NCBI Conserved Domain Search

Conserved domains on [gi|2240672526|pdb|7MOU|A]

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Chain A, Tyrosine-protein phosphatase non-receptor type 1

Protein Classification

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

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

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List of domain hits

Name

Accession

Description

Interval

E-value

PTP_DSP_cys super family

cl28904

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...

21-289

0e+00

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

The actual alignment was detected with superfamily member cd14608:

Pssm-ID: 475123 [Multi-domain] Cd Length: 277 Bit Score: 618.19 E-value: 0e+00

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       21 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 100
Cdd:cd14608   1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      101 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 180
Cdd:cd14608  81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      181 YTTWPDFGVPESPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 260
Cdd:cd14608 161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 240

                       250       260
                ....*....|....*....|....*....
7MOU_A      261 FRMGLIQTADQLRFSYLAVIEGAKFIMGD 289
Cdd:cd14608 241 FRMGLIQTADQLRFSYLAVIEGAKFIMGD 269

Name

Accession

Description

Interval

E-value

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

21-289

0e+00

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: 618.19 E-value: 0e+00

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       21 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 100
Cdd:cd14608   1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      101 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 180
Cdd:cd14608  81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      181 YTTWPDFGVPESPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 260
Cdd:cd14608 161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 240

                       250       260
                ....*....|....*....|....*....
7MOU_A      261 FRMGLIQTADQLRFSYLAVIEGAKFIMGD 289
Cdd:cd14608 241 FRMGLIQTADQLRFSYLAVIEGAKFIMGD 269

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

8-281

1.33e-115

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 333.09 E-value: 1.33e-115

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A           8 MEKEFEQIDKSGSWaaiyqdirheasDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ---EDNDYINASLIKMEEAQR 84
Cdd:smart00194   2 LEEEFEKLDRLKPD------------DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPppgEGSDYINASYIDGPNGPK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A          85 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLE 164
Cdd:smart00194  70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGD--ITVTLKSVEKVDDYTIRTLE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A         165 LENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNEsgSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRK 244
Cdd:smart00194 148 VTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRK--SQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                          250       260       270
                   ....*....|....*....|....*....|....*..
7MOU_A         245 dpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:smart00194 226 ---EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

45-281

4.42e-111

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 320.73 E-value: 4.42e-111

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A         45 NKNRNRYRDVSPFDHSRIKL--HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKG 122
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLtgDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        123 SLKCAQYWPQKEEKEMIFEDtnLKLTLISE-DIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRF 201
Cdd:pfam00102  81 REKCAQYWPEEEGESLEYGD--FTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        202 KVNESgSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

PHA02742

protein tyrosine phosphatase; Provisional

25-286

1.68e-53

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 176.35 E-value: 1.68e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        25 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED--NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 102
Cdd:PHA02742  32 HEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDggDDFINASYVDGHNAKGRFICTQAPLEETALDFWQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       103 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEdtnlKLTLISEDIKS--YYTVRQLELENLTTQETREILHFH 180
Cdd:PHA02742 112 AIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHG----EFKIKTKKIKSfrNYAVTNLCLTDTNTGASLDIKHFA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       181 YTTWPDFGVPESPASFLNFRFKVNE---------SGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRkdpSSVDI 251
Cdd:PHA02742 188 YEDWPHGGLPRDPNKFLDFVLAVREadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNER---AIIPL 264

                        250       260       270
                 ....*....|....*....|....*....|....*
7MOU_A       252 KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFI 286
Cdd:PHA02742 265 LSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKLM 299

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

41-272

3.01e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 141.38 E-value: 3.01e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       41 KLPKNKNRNRYRDVSPFDHSRIklhQEDNDYINASLIKMEEAQRsYILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRV 118
Cdd:COG5599  38 QNINGSPLNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLasDDE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      119 MEKGSLKCAQYWPQKEEkemifedtNLKLTLISEDIKSYYTVRQLELENL------TTQETREILHFHYTTWPDFGVPES 192
Cdd:COG5599 114 ISKPKVKMPVYFRQDGE--------YGKYEVSSELTESIQLRDGIEARTYvltikgTGQKKIEIPVLHVKNWPDHGAISA 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      193 PAsFLNFRFKVNES-GSLSPEHGPVVVHCSAGIGRSGTYcLADTCLLLMDKRKDPSSVDIKKVLLEMRKFR-MGLIQTAD 270
Cdd:COG5599 186 EA-LKNLADLIDKKeKIKDPDKLLPVVHCRAGVGRTGTL-IACLALSKSINALVQITLSVEEIVIDMRTSRnGGMVQTSE 263


                ..
7MOU_A      271 QL 272
Cdd:COG5599 264 QL 265

Name

Accession

Description

Interval

E-value

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

21-289

0e+00

Pssm-ID: 350456 [Multi-domain] Cd Length: 277 Bit Score: 618.19 E-value: 0e+00

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       21 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 100
Cdd:cd14608   1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      101 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 180
Cdd:cd14608  81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      181 YTTWPDFGVPESPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 260
Cdd:cd14608 161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 240

                       250       260
                ....*....|....*....|....*....
7MOU_A      261 FRMGLIQTADQLRFSYLAVIEGAKFIMGD 289
Cdd:cd14608 241 FRMGLIQTADQLRFSYLAVIEGAKFIMGD 269

PTPc-N2

cd14607

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...

23-279

6.35e-170

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: 470.60 E-value: 6.35e-170

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       23 AIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 102
Cdd:cd14607   2 PLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      103 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYT 182
Cdd:cd14607  82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYT 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      183 TWPDFGVPESPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKrKDPSSVDIKKVLLEMRKFR 262
Cdd:cd14607 162 TWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEK-KDPDSVDIKQVLLDMRKYR 240

                       250
                ....*....|....*..
7MOU_A      263 MGLIQTADQLRFSYLAV 279
Cdd:cd14607 241 MGLIQTPDQLRFSYMAV 257

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

46-277

1.50e-168

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: 466.10 E-value: 1.50e-168

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       46 KNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK 125
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      126 CAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNE 205
Cdd:cd14545  81 CAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVRE 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7MOU_A      206 SGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRkDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYL 277
Cdd:cd14545 161 SGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKG-NPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

8-281

1.33e-115

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 333.09 E-value: 1.33e-115

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A           8 MEKEFEQIDKSGSWaaiyqdirheasDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ---EDNDYINASLIKMEEAQR 84
Cdd:smart00194   2 LEEEFEKLDRLKPD------------DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPppgEGSDYINASYIDGPNGPK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A          85 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLE 164
Cdd:smart00194  70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGD--ITVTLKSVEKVDDYTIRTLE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A         165 LENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNEsgSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRK 244
Cdd:smart00194 148 VTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRK--SQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                          250       260       270
                   ....*....|....*....|....*....|....*..
7MOU_A         245 dpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:smart00194 226 ---EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

45-281

4.42e-111

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 320.73 E-value: 4.42e-111

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A         45 NKNRNRYRDVSPFDHSRIKL--HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKG 122
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLtgDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        123 SLKCAQYWPQKEEKEMIFEDtnLKLTLISE-DIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRF 201
Cdd:pfam00102  81 REKCAQYWPEEEGESLEYGD--FTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        202 KVNESgSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

71-276

1.31e-91

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: 269.93 E-value: 1.31e-91

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLI 150
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGD--ITVTLV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNEsgSLSPEHGPVVVHCSAGIGRSGTY 230
Cdd:cd00047  79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK--EARKPNGPIVVHCSAGVGRTGTF 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
7MOU_A      231 CLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSY 276
Cdd:cd00047 157 IAIDILLERLEAEGE---VDVFEIVKALRKQRPGMVQTLEQYEFIY 199

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

25-277

5.31e-87

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: 260.76 E-value: 5.31e-87

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       25 YQDIRHE--ASDFPCrvAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCG 98
Cdd:cd14543   9 YEDIRREppAGTFLC--SLAPANQEKNRYGDVLCLDQSRVKLpkrnGDERTDYINANFMDGYKQKNAYIATQGPLPKTYS 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       99 HFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILH 178
Cdd:cd14543  87 DFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGD--LTVTNLSVENKEHYKKTTLEIHNTETDESRQVTH 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      179 FHYTTWPDFGVPESPASFLNFRFKVNESGSLS-----------PEHGPVVVHCSAGIGRSGTYCLADTCLllmDKRKDPS 247
Cdd:cd14543 165 FQFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICL---SQLEDVG 241

                       250       260       270
                ....*....|....*....|....*....|
7MOU_A      248 SVDIKKVLLEMRKFRMGLIQTADQLRFSYL 277
Cdd:cd14543 242 TLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

50-274

1.80e-74

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: 227.24 E-value: 1.80e-74

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       50 RYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK 125
Cdd:cd14548   1 RYTNILPYDHSRVKLIPineeEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      126 CAQYWPqKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENltTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNE 205
Cdd:cd14548  81 CDHYWP-FDQDPVYYGD--ITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
7MOU_A      206 sgSLSPEHGPVVVHCSAGIGRSGTYCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 274
Cdd:cd14548 156 --YIKQEKGPTIVHCSAGVGRTGTFIALDR---LLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

45-279

2.03e-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: 228.12 E-value: 2.03e-74

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       45 NKNRNRYRDVSPFDHSRIKLHQEDN-----DYINASLIKMEEAQR-------SYILTQGPLPNTCGHFWEMVWEQKSRGV 112
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRDPnvpgsDYINANYIRNENEGPttdenakTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      113 VMLNRVMEKGSLKCAQYWPQKEEKEmifEDTNLKLTLISEDIKSYYTVRQLELENL-TTQETREILHFHYTTWPDFGVPE 191
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWPDEGMQK---QYGPYRVQNVSEHDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      192 SPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQ 271
Cdd:cd14544 158 DPGGVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQ 237


                ....*...
7MOU_A      272 LRFSYLAV 279
Cdd:cd14544 238 YKFIYVAV 245

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

45-283

1.77e-72

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: 222.66 E-value: 1.77e-72

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       45 NKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVME 120
Cdd:cd14553   3 NKPKNRYANVIAYDHSRVILQPiegvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      121 KGSLKCAQYWPQK--EEKEMIFedtnlkLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLN 198
Cdd:cd14553  83 RSRVKCDQYWPTRgtETYGLIQ------VTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      199 FRFKVNESGslSPEHGPVVVHCSAGIGRSGTYCLADTCLllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLA 278
Cdd:cd14553 157 FLRRVKACN--PPDAGPIVVHCSAGVGRTGCFIVIDSML---ERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDA 231


                ....*
7MOU_A      279 VIEGA 283
Cdd:cd14553 232 LLEAV 236

PTPc-N3

cd14600

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...

40-274

1.98e-72

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: 223.96 E-value: 1.98e-72

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       40 AKLPKNKNRNRYRDVSPFDHSRIKLhQEDNDYINASLIKMEEAQRS----YILTQGPLPNTCGHFWEMVWEQKSRGVVML 115
Cdd:cd14600  35 AKLPQNMDKNRYKDVLPYDATRVVL-QGNEDYINASYVNMEIPSANivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      116 NRVMEKGSLKCAQYWPQKEEkemIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPAS 195
Cdd:cd14600 114 TTLTERGRTKCHQYWPDPPD---VMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7MOU_A      196 FLNFrfkVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDPSSVDIKKvllEMRKFRMGLIQTADQLRF 274
Cdd:cd14600 191 FLEF---VNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVR---KMRDQRAMMVQTSSQYKF 263

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

49-274

1.35e-68

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: 212.37 E-value: 1.35e-68

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       49 NRYRDVSPFDHSRIKL----HQEDnDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 124
Cdd:cd14615   1 NRYNNVLPYDISRVKLsvqsHSTD-DYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      125 KCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVN 204
Cdd:cd14615  80 KCEEYWPSKQKKDY----GDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVR 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      205 ESGSLSPEHGPVVVHCSAGIGRSGTYCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 274
Cdd:cd14615 156 EYMKQNPPNSPILVHCSAGVGRTGTFIAIDR---LIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

71-274

6.26e-68

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: 209.90 E-value: 6.26e-68

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLI 150
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETY----GNIQVTLL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENL------TTQETREILHFHYTTWPDFGVPESPASFLNFrfkVNESGSLSPEH-GPVVVHCSAG 223
Cdd:cd14549  77 STEVLATYTVRTFSLKNLklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPPGaGPIVVHCSAG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
7MOU_A      224 IGRSGTYCLADTCLLLMdkrKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 274
Cdd:cd14549 154 VGRTGTYIVIDSMLQQI---QDKGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201

PTPc-N3_4

cd14541

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

70-274

3.00e-66

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: 206.03 E-value: 3.00e-66

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       70 DYINASLIKME----EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkEEKEMIFEdtNL 145
Cdd:cd14541   1 DYINANYVNMEipgsGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPD-LGETMQFG--NL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      146 KLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKV--NESGSLSpehgPVVVHCSAG 223
Cdd:cd14541  78 QITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVrqNRVGMVE----PTVVHCSAG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
7MOU_A      224 IGRSGTYCLADTCLLLMDKRKDPSSVDIKKvllEMRKFRMGLIQTADQLRF 274
Cdd:cd14541 154 IGRTGVLITMETAMCLIEANEPVYPLDIVR---TMRDQRAMLIQTPSQYRF 201

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

71-276

3.49e-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: 205.56 E-value: 3.49e-66

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEA-QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedtNLKLTL 149
Cdd:cd18533   1 YINASYITLPGTsSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYG---DLTVEL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      150 IS--EDIKSYYTVRQLELeNLTTQETREILHFHYTTWPDFGVPESPASFLN---FRFKVNESGSLSPehgPVVVHCSAGI 224
Cdd:cd18533  78 VSeeENDDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTlikLKRELNDSASLDP---PIIVHCSAGV 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
7MOU_A      225 GRSGTYCLADTCLLLMDK----RKDPSSVD--IKKVLLEMRKFRMGLIQTADQLRFSY 276
Cdd:cd18533 154 GRTGTFIALDSLLDELKRglsdSQDLEDSEdpVYEIVNQLRKQRMSMVQTLRQYIFLY 211

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

71-281

9.12e-66

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: 204.53 E-value: 9.12e-66

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKM--EEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtNLKLT 148
Cdd:cd14538   1 YINASHIRIpvGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICGG-RLEVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      149 LISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNesgsLSPEHGPVVVHCSAGIGRSG 228
Cdd:cd14538  80 LEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR----RIHNSGPIVVHCSAGIGRTG 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
7MOU_A      229 TYCLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14538 156 VLITIDVALGLIERDLP---FDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

49-274

1.26e-65

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: 205.12 E-value: 1.26e-65

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       49 NRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 124
Cdd:cd14619   1 NRFRNVLPYDWSRVPLkpihEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      125 KCAQYWPQkEEKEMIFEdtNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVN 204
Cdd:cd14619  81 KCEHYWPL-DYTPCTYG--HLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      205 ESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRF 274
Cdd:cd14619 158 QWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEG---LLGPFSFVQKMRENRPLMVQTESQYVF 224

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

1-281

6.15e-65

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: 204.91 E-value: 6.15e-65

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        1 GHMASMEMEKEFEQIDK-SGSWAAIyqdIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINAS 75
Cdd:cd14610   2 GHMILSYMEDHLKNKNRlEKEWEAL---CAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENShshsDYINAS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       76 LIkMEEAQR--SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkeekemifEDTNL----KLTL 149
Cdd:cd14610  79 PI-MDHDPRnpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPD--------EGSNLyhiyEVNL 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      150 ISEDIKSY-YTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNEsgSLSPEHGPVVVHCSAGIGRSG 228
Cdd:cd14610 150 VSEHIWCEdFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRSG 227

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
7MOU_A      229 TYCLADTCLLLMdkRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14610 228 TYILIDMVLNKM--AKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278

PTPc-N6

cd14606

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...

43-286

7.98e-65

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: 204.34 E-value: 7.98e-65

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       43 PKNKNRNRYRDVSPFDHSRIKLHQEDN-----DYINASLIK-----MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGV 112
Cdd:cd14606  16 PENKSKNRYKNILPFDHSRVILQGRDSnipgsDYINANYVKnqllgPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      113 VMLNRVMEKGSLKCAQYWPqkeEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQET-REILHFHYTTWPDFGVPE 191
Cdd:cd14606  96 VMTTREVEKGRNKCVPYWP---EVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      192 SPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQ 271
Cdd:cd14606 173 EPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQ 252

                       250
                ....*....|....*
7MOU_A      272 LRFSYLAViegAKFI 286
Cdd:cd14606 253 YKFIYVAI---AQFI 264

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

49-274

1.13e-64

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: 202.24 E-value: 1.13e-64

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       49 NRYRDVSPFDHSRIKLHQEDND----YINASLIK---MEEaqRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 121
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDplssYINANYIRgydGEE--KAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      122 gSLKCAQYWPqkEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENLTtqETREILHFHYTTWPDFGVPESPASFLNFRF 201
Cdd:cd14547  79 -KEKCAQYWP--EEENETYGD--FEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQ 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7MOU_A      202 KVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTClllMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 274
Cdd:cd14547 152 EVEEARQTEPHRGPIVVHCSAGIGRTGCFIATSIG---CQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

44-280

2.19e-64

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: 201.98 E-value: 2.19e-64

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       44 KNKNRNRYRDVSPFDHSRIKLHQEdNDYINASLIKMEEAQRS--YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 121
Cdd:cd14597   2 ENRKKNRYKNILPYDTTRVPLGDE-GGYINASFIKMPVGDEEfvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      122 GSLKCAQYWPQKEEKEMIFEDtNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESP---ASFLN 198
Cdd:cd14597  81 GKIKCQRYWPEILGKTTMVDN-RLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPeqlLTFIS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      199 FRFKVNESgslspehGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLA 278
Cdd:cd14597 160 YMRHIHKS-------GPIITHCSAGIGRSGTLICIDVVLGLISKDLD---FDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                ..
7MOU_A      279 VI 280
Cdd:cd14597 230 IL 231

PTPc-N11

cd14605

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...

44-279

5.23e-64

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: 201.78 E-value: 5.23e-64

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       44 KNKNRNRYRDVSPFDHSRIKLHQED-----NDYINASLIKME--------EAQRSYILTQGPLPNTCGHFWEMVWEQKSR 110
Cdd:cd14605   1 ENKNKNRYKNILPFDHTRVVLHDGDpnepvSDYINANIIMPEfetkcnnsKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      111 GVVMLNRVMEKGSLKCAQYWPqkeEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQET-REILHFHYTTWPDFGV 189
Cdd:cd14605  81 VIVMTTKEVERGKSKCVKYWP---DEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      190 PESPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTA 269
Cdd:cd14605 158 PSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTE 237

                       250
                ....*....|
7MOU_A      270 DQLRFSYLAV 279
Cdd:cd14605 238 AQYRFIYMAV 247

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

43-281

3.81e-63

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: 200.26 E-value: 3.81e-63

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       43 PKNKNRNRYRDVSPFDHSRIKLH------QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLN 116
Cdd:cd17667  25 PDNKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      117 RVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTT-----------QETREILHFHYTTWP 185
Cdd:cd17667 105 NLVEKGRRKCDQYWPTENSEEY----GNIIVTLKSTKIHACYTVRRFSIRNTKVkkgqkgnpkgrQNERTVIQYHYTQWP 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      186 DFGVPESPASFLNFRFKvnESGSLSPEHGPVVVHCSAGIGRSGTYCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGL 265
Cdd:cd17667 181 DMGVPEYALPVLTFVRR--SSAARTPEMGPVLVHCSAGVGRTGTYIVIDS---MLQQIKDKSTVNVLGFLKHIRTQRNYL 255

                       250
                ....*....|....*.
7MOU_A      266 IQTADQLRFSYLAVIE 281
Cdd:cd17667 256 VQTEEQYIFIHDALLE 271

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

2-281

3.90e-63

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: 200.26 E-value: 3.90e-63

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        2 HMASMEMEKEFEQIDK-SGSWAAIyqdIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINAS- 75
Cdd:cd14609   1 HMILAYMEDHLRNRDRlAKEWQAL---CAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNpsrsDYINASp 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       76 LIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEK-EMIFEdtnlkLTLISEDI 154
Cdd:cd14609  78 IIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSlYHIYE-----VNLVSEHI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      155 KSY-YTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNEsgSLSPEHGPVVVHCSAGIGRSGTYCLA 233
Cdd:cd14609 153 WCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRTGTYILI 230

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
7MOU_A      234 DTCLLLMdkRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14609 231 DMVLNRM--AKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276

R-PTP-N-N2

cd14546

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...

71-281

6.95e-62

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: 194.59 E-value: 6.95e-62

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIkMEEAQRS--YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQK-EEKEMIFEdtnlkL 147
Cdd:cd14546   1 YINASTI-YDHDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYE-----V 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      148 TLISEDIKS-YYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESgslspEHG---PVVVHCSAG 223
Cdd:cd14546  75 HLVSEHIWCdDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKS-----YRGrscPIVVHCSDG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
7MOU_A      224 IGRSGTYCLADtcLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14546 150 AGRTGTYILID--MVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

49-277

6.77e-61

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: 192.83 E-value: 6.77e-61

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       49 NRYRDVSPFDHSRIKLHQEDN----DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 124
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDdpcsDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      125 KCAQYWPQKEEKeMIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQET-REILHFHYTTWPDFGVPESPASFLNFRFKV 203
Cdd:cd14617  81 KCDHYWPADQDS-LYYGD--LIVQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVRTV 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7MOU_A      204 NESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDkRKDpsSVDIKKVLLEMRKFRMGLIQTADQlrFSYL 277
Cdd:cd14617 158 RDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLD-SKD--SVDIYGAVHDLRLHRVHMVQTECQ--YVYL 226

PTPc-N21_14

cd14540

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

71-281

6.93e-61

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: 192.29 E-value: 6.93e-61

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEE--AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLT 148
Cdd:cd14540   1 YINASHITATVggKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      149 LISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNF-------RFKVNESGSLSPEHGPVVVHCS 221
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvRRHTNQDVAGHNRNPPTLVHCS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      222 AGIGRSGTYCLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14540 161 AGVGRTGVVILADLMLYCLDHNEE---LDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

5-283

8.26e-61

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: 194.10 E-value: 8.26e-61

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        5 SMEMEKEFEQIDKSgswaaiyQDIRHEASDfpcrvakLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKME 80
Cdd:cd14626  15 GLKFSQEYESIDPG-------QQFTWENSN-------LEVNKPKNRYANVIAYDHSRVILTSVDgvpgSDYINANYIDGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       81 EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQK--EEKEMIfedtnlKLTLISEDIKSYY 158
Cdd:cd14626  81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRgtETYGMI------QVTLLDTVELATY 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      159 TVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGslSPEHGPVVVHCSAGIGRSGTYCLADTcll 238
Cdd:cd14626 155 SVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACN--PPDAGPMVVHCSAGVGRTGCFIVIDA--- 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
7MOU_A      239 LMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGA 283
Cdd:cd14626 230 MLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

25-281

1.00e-60

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: 193.50 E-value: 1.00e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       25 YQDIRHEASDF------PCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLP 94
Cdd:cd14603   4 FSEIRACSAAFkadyvcSTVAGGRKENVKKNRYKDILPYDQTRVILsllqEEGHSDYINANFIKGVDGSRAYIATQGPLS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       95 NTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMI--FEDTNLKLTLISEDIksyyTVRQLELEnlTTQE 172
Cdd:cd14603  84 HTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTgpFTITLVKEKRLNEEV----ILRTLKVT--FQKE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      173 TREILHFHYTTWPDFGVPESPASFLNFRFKVNESGSLSPEhgPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDPSSVDIK 252
Cdd:cd14603 158 SRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPE--PLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIF 235

                       250       260
                ....*....|....*....|....*....
7MOU_A      253 KVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14603 236 DVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

5-282

1.10e-59

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: 191.46 E-value: 1.10e-59

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        5 SMEMEKEFEQIDKsgswaaiyqdirheASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKME 80
Cdd:cd14625  21 NLKLSQEYESIDP--------------GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEgimgSDYINANYIDGY 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       81 EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedtnLKLTLISEDIKSYYTV 160
Cdd:cd14625  87 RKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGM----IQVTLLDTIELATFCV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      161 RQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGslSPEHGPVVVHCSAGIGRSGTYCLADTcllLM 240
Cdd:cd14625 163 RTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCN--PPDAGPIVVHCSAGVGRTGCFIVIDA---ML 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
7MOU_A      241 DKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEG 282
Cdd:cd14625 238 ERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEA 279

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

27-279

2.38e-58

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.

Pssm-ID: 350462 [Multi-domain] Cd Length: 245 Bit Score: 187.02 E-value: 2.38e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       27 DIRHEASDfpcrvakLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 102
Cdd:cd14614   1 DIPHFAAD-------LPVNRCKNRYTNILPYDFSRVKLvsmhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      103 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKeMIFEDTNLKltLISEDIKSYYTVRQLELEnlTTQETREILHFHYT 182
Cdd:cd14614  74 MVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEP-VAYGDITVE--MLSEEEQPDWAIREFRVS--YADEVQDVMHFNYT 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      183 TWPDFGVPESPA--SFLNFRFKVNESGSLSPehGPVVVHCSAGIGRSGTYCLADTcllLMDKRKDPSSVDIKKVLLEMRK 260
Cdd:cd14614 149 AWPDHGVPTANAaeSILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEMRS 223

                       250
                ....*....|....*....
7MOU_A      261 FRMGLIQTADQLRFSYLAV 279
Cdd:cd14614 224 YRMSMVQTEEQYIFIHQCV 242

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

42-277

4.36e-57

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: 183.50 E-value: 4.36e-57

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       42 LPKNKNRNRYRDVSPFDHSRIKL-----HQEDNDYINASLIK-MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML 115
Cdd:cd14612  12 IPGHASKDRYKTILPNPQSRVCLrragsQEEEGSYINANYIRgYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      116 NRVMEKGSlKCAQYWPQKEEKEMIFEdtnlkltLISEDIKSY--YTVRQLELEnlTTQETREILHFHYTTWPDFGVPESP 193
Cdd:cd14612  92 TKLKEKKE-KCVHYWPEKEGTYGRFE-------IRVQDMKECdgYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      194 ASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADT-CLLLmdkrKDPSSVDIKKVLLEMRKFRMGLIQTADQL 272
Cdd:cd14612 162 GPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIgCQQL----KDTGKVDILGIVCQLRLDRGGMIQTSEQY 237


                ....*
7MOU_A      273 RFSYL 277
Cdd:cd14612 238 QFLHH 242

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

49-274

8.33e-57

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: 182.45 E-value: 8.33e-57

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       49 NRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 124
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQlggePHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      125 KCAQYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVN 204
Cdd:cd14618  81 LCDHYWPSESTP---VSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      205 ESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRF 274
Cdd:cd14618 158 EHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEK---VVDVFNTVYILRMHRYLMIQTLSQYIF 224

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

71-281

3.94e-56

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: 179.94 E-value: 3.94e-56

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKME--EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifEDTNLKLT 148
Cdd:cd14596   1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPM--ELENYQLR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      149 LISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGSLspehGPVVVHCSAGIGRSG 228
Cdd:cd14596  79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT----GPIVVHCSAGIGRAG 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
7MOU_A      229 TYCLADTCLLLMDKRkdpSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14596 155 VLICVDVLLSLIEKD---LSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

5-282

6.05e-56

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: 181.85 E-value: 6.05e-56

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        5 SMEMEKEFEQIDKsgswaaiyqdirheASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKME 80
Cdd:cd14624  21 NLKFSQEYESIDP--------------GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEgipgSDYINANYIDGY 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       81 EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedtnLKLTLISEDIKSYYTV 160
Cdd:cd14624  87 RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGL----IQVTLLDTVELATYCV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      161 RQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGslSPEHGPVVVHCSAGIGRSGTYCLADTcllLM 240
Cdd:cd14624 163 RTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCN--PPDAGPMVVHCSAGVGRTGCFIVIDA---ML 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
7MOU_A      241 DKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEG 282
Cdd:cd14624 238 ERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEA 279

PTPc-N4

cd14601

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...

70-281

6.80e-56

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: 179.37 E-value: 6.80e-56

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       70 DYINASLIKMEEAQRS----YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEmifEDTNL 145
Cdd:cd14601   1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS---SYGGF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      146 KLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGSLSPEhgPVVVHCSAGIG 225
Cdd:cd14601  78 QVTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDE--PVVVHCSAGIG 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
7MOU_A      226 RSGTYCLADTCLLLMDKRKDPSSVDIKKVlleMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14601 156 RTGVLITMETAMCLIECNQPVYPLDIVRT---MRDQRAMMIQTPSQYRFVCEAILK 208

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

35-279

1.00e-55

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: 181.67 E-value: 1.00e-55

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       35 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSR 110
Cdd:cd14604  47 YPTATGEKEENVKKNRYKDILPFDHSRVKLtlktSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      111 GVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVP 190
Cdd:cd14604 127 IIVMACREFEMGRKKCERYWPLYGEEPMTF--GPFRISCEAEQARTDYFIRTLLLE--FQNETRRLYQFHYVNWPDHDVP 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      191 ESPASFLNFRFKVNESGslSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTAD 270
Cdd:cd14604 203 SSFDSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKE 280


                ....*....
7MOU_A      271 QLRFSYLAV 279
Cdd:cd14604 281 QYELVHRAI 289

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

44-282

1.42e-55

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: 179.45 E-value: 1.42e-55

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       44 KNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVM 119
Cdd:cd14630   2 ENRNKNRYGNIISYDHSRVRLQLLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      120 EKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNF 199
Cdd:cd14630  82 EVGRVKCVRYWPDDTE---VYGD--IKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      200 RFKVNESGslSPEHGPVVVHCSAGIGRSGTYCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAV 279
Cdd:cd14630 157 VRQVKFLN--PPDAGPIVVHCSAGAGRTGCFIAIDI---MLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231


                ...
7MOU_A      280 IEG 282
Cdd:cd14630 232 LEA 234

PTPc-N22

cd14602

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...

48-281

1.66e-54

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: 176.57 E-value: 1.66e-54

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       48 RNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGS 123
Cdd:cd14602   1 KNRYKDILPYDHSRVELSlitsDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      124 LKCAQYWpqKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLttQETREILHFHYTTWPDFGVPESPASFLNFrfkV 203
Cdd:cd14602  81 KKCERYW--AEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILEL---I 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7MOU_A      204 NESGSLSP-EHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14602 154 WDVRCYQEdDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

40-278

1.34e-53

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: 174.25 E-value: 1.34e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       40 AKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML 115
Cdd:cd14554   1 ANLPCNKFKNRLVNILPYESTRVCLQPirgvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      116 NRVMEKGSLKCAQYWPQKEEKEMIFedtnlkltLISEDIKSY----YTVRQLELENLTTQETREILHFHYTTWPDFGVPE 191
Cdd:cd14554  81 TKLREMGREKCHQYWPAERSARYQY--------FVVDPMAEYnmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPK 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      192 SPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQ 271
Cdd:cd14554 153 SGEGFIDFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFI---TLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQ 229


                ....*..
7MOU_A      272 LRFSYLA 278
Cdd:cd14554 230 YQFCYRA 236

PHA02742

protein tyrosine phosphatase; Provisional

25-286

1.68e-53

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 176.35 E-value: 1.68e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        25 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED--NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 102
Cdd:PHA02742  32 HEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDggDDFINASYVDGHNAKGRFICTQAPLEETALDFWQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       103 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEdtnlKLTLISEDIKS--YYTVRQLELENLTTQETREILHFH 180
Cdd:PHA02742 112 AIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHG----EFKIKTKKIKSfrNYAVTNLCLTDTNTGASLDIKHFA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       181 YTTWPDFGVPESPASFLNFRFKVNE---------SGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRkdpSSVDI 251
Cdd:PHA02742 188 YEDWPHGGLPRDPNKFLDFVLAVREadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNER---AIIPL 264

                        250       260       270
                 ....*....|....*....|....*....|....*
7MOU_A       252 KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFI 286
Cdd:PHA02742 265 LSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKLM 299

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

49-274

5.54e-53

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: 172.40 E-value: 5.54e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       49 NRYRDVSPFDHSRIKLHQE----DNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 124
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADagvpGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      125 KCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENltTQETREILHFHYTTWPDFGVPESPASFLNFRFKVN 204
Cdd:cd14616  81 RCHQYWPEDNKPVTVFGD--IVITKLMEDVQIDWTIRDLKIER--HGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      205 esGSLSPEHGPVVVHCSAGIGRSGTYCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 274
Cdd:cd14616 157 --ASRAHDNTPMIVHCSAGVGRTGVFIALDH---LTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

71-276

1.70e-52

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: 170.64 E-value: 1.70e-52

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIK-MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTL 149
Cdd:cd14539   1 YINASLIEdLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGA--ITVSL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      150 ISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGSLS-PEHGPVVVHCSAGIGRSG 228
Cdd:cd14539  79 QSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQrSLQTPIVVHCSSGVGRTG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
7MOU_A      229 TYCLADTCLLLMdkRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 276
Cdd:cd14539 159 AFCLLYAAVQEI--EAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

31-282

2.35e-52

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

Pssm-ID: 350481 [Multi-domain] Cd Length: 273 Bit Score: 172.53 E-value: 2.35e-52

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       31 EASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWE 106
Cdd:cd14633  26 EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQpiegETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWH 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      107 QKSRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPD 186
Cdd:cd14633 106 ENTASIIMVTNLVEVGRVKCCKYWPDDTE---IYKD--IKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPD 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      187 FGVPESPASFLNFRFKVNESGslSPEHGPVVVHCSAGIGRSGTYCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLI 266
Cdd:cd14633 181 HGVPYHATGLLGFVRQVKSKS--PPNAGPLVVHCSAGAGRTGCFIVID---IMLDMAEREGVVDIYNCVRELRSRRVNMV 255

                       250
                ....*....|....*.
7MOU_A      267 QTADQLRFSYLAVIEG 282
Cdd:cd14633 256 QTEEQYVFIHDAILEA 271

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

51-281

6.32e-52

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: 169.74 E-value: 6.32e-52

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       51 YRDVSPFDHSRIKLHQED----NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKC 126
Cdd:cd14620   1 YPNILPYDHSRVILSQLDgipcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      127 AQYWPQkeekEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTT---QETREILHFHYTTWPDFGVPESPASFLNFRFKV 203
Cdd:cd14620  81 YQYWPD----QGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKV 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7MOU_A      204 NesgSLSPEH-GPVVVHCSAGIGRSGTYCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14620 157 K---SVNPVHaGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

8-281

4.37e-51

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: 169.91 E-value: 4.37e-51

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        8 MEKEFEQIDKSGSWAAiyqdiRHEASDFPCrvaklpkNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQ 83
Cdd:cd14628  27 MELEFKRLASSKAHTS-----RFISANLPC-------NKFKNRLVNIMPYESTRVCLQPirgvEGSDYINASFIDGYRQQ 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       84 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedtnLKLTLISEDIKSYYTVRQL 163
Cdd:cd14628  95 KAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQY----FVVDPMAEYNMPQYILREF 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      164 ELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCladTCLLLMDKR 243
Cdd:cd14628 171 KVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFI---TLSIVLERM 247

                       250       260       270
                ....*....|....*....|....*....|....*...
7MOU_A      244 KDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14628 248 RYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285

PTPc-N14

cd14599

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...

25-281

5.90e-51

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: 169.41 E-value: 5.90e-51

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       25 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL--HQEDND-YINASLIK--MEEAQRSYILTQGPLPNTCGH 99
Cdd:cd14599  18 YEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvpTKENNTgYINASHIKvtVGGEEWHYIATQGPLPHTCHD 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      100 FWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHF 179
Cdd:cd14599  98 FWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHL 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      180 HYTTWPDFGVPESPASFLNF--------RFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKdpsSVDI 251
Cdd:cd14599 178 QYTDWPDHGCPEEVQGFLSYleeiqsvrRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNE---KVEV 254

                       250       260       270
                ....*....|....*....|....*....|
7MOU_A      252 KKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14599 255 PVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284

PTPc-N22_18_12

cd14542

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...

71-276

6.48e-51

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: 166.44 E-value: 6.48e-51

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEdtNLKLTLI 150
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFG--PFKISLE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSY-YTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASFLN----FRfKVNESGSLspehgPVVVHCSAGIG 225
Cdd:cd14542  79 KEKRVGPdFLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVDPILDlvrlVR-DYQGSEDV-----PICVHCSAGCG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
7MOU_A      226 RSGTYCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 276
Cdd:cd14542 151 RTGTICAIDYVWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201

R-PTPc-A-1

cd14621

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...

37-289

7.63e-51

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: 169.05 E-value: 7.63e-51

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       37 CRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGV 112
Cdd:cd14621  44 CEAASKEENKEKNRYVNILPYDHSRVHLTPvegvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATI 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      113 VMLNRVMEKGSLKCAQYWPQkeekEMIFEDTNLKLTLISEDIKSYYTVRQLELENL----TTQETREILHFHYTTWPDFG 188
Cdd:cd14621 124 VMVTNLKERKECKCAQYWPD----QGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVgdvtNKKPQRLITQFHFTSWPDFG 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      189 VPESPASFLNFRFKVNesgSLSPEH-GPVVVHCSAGIGRSGTYCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQ 267
Cdd:cd14621 200 VPFTPIGMLKFLKKVK---NCNPQYaGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQRCQMVQ 273

                       250       260
                ....*....|....*....|..
7MOU_A      268 TADQLRFSYLAVIEgaKFIMGD 289
Cdd:cd14621 274 TDMQYVFIYQALLE--HYLYGD 293

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

2-281

7.01e-50

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: 166.45 E-value: 7.01e-50

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        2 HMASMEMEkeFEQIDKSGSWAAiyqdiRHEASDFPCrvaklpkNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLI 77
Cdd:cd14627  24 HVTGMELE--FKRLANSKAHTS-----RFISANLPC-------NKFKNRLVNIMPYETTRVCLQPirgvEGSDYINASFI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       78 KMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedtnLKLTLISEDIKSY 157
Cdd:cd14627  90 DGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQY----FVVDPMAEYNMPQ 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      158 YTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCladTCL 237
Cdd:cd14627 166 YILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFI---TLS 242

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
7MOU_A      238 LLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14627 243 IVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286

R-PTPc-Z-1

cd17668

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...

71-280

8.98e-50

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: 163.61 E-value: 8.98e-50

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLI 150
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEY----GNFLVTQK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLTT--------QETREILHFHYTTWPDFGVPESPASFLNFRFKvnESGSLSPEHGPVVVHCSA 222
Cdd:cd17668  77 SVQVLAYYTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRK--ASYAKRHAVGPVVVHCSA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
7MOU_A      223 GIGRSGTYCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 280
Cdd:cd17668 155 GVGRTGTYIVLDS---MLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

71-281

1.70e-49

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

Pssm-ID: 350403 [Multi-domain] Cd Length: 204 Bit Score: 162.78 E-value: 1.70e-49

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLI 150
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE---VYGD--IKVTLV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGslSPEHGPVVVHCSAGIGRSGTY 230
Cdd:cd14555  76 ETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASN--PPSAGPIVVHCSAGAGRTGCY 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
7MOU_A      231 CLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14555 154 IVIDI---MLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

71-271

2.74e-49

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: 162.30 E-value: 2.74e-49

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTli 150
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKIN-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLTTQET-REILHFHYTTWPDFGVPESPASFLNFRFKVNE-SGSLSpehGPVVVHCSAGIGRSG 228
Cdd:cd14557  79 EEKICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAfNNFFS---GPIVVHCSAGVGRTG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
7MOU_A      229 TYCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQ 271
Cdd:cd14557 156 TYIGIDA---MLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQ 195

PHA02746

protein tyrosine phosphatase; Provisional

12-279

6.87e-49

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 164.82 E-value: 6.87e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        12 FEQIDKSGSWAAIYQDiRHEASDFPCRVAK----LPKNKNRNRYRDVSPFDHSRIKLH---------------------Q 66
Cdd:PHA02746  15 FDKTNHAKFCEFVLLE-HAEVMDIPIRGTTnhflKKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkievtS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        67 EDND--YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVmEKGSLKCAQYWPQKEEKEMIFEDTN 144
Cdd:PHA02746  94 EDNAenYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEDSELAFGRFV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       145 LKLTLISEDikSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNE--------SGSLSPEHGPV 216
Cdd:PHA02746 173 AKILDIIEE--LSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqADNDPQTLGPI 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
7MOU_A       217 VVHCSAGIGRSGTYCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAV 279
Cdd:PHA02746 251 VVHCSAGIGRAGTFCAIDNALEQLEKEK---EVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

71-276

3.30e-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: 159.48 E-value: 3.30e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKemiFEDtnLKLTLI 150
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT---YGD--IEVELK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNF----RFKVNESGSLSPEHGPVVVHCSAGIGR 226
Cdd:cd14558  76 DTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMiksiKQKLPYKNSKHGRSVPIVVHCSDGSSR 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
7MOU_A      227 SGTYCladtCLL-LMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 276
Cdd:cd14558 156 TGIFC----ALWnLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

PTPc_plant_PTP1

cd17658

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...

71-276

4.31e-48

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: 159.17 E-value: 4.31e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQR--SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL-KCAQYWPQKEEKEMIFEDTNLKL 147
Cdd:cd17658   1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      148 TLISEDIKSyYTVRQLELENLTTQET-REILHFHYTTWPDFGVPESPASflnFRFKVNESGSLSPEHGPVVVHCSAGIGR 226
Cdd:cd17658  81 KKLKHSQHS-ITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRS---VRELLKRLYGIPPSAGPIVVHCSAGIGR 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
7MOU_A      227 SGTYCLADTCLLLMDKrKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 276
Cdd:cd17658 157 TGAYCTIHNTIRRILE-GDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

50-281

5.02e-48

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: 159.83 E-value: 5.02e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       50 RYRDVSPFDHSRI----KLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK 125
Cdd:cd14623   1 RVLQIIPYEFNRViipvKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      126 CAQYWPQkeEKEMIFEDTNLKLTliSEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNE 205
Cdd:cd14623  81 CAQYWPS--DGSVSYGDITIELK--KEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7MOU_A      206 SGSLSPEHgPVVVHCSAGIGRSGTYCLADTCLllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14623 157 QQQQSGNH-PITVHCSAGAGRTGTFCALSTVL---ERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

40-281

9.78e-48

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.

Pssm-ID: 350477 [Multi-domain] Cd Length: 291 Bit Score: 161.05 E-value: 9.78e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       40 AKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML 115
Cdd:cd14629  48 ANLPCNKFKNRLVNIMPYELTRVCLQPirgvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      116 NRVMEKGSLKCAQYWPQKEEKEMIFedtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPAS 195
Cdd:cd14629 128 TKLREMGREKCHQYWPAERSARYQY----FVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEG 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      196 FLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFS 275
Cdd:cd14629 204 FIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFI---TLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLC 280


                ....*.
7MOU_A      276 YLAVIE 281
Cdd:cd14629 281 YRAALE 286

PHA02738

hypothetical protein; Provisional

44-279

3.26e-47

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 160.48 E-value: 3.26e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        44 KNKNRNRYRDVSPFDHSRIKLHQEDN--DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 121
Cdd:PHA02738  48 KNRKLNRYLDAVCFDHSRVILPAERNrgDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEN 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       122 GSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELENlTTQETREILHFHYTTWPDFGVPESPASFLNF-- 199
Cdd:PHA02738 128 GREKCFPYWSDVEQGSIRF--GKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFvl 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       200 ------------RFKVNESGSLSPehgPVVVHCSAGIGRSGTYCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQ 267
Cdd:PHA02738 205 evrqcqkelaqeSLQIGHNRLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACA---TVSIPSIVSSIRNQRYYSLF 278

                        250
                 ....*....|..
7MOU_A       268 TADQLRFSYLAV 279
Cdd:PHA02738 279 IPFQYFFCYRAV 290

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

48-274

5.06e-47

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: 157.00 E-value: 5.06e-47

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       48 RNRYRDVSPFDHSRIKLHQEDND-----YINASLIK-MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 121
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNSNdslstYINANYIRgYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      122 GSlKCAQYWPqkeEKEMIFEDTNLKLTLISEdiKSYYTVRQLELENltTQETREILHFHYTTWPDFGVPESPASFLNFRF 201
Cdd:cd14611  82 NE-KCVLYWP---EKRGIYGKVEVLVNSVKE--CDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLML 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7MOU_A      202 KVNESGSLSPEHGPVVVHCSAGIGRSGTYcLADT--CLLLmdkrKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 274
Cdd:cd14611 154 DVEEDRLASPGRGPVVVHCSAGIGRTGCF-IATTigCQQL----KEEGVVDVLSIVCQLRVDRGGMVQTSEQYEF 223

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

48-274

1.54e-46

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.

Pssm-ID: 350461 [Multi-domain] Cd Length: 258 Bit Score: 156.95 E-value: 1.54e-46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       48 RNRYRDVSPFDHSRIKLHQEDND-----YINASLIK-MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 121
Cdd:cd14613  28 KNRYKTILPNPHSRVCLTSPDQDdplssYINANYIRgYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      122 GSlKCAQYWPqkeEKEMIFE--DTNLKLTLISEDiksyYTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASFLNF 199
Cdd:cd14613 108 NE-KCTEYWP---EEQVTYEgiEITVKQVIHADD----YRLRLITLK--SGGEERGLKHYWYTSWPDQKTPDNAPPLLQL 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7MOU_A      200 RFKVNESGSLSPE-HGPVVVHCSAGIGRSGtyCLADTCLLLMdKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 274
Cdd:cd14613 178 VQEVEEARQQAEPnCGPVIVHCSAGIGRTG--CFIATSICCK-QLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQF 250

R-PTPc-A-E-1

cd14551

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...

71-276

5.60e-46

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: 153.53 E-value: 5.60e-46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLI 150
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTY----GNLRVRVE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQL----ELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNesgSLSPEH-GPVVVHCSAGIG 225
Cdd:cd14551  77 DTVVLVDYTTRKFciqkVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVK---SANPPRaGPIVVHCSAGVG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
7MOU_A      226 RSGTYCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 276
Cdd:cd14551 154 RTGTFIVIDA---MLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

71-279

7.72e-46

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: 153.19 E-value: 7.72e-46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPqkEEKEMIFEDTNLKLTli 150
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELK-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGSLSPEHgPVVVHCSAGIGRSGTY 230
Cdd:cd14552  77 DQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH-PITVHCSAGAGRTGTF 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
7MOU_A      231 CLADTCLllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAV 279
Cdd:cd14552 156 CALSTVL---ERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

69-282

1.70e-45

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: 152.87 E-value: 1.70e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       69 NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLT 148
Cdd:cd14631  13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE---VYGD--FKVT 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      149 LISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGslSPEHGPVVVHCSAGIGRSG 228
Cdd:cd14631  88 CVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSN--PPSAGPIVVHCSAGAGRTG 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
7MOU_A      229 TYCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEG 282
Cdd:cd14631 166 CYIVID---IMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

71-282

2.85e-45

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: 152.13 E-value: 2.85e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPqkEEKEMIfedTNLKLTLI 150
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP--DDSDTY---GDIKITLL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNesGSLSPEHGPVVVHCSAGIGRSGTY 230
Cdd:cd14632  76 KTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVK--ASTPPDAGPVVVHCSAGAGRTGCY 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
7MOU_A      231 CLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEG 282
Cdd:cd14632 154 IVLD---VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202

PHA02747

protein tyrosine phosphatase; Provisional

43-274

6.32e-43

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 149.00 E-value: 6.32e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        43 PKNKNRNRYRDVSPFDHSRIKLHQ---EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVM 119
Cdd:PHA02747  49 PENQPKNRYWDIPCWDHNRVILDSgggSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       120 E-KGSLKCAQYWPQKEEKEMIFEDTNLKLTLISedIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLN 198
Cdd:PHA02747 129 GtNGEEKCYQYWCLNEDGNIDMEDFRIETLKTS--VRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIK 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       199 FRFKVN----ESGSL-SPEHG---PVVVHCSAGIGRSGTYCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTAD 270
Cdd:PHA02747 207 FIKIIDinrkKSGKLfNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRK---AICLAKTAEKIREQRHAGIMNFD 283


                 ....
7MOU_A       271 QLRF 274
Cdd:PHA02747 284 DYLF 287

PTPc-N21

cd14598

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...

71-281

3.26e-42

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: 144.73 E-value: 3.26e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKME--EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLT 148
Cdd:cd14598   1 YINASHIKVTvgGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      149 LISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNF-------RFKVNESGSLSPEHGPVVVHCS 221
Cdd:cd14598  81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIDPKSPNPPVLVHCS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      222 AGIGRSGTYCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14598 161 AGVGRTGVVILSEIMIACLEHNE---MLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

175-281

2.47e-40

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 135.95 E-value: 2.47e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A         175 EILHFHYTTWPDFGVPESPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDpsSVDIKKV 254
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAG--EVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
7MOU_A         255 LLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

175-281

2.47e-40

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: 135.95 E-value: 2.47e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A         175 EILHFHYTTWPDFGVPESPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLADTCLLLMDKRKDpsSVDIKKV 254
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAG--EVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
7MOU_A         255 LLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

41-272

3.01e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 141.38 E-value: 3.01e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       41 KLPKNKNRNRYRDVSPFDHSRIklhQEDNDYINASLIKMEEAQRsYILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRV 118
Cdd:COG5599  38 QNINGSPLNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLasDDE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      119 MEKGSLKCAQYWPQKEEkemifedtNLKLTLISEDIKSYYTVRQLELENL------TTQETREILHFHYTTWPDFGVPES 192
Cdd:COG5599 114 ISKPKVKMPVYFRQDGE--------YGKYEVSSELTESIQLRDGIEARTYvltikgTGQKKIEIPVLHVKNWPDHGAISA 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      193 PAsFLNFRFKVNES-GSLSPEHGPVVVHCSAGIGRSGTYcLADTCLLLMDKRKDPSSVDIKKVLLEMRKFR-MGLIQTAD 270
Cdd:COG5599 186 EA-LKNLADLIDKKeKIKDPDKLLPVVHCRAGVGRTGTL-IACLALSKSINALVQITLSVEEIVIDMRTSRnGGMVQTSE 263


                ..
7MOU_A      271 QL 272
Cdd:COG5599 264 QL 265

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

70-279

9.98e-39

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).

Pssm-ID: 350470 [Multi-domain] Cd Length: 205 Bit Score: 135.13 E-value: 9.98e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       70 DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkeEKEMIFEDTNLKLTl 149
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEIK- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      150 iSEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFRFKVNESGSLSPEHgPVVVHCSAGIGRSGT 229
Cdd:cd14622  78 -NDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH-PIVVHCSAGAGRTGT 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
7MOU_A      230 YCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAV 279
Cdd:cd14622 156 FIALSN---ILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

71-276

9.07e-38

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

Pssm-ID: 350404 [Multi-domain] Cd Length: 201 Bit Score: 132.53 E-value: 9.07e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRvMEKGSLKCAQYWPQKEEKEMifedTNLKLTLI 150
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWPDEGSGTY----GPIQVEFV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLT--TQETREILHFHYTTWPDFG-VPESPASFLNFRFKVN----ESGSlspehGPVVVHCSAG 223
Cdd:cd14556  76 STTIDEDVISRIFRLQNTTrpQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEkwqeQSGE-----GPIVVHCLNG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
7MOU_A      224 IGRSGTYCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 276
Cdd:cd14556 151 VGRSGVFC---AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200

R5-PTP-2

cd14550

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

71-276

2.57e-31

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: 115.50 E-value: 2.57e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGslKCAQYWPQKeEKEMIFEdtNLKLTLI 150
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTK-EKPLECE--TFKVTLS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSY-----YTVRQLELENltTQETR--EILHFHYTTWPDfgvPESPAS-FLNFRFKVNESGSLSpeHGPVVVHCSA 222
Cdd:cd14550  76 GEDHSCLsneirLIVRDFILES--TQDDYvlEVRQFQCPSWPN---PCSPIHtVFELINTVQEWAQQR--DGPIVVHDRY 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
7MOU_A      223 GIGRSGTYCLADTcllLMDKRKDPSSVDIKKV--LLEMRkfRMGLIQTADQLRFSY 276
Cdd:cd14550 149 GGVQAATFCALTT---LHQQLEHESSVDVYQVakLYHLM--RPGVFTSKEDYQFLY 199

R-PTPc-T-2

cd14634

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...

71-281

1.57e-27

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

Pssm-ID: 350482 [Multi-domain] Cd Length: 206 Bit Score: 105.87 E-value: 1.57e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRvMEKGSLkCAQYWPQKEEKEMifedTNLKLTLI 150
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL-CMQYWPEKTSCCY----GPIQVEFV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLTTQET--REILHFHYTTWPDF-GVPESPASFLNFRFKVNE-SGSLSPEHGPVVVHCSAGIGR 226
Cdd:cd14634  75 SADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKwQEQYDGREGRTVVHCLNGGGR 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
7MOU_A      227 SGTYC-LADTCLLLMDKrkdpSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14634 155 SGTFCaICSVCEMIQQQ----NIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

R-PTPc-U-2

cd14637

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...

71-281

2.02e-26

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: 103.06 E-value: 2.02e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL-KCAQYWPQKEEKEMIFEDTNLKLTL 149
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      150 ISEDIKSyytvRQLELENLTTQETREIL--HFHYTTWPDF-GVPESPASFLNFRFKVNESGSLSPEhGPVVVHCSAGIGR 226
Cdd:cd14637  81 ADEDIVT----RLFRVQNITRLQEGHLMvrHFQFLRWSAYrDTPDSKKAFLHLLASVEKWQRESGE-GRTVVHCLNGGGR 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
7MOU_A      227 SGTYCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14637 156 SGTYC---ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207

R-PTP-Z-2

cd17669

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

71-280

3.46e-24

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: 96.99 E-value: 3.46e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAqYWPQKEEKeMIFEdtNLKLTLI 150
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEP-INCE--TFKVTLI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLTTQETR-----EILHFHYTTWPDfgvPESPASflnfrfKVNESGSLSPEH-----GPVVVHC 220
Cdd:cd17669  77 AEEHKCLSNEEKLIIQDFILEATQddyvlEVRHFQCPKWPN---PDSPIS------KTFELISIIKEEaanrdGPMIVHD 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      221 SAGIGRSGTYCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 280
Cdd:cd17669 148 EHGGVTAGTFCALTT---LMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

PHA02740

protein tyrosine phosphatase; Provisional

45-287

4.89e-24

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 98.50 E-value: 4.89e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A        45 NKNRNRYRD------VSPFDHSRIKLhQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRV 118
Cdd:PHA02740  47 AQAENKAKDenlalhITRLLHRRIKL-FNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       119 MEKgslKC-AQYWPQKEEKEMIFEDTNLK-LTLIsedIKSYYTVRQLELENLTTQEtREILHFHYTTWPDFGVPESPASF 196
Cdd:PHA02740 126 ADK---KCfNQFWSLKEGCVITSDKFQIEtLEII---IKPHFNLTLLSLTDKFGQA-QKISHFQYTAWPADGFSHDPDAF 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       197 LNFRFKVNESGSLSPEH------GPVVVHCSAGIGRSGTYCLADTCLLLMDKrkdPSSVDIKKVLLEMRKFRMGLIQTAD 270
Cdd:PHA02740 199 IDFFCNIDDLCADLEKHkadgkiAPIIIDCIDGISSSAVFCVFDICATEFDK---TGMLSIANALKKVRQKKYGCMNCLD 275

                        250
                 ....*....|....*....
7MOU_A       271 QLRFSY--LAVIEGAKFIM 287
Cdd:PHA02740 276 DYVFCYhlIAAYLKEKFDI 294

R-PTPc-M-2

cd14635

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...

71-281

1.23e-22

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

Pssm-ID: 350483 [Multi-domain] Cd Length: 206 Bit Score: 92.83 E-value: 1.23e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVmEKGSLkCAQYWPQKEekemIFEDTNLKLTLI 150
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQL-CPQYWPENG----VHRHGPIQVEFV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      151 SEDIKSYYTVRQLELENLTTQET--REILHFHYTTWPDF-GVPESPASFLNFRFKVNE-SGSLSPEHGPVVVHCSAGIGR 226
Cdd:cd14635  75 SADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKwQEEYNGGEGRTVVHCLNGGGR 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
7MOU_A      227 SGTYC-LADTCLLLMDKRkdpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14635 155 SGTFCaISIVCEMLRHQR----AVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206

R-PTPc-K-2

cd14636

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...

71-281

1.67e-22

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: 92.40 E-value: 1.67e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRV-MEKGslkCAQYWPqkEEKEMIFEDTNLKLTL 149
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWP--EEGMLRYGPIQVECMS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      150 ISEDIKsyYTVRQLELENLTTQETREIL--HFHYTTWPDF-GVPESPASFLNFRFKVNESGSLSPE-HGPVVVHCSAGIG 225
Cdd:cd14636  76 CSMDCD--VISRIFRICNLTRPQEGYLMvqQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgEGRTIIHCLNGGG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
7MOU_A      226 RSGTYClADTCLLLMDKRKDpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 281
Cdd:cd14636 154 RSGMFC-AISIVCEMIKRQN--VVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

71-280

1.01e-21

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: 90.51 E-value: 1.01e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       71 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRVMEKGSLkcaQYWPQKEEKemiFEDTNLKLT 148
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQGLAEDEF---VYWPSREES---MNCEAFTVT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      149 LISEDIKSYYTVRQLELENLTTQETR-----EILHFHYTTWPDfgvPESPASFLNFRFKVNESGSLSPEhGPVVVHCSAG 223
Cdd:cd17670  75 LISKDRLCLSNEEQIIIHDFILEATQddyvlEVRHFQCPKWPN---PDAPISSTFELINVIKEEALTRD-GPTIVHDEFG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
7MOU_A      224 IGRSGTYCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 280
Cdd:cd17670 151 AVSAGTLCALTT---LSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

149-274

2.72e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 57.29 E-value: 2.72e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      149 LISEDIKSYYTVRQLELENLTTQETREILHFHYTtWPDFGVPEsPASFLNFRFKVNEsgsLSPEHGPVVVHCSAGIGRSG 228
Cdd:COG2453  21 LKREGIDAVVSLTEEEELLLGLLEEAGLEYLHLP-IPDFGAPD-DEQLQEAVDFIDE---ALREGKKVLVHCRGGIGRTG 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
7MOU_A      229 TycLAdTCLLLMDKrkdpssVDIKKVLLEMRKFRMGLIQTADQLRF 274
Cdd:COG2453  96 T--VA-AAYLVLLG------LSAEEALARVRAARPGAVETPAQRAF 132

PTP_YopH-like

cd14559

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...

49-272

8.73e-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: 57.79 E-value: 8.73e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A       49 NRYRDVSpfdhSRIKLhqEDNDYINASLIKMEEaQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRVMEKGSLKc 126
Cdd:cd14559   1 NRFTNIQ----TRVST--PVGKNLNANRVQIGN-KNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLasNKDIQRKGLP- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      127 aQYWPQKEEKEmifedtnlKLTLISEDIKSYYTVRQLELE--NLTT---QETREILHFHYTTWPDFG------------- 188
Cdd:cd14559  73 -PYFRQSGTYG--------SVTVKSKKTGKDELVDGLKADmyNLKItdgNKTITIPVVHVTNWPDHTaisseglkeladl 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      189 VPESPASFLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYcLADTCLLlmdkrKDPSSVDIKKVLLEMRKFRMG-LIQ 267
Cdd:cd14559 144 VNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQL-AAAMELN-----KSPNNLSVEDIVSDMRTSRNGkMVQ 217


                ....*
7MOU_A      268 TADQL 272
Cdd:cd14559 218 KDEQL 222

CDKN3-like

cd14505

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...

147-274

8.32e-09

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: 53.81 E-value: 8.32e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      147 LTLISEDIKSYYTVRQLelenLTTQETREILHFHYTTwPDFGVPESPASFLnfrfKVNESgsLSPEHGP---VVVHCSAG 223
Cdd:cd14505  48 VTLCTDGELEELGVPDL----LEQYQQAGITWHHLPI-PDGGVPSDIAQWQ----ELLEE--LLSALENgkkVLIHCKGG 116

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
7MOU_A      224 IGRSGTYCladTCLLLMDKRKDPSSVDIKKVllemRKFRMGLIQTADQLRF 274
Cdd:cd14505 117 LGRTGLIA---ACLLLELGDTLDPEQAIAAV----RALRPGAIQTPKQENF 160

DUSP23

cd14504

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...

185-274

1.03e-08

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: 53.05 E-value: 1.03e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      185 PDFGVP--ESPASFLNFRFKVNESGslspehGPVVVHCSAGIGRSGTYcLAdtCLLLMdKRKDPSSVDIKKVllemRKFR 262
Cdd:cd14504  58 EDYTPPtlEQIDEFLDIVEEANAKN------EAVLVHCLAGKGRTGTM-LA--CYLVK-TGKISAVDAINEI----RRIR 123

                        90
                ....*....|..
7MOU_A      263 MGLIQTADQLRF 274
Cdd:cd14504 124 PGSIETSEQEKF 135

PTP_DSP_cys

cd14494

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...

209-274

4.52e-06

Pssm-ID: 350344 [Multi-domain] Cd Length: 113 Bit Score: 44.65 E-value: 4.52e-06

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
7MOU_A      209 LSPEHgPVVVHCSAGIGRSGTYCladTCLLLMDKRKDPssvdiKKVLLEMRKFR-MGLIQTADQLRF 274
Cdd:cd14494  53 EKPGE-PVLVHCKAGVGRTGTLV---ACYLVLLGGMSA-----EEAVRIVRLIRpGGIPQTIEQLDF 110

DUSP14

cd14572

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...

178-233

1.72e-05

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), 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. DUSP14 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. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses.

Pssm-ID: 350420 [Multi-domain] Cd Length: 150 Bit Score: 44.09 E-value: 1.72e-05

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
7MOU_A      178 HFHYTTWPDFGVPESPASfLNFRFKVNESGSLSPEHGPVVVHCSAGIGRSGTYCLA 233
Cdd:cd14572  51 QFEYVKVPLADMPHAPIS-LYFDSVADKIHSVGRKHGATLVHCAAGVSRSATLCIA 105

PTP_PTPDC1

cd14506

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...

179-274

4.15e-05

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: 43.49 E-value: 4.15e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7MOU_A      179 FHYTTWPDFGVPeSPASFLNFrFKVNESgSLSpEHGPVVVHCSAGIGRSGtycLADTCLLLMDKRKDPSSVdIKKVllem 258
Cdd:cd14506  79 FYNFGWKDYGVP-SLTTILDI-VKVMAF-ALQ-EGGKVAVHCHAGLGRTG---VLIACYLVYALRMSADQA-IRLV---- 146

                        90
                ....*....|....*.
7MOU_A      259 RKFRMGLIQTADQLRF 274
Cdd:cd14506 147 RSKRPNSIQTRGQVLC 162

DSPc

pfam00782

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...

212-244

3.54e-04

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.

Pssm-ID: 395632 [Multi-domain] Cd Length: 127 Bit Score: 39.55 E-value: 3.54e-04

                          10        20        30
                  ....*....|....*....|....*....|...
7MOU_A        212 EHGPVVVHCSAGIGRSGTYCLAdtclLLMDKRK 244
Cdd:pfam00782  68 KGGKVLVHCQAGISRSATLIIA----YLMKTRN 96

DSP_MKP_classI

cd14565

dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...

212-233

5.19e-04

dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class I MKPs consist of DUSP1/MKP-1, DUSP2 (PAC1), DUSP4/MKP-2 and DUSP5. They are all mitogen- and stress-inducible nuclear MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.

Pssm-ID: 350413 [Multi-domain] Cd Length: 138 Bit Score: 39.29 E-value: 5.19e-04

                        10        20
                ....*....|....*....|..
7MOU_A      212 EHGPVVVHCSAGIGRSGTYCLA 233
Cdd:cd14565  77 SGGRVLVHCQAGISRSATICLA 98

DSPc

smart00195

Dual specificity phosphatase, catalytic domain;

212-244

6.83e-04

Dual specificity phosphatase, catalytic domain;

Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 39.19 E-value: 6.83e-04

                           10        20        30
                   ....*....|....*....|....*....|...
7MOU_A         212 EHGPVVVHCSAGIGRSGTYCLAdtclLLMDKRK 244
Cdd:smart00195  77 KGGKVLVHCQAGVSRSATLIIA----YLMKTRN 105

DSP_DUSP4

cd14640

dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...

208-243

1.49e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual specificity protein phosphatase 4 (DUSP4), also called mitogen-activated protein kinase (MAPK) phosphatase 2 (MKP-2), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP4 regulates either ERK or c-JUN N-terminal kinase (JNK), depending on the cell type. It dephosphorylates nuclear JNK and induces apoptosis in diffuse large B cell lymphoma (DLBCL) cells. It acts as a negative regulator of macrophage M1 activation and inhibits inflammation during macrophage-adipocyte interaction. It has been linked to different aspects of cancer: it may have a role in the development of ovarian cancers, oesophagogastric rib metastasis, and pancreatic tumours; it may also be a candidate tumor suppressor gene, with its deletion implicated in breast cancer, prostate cancer, and gliomas. DUSP4/MKP-2 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.

Pssm-ID: 350488 [Multi-domain] Cd Length: 141 Bit Score: 38.09 E-value: 1.49e-03

                        10        20        30
                ....*....|....*....|....*....|....*.
7MOU_A      208 SLSPEHGPVVVHCSAGIGRSGTYCLAdtcLLLMDKR 243
Cdd:cd14640  73 SVKDCNGRVLVHCQAGISRSATICLA---YLMMKKR 105

PTP_PTEN-like

cd14497

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...

208-276

1.79e-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: 38.33 E-value: 1.79e-03

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7MOU_A      208 SLSPEHgPVVVHCSAGIGRSGTYCladTCLLLMDKRKdpSSVDIKKVLLEMRKFRMGL--IQTADQLRFSY 276
Cdd:cd14497  91 SEDPNN-VAVVHCKAGKGRTGTVI---CAYLLYYGQY--STADEALEYFAKKRFKEGLpgVTIPSQLRYLQ 155

DSP

cd14498

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...

212-244

2.10e-03

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.

Pssm-ID: 350348 [Multi-domain] Cd Length: 135 Bit Score: 37.53 E-value: 2.10e-03

                        10        20        30
                ....*....|....*....|....*....|...
7MOU_A      212 EHGPVVVHCSAGIGRSGTYCLAdtclLLMDKRK 244
Cdd:cd14498  78 KGGKVLVHCQAGVSRSATIVIA----YLMKKYG 106

DUSP14-like

cd14514

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...

213-233

6.59e-03

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.

Pssm-ID: 350364 [Multi-domain] Cd Length: 133 Bit Score: 35.99 E-value: 6.59e-03

                        10        20
                ....*....|....*....|.
7MOU_A      213 HGPVVVHCSAGIGRSGTYCLA 233
Cdd:cd14514  77 GGRTLVHCVAGVSRSATLCLA 97

TpbA-like

cd14529

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...

213-231

8.08e-03

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.

Pssm-ID: 350378 [Multi-domain] Cd Length: 158 Bit Score: 36.20 E-value: 8.08e-03

                        10
                ....*....|....*....
7MOU_A      213 HGPVVVHCSAGIGRSGTYC 231
Cdd:cd14529  89 PGPVLIHCKHGKDRTGLVS 107

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