD 231
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 915-1156 1.36e-74

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: 247.52  E-value: 1.36e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  915 NRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRh 994
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  995 paehtvgnatlgraaspgmVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTV---QKKGYHeiRELRLFHFTSW 1069
Cdd:cd14617     80 -------------------VKCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcseEQLDAP--RLVRHFHYTVW 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1070 PDHGVPCYATGLLGFVRQVK-FLN-PPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQ 1147
Cdd:cd14617    139 PDHGVPETTQSLIQFVRTVRdYINrTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQ 218


                   ....*....
gi 2018536931 1148 TEEQYVFVH 1156
Cdd:cd14617    219 TECQYVYLH 227
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 911-1159 2.18e-74

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: 247.76  E-value: 2.18e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  911 NRNKNRYGNIISYDHSRVRLLVLDGD-PHSDYINANYI-----DGYHRP--RHYIATQGPMQETVKDFWRMIWQENSASI 982
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  983 VMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYWPDD--TEVYGDIKVTLIETEPLAEYVIRTFTVQKKG-YHEIR 1059
Cdd:cd14544     81 VMTTKEVERGKN--------------------KCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDqGDPIR 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1060 ELRLFHFTSWPDHGVPCYATGLLGFVRQV--KFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGV---VDIFNC 1134
Cdd:cd14544    141 EIWHYQYLSWPDHGVPSDPGGVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKT 220

                          250       260
                   ....*....|....*....|....*
gi 2018536931 1135 VRELRAQRVNLVQTEEQYVFVHDAI 1159
Cdd:cd14544    221 IQMVRSQRSGMVQTEAQYKFIYVAV 245
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 915-1160 3.20e-72

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: 241.00  E-value: 3.20e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  915 NRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRh 994
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGR- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  995 paehtvgnatlgraaspgmVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDH 1072
Cdd:cd14618     80 -------------------VLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDH 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1073 GVPCYATGLLGFVRQVK--FLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEE 1150
Cdd:cd14618    141 GIPESTSSLMAFRELVRehVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLS 220

                          250
                   ....*....|
gi 2018536931 1151 QYVFVHDAIL 1160
Cdd:cd14618    221 QYIFLHSCIL 230
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 904-1160 4.48e-72

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: 240.95  E-value: 4.48e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  904 DTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIV 983
Cdd:cd14614      5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  984 MVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWP--DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIREL 1061
Cdd:cd14614     85 MLTQCNEKRR--------------------VKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDV 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1062 RLFHFTSWPDHGVPCY--ATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELR 1139
Cdd:cd14614    143 MHFNYTAWPDHGVPTAnaAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMR 222

                          250       260
                   ....*....|....*....|.
gi 2018536931 1140 AQRVNLVQTEEQYVFVHDAIL 1160
Cdd:cd14614    223 SYRMSMVQTEEQYIFIHQCVQ 243
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 911-1160 7.89e-72

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: 240.12  E-value: 7.89e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  911 NRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVE 990
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  991 VGRHpaehtvgnatlgraaspgmvKCVRYWPDDTEVygdiKVTLIETEPLAE-----YVIRTFTVQKKGYHEIRELRLFH 1065
Cdd:cd14554     86 MGRE--------------------KCHQYWPAERSA----RYQYFVVDPMAEynmpqYILREFKVTDARDGQSRTVRQFQ 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1066 FTSWPDHGVPCYATGLLGFVRQVK--FLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRV 1143
Cdd:cd14554    142 FTDWPEQGVPKSGEGFIDFIGQVHktKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRP 221

                          250
                   ....*....|....*..
gi 2018536931 1144 NLVQTEEQYVFVHDAIL 1160
Cdd:cd14554    222 AMVQTEDQYQFCYRAAL 238
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 941-1156 7.90e-72

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: 238.66  E-value: 7.90e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYW 1020
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEK--------------------KCSQYW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTE-VYGDIKVTLIETEPLAEYVIRTFTVQKK----GYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPE 1095
Cdd:cd14551     61 PDQGCwTYGNLRVRVEDTVVLVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPR 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1096 AGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVH 1156
Cdd:cd14551    141 AGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 941-1160 1.23e-71

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: 238.34  E-value: 1.23e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYW 1020
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR--------------------KCDQYW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 P-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQ--------KKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFL 1091
Cdd:cd17668     61 PaDGSEEYGNFLVTQKSVQVLAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYA 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018536931 1092 NPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAIL 1160
Cdd:cd17668    141 KRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 910-1159 6.72e-68

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: 229.52  E-value: 6.72e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  910 ENRNKNRYGNIISYDHSRVRLLvlDGDPH---SDYINANYIDGYH-------RP-RHYIATQGPMQETVKDFWRMIWQEN 978
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLH--DGDPNepvSDYINANIIMPEFetkcnnsKPkKSYIATQGCLQNTVNDFWRMVFQEN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  979 SASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYWPDDTEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGYH 1056
Cdd:cd14605     79 SRVIVMTTKEVERGKS--------------------KCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGQG 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1057 EI-RELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNP--PEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGV---VD 1130
Cdd:cd14605    139 NTeRTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQEsiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdID 218

                          250       260
                   ....*....|....*....|....*....
gi 2018536931 1131 IFNCVRELRAQRVNLVQTEEQYVFVHDAI 1159
Cdd:cd14605    219 VPKTIQMVRSQRSGMVQTEAQYRFIYMAV 247
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 941-1157 1.22e-66

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: 224.05  E-value: 1.22e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYID-GYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVgrhpaehtvgnatlgraaspGMVKCVRY 1019
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVEN--------------------GREKCDQY 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1020 WPD--DTEVYGDIKVTLIETE--PLAEYVIRTFTVQKKGyHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLN--P 1093
Cdd:cd18533     61 WPSgeYEGEYGDLTVELVSEEenDDGGFIVREFELSKED-GKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNdsA 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018536931 1094 PEAGPIVVHCSAGAGRTGCFIAIDTMLDMAEN--------EGVVD-IFNCVRELRAQRVNLVQTEEQYVFVHD 1157
Cdd:cd18533    140 SLDPPIIVHCSAGVGRTGTFIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 941-1156 3.41e-66

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: 222.39  E-value: 3.41e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYW 1020
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNR--------------------NKCAQYW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 P---DDTEVYGDIKVTLIETEPLAEYVIRTFTV-QKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEA 1096
Cdd:cd14557     61 PsmeEGSRAFGDVVVKINEEKICPDYIIRKLNInNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFS 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1097 GPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVH 1156
Cdd:cd14557    141 GPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1250-1451 1.18e-65

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: 220.62  E-value: 1.18e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDTAQfCMQYWPEKTSG--CYGPIQVEFVS 1324
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTnlvEKGREK-CERYWPEEGGKplEYGDITVTLVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1325 ADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAyRDTPPSKRSLLKVVRRLEKWQEQYDGRegrTVVHCLNGGGRS 1404
Cdd:cd00047     80 EEELSDYTIRTLELSPKGCSES--REVTHLHYTGWPD-HGVPSSPEDLLALVRRVRKEARKPNGP---IVVHCSAGVGRT 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2018536931 1405 GTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd00047    154 GTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 914-1159 2.24e-65

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: 222.43  E-value: 2.24e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  914 KNRYGNIISYDHSRVRLLVLD-GDPHSDYINANYIDGY-HRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEV 991
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  992 GRhpaehtvgnatlgraaspgmvKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGyhEIRELRLFHFTSWPD 1071
Cdd:cd14613    108 NE---------------------KCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1072 HGVPCYATGLLGFVRQVKFLN---PPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQT 1148
Cdd:cd14613    165 QKTPDNAPPLLQLVQEVEEARqqaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQT 244

                          250
                   ....*....|.
gi 2018536931 1149 EEQYVFVHDAI 1159
Cdd:cd14613    245 CEQYQFVHHVL 255
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 899-1161 6.75e-64

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: 218.60  E-value: 6.75e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  899 QTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGD-PHSDYINANYIDGY-----HRPRHYIATQGPMQETVKDFWR 972
Cdd:cd14606      6 NLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  973 MIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYWPD--DTEVYGDIKVTLIETEPLAEYVIRTFTV 1050
Cdd:cd14606     86 MAWQENSRVIVMTTREVEKGRN--------------------KCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQV 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1051 QKKGYHE-IRELRLFHFTSWPDHGVPCYATGLLGFVRQV--KFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEG 1127
Cdd:cd14606    146 SPLDNGElIREIWHYQYLSWPDHGVPSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKG 225

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2018536931 1128 V---VDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14606    226 LdcdIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQ 262
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 894-1161 1.56e-63

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: 217.39  E-value: 1.56e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  894 ALPEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRM 973
Cdd:cd14603     13 AFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRM 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  974 IWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYWP--DDTEVYGDIKVTLI-ETEPLAEYVIRTFTV 1050
Cdd:cd14603     93 IWQYGVKVILMACREIEMGKK--------------------KCERYWAqeQEPLQTGPFTITLVkEKRLNEEVILRTLKV 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1051 QKKgyHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVD 1130
Cdd:cd14603    153 TFQ--KESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPP 230

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2018536931 1131 ---IFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14603    231 dfsIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 915-1156 7.30e-63

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: 213.61  E-value: 7.30e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  915 NRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRh 994
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  995 paehtvgnatlgraaspgmVKCVRYWPDDTE---VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIreLRLFHFTSWPD 1071
Cdd:cd14616     80 -------------------IRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPE 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1072 HGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQ 1151
Cdd:cd14616    139 HGVPESSAPLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQ 218


                   ....*
gi 2018536931 1152 YVFVH 1156
Cdd:cd14616    219 YIFLH 223
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 904-1159 9.34e-63

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: 216.34  E-value: 9.34e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  904 DTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIV 983
Cdd:cd14604     50 ATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIV 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  984 MVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIRE 1060
Cdd:cd14604    130 MACREFEMGRK--------------------KCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQ--NETRR 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1061 LRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAID---TMLDMAENEGVVDIFNCVRE 1137
Cdd:cd14604    188 LYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQE 267

                          250       260
                   ....*....|....*....|..
gi 2018536931 1138 LRAQRVNLVQTEEQYVFVHDAI 1159
Cdd:cd14604    268 MRTQRHSAVQTKEQYELVHRAI 289
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 866-1161 1.03e-62

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: 216.14  E-value: 1.03e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  866 PAIRVADLLQHITQMKRGQGY-GFKEEYEAL--PEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYI 942
Cdd:cd14628      4 PARNLYAYIQKLTQIETGENVtGMELEFKRLasSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  943 NANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYWPD 1022
Cdd:cd14628     84 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE--------------------KCHQYWPA 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1023 DTEVygdiKVTLIETEPLAE-----YVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPP--E 1095
Cdd:cd14628    144 ERSA----RYQYFVVDPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQ 219

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931 1096 AGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14628    220 DGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 941-1159 6.50e-62

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: 210.20  E-value: 6.50e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYW 1020
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQN--------------------KCAQYW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTEV-YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQV-KFLNPPEAGP 1098
Cdd:cd14552     61 PEDGSVsSGDITVELKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHP 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1099 IVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAI 1159
Cdd:cd14552    141 ITVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 941-1162 9.28e-62

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: 209.92  E-value: 9.28e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYI------DGYHrprhYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmV 1014
Cdd:cd14538      1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGK--------------------V 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1015 KCVRYWPDDTE----VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKF 1090
Cdd:cd14538     57 KCHRYWPDSLNkpliCGGRLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRR 136

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018536931 1091 LNppEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEA 1162
Cdd:cd14538    137 IH--NSGPIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 866-1161 2.60e-61

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: 211.90  E-value: 2.60e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  866 PAIRVADLLQHITQMKRGQGY-GFKEEYEAL--PEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYI 942
Cdd:cd14627      5 PARNLYSYIQKLAQVEVGEHVtGMELEFKRLanSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  943 NANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYWPD 1022
Cdd:cd14627     85 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGRE--------------------KCHQYWPA 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1023 DTEVygdiKVTLIETEPLAE-----YVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPP--E 1095
Cdd:cd14627    145 ERSA----RYQYFVVDPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQ 220

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931 1096 AGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14627    221 DGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 916-1161 3.14e-61

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: 209.13  E-value: 3.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  916 RYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHp 995
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  996 aehtvgnatlgraaspgmvKCVRYWPDDTEV-YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGV 1074
Cdd:cd14623     80 -------------------KCAQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGI 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1075 PCYATGLLGFVRQVKfLNPPEAG--PIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQY 1152
Cdd:cd14623    141 PSDGKGMINIIAAVQ-KQQQQSGnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQY 219


                   ....*....
gi 2018536931 1153 VFVHDAILE 1161
Cdd:cd14623    220 EFCYKVVQE 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 914-1161 2.49e-60

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: 207.00  E-value: 2.49e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  914 KNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGR 993
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  994 HpaehtvgnatlgraaspgmvKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKgyHEIRELRLFHFTSWP 1070
Cdd:cd14602     81 K--------------------KCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWP 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1071 DHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAEnEGVV----DIFNCVRELRAQRVNLV 1146
Cdd:cd14602    139 DHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLV 217

                          250
                   ....*....|....*
gi 2018536931 1147 QTEEQYVFVHDAILE 1161
Cdd:cd14602    218 QTKEQYELVYNAVIE 232
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 941-1157 6.00e-60

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: 204.55  E-value: 6.00e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYW 1020
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQ--------------------EQCAQYW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKF---LNPPEAG 1097
Cdd:cd14558     61 GDEKKTYGDIEVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQklpYKNSKHG 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018536931 1098 ---PIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHD 1157
Cdd:cd14558    141 rsvPIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 914-1156 1.36e-59

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: 204.38  E-value: 1.36e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  914 KNRYGNIISYDHSRVRLLVLD-GDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEV 991
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  992 GRhpaehtvgnatlgraaspgmvKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGyhEIRELRLFHFTSWPD 1071
Cdd:cd14611     82 NE---------------------KCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPD 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1072 HGVPCYATGLLGFVRQVK--FLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTE 1149
Cdd:cd14611    139 HKTPDSAQPLLQLMLDVEedRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTS 218


                   ....*..
gi 2018536931 1150 EQYVFVH 1156
Cdd:cd14611    219 EQYEFVH 225
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 940-1162 4.43e-59

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: 202.56  E-value: 4.43e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  940 DYINANYIDgYHRPRH-----YIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmV 1014
Cdd:cd14541      1 DYINANYVN-MEIPGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGR--------------------V 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1015 KCVRYWPD--DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLN 1092
Cdd:cd14541     60 KCHQYWPDlgETMQFGNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNR 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1093 PPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEA 1162
Cdd:cd14541    140 VGMVEPTVVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 941-1156 5.63e-59

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: 201.88  E-value: 5.63e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYW 1020
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKK--------------------KCERYW 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 P---DDTEVYGDIKVTLIETEPLAE-YVIRTFTVQKKgyHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEA 1096
Cdd:cd14542     61 PeegEEQLQFGPFKISLEKEKRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSED 138

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018536931 1097 GPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVD---IFNCVRELRAQRVNLVQTEEQYVFVH 1156
Cdd:cd14542    139 VPICVHCSAGCGRTGTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 866-1161 9.22e-59

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: 204.57  E-value: 9.22e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  866 PAIRVADLLQHITQMKRGQGYGFKE-EYEAL--PEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYI 942
Cdd:cd14629      5 PARNLYAHIQKLTQVPPGESVTAMElEFKLLanSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  943 NANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYWPD 1022
Cdd:cd14629     85 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE--------------------KCHQYWPA 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1023 DTEVygdiKVTLIETEPLAE-----YVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPP--E 1095
Cdd:cd14629    145 ERSA----RYQYFVVDPMAEynmpqYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQfgQ 220

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931 1096 AGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14629    221 DGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 914-1156 1.05e-58

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: 202.76  E-value: 1.05e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  914 KNRYGNIISYDHSRVRL-LVLDGDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEv 991
Cdd:cd14612     18 KDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE- 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  992 grhpaehtvgnatlgraaspGMVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGyhEIRELRLFHFTSWPD 1071
Cdd:cd14612     97 --------------------KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPD 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1072 HGVPCYATGLLGFVRQVK--FLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTE 1149
Cdd:cd14612    155 HQTPESAGPLLRLVAEVEesRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTS 234


                   ....*..
gi 2018536931 1150 EQYVFVH 1156
Cdd:cd14612    235 EQYQFLH 241
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 910-1160 2.43e-57

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: 198.52  E-value: 2.43e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  910 ENRNKNRYGNIISYDHSRVRLlvldGDPHsDYINANYI-----DGYHRprhYIATQGPMQETVKDFWRMIWQENSASIVM 984
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIkmpvgDEEFV---YIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  985 VTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWPDD----TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRE 1060
Cdd:cd14597     74 MTQEVEGGK--------------------IKCQRYWPEIlgktTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRH 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1061 LRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNppEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRA 1140
Cdd:cd14597    134 ITHLNFTAWPDHDTPSQPEQLLTFISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRL 211

                          250       260
                   ....*....|....*....|
gi 2018536931 1141 QRVNLVQTEEQYVFVHDAIL 1160
Cdd:cd14597    212 QRHGMVQTEDQYIFCYQVIL 231
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 914-1154 4.44e-57

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: 197.61  E-value: 4.44e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  914 KNRYGNIISYDHSRVRLLVLDGDphSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEvgr 993
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLME--- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  994 hpaehtvgnatlgraasPGMVKCVRYWPDDtEVYGDI------KVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFT 1067
Cdd:cd14545     76 -----------------KGQIKCAQYWPQG-EGNAMIfedtglKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYT 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1068 SWPDHGVPCYATGLLGF---VRQVKFLNpPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGV--VDIFNCVRELRAQR 1142
Cdd:cd14545    138 TWPDFGVPESPAAFLNFlqkVRESGSLS-SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYR 216

                          250
                   ....*....|..
gi 2018536931 1143 VNLVQTEEQYVF 1154
Cdd:cd14545    217 MGLIQTPDQLRF 228
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 29-189 1.67e-56

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 192.94  E-value: 1.67e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931    29 AGGCSFDEHySNCGYSVALgTNGFTWEQINTWEK---PMLDQAVPTGSFMMVNSSGRASGQKAHLLLPTLKEN-DTHCID 104
Cdd:smart00137    3 PGNCDFEEG-STCGWHQDS-NDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   105 FHYYFSsrdRSSPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTfWPHFYQVIFESVSLKGHPGYIAVDEVRV 184
Cdd:smart00137   81 FWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 2018536931   185 LAHPC 189
Cdd:smart00137  157 SNGPC 161
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 888-1161 6.00e-56

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: 196.43  E-value: 6.00e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  888 FKEEYEALP--EGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGyHRPRH--YIATQGPM 963
Cdd:cd14610     19 LEKEWEALCayQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRNpaYIATQGPL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  964 QETVKDFWRMIWQENSASIVMVTNLVEvgrhpaehtvgnatlgraasPGMVKCVRYWPDD-TEVYGDIKVTLIETEPLAE 1042
Cdd:cd14610     98 PATVADFWQMVWESGCVVIVMLTPLAE--------------------NGVKQCYHYWPDEgSNLYHIYEVNLVSEHIWCE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1043 -YVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLD 1121
Cdd:cd14610    158 dFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLN 237

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2018536931 1122 -MAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14610    238 kMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 890-1161 9.61e-55

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: 192.56  E-value: 9.61e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  890 EEYEALP--EGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGyHRPR--HYIATQGPMQE 965
Cdd:cd14609     19 KEWQALCayQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSH 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  966 TVKDFWRMIWQENSASIVMVTNLVEvgrhpaehtvgnatlgraasPGMVKCVRYWPDD-TEVYGDIKVTLIETEPLAE-Y 1043
Cdd:cd14609     98 TIADFWQMVWENGCTVIVMLTPLVE--------------------DGVKQCDRYWPDEgSSLYHIYEVNLVSEHIWCEdF 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1044 VIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLD-M 1122
Cdd:cd14609    158 LVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrM 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2018536931 1123 AENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14609    238 AKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 906-1170 3.01e-54

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: 191.01  E-value: 3.01e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  906 AKEDENRNKNRYGNIISYDHSRVRLLVLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMv 985
Cdd:cd14608     20 AKLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVM- 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  986 tnlvevgrhpaehtvgnatLGRAASPGMVKCVRYWPDDTE---VYGD--IKVTLIETEPLAEYVIRTFTVQKKGYHEIRE 1060
Cdd:cd14608     95 -------------------LNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETRE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1061 LRLFHFTSWPDHGVPCYATGLLGF---VRQVKFLNpPEAGPIVVHCSAGAGRTGCFIAIDT---MLDMAENEGVVDIFNC 1134
Cdd:cd14608    156 ILHFHYTTWPDFGVPESPASFLNFlfkVRESGSLS-PEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKV 234

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2018536931 1135 VRELRAQRVNLVQTEEQYVFVHDAILEAC--LCGNTAI 1170
Cdd:cd14608    235 LLEMRKFRMGLIQTADQLRFSYLAVIEGAkfIMGDSSV 272
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 940-1159 4.55e-53

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: 184.82  E-value: 4.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  940 DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRY 1019
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQE--------------------KCVQY 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1020 WPDDTEV-YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKfLNPPEAG- 1097
Cdd:cd14622     61 WPSEGSVtHGEITIEIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQ-KQQQQTGn 139

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018536931 1098 -PIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAI 1159
Cdd:cd14622    140 hPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 906-1160 1.38e-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: 186.21  E-value: 1.38e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  906 AKEDENRNKNRYGNIISYDHSRVrllVLDGDphSDYINANYID----GYHRPRHYIATQGPMQETVKDFWRMIWQENSAS 981
Cdd:cd14600     35 AKLPQNMDKNRYKDVLPYDATRV---VLQGN--EDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  982 IVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVRYWPDDTEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIR 1059
Cdd:cd14600    110 IVMLTTLTERGR--------------------TKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEER 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1060 ELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPpEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELR 1139
Cdd:cd14600    170 TVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMR 248

                          250       260
                   ....*....|....*....|.
gi 2018536931 1140 AQRVNLVQTEEQYVFVHDAIL 1160
Cdd:cd14600    249 DQRAMMVQTSSQYKFVCEAIL 269
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 906-1159 3.86e-50

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: 178.62  E-value: 3.86e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  906 AKEDENRNKNRYGNIISYDHSRVRLLVLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMV 985
Cdd:cd14607     19 AKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  986 TNLVEvgrhpaehtvgnatlgraasPGMVKCVRYWPDDTE---VYGD--IKVTLIETEPLAEYVIRTFTVQKKGYHEIRE 1060
Cdd:cd14607     95 NRIVE--------------------KDSVKCAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1061 LRLFHFTSWPDHGVPCYATGLLGF---VRQVKFLNpPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEG--VVDIFNCV 1135
Cdd:cd14607    155 ISHFHYTTWPDFGVPESPASFLNFlfkVRESGSLS-PEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVL 233

                          250       260
                   ....*....|....*....|....
gi 2018536931 1136 RELRAQRVNLVQTEEQYVFVHDAI 1159
Cdd:cd14607    234 LDMRKYRMGLIQTPDQLRFSYMAV 257
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 941-1161 3.25e-49

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: 174.57  E-value: 3.25e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGY--HRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVR 1018
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGR--------------------EKCFR 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1019 YWPD-----DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGF------VR- 1086
Cdd:cd14540     61 YWPTlggehDALTFGEYKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsVRr 140

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018536931 1087 ---QVKFLNPPEAgPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14540    141 htnQDVAGHNRNP-PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 941-1161 7.65e-49

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: 173.01  E-value: 7.65e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGyHRPRH--YIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVgrhpaehtvgnatlgraaspGMVKCVR 1018
Cdd:cd14546      1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQEN--------------------GVKQCAR 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1019 YWPDD-TEVYGDIKVTLI-ETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEA 1096
Cdd:cd14546     60 YWPEEgSEVYHIYEVHLVsEHIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRS 139

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931 1097 GPIVVHCSAGAGRTGCFIAIDTMLD-MAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14546    140 CPIVVHCSDGAGRTGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 941-1157 1.79e-48

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: 171.44  E-value: 1.79e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLvevgrhpaehtvgnatlgraaSPGMVKCVRYW 1020
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQL---------------------DPKDQSCPQYW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTE-VYGDIKVTLIETEpLAEYVI-RTFTVQ--KKGYHEIRELRLFHFTSWPDHG-VPCYATGLLGFVRQV-KFLNPP 1094
Cdd:cd14556     60 PDEGSgTYGPIQVEFVSTT-IDEDVIsRIFRLQntTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQS 138

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018536931 1095 EAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHD 1157
Cdd:cd14556    139 GEGPIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1218-1454 3.33e-48

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 172.32  E-value: 3.33e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1218 LPRNHDKNRSMDVLPLDR---CLPFLISVDGesSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML 1294
Cdd:cd14554      3 LPCNKFKNRLVNILPYEStrvCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1295 ---NEMDTAQfCMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNmARpQDGYRIVQHLQYIGWPAyRDTPPSKRS 1371
Cdd:cd14554     81 tklREMGREK-CHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTD-AR-DGQSRTVRQFQFTDWPE-QGVPKSGEG 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1372 LLKVVRRLEKWQEQYdGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14554    157 FIDFIGQVHKTKEQF-GQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235


                   ...
gi 2018536931 1452 VAL 1454
Cdd:cd14554    236 AAL 238
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1250-1451 9.67e-48

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: 169.50  E-value: 9.67e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DTAQFCMQYWPEKTSgCYGPIQVEFVSADI 1327
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELkeGDQEQCAQYWGDEKK-TYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1328 DEDIIHRIFRICNMARPQDgyRIVQHLQYIGWpAYRDTPPSKRSLLKVVRRLEKWQEQYDGREGRT---VVHCLNGGGRS 1404
Cdd:cd14558     80 SPTYTVRVFEITHLKRKDS--RTVYQYQYHKW-KGEELPEKPKDLVDMIKSIKQKLPYKNSKHGRSvpiVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2018536931 1405 GTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14558    157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 940-1161 7.58e-47

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: 167.43  E-value: 7.58e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  940 DYINANYIDgYHRP-----RHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmV 1014
Cdd:cd14601      1 DYINANYIN-MEIPsssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGR--------------------V 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1015 KCVRYWPD--DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLN 1092
Cdd:cd14601     60 KCHQYWPEpsGSSSYGGFQVTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKR 139

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018536931 1093 PPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14601    140 AGKDEPVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1250-1452 9.18e-47

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: 166.68  E-value: 9.18e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD--TAQFCMQYWPEKTSGCYGPIQVEFVSADI 1327
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKerSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1328 DEDIIHRIFRICNmARPQDGyRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLEKwQEQYDGrEGRTVVHCLNGGGRSGTF 1407
Cdd:cd14552     81 YEDYTLRDFLVTK-GKGGST-RTVRQFHFHGWPEV-GIPDNGKGMIDLIAAVQK-QQQQSG-NHPITVHCSAGAGRTGTF 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2018536931 1408 CAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEV 1452
Cdd:cd14552    156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 941-1162 3.96e-46

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: 164.92  E-value: 3.96e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGY--HRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgmVKCVR 1018
Cdd:cd14596      1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGK--------------------VKCHR 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1019 YWPD---DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNppE 1095
Cdd:cd14596     61 YWPEtlqEPMELENYQLRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--N 138

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018536931 1096 AGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEA 1162
Cdd:cd14596    139 TGPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
910-1152 5.22e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.58  E-value: 5.22e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  910 ENRNKNRYGNIISYDHSRVRllvldgdPHSDYINANYIDGYhRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLV 989
Cdd:COG5599     41 NGSPLNRFRDIQPYKETALR-------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  990 EVgrhpaehtvgnatlgraaSPGMVKCVRYWPDDTEvYG--DIKVTLIETEPLAEYV-IRTFTVQKKGY-HEIRELRLFH 1065
Cdd:COG5599    113 EI------------------SKPKVKMPVYFRQDGE-YGkyEVSSELTESIQLRDGIeARTYVLTIKGTgQKKIEIPVLH 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1066 FTSWPDHGVPCYAT--GLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDM--AENEGVVDIFNCVRELRAQ 1141
Cdd:COG5599    174 VKNWPDHGAISAEAlkNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRTS 253

                          250
                   ....*....|..
gi 2018536931 1142 RVN-LVQTEEQY 1152
Cdd:COG5599    254 RNGgMVQTSEQL 265
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1226-1451 2.20e-45

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: 163.68  E-value: 2.20e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1226 RSMDVLPLDRCLPFLISVDGES-SNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDTAQF- 1302
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLtQCMEKGRVk 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1303 CMQYWPEKTSGC-YGPIQVEFVSADIDEDIIHRIFRICNmarpQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLEK 1381
Cdd:cd14548     81 CDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKLER----GDEVRSVRQFHFTAWPDH-GVPEAPDSLLRFVRLVRD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1382 WQEQydgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14548    156 YIKQ---EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PHA02738 PHA02738
hypothetical protein; Provisional
 908-1159 2.36e-45

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 167.02  E-value: 2.36e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  908 EDENRNKNRYGNIISYDHSRVRLLVLDGdpHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTN 987
Cdd:PHA02738    46 EKKNRKLNRYLDAVCFDHSRVILPAERN--RGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  988 LVEVGRHpaehtvgnatlgraaspgmvKCVRYWPD---DTEVYGDIKVTLIETEPLAEYVIRTFTVqKKGYHEIRELRLF 1064
Cdd:PHA02738   124 KKENGRE--------------------KCFPYWSDveqGSIRFGKFKITTTQVETHPHYVKSTLLL-TDGTSATQTVTHF 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1065 HFTSWPDHGVPCYATGLLGFVRQVK----------------FLNPPeagPIVVHCSAGAGRTGCFIAIDTMLDMAENEGV 1128
Cdd:PHA02738   183 NFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighnRLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACAT 259

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2018536931 1129 VDIFNCVRELRAQRVNLVQTEEQYVFVHDAI 1159
Cdd:PHA02738   260 VSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 890-1156 2.84e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 166.33  E-value: 2.84e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  890 EEYEALPEGQTASWDTAKEDENRNKNRYGNIISYDHSRVrLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKD 969
Cdd:PHA02747    30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRV-ILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCAD 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  970 FWRMIWQENSASIVMVTnlvevgrhPAEHTVGNAtlgraaspgmvKCVRYW---PDDTEVYGDIKVTLIETEPLAEYVIR 1046
Cdd:PHA02747   109 FWKAVWQEHCSIIVMLT--------PTKGTNGEE-----------KCYQYWclnEDGNIDMEDFRIETLKTSVRAKYILT 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1047 TFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGF------VRQV--KFLNPPEA--GPIVVHCSAGAGRTGCFIAI 1116
Cdd:PHA02747   170 LIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFikiidiNRKKsgKLFNPKDAllCPIVVHCSDGVGKTGIFCAV 249

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2018536931 1117 DTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVH 1156
Cdd:PHA02747   250 DICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1249-1456 1.84e-44

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: 160.17  E-value: 1.84e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1249 NYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDT--AQFCMQYWPEKTSGCYGPIQVEFVSAD 1326
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEreQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1327 IDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLEKWQEQYDGREgrTVVHCLNGGGRSGT 1406
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQT--RLVRQFHFHGWPEI-GIPAEGKGMIDLIAAVQKQQQQTGNHP--IVVHCSAGAGRTGT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1407 FCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEY 1456
Cdd:cd14622    156 FIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1168-1460 2.65e-44

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 162.98  E-value: 2.65e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1168 TAIPVCEFRSLYYNISRLDPQTNSSQIKDEFQTLniVTPRVRPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDG-E 1246
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRL--ASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1247 SSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTA--QFCMQYWPEKTSGCYgpiQVEFVS 1324
Cdd:cd14628     79 GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMgrEKCHQYWPAERSARY---QYFVVD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1325 ADIDEDIIHRIFRICNMARPQDGY-RIVQHLQYIGWPAyRDTPPSKRSLLKVVRRLEKWQEQYdGREGRTVVHCLNGGGR 1403
Cdd:cd14628    156 PMAEYNMPQYILREFKVTDARDGQsRTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPISVHCSAGVGR 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2018536931 1404 SGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYLSSF 1460
Cdd:cd14628    234 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSF 290
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1167-1459 2.73e-44

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 162.98  E-value: 2.73e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1167 NTAIPVcefRSLYYNISRL---DPQTNSSQIKDEFQTLniVTPRVRPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISV 1243
Cdd:cd14627      1 NTEVPA---RNLYSYIQKLaqvEVGEHVTGMELEFKRL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1244 DG-ESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTA--QFCMQYWPEKTSGCYgpiQV 1320
Cdd:cd14627     76 RGvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMgrEKCHQYWPAERSARY---QY 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1321 EFVSADIDEDIIHRIFRICNMARPQDGY-RIVQHLQYIGWPAyRDTPPSKRSLLKVVRRLEKWQEQYdGREGRTVVHCLN 1399
Cdd:cd14627    153 FVVDPMAEYNMPQYILREFKVTDARDGQsRTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPISVHCSA 230

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1400 GGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYLSS 1459
Cdd:cd14627    231 GVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1212-1450 5.96e-44

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: 160.99  E-value: 5.96e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1212 DCSigLLPRNHDKNRSMDVLPLDRCLPFLISVDG-ESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSS 1290
Cdd:cd14543     22 LCS--LAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1291 VVMLNEMDTA--QFCMQYWP--EKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMArpQDGYRIVQHLQYIGWPAYrDTP 1366
Cdd:cd14543    100 IVMTTRVVERgrVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTE--TDESRQVTHFQFTSWPDF-GVP 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1367 PSKRSLL---KVVRRLEKWQEQYDGREGR-------TVVHCLNGGGRSGTFCA--ICsvCEMIQQQNIIDVFHIVKTLRN 1434
Cdd:cd14543    177 SSAAALLdflGEVRQQQALAVKAMGDRWKghppgppIVVHCSAGIGRTGTFCTldIC--LSQLEDVGTLNVMQTVRRMRT 254

                          250
                   ....*....|....*.
gi 2018536931 1435 NKSNMVETLEQYKFVY 1450
Cdd:cd14543    255 QRAFSIQTPDQYYFCY 270
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 888-1161 1.24e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 161.32  E-value: 1.24e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  888 FKEEYEALPEGQTA-SWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDphSDYINANYIDGYHRPRHYIATQGPMQET 966
Cdd:PHA02742    28 LKEEHEHIMQEIVAfSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDGG--DDFINASYVDGHNAKGRFICTQAPLEET 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  967 VKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVRYW---PDDTEVYGDIKVTLIETEPLAEY 1043
Cdd:PHA02742   106 ALDFWQAIFQDQVRVIVMITKIMEDGKE--------------------ACYPYWmphERGKATHGEFKIKTKKIKSFRNY 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1044 VIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFL-----------NPPEAGPIVVHCSAGAGRTGC 1112
Cdd:PHA02742   166 AVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGA 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2018536931 1113 FIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:PHA02742   246 FCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1167-1460 2.14e-43

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: 160.28  E-value: 2.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1167 NTAIPVcefRSLYYNISRLD---PQTNSSQIKDEFQTLniVTPRVRPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISV 1243
Cdd:cd14629      1 NTEVPA---RNLYAHIQKLTqvpPGESVTAMELEFKLL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1244 DG-ESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTA--QFCMQYWPEKTSGCYgpiQV 1320
Cdd:cd14629     76 RGvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMgrEKCHQYWPAERSARY---QY 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1321 EFVSADIDEDIIHRIFRICNMARPQDGY-RIVQHLQYIGWPAyRDTPPSKRSLLKVVRRLEKWQEQYdGREGRTVVHCLN 1399
Cdd:cd14629    153 FVVDPMAEYNMPQYILREFKVTDARDGQsRTIRQFQFTDWPE-QGVPKTGEGFIDFIGQVHKTKEQF-GQDGPITVHCSA 230

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1400 GGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYLSSF 1460
Cdd:cd14629    231 GVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSF 291
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 941-1154 5.44e-43

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: 156.09  E-value: 5.44e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRH--YIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraaspgMVKCVR 1018
Cdd:cd17658      1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYS-------------------TAKCAD 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1019 YWPD---DTEVYGDIKVTlIETEPLAEYVI--RTFTVQKKgYHEIRELRLFH--FTSWPDHGVPCYATGLLGFVRQVkFL 1091
Cdd:cd17658     62 YFPAeenESREFGRISVT-NKKLKHSQHSItlRVLEVQYI-ESEEPPLSVLHiqYPEWPDHGVPKDTRSVRELLKRL-YG 138

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018536931 1092 NPPEAGPIVVHCSAGAGRTGCFIAIDTMLD--MAENEGVVDIFNCVRELRAQRVNLVQTEEQYVF 1154
Cdd:cd17658    139 IPPSAGPIVVHCSAGIGRTGAYCTIHNTIRriLEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1221-1459 1.26e-42

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: 156.02  E-value: 1.26e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1221 NHDKNRSMDVLPLDRCLPFLISVDG-ESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EM 1297
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTklEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1298 DTAQFCMQYWPEKTSGCYGPIQVEFVsadideDIIH------RIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRS 1371
Cdd:cd14553     83 RSRVKCDQYWPTRGTETYGLIQVTLL------DTVElatytvRTFALHKNGSSEK--REVRQFQFTAWPDH-GVPEHPTP 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1372 LLKVVRRLeKWQEQYDGreGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14553    154 FLAFLRRV-KACNPPDA--GPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHD 230


                   ....*...
gi 2018536931 1452 VALEYLSS 1459
Cdd:cd14553    231 ALLEAVTC 238
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1246-1455 1.77e-42

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: 155.59  E-value: 1.77e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1246 ESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDT--AQFCMQYWPEKTSGCYGPIQVEFV 1323
Cdd:cd14623     22 ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErgQEKCAQYWPSDGSVSYGDITIELK 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1324 SADIDEDIIHRIFRICNMArpQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLEKwQEQYDGREGRTVvHCLNGGGR 1403
Cdd:cd14623    102 KEEECESYTVRDLLVTNTR--ENKSRQIRQFHFHGWPEV-GIPSDGKGMINIIAAVQK-QQQQSGNHPITV-HCSAGAGR 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2018536931 1404 SGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14623    177 TGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 891-1161 3.38e-42

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: 156.70  E-value: 3.38e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  891 EYEALPEGQT-ASWDTAKEDENRNKNRYGNIISYDHSRVRLlVLDGDPHSDYINANYIDGYHRPR--HYIATQGPMQETV 967
Cdd:cd14599     17 EYEQIPKKKAdGVFTTATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGGEewHYIATQGPLPHTC 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  968 KDFWRMIWQENSASIVMVTNLVEVGRhPAEHtvgnatlgraaspgmvkcvRYWPD-----DTEVYGDIKVTLIETEPLAE 1042
Cdd:cd14599     96 HDFWQMVWEQGVNVIAMVTAEEEGGR-SKSH-------------------RYWPKlgskhSSATYGKFKVTTKFRTDSGC 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1043 YVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQV--------------KFLNPPeagpIVVHCSAGAG 1108
Cdd:cd14599    156 YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIqsvrrhtnsmldstKNCNPP----IVVHCSAGVG 231

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2018536931 1109 RTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14599    232 RTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1186-1455 8.19e-42

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 155.60  E-value: 8.19e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1186 DPQTNSSQIKDEFQTLniVTPRVRPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDGES-SNYINAA-LMDSHKQPA 1263
Cdd:cd14610     11 DHLKNKNRLEKEWEAL--CAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHShSDYINASpIMDHDPRNP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1264 AFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DTAQFCMQYWPEKTSGCYGPIQVEFVSADI-DEDIIHRIFRICN 1340
Cdd:cd14610     89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLaeNGVKQCYHYWPDEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKN 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1341 MARPQDgyRIVQHLQYIGWPAyRDTPPSKRSLLKVVRRLEKWqeqYDGREGRTVVHCLNGGGRSGTFCAICSVC-EMIQQ 1419
Cdd:cd14610    169 LQTNET--RTVTQFHFLSWND-QGVPASTRSLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRSGTYILIDMVLnKMAKG 242

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2018536931 1420 QNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14610    243 AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 941-1157 2.48e-41

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 151.38  E-value: 2.48e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGY--HRPRhYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVR 1018
Cdd:cd14539      1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQ--------------------KVHR 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1019 YWPDD---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQV-KFLNP- 1093
Cdd:cd14539     60 YWPTErgqALVYGAITVSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhSHYLQq 139

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931 1094 -PEAGPIVVHCSAGAGRTGCF-IAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHD 1157
Cdd:cd14539    140 rSLQTPIVVHCSSGVGRTGAFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 32-189 4.04e-41

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 148.68  E-value: 4.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   32 CSFDEHYsnCGYSVALgTNGFTWEQINTWEK-----PMLDQAVPTGSFMMVNSSGRASGQKAHLLLPTLKEN-DTHCIDF 105
Cdd:cd06263      1 CDFEDGL--CGWTQDS-TDDFDWTRVSGSTPspgtpPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  106 HYYFSSRDrssPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTFWPHFyQVIFESVSLKGHPGYIAVDEVRVL 185
Cdd:cd06263     78 WYHMYGSG---VGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPF-QVVFEGVRGSGSRGDIALDDISLS 153


                   ....
gi 2018536931  186 AHPC 189
Cdd:cd06263    154 PGPC 157
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1225-1450 1.17e-39

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: 147.16  E-value: 1.17e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1225 NRSMDVLP--LDR-CLPflISVDGESSNYINAALMDSHK-QPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTA 1300
Cdd:cd14547      1 NRYKTILPneHSRvCLP--SVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1301 -QFCMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRIcnmaRPQDGYRIVQHLQYIGWPAYRdTPPSKRSLLKVVRRL 1379
Cdd:cd14547     79 kEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTL----KYGGEKRYLKHYWYTSWPDHK-TPEAAQPLLSLVQEV 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1380 EKWQEQYDGReGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVY 1450
Cdd:cd14547    154 EEARQTEPHR-GPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 910-1159 3.09e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 149.41  E-value: 3.09e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  910 ENRNKNRYGNIISYDHSRV-------------------RLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDF 970
Cdd:PHA02746    50 ENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDF 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  971 WRMIWQENSASIVmvtNLVEVGRhpaEHTvgnatlgraaspgmvKCVRYW--PDDTEV-YGDIKVTLIETEPLAEYVIRT 1047
Cdd:PHA02746   130 FKLISEHESQVIV---SLTDIDD---DDE---------------KCFELWtkEEDSELaFGRFVAKILDIIEELSFTKTR 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1048 FTVQKKGYHEIRELRLFHFTSWPDHGVPcyaTGLLGFVRQVKFLN-------------PPEAGPIVVHCSAGAGRTGCFI 1114
Cdd:PHA02746   189 LMITDKISDTSREIHHFWFPDWPDNGIP---TGMAEFLELINKVNeeqaelikqadndPQTLGPIVVHCSAGIGRAGTFC 265

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2018536931 1115 AIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAI 1159
Cdd:PHA02746   266 AIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1250-1451 5.74e-39

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: 144.70  E-value: 5.74e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAalmdSHKQPAA-----FVVTQHPLPNTVADFWRLVFDYNCSSVVMLnemdTAQF------CMQYWPEKTSGC-YGP 1317
Cdd:cd18533      1 YINA----SYITLPGtsskrYIATQGPLPATIGDFWKMIWQNNVGVIVML----TPLVengrekCDQYWPSGEYEGeYGD 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1318 IQVEFVSADIDEDIIHrIFRICNMARPQDGYRIVQHLQYIGWPAYRdTPPSKRSLLKVVRrlEKWQEQYDGREGR-TVVH 1396
Cdd:cd18533     73 LTVELVSEEENDDGGF-IVREFELSKEDGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLIK--LKRELNDSASLDPpIIVH 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018536931 1397 CLNGGGRSGTFCAICSVCEMIQQQNIID---------VFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd18533    149 CSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1060-1161 7.92e-39

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 140.19  E-value: 7.92e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1060 ELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNP--PEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENE-GVVDIFNCVR 1136
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2018536931  1137 ELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1060-1161 7.92e-39

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: 140.19  E-value: 7.92e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1060 ELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNP--PEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENE-GVVDIFNCVR 1136
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2018536931  1137 ELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1225-1454 8.23e-39

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: 145.09  E-value: 8.23e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1225 NRSMDVLPLDRCLPFLISVDGES-SNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDTAQ- 1301
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVgMENGRv 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1302 FCMQYWP-EKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSLLkVVRRLE 1380
Cdd:cd14618     81 LCDHYWPsESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE--RRVKHLHYTAWPDH-GIPESTSSLM-AFRELV 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018536931 1381 KWQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVAL 1454
Cdd:cd14618    157 REHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1218-1451 1.65e-38

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: 144.65  E-value: 1.65e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1218 LPRNHDKNRSMDVLPLDRCLPFLISV-DGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNE 1296
Cdd:cd14614      9 LPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1297 MDTAQF--CMQYWP-EKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDgyriVQHLQYIGWPAYR-DTPPSKRSL 1372
Cdd:cd14614     89 CNEKRRvkCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHGvPTANAAESI 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018536931 1373 LKVVRRLekwQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14614    165 LQFVQMV---RQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1229-1455 3.03e-38

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: 143.16  E-value: 3.03e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1229 DVLPLDRCLPFLISVDG-ESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD--TAQFCMQ 1305
Cdd:cd14620      3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKerKEEKCYQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1306 YWPEKTSGCYGPIQVEFvsadidEDII----HRIFRICNMARPQDGY---RIVQHLQYIGWPAYrDTPPSKRSLLKVVRR 1378
Cdd:cd14620     83 YWPDQGCWTYGNIRVAV------EDCVvlvdYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDF-GVPFTPIGMLKFLKK 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018536931 1379 LEKWQEQYdgrEGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14620    156 VKSVNPVH---AGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1225-1455 5.39e-38

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: 142.65  E-value: 5.39e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1225 NRSMDVLPLDRCLPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML---NEMDTAQ 1301
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLtkcVEQGRTK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1302 fCMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrdTPPSKRSLLKVVRRLEK 1381
Cdd:cd14615     81 -CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNES--RTVRHFHFTSWPDH--GVPETTDLLINFRHLVR 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018536931 1382 WQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14615    156 EYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 32-190 1.16e-37

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 139.03  E-value: 1.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   32 CSFDEHYSnCGYSVALGTnGFTWEQINTWE---KPMLD--QAVPTGSFMMVNSSGRASGQKAHLLLPTLKENDT-HCIDF 105
Cdd:pfam00629    1 CDFEDGNL-CGWTQDSSD-DFDWERVSGPSvktGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  106 HYYFSSrdrSSPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTFwPHFYQVIFESVSLKGHPGYIAVDEVRVL 185
Cdd:pfam00629   79 WYHMSG---SGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLS 154


                   ....*
gi 2018536931  186 AHPCR 190
Cdd:pfam00629  155 SGPCP 159
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1186-1455 2.86e-37

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: 142.10  E-value: 2.86e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1186 DPQTNSSQIKDEFQTLniVTPRVRPEDCSIGLLPRNHDKNRSMDVLPLDRC-LPFLISVDGESSNYINAA-LMDSHKQPA 1263
Cdd:cd14609      9 DHLRNRDRLAKEWQAL--CAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHArIKLKAESNPSRSDYINASpIIEHDPRMP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1264 AFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DTAQFCMQYWPEKTSGCYGPIQVEFVSADI-DEDIIHRIFRICN 1340
Cdd:cd14609     87 AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIwCEDFLVRSFYLKN 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1341 MARPQDgyRIVQHLQYIGWPAyRDTPPSKRSLLKVVRRLEKwqeQYDGREGRTVVHCLNGGGRSGTFCAICSVC-EMIQQ 1419
Cdd:cd14609    167 VQTQET--RTLTQFHFLSWPA-EGIPSSTRPLLDFRRKVNK---CYRGRSCPIIVHCSDGAGRTGTYILIDMVLnRMAKG 240

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2018536931 1420 QNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14609    241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1250-1450 4.70e-37

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: 139.12  E-value: 4.70e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAA-LMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML---NEMDTAQfCMQYWPEKTSGCYGPIQVEFVSA 1325
Cdd:cd14546      1 YINAStIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLtrlQENGVKQ-CARYWPEEGSEVYHIYEVHLVSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1326 DI-DEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAyRDTPPSKRSLLKVVRRLEKwqeQYDGREGRTVVHCLNGGGRS 1404
Cdd:cd14546     80 HIwCDDYLVRSFYLKNLQTSET--RTVTQFHFLSWPD-EGIPASAKPLLEFRRKVNK---SYRGRSCPIVVHCSDGAGRT 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2018536931 1405 GTFCAICSVCE-MIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVY 1450
Cdd:cd14546    154 GTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1225-1457 4.86e-37

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 140.02  E-value: 4.86e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1225 NRSMDVLPLDRC-LPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDTAQF 1302
Cdd:cd14619      1 NRFRNVLPYDWSrVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLtNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1303 -CMQYWPEKTSGC-YGPIQVEFVSADIDEDIIHRIFRICNMArpQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLE 1380
Cdd:cd14619     81 kCEHYWPLDYTPCtYGHLRVTVVSEEVMENWTVREFLLKQVE--EQKTLSVRHFHFTAWPDH-GVPSSTDTLLAFRRLLR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018536931 1381 KWQEQYDgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYL 1457
Cdd:cd14619    158 QWLDQTM-SGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1250-1451 5.79e-37

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: 138.64  E-value: 5.79e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDTAQF-CMQYWPEKTSGCYGPIQVEFVSADI 1327
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMItNLVERGRRkCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1328 DEDIIHRIFRICNM----ARPQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRlekwQEQYDGRE-GRTVVHCLNGGG 1402
Cdd:cd14549     81 LATYTVRTFSLKNLklkkVKGRSSERVVYQYHYTQWPDH-GVPDYTLPVLSFVRK----SSAANPPGaGPIVVHCSAGVG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2018536931 1403 RSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14549    156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1221-1455 4.62e-36

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: 138.63  E-value: 4.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1221 NHDKNRSMDVLPLDRCLPFLISVDG-ESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDT 1299
Cdd:cd14626     41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1300 AQF--CMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSLLKVVR 1377
Cdd:cd14626    121 KSRvkCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEK--REVRQFQFMAWPDH-GVPEYPTPILAFLR 197

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018536931 1378 RLEKWQEQydgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14626    198 RVKACNPP---DAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1250-1451 3.64e-35

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: 133.22  E-value: 3.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQFCMQYWP--EKTSGCyGPIQVEFVSADI 1327
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPtkEKPLEC-ETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1328 -----DEDIIHRIFRICNMarpQDGYRI-VQHLQYIGWPAyRDTPPSkrsllKVVRRLEKWQEQYDGREGRTVVHCLNGG 1401
Cdd:cd14550     80 sclsnEIRLIVRDFILEST---QDDYVLeVRQFQCPSWPN-PCSPIH-----TVFELINTVQEWAQQRDGPIVVHDRYGG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1402 GRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14550    151 VQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1208-1450 4.59e-35

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: 134.58  E-value: 4.59e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1208 VRPEDCSIgllPRNHDKNRSMDVLPLDR---CLPFLISVDgESSNYINAA-LMDSHKQPAAFVVTQHPLPNTVADFWRLV 1283
Cdd:cd14612      5 VSPEELDI---PGHASKDRYKTILPNPQsrvCLRRAGSQE-EEGSYINANyIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1284 FDYNCSSVVMLNEM-DTAQFCMQYWPEKtSGCYGPIQVEFVSA-DIDEDIIHRIfricnMARPQDGYRIVQHLQYIGWPA 1361
Cdd:cd14612     81 WQEECPIIVMITKLkEKKEKCVHYWPEK-EGTYGRFEIRVQDMkECDGYTIRDL-----TIQLEEESRSVKHYWFSSWPD 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1362 YRdTPPSKRSLLKVVRRLEKwQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVE 1441
Cdd:cd14612    155 HQ-TPESAGPLLRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQ 232


                   ....*....
gi 2018536931 1442 TLEQYKFVY 1450
Cdd:cd14612    233 TSEQYQFLH 241
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1250-1457 6.01e-35

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: 132.88  E-value: 6.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAalmdSH------KQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN-EMDTAQF-CMQYWPE---KTSGCYGPI 1318
Cdd:cd14538      1 YINA----SHiripvgGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTqDVEGGKVkCHRYWPDslnKPLICGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1319 QVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLEKWQeqydgREGRTVVHCL 1398
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEV--HHITHLNFTTWPDH-GTPQSADPLLRFIRYMRRIH-----NSGPIVVHCS 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2018536931 1399 NGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYL 1457
Cdd:cd14538    149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1213-1456 7.09e-35

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: 135.92  E-value: 7.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1213 CSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDG-ESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSV 1291
Cdd:cd14621     44 CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATI 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1292 VMLNEMDTAQ--FCMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMA-----RPQdgyRIVQHLQYIGWPAYrD 1364
Cdd:cd14621    124 VMVTNLKERKecKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGdvtnkKPQ---RLITQFHFTSWPDF-G 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1365 TPPSKRSLLKVVRRLEKWQEQYdgrEGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLE 1444
Cdd:cd14621    200 VPFTPIGMLKFLKKVKNCNPQY---AGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDM 276

                          250
                   ....*....|..
gi 2018536931 1445 QYKFVYEVALEY 1456
Cdd:cd14621    277 QYVFIYQALLEH 288
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1221-1455 7.49e-35

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: 133.61  E-value: 7.49e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1221 NHDKNRSMDVLPLDRCLPFLISVDGES-SNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMD 1298
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVtNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1299 TAQF-CMQYWPEKTSgCYGPIQVEFVSADIDEDIIHRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVVR 1377
Cdd:cd14630     83 VGRVkCVRYWPDDTE-VYGDIKVTLIETEPLAEYVIRTFTV--QKKGYHEIREIRQFHFTSWPDH-GVPCYATGLLGFVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018536931 1378 RLeKWQEQYDGreGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14630    159 QV-KFLNPPDA--GPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1208-1452 1.19e-34

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: 133.83  E-value: 1.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1208 VRPEDCSIGLLPRnhdKNRSMDVLPLDRCLPFLISVDGES--SNYINAALMDSH-KQPAAFVVTQHPLPNTVADFWRLVF 1284
Cdd:cd14613     15 VDPKEYDIPGLVR---KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVW 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1285 DYNCSSVVML-NEMDTAQFCMQYWPEKtSGCYGPIQVEFVSADIDEDIIHRIFRIcnmaRPQDGYRIVQHLQYIGWPAYR 1363
Cdd:cd14613     92 QERSPIIVMItNIEEMNEKCTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITL----KSGGEERGLKHYWYTSWPDQK 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1364 dTPPSKRSLLKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETL 1443
Cdd:cd14613    167 -TPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTC 245


                   ....*....
gi 2018536931 1444 EQYKFVYEV 1452
Cdd:cd14613    246 EQYQFVHHV 254
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1225-1451 1.52e-34

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: 132.74  E-value: 1.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1225 NRSMDVLPLDRCLPFLISVDGES-SNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDTA 1300
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTqcvEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1301 QfCMQYWP-EKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARpQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRL 1379
Cdd:cd14617     81 K-CDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQ-LDAPRLVRHFHYTVWPDH-GVPETTQSLIQFVRTV 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018536931 1380 EKWQEQYDGrEGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14617    158 RDYINRTPG-SGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1250-1455 1.90e-34

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: 131.58  E-value: 1.90e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDTAQF-CMQYWPEKTSgCYGPIQVEFVSADI 1327
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVtNLVEVGRVkCSRYWPDDTE-VYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1328 DEDIIHRIFricnmARPQDGY---RIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLeKWQEQYDGreGRTVVHCLNGGGRS 1404
Cdd:cd14555     80 LAEYVVRTF-----ALERRGYheiREVRQFHFTGWPDH-GVPYHATGLLGFIRRV-KASNPPSA--GPIVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1405 GTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1215-1455 2.19e-34

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: 133.41  E-value: 2.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1215 IGLLPRNHDKNRSMDVLPLDR---CLPFLisVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSV 1291
Cdd:cd14603     24 AGGRKENVKKNRYKDILPYDQtrvILSLL--QEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVI 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1292 VM-LNEMDTA-QFCMQYWP-EKTSGCYGPIQVEFVSAD-IDEDIIHRIFRIcnmaRPQDGYRIVQHLQYIGWPAyRDTPP 1367
Cdd:cd14603    102 LMaCREIEMGkKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKV----TFQKESRSVSHFQYMAWPD-HGIPD 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1368 SKRSLLKVVRRLEKWQEqydgrEGRT--VVHCLNGGGRSGTFCAICSVCEMIQQQNIID---VFHIVKTLRNNKSNMVET 1442
Cdd:cd14603    177 SPDCMLAMIELARRLQG-----SGPEplCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQT 251

                          250
                   ....*....|...
gi 2018536931 1443 LEQYKFVYEVALE 1455
Cdd:cd14603    252 EEQYEFLYHTVAQ 264
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1250-1451 2.47e-34

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: 131.19  E-value: 2.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDT--AQFCMQYWPEKTSGCYGPIQV--EFVSA 1325
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErkEKKCSQYWPDQGCWTYGNLRVrvEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1326 DIDEDI----IHRIFRICNMARPqdgyRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLEKWQEQYDGRegrTVVHCLNGG 1401
Cdd:cd14551     81 LVDYTTrkfcIQKVNRGIGEKRV----RLVTQFHFTSWPDF-GVPFTPIGMLKFLKKVKSANPPRAGP---IVVHCSAGV 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1402 GRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14551    153 GRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 941-1161 7.51e-34

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: 130.48  E-value: 7.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRH--YIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHpaehtvgnatlgraaspgmvKCVR 1018
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGRE--------------------KSFR 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1019 YWP-----DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFL-- 1091
Cdd:cd14598     61 YWPrlgsrHNTVTYGRFKITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrr 140

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018536931 1092 --------NPPEAgPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14598    141 htnstidpKSPNP-PVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1250-1450 1.13e-33

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: 129.08  E-value: 1.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDTAQF-CMQYWPEK--TSGCYGPIQVEFVSA 1325
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKKkCERYWPEEgeEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1326 D-IDEDIIHRIFRicnmARPQDGYRIVQHLQYIGWPAyRDTPPSKRSLLKVVRRLEKWQEQydgREGRTVVHCLNGGGRS 1404
Cdd:cd14542     81 KrVGPDFLIRTLK----VTFQKESRTVYQFHYTAWPD-HGVPSSVDPILDLVRLVRDYQGS---EDVPICVHCSAGCGRT 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2018536931 1405 GTFCAICSVCEMIQQQNIID---VFHIVKTLRNNKSNMVETLEQYKFVY 1450
Cdd:cd14542    153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1250-1451 1.65e-33

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 128.66  E-value: 1.65e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDsHKQPAA--FVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDTA-QFCMQYWPEK--TSGCYGPIQVEFV 1323
Cdd:cd14539      1 YINASLIE-DLTPYCprFIATQAPLPGTAADFWLMVYEQQVSVIVMLvSEQENEkQKVHRYWPTErgQALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1324 SADIDEDIIHRIFRICNmaRPQDGYRIVQHLQYIGWPAYRdTPPSKRSLLKVVRRLEKWQEQYDGREGRTVVHCLNGGGR 1403
Cdd:cd14539     80 SVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2018536931 1404 SGTFC-AICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14539    157 TGAFClLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1224-1450 1.94e-33

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: 129.27  E-value: 1.94e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1224 KNRSMDVLP--LDRCLPFLISVDGESSNYINAALMDSHK-QPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DT 1299
Cdd:cd14611      2 KNRYKTILPnpHSRVCLKPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1300 AQFCMQYWPEKtSGCYGPIQVEFVSADideDIIHRIFRicNMARPQDGY-RIVQHLQYIGWPAYRdTPPSKRSLLKVVRR 1378
Cdd:cd14611     82 NEKCVLYWPEK-RGIYGKVEVLVNSVK---ECDNYTIR--NLTLKQGSQsRSVKHYWYTSWPDHK-TPDSAQPLLQLMLD 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018536931 1379 LEKWQEQYDGReGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVY 1450
Cdd:cd14611    155 VEEDRLASPGR-GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 941-1154 2.32e-33

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: 128.21  E-value: 2.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHPAehtvgnatlgraaspgmvkcvrYW 1020
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI----------------------YW 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTEV--YGDIKVTLIETE-----PLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATglLGFVRQVKFLNP 1093
Cdd:cd14550     59 PTKEKPleCETFKVTLSGEDhsclsNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQ 136

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1094 PEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVF 1154
Cdd:cd14550    137 QRDGPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1219-1455 5.96e-33

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: 129.39  E-value: 5.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1219 PRNHDKNRSMDVLPLDRC---LPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN 1295
Cdd:cd17667     25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1296 EM--DTAQFCMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICN--MARPQDG-------YRIVQHLQYIGWPAYrD 1364
Cdd:cd17667    105 NLveKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkVKKGQKGnpkgrqnERTVIQYHYTQWPDM-G 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1365 TPPSKRSLLKVVRRLEKWQEQydgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLE 1444
Cdd:cd17667    184 VPEYALPVLTFVRRSSAARTP---EMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEE 260

                          250
                   ....*....|.
gi 2018536931 1445 QYKFVYEVALE 1455
Cdd:cd17667    261 QYIFIHDALLE 271
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1250-1455 7.14e-33

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: 127.09  E-value: 7.14e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DTAQF-CMQYWPEkTSGCYGPIQVEFVSADI 1327
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLvEVGRVkCSKYWPD-DSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1328 DEDIIHRIFricnmARPQDGYRI---VQHLQYIGWPAYrDTPPSKRSLLKVVRRLeKWQEQYDGreGRTVVHCLNGGGRS 1404
Cdd:cd14632     80 LAEYSVRTF-----ALERRGYSArheVKQFHFTSWPEH-GVPYHATGLLAFIRRV-KASTPPDA--GPVVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1405 GTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1218-1455 7.54e-33

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: 129.44  E-value: 7.54e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1218 LPRNHDKNRSMDVLPLDRCLPFLISVDG-ESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNE 1296
Cdd:cd14625     44 LEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1297 MDTAQF--CMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSLLK 1374
Cdd:cd14625    124 LEEKSRikCDQYWPSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEK--REVRQFQFTAWPDH-GVPEYPTPFLA 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1375 VVRRLEKWQEQydgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVAL 1454
Cdd:cd14625    201 FLRRVKTCNPP---DAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277


                   .
gi 2018536931 1455 E 1455
Cdd:cd14625    278 E 278
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1223-1450 1.11e-32

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: 127.12  E-value: 1.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1223 DKNRSMDVLPLDRCLpflISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDTAQ 1301
Cdd:cd14545      2 NRYRDRDPYDHDRSR---VKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKlMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1302 F-CMQYWPEKTSGCY----GPIQVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYR--DTPPSKRSLLK 1374
Cdd:cd14545     79 IkCAQYWPQGEGNAMifedTGLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDFGvpESPAAFLNFLQ 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018536931 1375 VVRRLEKWQEQYdgreGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNI--IDVFHIVKTLRNNKSNMVETLEQYKFVY 1450
Cdd:cd14545    157 KVRESGSLSSDV----GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1244-1455 1.27e-32

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: 126.67  E-value: 1.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1244 DGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDTAQF-CMQYWPEKTSgCYGPIQVE 1321
Cdd:cd14631      9 DDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPDDTE-VYGDFKVT 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1322 FVSADIDEDIIHRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLEKWQEQydgREGRTVVHCLNGG 1401
Cdd:cd14631     88 CVEMEPLAEYVVRTFTL--ERRGYNEIREVKQFHFTGWPDH-GVPYHATGLLSFIRRVKLSNPP---SAGPIVVHCSAGA 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2018536931 1402 GRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14631    162 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 941-1161 1.91e-32

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: 125.90  E-value: 1.91e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLvevgrhpaehtvGNATLgraaspgmvkCVRYW 1020
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM------------DAAQL----------CMQYW 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTE-VYGDIKVTLIETEPLAEYVIRTFTV-----QKKGYheiRELRLFHFTSWPDH-GVPCYATGLLGFVRQV-KFLN 1092
Cdd:cd14634     59 PEKTScCYGPIQVEFVSADIDEDIISRIFRIcnmarPQDGY---RIVQHLQYIGWPAYrDTPPSKRSILKVVRRLeKWQE 135

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1093 PPEA--GPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14634    136 QYDGreGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1221-1455 2.65e-32

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: 127.47  E-value: 2.65e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1221 NHDKNRSMDVLPLDRCLPFLISVDGES-SNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMD 1298
Cdd:cd14633     40 NRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVE 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1299 TAQF-CMQYWPEKTSgCYGPIQVEFVSADIDEDIIHRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVVR 1377
Cdd:cd14633    120 VGRVkCCKYWPDDTE-IYKDIKVTLIETELLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVR 195

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018536931 1378 RLekwQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14633    196 QV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1213-1455 2.71e-31

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: 124.75  E-value: 2.71e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1213 CSIGLLPRNHDKNRSMDVLPLDRCLpflISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVV 1292
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSR---IKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1293 MLNE-MDTAQF-CMQYWPEKTSGCY----GPIQVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAY--RD 1364
Cdd:cd14608     94 MLNRvMEKGSLkCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQET--REILHFHYTTWPDFgvPE 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1365 TPPSKRSLLKVVRRLEKWQEQYdgreGRTVVHCLNGGGRSGTFCaICSVCEMIQQQ----NIIDVFHIVKTLRNNKSNMV 1440
Cdd:cd14608    172 SPASFLNFLFKVRESGSLSPEH----GPVVVHCSAGIGRSGTFC-LADTCLLLMDKrkdpSSVDIKKVLLEMRKFRMGLI 246

                          250
                   ....*....|....*
gi 2018536931 1441 ETLEQYKFVYEVALE 1455
Cdd:cd14608    247 QTADQLRFSYLAVIE 261
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 941-1161 6.41e-31

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: 121.29  E-value: 6.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLvevgrhpaehtvgNATLGraaspgmvkCVRYW 1020
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV-------------DLAQG---------CPQYW 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTEV-YGDIKVTLIETEPLAEYVIRTF-----TVQKKGYHEIRElrlFHFTSWPDH-GVPCYATGLLGFVRQV-KFLN 1092
Cdd:cd14636     59 PEEGMLrYGPIQVECMSCSMDCDVISRIFricnlTRPQEGYLMVQQ---FQYLGWASHrEVPGSKRSFLKLILQVeKWQE 135

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1093 PPEAGP--IVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14636    136 ECDEGEgrTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1205-1450 6.67e-31

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: 124.27  E-value: 6.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1205 TPRVRPEDcsIGLLPRNHDKNRSMDVLPLDRC-LPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLV 1283
Cdd:cd14604     43 TEKIYPTA--TGEKEENVKKNRYKDILPFDHSrVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMI 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1284 FDYNCSSVVMLN---EMDTAQfCMQYWPEKTSG--CYGPIQVEFVSADIDEDIIHRIFricnMARPQDGYRIVQHLQYIG 1358
Cdd:cd14604    121 WEYNVAIIVMACrefEMGRKK-CERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTL----LLEFQNETRRLYQFHYVN 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1359 WPAYrDTPPSKRSLLKVVRRLEKWQEQYDgreGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHIVKTLRNN 1435
Cdd:cd14604    196 WPDH-DVPSSFDSILDMISLMRKYQEHED---VPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQ 271

                          250
                   ....*....|....*
gi 2018536931 1436 KSNMVETLEQYKFVY 1450
Cdd:cd14604    272 RHSAVQTKEQYELVH 286
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1250-1454 8.94e-31

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: 120.87  E-value: 8.94e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DTAQFCMQYWPEKTS--GCYGpIQVEFVSAD 1326
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGqNMAEDEFVYWPNKDEpiNCET-FKVTLIAEE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1327 I-----DEDIIHRIFRICNMarpQDGYRI-VQHLQYIGWPAyRDTPPSKR-SLLKVVRrlekwqEQYDGREGRTVVHCLN 1399
Cdd:cd17669     80 HkclsnEEKLIIQDFILEAT---QDDYVLeVRHFQCPKWPN-PDSPISKTfELISIIK------EEAANRDGPMIVHDEH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2018536931 1400 GGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVAL 1454
Cdd:cd17669    150 GGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1224-1455 1.35e-30

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: 121.49  E-value: 1.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1224 KNRSMDVLPLDRC---LPFLISvdGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EM 1297
Cdd:cd14602      1 KNRYKDILPYDHSrveLSLITS--DEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACmefEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1298 DTAQfCMQYWPEKTSGC--YGPIQVEFVSADIDEDIIHRIFRicnmARPQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKV 1375
Cdd:cd14602     79 GKKK-CERYWAEPGEMQleFGPFSVTCEAEKRKSDYIIRTLK----VKFNSETRTIYQFHYKNWPDH-DVPSSIDPILEL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1376 VRRLEKWQEQydgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHI---VKTLRNNKSNMVETLEQYKFVYEV 1452
Cdd:cd14602    153 IWDVRCYQED---DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVfslIQEMRTQRPSLVQTKEQYELVYNA 229


                   ...
gi 2018536931 1453 ALE 1455
Cdd:cd14602    230 VIE 232
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1218-1458 3.23e-30

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: 121.76  E-value: 3.23e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1218 LPRNHDKNRSMDVLPLDRCLPFLISVDG-ESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNE 1296
Cdd:cd14624     44 LEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1297 MDTAQF--CMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSLLK 1374
Cdd:cd14624    124 LEERSRvkCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEK--REVRQFQFTAWPDH-GVPEHPTPFLA 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1375 VVRRLEKWQEQydgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVAL 1454
Cdd:cd14624    201 FLRRVKTCNPP---DAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277


                   ....
gi 2018536931 1455 EYLS 1458
Cdd:cd14624    278 EAVT 281
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1250-1451 3.52e-30

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: 119.16  E-value: 3.52e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDTAQfCMQYWP--EKTSGCYGPIQVEFVS 1324
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTrceEGNRNK-CAQYWPsmEEGSRAFGDVVVKINE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1325 ADIDEDIIHRIFRICNmARPQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLEKWQEQYdgrEGRTVVHCLNGGGRS 1404
Cdd:cd14557     80 EKICPDYIIRKLNINN-KKEKGSGREVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFNNFF---SGPIVVHCSAGVGRT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2018536931 1405 GTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14557    155 GTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1221-1457 3.86e-30

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: 119.93  E-value: 3.86e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1221 NHDKNRSMDVLPLDRCLPFLisvdGESSNYINAAL--MDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEM 1297
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMtQEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1298 DTAQF-CMQYWPE---KTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQdgYRIVQHLQYIGWPAYrDTPPSKRSLL 1373
Cdd:cd14597     79 EGGKIkCQRYWPEilgKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTRE--VRHITHLNFTAWPDH-DTPSQPEQLL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1374 KVVRRLekwqeQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVA 1453
Cdd:cd14597    156 TFISYM-----RHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                   ....
gi 2018536931 1454 LEYL 1457
Cdd:cd14597    231 LYVL 234
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1250-1457 7.52e-30

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: 118.71  E-value: 7.52e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAalmdSHKQPAA------FVVTQHPLPNTVADFWRLVFDYNCSSVVML--NEMDTAQFCMQYWPEKTSGC----YGP 1317
Cdd:cd14540      1 YINA----SHITATVggkqrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVtaEEEGGREKCFRYWPTLGGEHdaltFGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1318 IQVEFVSADIDEDIIHRIFRICNMarPQDGYRIVQHLQYIGWPAYrDTPPSKRSLL------KVVRRLEKWQEQYDGREG 1391
Cdd:cd14540     77 YKVSTKFSVSSGCYTTTGLRVKHT--LSGQSRTVWHLQYTDWPDH-GCPEDVSGFLdfleeiNSVRRHTNQDVAGHNRNP 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931 1392 RTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYL 1457
Cdd:cd14540    154 PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1221-1457 1.13e-29

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: 119.10  E-value: 1.13e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1221 NHDKNRSMDVLPLDRCLPFLISVDGE--SSNYINA------ALMDSHKQPA-AFVVTQHPLPNTVADFWRLVFDYNCSSV 1291
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvpGSDYINAnyirneNEGPTTDENAkTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1292 VMLNEM--DTAQFCMQYWP-EKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDGyRIVQHLQYIGWPAYrdTPPS 1368
Cdd:cd14544     81 VMTTKEveRGKNKCVRYWPdEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPI-REIWHYQYLSWPDH--GVPS 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1369 KRSllKVVRRLEKWQEQYDGR--EGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHIVKTLRNNKSNMVETL 1443
Cdd:cd14544    158 DPG--GVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTE 235

                          250
                   ....*....|....
gi 2018536931 1444 EQYKFVYEVALEYL 1457
Cdd:cd14544    236 AQYKFIYVAVAQYI 249
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1250-1457 2.24e-29

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: 116.77  E-value: 2.24e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAA--LMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN-EMDTAQF-CMQYWPEKTSGcygPIQVEFVSA 1325
Cdd:cd14596      1 YINASyiTMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKVkCHRYWPETLQE---PMELENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1326 DIDEDIIHRIF--RICNMARPQDG-YRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLEKWQeqydgREGRTVVHCLNGGG 1402
Cdd:cd14596     78 RLENYQALQYFiiRIIKLVEKETGeNRLIKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVH-----NTGPIVVHCSAGIG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2018536931 1403 RSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYL 1457
Cdd:cd14596    152 RAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1221-1459 3.67e-29

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: 117.81  E-value: 3.67e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1221 NHDKNRSMDVLPLDRCLPFLISVD--GESSNYINAALM--------DSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSS 1290
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHDGDpnEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1291 VVMLN-EMDTAQF-CMQYWPEKTS-GCYGPIQVEFVSADIDEDIIHRIFRICNMARpQDGYRIVQHLQYIGWPAYrDTPP 1367
Cdd:cd14605     82 IVMTTkEVERGKSkCVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKLSKVGQ-GNTERTVWQYHFRTWPDH-GVPS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1368 SKRSLLKVVRRLEKWQEQYDGrEGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHIVKTLRNNKSNMVETLE 1444
Cdd:cd14605    160 DPGGVLDFLEEVHHKQESIMD-AGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEA 238

                          250
                   ....*....|....*
gi 2018536931 1445 QYKFVYEVALEYLSS 1459
Cdd:cd14605    239 QYRFIYMAVQHYIET 253
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1219-1458 6.62e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 118.95  E-value: 6.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1219 PRNHDKNRSMDVLPLDRCLPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN--- 1295
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1296 EMDTAQFCMQYW--PEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNmaRPQDGYRIVQHLQYIGWPAYrDTPPSKRSLL 1373
Cdd:PHA02747   129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1374 KVVRRLEKWQEQY-------DGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQY 1446
Cdd:PHA02747   206 KFIKIIDINRKKSgklfnpkDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                          250
                   ....*....|....*
gi 2018536931 1447 KFV---YEVALEYLS 1458
Cdd:PHA02747   286 LFIqpgYEVLHYFLS 300
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1216-1459 8.45e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 117.29  E-value: 8.45e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1216 GLLPRNHDKNRSMDVLPLDRCLPFLISVDGE-------SSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNC 1288
Cdd:cd14606     13 GQRPENKSKNRYKNILPFDHSRVILQGRDSNipgsdyiNANYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENS 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1289 SSVVMLN-EMDTAQF-CMQYWPE-KTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARpQDGYRIVQHLQYIGWPAYrDT 1365
Cdd:cd14606     93 RVIVMTTrEVEKGRNkCVPYWPEvGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDN-GELIREIWHYQYLSWPDH-GV 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1366 PPSKRSLLKVVRRLEKWQEQYDgREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHIVKTLRNNKSNMVET 1442
Cdd:cd14606    171 PSEPGGVLSFLDQINQRQESLP-HAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQT 249

                          250
                   ....*....|....*..
gi 2018536931 1443 LEQYKFVYEVALEYLSS 1459
Cdd:cd14606    250 EAQYKFIYVAIAQFIET 266
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 941-1161 9.24e-29

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: 115.39  E-value: 9.24e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEvgrhpaehtvgnatlGRAASPgmvkCVRYW 1020
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQ---------------SNSAWP----CLQYW 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREL--RLFHFTSW-PDHGVPCYATGLLGFVRQV-KFLNPPE 1095
Cdd:cd14637     62 PEPgLQQYGPMEVEFVSGSADEDIVTRLFRVQNITRLQEGHLmvRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESG 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931 1096 AGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14637    142 EGRTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1248-1451 1.18e-28

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: 115.39  E-value: 1.18e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1248 SNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDTAQF-CMQYWPE--KTSGCYGPIQVEFV 1323
Cdd:cd14616     25 SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQcFEKGRIrCHQYWPEdnKPVTVFGDIVITKL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1324 SADIDEDIIHRIFRIcnmARPQDgYRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLekwQEQYDGREGRTVVHCLNGGGR 1403
Cdd:cd14616    105 MEDVQIDWTIRDLKI---ERHGD-YMMVRQCNFTSWPEH-GVPESSAPLIHFVKLV---RASRAHDNTPMIVHCSAGVGR 176

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2018536931 1404 SGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14616    177 TGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1250-1454 1.37e-28

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: 114.73  E-value: 1.37e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMD----SHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLnemdTAQF------CMQYWPE--KTSGcYGP 1317
Cdd:cd14541      2 YINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVML----TTLVergrvkCHQYWPDlgETMQ-FGN 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1318 IQVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLEKWQEqydGREGRTVVHC 1397
Cdd:cd14541     77 LQITCVSEEVTPSFAFREFILTNTNTGEE--RHITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRV---GMVEPTVVHC 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2018536931 1398 LNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVAL 1454
Cdd:cd14541    151 SAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1250-1451 2.78e-28

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 113.92  E-value: 2.78e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DTAQFCMQYWPEKTSGCYGPIQVEFVSADI 1327
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1328 DEDIIHRIFRICNM--------ARPQDgyRIVQHLQYIGWPAYrDTPPSKRSLLKVVRrleKWQEQYDGREGRTVVHCLN 1399
Cdd:cd17668     81 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYTLPVLTFVR---KASYAKRHAVGPVVVHCSA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2018536931 1400 GGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd17668    155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 941-1160 5.78e-28

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 112.78  E-value: 5.78e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNlvevGRHPAEHtvgnatlgraaspgmvKCVrYW 1020
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPD----GQNMAED----------------EFV-YW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTE--VYGDIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATglLGFVRQVKFLNP 1093
Cdd:cd17669     60 PNKDEpiNCETFKVTLIAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAA 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018536931 1094 PEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAIL 1160
Cdd:cd17669    138 NRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1250-1451 5.81e-28

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: 112.94  E-value: 5.81e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALM--DSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQF---CMQYWP--EKTSGCYGPIQVEF 1322
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStakCADYFPaeENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1323 VSADIDEDIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLekwqEQYDGREGRTVVHCLNGGG 1402
Cdd:cd17658     81 KKLKHSQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDH-GVPKDTRSVRELLKRL----YGIPPSAGPIVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1403 RSGTFCAICSVCEMIQQQNI--IDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd17658    156 RTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1218-1454 8.10e-28

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: 114.56  E-value: 8.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1218 LPRNHDKNRSMDVLPLDRCLPFLisvdGESSNYINAALMDShKQPAA-----FVVTQHPLPNTVADFWRLVFDYNCSSVV 1292
Cdd:cd14600     37 LPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNM-EIPSAnivnkYIATQGPLPHTCAQFWQVVWEQKLSLIV 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1293 MLNEMDTA--QFCMQYWPEKTSGC-YGPIQVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSK 1369
Cdd:cd14600    112 MLTTLTERgrTKCHQYWPDPPDVMeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEE--RTVTHLQYVAWPDH-GVPDDS 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1370 RSLLKVVRRLEKWQEQYDgregRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFV 1449
Cdd:cd14600    189 SDFLEFVNYVRSKRVENE----PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFV 264


                   ....*
gi 2018536931 1450 YEVAL 1454
Cdd:cd14600    265 CEAIL 269
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1250-1454 8.97e-28

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: 112.46  E-value: 8.97e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDTAQFCMQYWP--EKTSGCYGpIQVEFVSAD 1326
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQGLAEDEFVYWPsrEESMNCEA-FTVTLISKD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1327 I------DEDIIHRIFricnMARPQDGYRI-VQHLQYIGWPAYRDTPPSKRSLLKVVRrlekwqEQYDGREGRTVVHCLN 1399
Cdd:cd17670     80 RlclsneEQIIIHDFI----LEATQDDYVLeVRHFQCPKWPNPDAPISSTFELINVIK------EEALTRDGPTIVHDEF 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2018536931 1400 GGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVAL 1454
Cdd:cd17670    150 GAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 941-1161 9.52e-28

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: 112.09  E-value: 9.52e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLvevgrHPAEhtvgnatlgraaspgmvKCVRYW 1020
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-----DPAQ-----------------LCPQYW 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDD-TEVYGDIKVTLIETEPLAEYVIRTFTV-----QKKGYHEIRElrlFHFTSWPDH-GVPCYATGLLGFVRQV-KFLN 1092
Cdd:cd14635     59 PENgVHRHGPIQVEFVSADLEEDIISRIFRIynaarPQDGYRMVQQ---FQFLGWPMYrDTPVSKRSFLKLIRQVdKWQE 135

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1093 PPEAGP--IVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILE 1161
Cdd:cd14635    136 EYNGGEgrTVVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 941-1160 9.39e-27

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: 109.38  E-value: 9.39e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  941 YINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNlvevgrhpaehtvgNATLGRAASPgmvkcvrYW 1020
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--------------NQGLAEDEFV-------YW 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1021 PDDTEVYG--DIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATglLGFVRQVKFLNP 1093
Cdd:cd17670     60 PSREESMNceAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEAL 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018536931 1094 PEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAIL 1160
Cdd:cd17670    138 TRDGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1350-1455 1.46e-26

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: 105.13  E-value: 1.46e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1350 IVQHLQYIGWPAyRDTPPSKRSLLKVVRRLEKWQEQYDGReGRTVVHCLNGGGRSGTFCAICSVCEMI-QQQNIIDVFHI 1428
Cdd:smart00012    1 TVKHYHYTGWPD-HGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 2018536931  1429 VKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:smart00012   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1350-1455 1.46e-26

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 105.13  E-value: 1.46e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  1350 IVQHLQYIGWPAyRDTPPSKRSLLKVVRRLEKWQEQYDGReGRTVVHCLNGGGRSGTFCAICSVCEMI-QQQNIIDVFHI 1428
Cdd:smart00404    1 TVKHYHYTGWPD-HGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 2018536931  1429 VKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:smart00404   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1219-1450 1.12e-25

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: 107.74  E-value: 1.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1219 PRNHDKNRSMDVLPLDRCLpflISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLN--- 1295
Cdd:cd14607     22 PENRNRNRYRDVSPYDHSR---VKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNriv 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1296 EMDTAQfCMQYWP----EKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRS 1371
Cdd:cd14607     99 EKDSVK-CAQYWPtdeeEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGET--RTISHFHYTTWPDF-GVPESPAS 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1372 LLKVVRRLEKwQEQYDGREGRTVVHCLNGGGRSGTFCAI--CSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFV 1449
Cdd:cd14607    175 FLNFLFKVRE-SGSLSPEHGPAVVHCSAGIGRSGTFSLVdtCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFS 253


                   .
gi 2018536931 1450 Y 1450
Cdd:cd14607    254 Y 254
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1247-1455 6.12e-25

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 104.26  E-value: 6.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1247 SSNYINAALmDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLnemdTAQF------CMQYWPEKT-SGCYGPIQ 1319
Cdd:cd14601      4 NANYINMEI-PSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVML----TTQVergrvkCHQYWPEPSgSSSYGGFQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1320 VEFVSADIDEDIIHRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSLLKVVRRLekwQEQYDGREGRTVVHCLN 1399
Cdd:cd14601     79 VTCHSEEGNPAYVFREMTLTNLEKNES--RPLTQIQYIAWPDH-GVPDDSSDFLDFVCLV---RNKRAGKDEPVVVHCSA 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931 1400 GGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14601    153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1176-1456 3.68e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 101.62  E-value: 3.68e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1176 RSLYYNISRLDPQTNSSQI-KDEFQtlNIVTPRVrPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDGeSSNYINAA 1254
Cdd:PHA02742     9 NSFAKNCEQLIEESNLAEIlKEEHE--HIMQEIV-AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINAS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1255 LMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DTAQFCMQYW--PEKTSGCYGPIQVEfvSADIDED 1330
Cdd:PHA02742    85 YVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKImeDGKEACYPYWmpHERGKATHGEFKIK--TKKIKSF 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1331 IIHRIFRICNMARPQDGYRIVQHLQYIGWPaYRDTPPSKRSLLKVVRRLEKWQEQYD--------GREGRTVVHCLNGGG 1402
Cdd:PHA02742   163 RNYAVTNLCLTDTNTGASLDIKHFAYEDWP-HGGLPRDPNKFLDFVLAVREADLKADvdikgeniVKEPPILVHCSAGLD 241

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2018536931 1403 RSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEY 1456
Cdd:PHA02742   242 RAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 295
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1222-1452 3.77e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 102.03  E-value: 3.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1222 HDKNRSMDVLPLDRCLPFLISVDgESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTA- 1300
Cdd:PHA02746    73 HESLKMFDVGDSDGKKIEVTSED-NAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDd 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1301 QFCMQYW--PEKTSGCYGPIQVEFVsaDIDEDIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKVV-- 1376
Cdd:PHA02746   152 EKCFELWtkEEDSELAFGRFVAKIL--DIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDN-GIPTGMAEFLELInk 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1377 -----RRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:PHA02746   229 vneeqAELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYK 308


                   .
gi 2018536931 1452 V 1452
Cdd:PHA02746   309 A 309
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1206-1457 1.26e-20

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: 93.91  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1206 PRVRPEDC-SIGLLPRNHDKNRSMDVLPLDRCLPFLISVDGESSNYINAalmdSHKQPAA------FVVTQHPLPNTVAD 1278
Cdd:cd14599     22 PKKKADGVfTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINA----SHIKVTVggeewhYIATQGPLPHTCHD 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1279 FWRLVFDYNCSSVVMLN--EMDTAQFCMQYWP----EKTSGCYGPIQVEfVSADIDEDIIHRI-FRICNMARPQDgyRIV 1351
Cdd:cd14599     98 FWQMVWEQGVNVIAMVTaeEEGGRSKSHRYWPklgsKHSSATYGKFKVT-TKFRTDSGCYATTgLKVKHLLSGQE--RTV 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1352 QHLQYIGWPAYrDTPPSKRSLL-------KVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIID 1424
Cdd:cd14599    175 WHLQYTDWPDH-GCPEEVQGFLsyleeiqSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVE 253

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2018536931 1425 VFHIVKTLRNNKSNMVETLEQYKFVYEVALEYL 1457
Cdd:cd14599    254 VPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PHA02738 PHA02738
hypothetical protein; Provisional
 1220-1459 5.20e-17

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 83.82  E-value: 5.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1220 RNHDKNRSMDVLPLDRCLPFLiSVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVML--NEM 1297
Cdd:PHA02738    48 KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLckKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1298 DTAQFCMQYWP--EKTSGCYGPIQVEFVSAdidEDIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSLLKV 1375
Cdd:PHA02738   127 NGREKCFPYWSdvEQGSIRFGKFKITTTQV---ETHPHYVKSTLLLTDGTSATQTVTHFNFTAWPDH-DVPKNTSEFLNF 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1376 VrrLEKWQEQYDGREGR------------TVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETL 1443
Cdd:PHA02738   203 V--LEVRQCQKELAQESlqighnrlqpppIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIP 280

                          250
                   ....*....|....*.
gi 2018536931 1444 EQYKFVYEVALEYLSS 1459
Cdd:PHA02738   281 FQYFFCYRAVKRYVNL 296
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1250-1457 1.42e-16

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: 80.40  E-value: 1.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1250 YINAalmdSHKQPAA------FVVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDTAQFCMQYWP------------- 1308
Cdd:cd14598      1 YINA----SHIKVTVggkewdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaeEEGGREKSFRYWPrlgsrhntvtygr 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1309 -------EKTSGCYGPIQVefvsadidediihrifRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSLL------KV 1375
Cdd:cd14598     77 fkittrfRTDSGCYATTGL----------------KIKHLLTGQE--RTVWHLQYTDWPEH-GCPEDLKGFLsyleeiQS 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1376 VRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALE 1455
Cdd:cd14598    138 VRRHTNSTIDPKSPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217


                   ..
gi 2018536931 1456 YL 1457
Cdd:cd14598    218 FL 219
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 868-1159 3.95e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 71.92  E-value: 3.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  868 IRVADLLQHITQmkrgqgygfkeEYEAL-PEGQTASWDTAKEDENRNKNRYG--NIISYDHSRVRLLvldgdPHSDYINA 944
Cdd:PHA02740    18 INKPDLLSCIIK-----------EYRAIvPEHEDEANKACAQAENKAKDENLalHITRLLHRRIKLF-----NDEKVLDA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  945 NYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVgrhpaehtvgnatlgraaspgmvKCV-RYWPDD 1023
Cdd:PHA02740    82 RFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK-----------------------KCFnQFWSLK 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1024 ---TEVYGDIKVTLIE--TEPLAEYVIRTFTVQKKgyhEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFL------- 1091
Cdd:PHA02740   139 egcVITSDKFQIETLEiiIKPHFNLTLLSLTDKFG---QAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadlekh 215

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018536931 1092 -NPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAI 1159
Cdd:PHA02740   216 kADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
fn3 pfam00041
Fibronectin type III domain;
502-577 7.50e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 7.50e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931  502 IYIQWKPPNETNGVITLYEINYKAVGSLDPSADLSSqrgkvfkLRNETHHLFVGLYPGTTYSFTIKASTAKGFGPP 577
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 502-584 3.27e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.97  E-value: 3.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  502 IYIQWKPPNETNGVITLYEINYKAVGSlDPSADLSSQRGkvfklrNETHHLFVGLYPGTTYSFTIKASTAKGFGPPVTTR 581
Cdd:cd00063     17 VTLSWTPPEDDGGPITGYVVEYREKGS-GDWKEVEVTPG------SETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESV 89


                   ...
gi 2018536931  582 IAT 584
Cdd:cd00063     90 TVT 92
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 942-1153 8.42e-10

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 60.49  E-value: 8.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  942 INANY--IDGYHRprhYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRhpaehtvgnatlgraasPGMVKCVRy 1019
Cdd:cd14559     18 LNANRvqIGNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQR-----------------KGLPPYFR- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1020 wPDDTevYGDIKVTLIETEPLA--------EYVIRTfTVQKKGYHeireLRLFHFTSWPDHG-VPCYAT----GLLGFVR 1086
Cdd:cd14559     77 -QSGT--YGSVTVKSKKTGKDElvdglkadMYNLKI-TDGNKTIT----IPVVHVTNWPDHTaISSEGLkelaDLVNKSA 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018536931 1087 QVKFLNPPEAGPI----------VVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIfncVRELRAQR-VNLVQTEEQYV 1153
Cdd:cd14559    149 EEKRNFYKSKGSSaindknkllpVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRTSRnGKMVQKDEQLD 223
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1221-1458 1.88e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 60.75  E-value: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1221 NHDKNRSMD---VLPLDRCLPFLISVDGESsNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM 1297
Cdd:PHA02740    47 AQAENKAKDenlALHITRLLHRRIKLFNDE-KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1298 DTAQFCMQYWP--EKTSGCYGPIQVEFVSADIDEdiiHRIFRICNMARPQDGYRIVQHLQYIGWP---------AYRDTP 1366
Cdd:PHA02740   126 ADKKCFNQFWSlkEGCVITSDKFQIETLEIIIKP---HFNLTLLSLTDKFGQAQKISHFQYTAWPadgfshdpdAFIDFF 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1367 PSKRSLLKVVRRlekwqEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQY 1446
Cdd:PHA02740   203 CNIDDLCADLEK-----HKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDY 277

                          250
                   ....*....|..
gi 2018536931 1447 KFVYEVALEYLS 1458
Cdd:PHA02740   278 VFCYHLIAAYLK 289
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1032-1157 1.04e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 55.36  E-value: 1.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1032 VTLIETEPLAEYVIRTFTVQkkgYHEIRelrlfhftsWPDHGVPCYATgLLGFVRQVKFLNPpEAGPIVVHCSAGAGRTG 1111
Cdd:COG2453     30 VSLTEEEELLLGLLEEAGLE---YLHLP---------IPDFGAPDDEQ-LQEAVDFIDEALR-EGKKVLVHCRGGIGRTG 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2018536931 1112 CFIAidtMLDMAENEGVVDIFNCVRELRAQRvnlVQTEEQYVFVHD 1157
Cdd:COG2453     96 TVAA---AYLVLLGLSAEEALARVRAARPGA---VETPAQRAFLER 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1089-1157 4.48e-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: 52.74  E-value: 4.48e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1089 KFLNPPEagPIVVHCSAGAGRTGCFIAIDTMLDMAEnegvvDIFNCVRELRAQRVN-LVQTEEQYVFVHD 1157
Cdd:cd14494     51 QAEKPGE--PVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1064-1157 5.26e-08

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: 55.05  E-value: 5.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1064 FHFTSWPDHGVPCYATgLLGFVRQVKFLnPPEAGPIVVHCSAGAGRTGCFIA--IDTMLDMAENEgvvdifnCVRELRAQ 1141
Cdd:cd14506     79 FYNFGWKDYGVPSLTT-ILDIVKVMAFA-LQEGGKVAVHCHAGLGRTGVLIAcyLVYALRMSADQ-------AIRLVRSK 149

                           90
                   ....*....|....*.
gi 2018536931 1142 RVNLVQTEEQYVFVHD 1157
Cdd:cd14506    150 RPNSIQTRGQVLCVRE 165
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 390-480 7.60e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 51.34  E-value: 7.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  390 PQNVEIVDIRARQLTLQWEPFGYAVTRCHSYnlTVQYQYVFNQQQYEAEEVIQTSSHYTLRGLRPFMTIRLRLLLSNPEG 469
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGY--VVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 2018536931  470 RME-SEELVVQT 480
Cdd:cd00063     82 ESPpSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 502-575 6.76e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.38  E-value: 6.76e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018536931   502 IYIQWKPPNETNGviTLYEINYKAVGSldpsaDLSSQRGKVFKLRNETHHLFVGLYPGTTYSFTIKASTAKGFG 575
Cdd:smart00060   17 VTLSWEPPPDDGI--TGYIVGYRVEYR-----EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1265-1447 3.66e-06

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: 49.71  E-value: 3.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1265 FVVTQHPLPNTVADFWRLVFDYNCSSVVML---NEMDTAQFcmqywPE--KTSGCYGPIQV--EFVSADIDEDIIhrIFR 1337
Cdd:cd14559     31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLasnKDIQRKGL-----PPyfRQSGTYGSVTVksKKTGKDELVDGL--KAD 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1338 ICNMARPQDGYRI---VQHLQyiGWPAYrdTPPSKRSLLKVVRRLEK-------------WQEQYDGREGRTVVHCLNGG 1401
Cdd:cd14559    104 MYNLKITDGNKTItipVVHVT--NWPDH--TAISSEGLKELADLVNKsaeekrnfykskgSSAINDKNKLLPVIHCRAGV 179

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2018536931 1402 GRSGTFcaICSVCeMIQQQNIIDVFHIVKTLRNNKSN-MVETLEQYK 1447
Cdd:cd14559    180 GRTGQL--AAAME-LNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLD 223
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 390-470 1.55e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.53  E-value: 1.55e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931   390 PQNVEIVDIRARQLTLQWEPFGYAVTRchSYNLTVQYQYVFNQQQYEAEEVIQTSSHYTLRGLRPFMTIRLRLLLSNPEG 469
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    .
gi 2018536931   470 R 470
Cdd:smart00060   82 E 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
390-632 2.10e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 49.23  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  390 PQNVEIVDIRARQLTLQWEP-FGYAVTrchSYNLtvqYQYVFNQQQYEAEEVIQTSShYTLRGLRPFMTIRLRLLLSNPE 468
Cdd:COG3401    236 PTGLTATADTPGSVTLSWDPvTESDAT---GYRV---YRSNSGDGPFTKVATVTTTS-YTDTGLTNGTTYYYRVTAVDAA 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  469 GRM--ESEELVVQTEEDVPGA-VPLESIQGGPfeEKIYIQWKPPneTNGVITLYEInYKAVGSldpsadlSSQRGKVFKL 545
Cdd:COG3401    309 GNEsaPSNVVSVTTDLTPPAApSGLTATAVGS--SSITLSWTAS--SDADVTGYNV-YRSTSG-------GGTYTKIAET 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931  546 RNETHHLFVGLYPGTTYSFTIKASTAKGFGPPVTTRI-ATKISAPSMPEYDTDTPLNETDTTITVMLKPAQSRGAPVSVY 624
Cdd:COG3401    377 VTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVsATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAA 456


                   ....*...
gi 2018536931  625 QLVVKEER 632
Cdd:COG3401    457 VLADGGDT 464
fn3 pfam00041
Fibronectin type III domain;
294-360 2.16e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 2.16e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931  294 PPELL---AVGATYL---WIKPNAnsiiGDGPIILKEVEYRTTTGTWAETHIVDSPN---YKLWHLDPDVEYEIRV 360
Cdd:pfam00041    2 APSNLtvtDVTSTSLtvsWTPPPD----GNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV 73
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1365-1451 3.01e-05

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: 44.65  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1365 TPPSKRSLLKVVRRLEKwqeqydgREGRTVVHCLNGGGRSGTFCAicsvCEMIQQQNiIDVFHIVKTLR-NNKSNMVETL 1443
Cdd:cd14494     38 TLAMVDRFLEVLDQAEK-------PGEPVLVHCKAGVGRTGTLVA----CYLVLLGG-MSAEEAVRIVRlIRPGGIPQTI 105


                   ....*...
gi 2018536931 1444 EQYKFVYE 1451
Cdd:cd14494    106 EQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1365-1449 8.42e-05

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 44.19  E-value: 8.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1365 TPPSKRSLLKVVRRLEKWQEQYDGregrTVVHCLNGGGRSGTFCAicsvCEMIQQQNI--IDVFHIVKTLRNNKsnmVET 1442
Cdd:cd14504     61 TPPTLEQIDEFLDIVEEANAKNEA----VLVHCLAGKGRTGTMLA----CYLVKTGKIsaVDAINEIRRIRPGS---IET 129


                   ....*..
gi 2018536931 1443 LEQYKFV 1449
Cdd:cd14504    130 SEQEKFV 136
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1027-1157 9.84e-05

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: 44.56  E-value: 9.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1027 YGDIKVTLIETEPLAEYVIRTF--TVQKKGyheireLRLFHFtSWPDHGVPcyatgllGFVRQVKFLNPP-----EAGP- 1098
Cdd:cd14505     43 GVDDVVTLCTDGELEELGVPDLleQYQQAG------ITWHHL-PIPDGGVP-------SDIAQWQELLEEllsalENGKk 108

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018536931 1099 IVVHCSAGAGRTGcFIAIDTMLDMAENEGVVDIFNCVRELR--AqrvnlVQTEEQYVFVHD 1157
Cdd:cd14505    109 VLIHCKGGLGRTG-LIAACLLLELGDTLDPEQAIAAVRALRpgA-----IQTPKQENFLHQ 163
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 289-360 1.01e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 42.22  E-value: 1.01e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018536931   289 PTPIAPPELLAVGATYL---WIKPNANSiiGDGPIILKEVEYRTTTGTWAETHIVDSPN-YKLWHLDPDVEYEIRV 360
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVtlsWEPPPDDG--ITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1333-1453 5.14e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 41.88  E-value: 5.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1333 HRIFRICNMARPQDGYRIVQ---HLQYIGWPAYRDTPPSKRSLLKVVRRLEKWQEQydgrEGRTVVHCLNGGGRSGTFCA 1409
Cdd:COG2453     24 EGIDAVVSLTEEEELLLGLLeeaGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALRE----GKKVLVHCRGGIGRTGTVAA 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2018536931 1410 icsvCEMIQQQniIDVFHIVKTLRNNKSNMVETLEQYKFVYEVA 1453
Cdd:COG2453    100 ----AYLVLLG--LSAEEALARVRAARPGAVETPAQRAFLERFA 137
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1085-1155 6.45e-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: 6.45e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018536931 1085 VRQVKFLNPPEA--GPIVVHCSAGAGRTG----CFIAIDTMLDMAEnegvvdifnCVRELRAQRVNLVQTEEQYVFV 1155
Cdd:cd14504     69 DEFLDIVEEANAknEAVLVHCLAGKGRTGtmlaCYLVKTGKISAVD---------AINEIRRIRPGSIETSEQEKFV 136
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 1030-1129 2.04e-03

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 41.98  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1030 IKVTLIETEplaEYVirtftVQKKGYHEIRELRLFHFtsWPDhgvPCYATGLLGFVRqvkflNPPEAGPIVVHCSAGAGR 1109
Cdd:cd14495    138 VKVESVRTE---EEL-----VKKKGAHYVRIAATDHV--WPD---DEEIDAFVAFYR-----SLPADAWLHFHCRAGKGR 199

                           90       100
                   ....*....|....*....|
gi 2018536931 1110 TGCFIAidtMLDMAENEGVV 1129
Cdd:cd14495    200 TTTFMV---MYDMLKNPKDV 216
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1392-1451 2.12e-03

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: 40.32  E-value: 2.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018536931 1392 RTVVHCLNGGGRSGTFCAicsvCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYE 1451
Cdd:cd14505    108 KVLIHCKGGLGRTGLIAA----CLLLELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1089-1115 3.21e-03

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 40.13  E-value: 3.21e-03
                           10        20
                   ....*....|....*....|....*....
gi 2018536931 1089 KFLNPPEA--GPIVVHCSAGAGRTGCFIA 1115
Cdd:cd14499    100 KFLDICENekGAIAVHCKAGLGRTGTLIA 128
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 1353-1409 3.37e-03

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: 39.87  E-value: 3.37e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2018536931 1353 HLQYIGWPAYrdTPPSKRSLLKVVRRLEKWqeqYDGREGRT-VVHCLNGGGRSGTFCA 1409
Cdd:cd14497     62 RVLHYGFPDH--HPPPLGLLLEIVDDIDSW---LSEDPNNVaVVHCKAGKGRTGTVIC 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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