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Conserved domains on  [gi|300795675|ref|NP_001178423|]
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receptor-type tyrosine-protein phosphatase U precursor [Bos taurus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 943-1147 2.47e-159

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: 478.01  E-value: 2.47e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETL 1022
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1023 AEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVML 1102
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795675 1103 DMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14632   161 DMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1232-1438 1.55e-149

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: 452.44  E-value: 1.55e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAWPCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNISRMQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAAVDKWQAESGDGRTIVHCLNGGGRSGTFC 1391
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300795675 1392 ACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 22-186 6.95e-55

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


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 188.32  E-value: 6.95e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675     22 TPAAGCTFEEtsdpAVPCEYSQAQYDDFQWEQVRIHPGTRAP---ADLPHGSYLVVNASQHAPGQRAHVIFQSLSEN-DT 97
Cdd:smart00137    1 TSPGNCDFEE----GSTCGWHQDSNDDGHWERVSSATGIPGPnrdHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675     98 HCVQFSYFLYsrdGHSPGTLGIYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALVSPDRRGYMGLD 177
Cdd:smart00137   77 HCLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALD 152


                    ....*....
gi 300795675    178 DILLLSYPC 186
Cdd:smart00137  153 DILLSNGPC 161
fn3 pfam00041
Fibronectin type III domain;
494-577 3.01e-14

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 3.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   494 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSVESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTG 572
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*
gi 300795675   573 KGFGQ 577
Cdd:pfam00041   79 GGEGP 83
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
347-624 2.41e-11

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 68.11  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  347 LDPDTEYEISVLLTrpGDGGTGRPGPPlVSRTKCAEPMRAPKGLAFAEIQARQLTLQWEP------LGYNVTRCHTYSVS 420
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRVYRSNSGDGP 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  421 LCyhyTLGSSHNqtvrecvkmergvSRYTIKNLLPYRNVHVRLVLTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 498
Cdd:COG3401   276 FT---KVATVTT-------------TSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  499 LEDM-IFLKWEEPQEPNglITQYEIsYQSVESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTGKGfgq 577
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 300795675  578 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 624
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
fn3 pfam00041
Fibronectin type III domain;
291-365 3.65e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   291 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---SLQTYKLWHLDPDTEYEISVlLTRPGD 364
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 300795675   365 G 365
Cdd:pfam00041   80 G 80
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 196-282 3.57e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 37.87  E-value: 3.57e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    196 GDVEVNAGQNASFQCmaAGRAAEAERFLLQRQSGALVPAAGVRHISHRRFLATFPLVAVSREDQDLYRCVSQAPRGaGVS 275
Cdd:smart00410    2 PSVTVKEGESVTLSC--EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78


                    ....*..
gi 300795675    276 NFAELIV 282
Cdd:smart00410   79 SGTTLTV 85
 
Name Accession Description Interval E-value
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 943-1147 2.47e-159

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: 478.01  E-value: 2.47e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETL 1022
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1023 AEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVML 1102
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795675 1103 DMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14632   161 DMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1232-1438 1.55e-149

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: 452.44  E-value: 1.55e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAWPCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNISRMQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAAVDKWQAESGDGRTIVHCLNGGGRSGTFC 1391
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300795675 1392 ACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
918-1143 9.27e-105

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 332.67  E-value: 9.27e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   918 RQEPMPAYDRHRVKLHPmlGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVK 997
Cdd:pfam00102    6 RYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   998 CSRYWP---EDSDMYGDIKITLVKTET-LAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS 1073
Cdd:pfam00102   84 CAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKS 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795675  1074 TP-PDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:pfam00102  164 SLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
893-1143 4.61e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 328.85  E-value: 4.61e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    893 GFKQEYESFFEGWDATKKKDKVKggRQEPM--------PAYDRHRVKLHPMLGDPDaDYINANYIDGYHRSNHFIATQGP 964
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAA--FPENRdknrykdvLPYDHTRVKLKPPPGEGS-DYINASYIDGPNGPKAYIATQGP 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    965 KPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRSFALERRGYSARH 1041
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1042 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLC 1121
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|..
gi 300795675   1122 SRRVNMIQTEEQYIFIHDAILE 1143
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1175-1438 4.10e-86

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 281.47  E-value: 4.10e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1175 QLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLVSTDGDPNNYINAALTDSYTRSAAFIVTLHPL 1254
Cdd:smart00194    1 GLEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1255 QSTTPDFWRLVYDYGCTSIVMLNQLhQSNSAWPCPQYWPEPGR--QQYGLMEVEFVSGTADEDLVARVFRVQNISrmQEG 1332
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTEL-VEKGREKCAQYWPDEEGepLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1333 HLLVRHFQFLRWSaYRDTPDSKKAFLHLLAAVDKWQaESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAA 1412
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 300795675   1413 KTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1203-1438 3.64e-72

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 240.99  E-value: 3.64e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  1203 NRDKNRSMDVLPPDRCLPFLvSTDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLhQS 1282
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL-EE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  1283 NSAWPCPQYWPEP--GRQQYGLMEVEFVSGTADE-DLVARVFRVQNISRMQEghLLVRHFQFLRWSAyRDTPDSKKAFLH 1359
Cdd:pfam00102   79 KGREKCAQYWPEEegESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEET--RTVKHFHYTGWPD-HGVPESPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675  1360 LLAAVDKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:pfam00102  156 LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 22-186 6.95e-55

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


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 188.32  E-value: 6.95e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675     22 TPAAGCTFEEtsdpAVPCEYSQAQYDDFQWEQVRIHPGTRAP---ADLPHGSYLVVNASQHAPGQRAHVIFQSLSEN-DT 97
Cdd:smart00137    1 TSPGNCDFEE----GSTCGWHQDSNDDGHWERVSSATGIPGPnrdHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675     98 HCVQFSYFLYsrdGHSPGTLGIYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALVSPDRRGYMGLD 177
Cdd:smart00137   77 HCLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALD 152


                    ....*....
gi 300795675    178 DILLLSYPC 186
Cdd:smart00137  153 DILLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 27-187 2.69e-49

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


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 172.16  E-value: 2.69e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    27 CTFEETSDpavpCEYSQAQYDDFQWEQVRIHPGTRAPA-----DLPHGSYLVVNASQHAPGQRAHVIFQSLSENDT-HCV 100
Cdd:pfam00629    1 CDFEDGNL----CGWTQDSSDDFDWERVSGPSVKTGPSsdhtqGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   101 QFSYFLYsrdGHSPGTLGIYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFwPNEYQVLFEALVSPDRRGYMGLDDIL 180
Cdd:pfam00629   77 RFWYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDIS 152


                   ....*..
gi 300795675   181 LLSYPCA 187
Cdd:pfam00629  153 LSSGPCP 159
PHA02738 PHA02738
hypothetical protein; Provisional
 905-1141 1.22e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 170.49  E-value: 1.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  905 WDATKKKDKVKggRQEPMPAYDRHRVKLhPMLGDpDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSI 984
Cdd:PHA02738   43 FNAEKKNRKLN--RYLDAVCFDHSRVIL-PAERN-RGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQII 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  985 VMITKLVEVGRVKCSRYWP--EDSDM-YGDIKITLVKTETLAEYvVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHAT 1061
Cdd:PHA02738  119 VMLCKKKENGREKCFPYWSdvEQGSIrFGKFKITTTQVETHPHY-VKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTS 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1062 GLLAFIRRVKA----------------STPPdagPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRV 1125
Cdd:PHA02738  198 EFLNFVLEVRQcqkelaqeslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRY 274

                         250
                  ....*....|....*.
gi 300795675 1126 NMIQTEEQYIFIHDAI 1141
Cdd:PHA02738  275 YSLFIPFQYFFCYRAV 290
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 27-186 2.54e-46

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


Pssm-ID: 99706  Cd Length: 157  Bit Score: 163.70  E-value: 2.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   27 CTFEETsdpavPCEYSQAQYDDFQWEQVRIHPGTRAPADL-----PHGSYLVVNASQHAPGQRAHVIFQSLSEN-DTHCV 100
Cdd:cd06263     1 CDFEDG-----LCGWTQDSTDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  101 QFSYFLYsrdGHSPGTLGIYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWpNEYQVLFEALVSPDRRGYMGLDDIL 180
Cdd:cd06263    76 SFWYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDIS 151


                  ....*.
gi 300795675  181 LLSYPC 186
Cdd:cd06263   152 LSPGPC 157
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
939-1137 8.96e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 132.14  E-value: 8.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  939 PDADYINANYIDGYhRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVG--RVKCSRYWPEDSDmYG--DIKI 1014
Cdd:COG5599    61 ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGE-YGkyEVSS 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1015 TLVKTETLAEYV-VRSFALERRGYSAR-HEVRQFHFTAWPEHGVPyHATGLLAFIRRVKAS---TPPDAGPVVIHCSAGT 1089
Cdd:COG5599   139 ELTESIQLRDGIeARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKekiKDPDKLLPVVHCRAGV 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 300795675 1090 GRTGCYIVLDVMLDM--AECEGVVDIYNCVKTL-CSRRVNMIQTEEQYIFI 1137
Cdd:COG5599   218 GRTGTLIACLALSKSinALVQITLSVEEIVIDMrTSRNGGMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1201-1440 1.48e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 103.16  E-value: 1.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1201 PRNRDKNRSMDVLPPDRCLPFLVSTDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLH 1280
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1281 QSNSAWPCPQYW--PEPGRQQYGLMEVEFVSGTADEDLVARVFRVQNISRMQEGHLlvRHFQFLRWSAYrDTPDSKKAFL 1358
Cdd:PHA02747  129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI--SHFQCSEWFED-ETPSDHPDFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1359 HLLAAVDKWQAESGDGRT---------IVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQY 1429
Cdd:PHA02747  206 KFIKIIDINRKKSGKLFNpkdallcpiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                         250
                  ....*....|....
gi 300795675 1430 HF---CYDVALEYL 1440
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
fn3 pfam00041
Fibronectin type III domain;
494-577 3.01e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 3.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   494 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSVESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTG 572
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*
gi 300795675   573 KGFGQ 577
Cdd:pfam00041   79 GGEGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 484-585 1.18e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.91  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  484 DVPGGIAAESLTftplEDMIFLKWEEPQEPNGLITQYEISYQSVESSDPA-VNVPGPrrtisklrNETYHVFSNLHPGTT 562
Cdd:cd00063     2 SPPTNLRVTDVT----STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeVEVTPG--------SETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....
gi 300795675  563 YLFSVRARTGKGFGQAA-LTEITT 585
Cdd:cd00063    70 YEFRVRAVNGGGESPPSeSVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
347-624 2.41e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 68.11  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  347 LDPDTEYEISVLLTrpGDGGTGRPGPPlVSRTKCAEPMRAPKGLAFAEIQARQLTLQWEP------LGYNVTRCHTYSVS 420
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRVYRSNSGDGP 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  421 LCyhyTLGSSHNqtvrecvkmergvSRYTIKNLLPYRNVHVRLVLTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 498
Cdd:COG3401   276 FT---KVATVTT-------------TSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  499 LEDM-IFLKWEEPQEPNglITQYEIsYQSVESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTGKGfgq 577
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 300795675  578 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 624
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 486-576 2.47e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.39  E-value: 2.47e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    486 PGGIAAESLTftplEDMIFLKWEEPQEPNGL--ITQYEISYQSVESSDPAVNVPGprrtisklrNETYHVFSNLHPGTTY 563
Cdd:smart00060    4 PSNLRVTDVT----STSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTP---------SSTSYTLTGLKPGTEY 70

                            90
                    ....*....|...
gi 300795675    564 LFSVRARTGKGFG 576
Cdd:smart00060   71 EFRVRAVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 386-481 2.95e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  386 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYSVSLCyhytlgSSHNQTVRECVKMERGVSRYTIKNLLPYRNVHVRLVL 465
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR------EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*..
gi 300795675  466 TNPEGR-KEGKEVTFQT 481
Cdd:cd00063    77 VNGGGEsPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
291-365 3.65e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   291 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---SLQTYKLWHLDPDTEYEISVlLTRPGD 364
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 300795675   365 G 365
Cdd:pfam00041   80 G 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 286-357 1.86e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.45  E-value: 1.86e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795675    286 PTPIAPPQLLRAGPTYLIIQ-LNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVSLQT-YKLWHLDPDTEYEISV 357
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 386-471 6.08e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.91  E-value: 6.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    386 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYSVSLCYHYTLGSSHNQTVREcvkmerGVSRYTIKNLLPYRNVHVRLVL 465
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP------SSTSYTLTGLKPGTEYEFRVRA 76


                    ....*.
gi 300795675    466 TNPEGR 471
Cdd:smart00060   77 VNGAGE 82
fn3 pfam00041
Fibronectin type III domain;
386-467 1.00e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.32  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   386 APKGLAFAEIQARQLTLQWEP--------LGYNVTRCHTYSVSLCYHYTLGSSHNqtvrecvkmergvsRYTIKNLLPYR 457
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgngpiTGYEVEYRPKNSGEPWNEITVPGTTT--------------SVTLTGLKPGT 67

                           90
                   ....*....|
gi 300795675   458 NVHVRLVLTN 467
Cdd:pfam00041   68 EYEVRVQAVN 77
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 196-282 3.57e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 37.87  E-value: 3.57e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    196 GDVEVNAGQNASFQCmaAGRAAEAERFLLQRQSGALVPAAGVRHISHRRFLATFPLVAVSREDQDLYRCVSQAPRGaGVS 275
Cdd:smart00410    2 PSVTVKEGESVTLSC--EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78


                    ....*..
gi 300795675    276 NFAELIV 282
Cdd:smart00410   79 SGTTLTV 85
 
Name Accession Description Interval E-value
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 943-1147 2.47e-159

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: 478.01  E-value: 2.47e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETL 1022
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1023 AEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVML 1102
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795675 1103 DMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14632   161 DMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1232-1438 1.55e-149

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: 452.44  E-value: 1.55e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAWPCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNISRMQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAAVDKWQAESGDGRTIVHCLNGGGRSGTFC 1391
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300795675 1392 ACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 943-1146 3.35e-145

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: 440.51  E-value: 3.35e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETL 1022
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1023 AEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVML 1102
Cdd:cd14555    81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIML 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 300795675 1103 DMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1146
Cdd:cd14555   161 DMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 878-1146 5.83e-139

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: 427.15  E-value: 5.83e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  878 DLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPDADYINANYIDGYH 953
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGqsapWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  954 RSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETLAEYVVRSFALE 1033
Cdd:cd14633    81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1034 RRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDI 1113
Cdd:cd14633   161 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 240

                         250       260       270
                  ....*....|....*....|....*....|...
gi 300795675 1114 YNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1146
Cdd:cd14633   241 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 929-1146 3.20e-123

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: 382.45  E-value: 3.20e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  929 RVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDM 1008
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1009 YGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAG 1088
Cdd:cd14631    81 YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 300795675 1089 TGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1146
Cdd:cd14631   161 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1232-1434 3.25e-120

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: 373.67  E-value: 3.25e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSnsAWPCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPK--DQSCPQYWPDEGSGTYGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNISRMQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAAVDKWQAESGDGRTIVHCLNGGGRSGTFC 1391
Cdd:cd14556    79 IDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 300795675 1392 ACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYD 1434
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 924-1147 4.20e-118

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: 369.35  E-value: 4.20e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  924 AYDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP 1003
Cdd:cd14630    14 SYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVGRVKCVRYWP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1004 EDSDMYGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVI 1083
Cdd:cd14630    94 DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPDAGPIVV 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795675 1084 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14630   174 HCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 924-1147 6.39e-111

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: 349.77  E-value: 6.39e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  924 AYDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP 1003
Cdd:cd14553    14 AYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSRVKCDQYWP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1004 -EDSDMYGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVV 1082
Cdd:cd14553    94 tRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKACNPPDAGPIV 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795675 1083 IHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14553   174 VHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
918-1143 9.27e-105

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 332.67  E-value: 9.27e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   918 RQEPMPAYDRHRVKLHPmlGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVK 997
Cdd:pfam00102    6 RYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   998 CSRYWP---EDSDMYGDIKITLVKTET-LAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS 1073
Cdd:pfam00102   84 CAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKS 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795675  1074 TP-PDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:pfam00102  164 SLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
893-1143 4.61e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 328.85  E-value: 4.61e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    893 GFKQEYESFFEGWDATKKKDKVKggRQEPM--------PAYDRHRVKLHPMLGDPDaDYINANYIDGYHRSNHFIATQGP 964
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAA--FPENRdknrykdvLPYDHTRVKLKPPPGEGS-DYINASYIDGPNGPKAYIATQGP 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    965 KPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRSFALERRGYSARH 1041
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1042 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLC 1121
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|..
gi 300795675   1122 SRRVNMIQTEEQYIFIHDAILE 1143
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 877-1147 7.98e-101

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: 323.53  E-value: 7.98e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  877 ADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPDADYINANYIDGY 952
Cdd:cd14626     1 SDLADNIERLKANDGLKFSQEYESIDPGqqftWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  953 HRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRSFA 1031
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPiRGTETYGMIQVTLLDTVELATYSVRTFA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1032 LERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVV 1111
Cdd:cd14626   161 LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 300795675 1112 DIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14626   241 DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 871-1148 3.04e-95

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: 308.20  E-value: 3.04e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  871 HPAVRVADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPDADYINA 946
Cdd:cd14624     1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGqqftWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  947 NYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAEY 1025
Cdd:cd14624    81 NYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPsRGTETYGLIQVTLLDTVELATY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1026 VVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMA 1105
Cdd:cd14624   161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 300795675 1106 ECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCG 1148
Cdd:cd14624   241 KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 871-1147 6.83e-95

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: 307.40  E-value: 6.83e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  871 HPAVRVADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPDADYINA 946
Cdd:cd14625     1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGqqftWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  947 NYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAEY 1025
Cdd:cd14625    81 NYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPsRGTETYGMIQVTLLDTIELATF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1026 VVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMA 1105
Cdd:cd14625   161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 300795675 1106 ECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14625   241 KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 943-1139 2.61e-93

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: 299.20  E-value: 2.61e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKT 1019
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKpleYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1020 ETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLD 1099
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 300795675 1100 VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd00047   161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 943-1139 1.12e-91

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: 295.03  E-value: 1.12e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPED-SDMYGDIKITLVKTET 1021
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1022 LAEYVVRSFAL------ERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCY 1095
Cdd:cd14549    81 LATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 300795675 1096 IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14549   161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1232-1438 4.44e-91

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: 293.47  E-value: 4.44e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLhqsNSAWPCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM---DAAQLCMQYWPEKTSCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNISRMQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAAVDKWQAE--SGDGRTIVHCLNGGGRSGT 1389
Cdd:cd14634    78 IDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1390 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1232-1438 7.26e-91

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: 292.70  E-value: 7.26e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSawpCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNISRMQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAAVDKWQAE--SGDGRTIVHCLNGGGRSGT 1389
Cdd:cd14636    78 MDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEEcdEGEGRTIIHCLNGGGRSGM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1390 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14636   158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 925-1138 1.41e-88

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: 286.94  E-value: 1.41e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 1004
Cdd:cd14548     8 YDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCDHYWPF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1005 DSD--MYGDIKITLVKTETLAEYVVRSFALERRGYSarHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVV 1082
Cdd:cd14548    88 DQDpvYYGDITVTMLSESVLPDWTIREFKLERGDEV--RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQEKGPTI 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795675 1083 IHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14548   166 VHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1175-1438 4.10e-86

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 281.47  E-value: 4.10e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1175 QLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLVSTDGDPNNYINAALTDSYTRSAAFIVTLHPL 1254
Cdd:smart00194    1 GLEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1255 QSTTPDFWRLVYDYGCTSIVMLNQLhQSNSAWPCPQYWPEPGR--QQYGLMEVEFVSGTADEDLVARVFRVQNISrmQEG 1332
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTEL-VEKGREKCAQYWPDEEGepLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1333 HLLVRHFQFLRWSaYRDTPDSKKAFLHLLAAVDKWQaESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAA 1412
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 300795675   1413 KTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1232-1438 4.42e-84

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: 273.49  E-value: 4.42e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLhqsNSAWPCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV---DPAQLCPQYWPENGVHRHGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNISRMQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAAVDKWQAE--SGDGRTIVHCLNGGGRSGT 1389
Cdd:cd14635    78 LEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1390 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14635   158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 924-1146 1.81e-76

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: 254.96  E-value: 1.81e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  924 AYDRHRVKLHPMLG--DPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRY 1001
Cdd:cd17667    38 AYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQY 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1002 WP-EDSDMYGDIKITLVKTETLAEYVVRSFALER-----------RGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRR 1069
Cdd:cd17667   118 WPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRR 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795675 1070 VKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1146
Cdd:cd17667   198 SSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 867-1152 1.41e-74

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: 250.33  E-value: 1.41e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  867 TGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESF-----FEGWDATKKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPDA 941
Cdd:cd14621     1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALpacpiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  942 DYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD-MYGDIKITLVKTE 1020
Cdd:cd14621    81 DYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCwTYGNIRVSVEDVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1021 TLAEYVVRSFALERRG----YSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYI 1096
Cdd:cd14621   161 VLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795675 1097 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTI 1152
Cdd:cd14621   241 VIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 925-1143 2.88e-72

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: 241.00  E-value: 2.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 1004
Cdd:cd14620     7 YDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQYWPD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1005 DSD-MYGDIKITLVKTETLAEYVVRSFALERR---GYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGP 1080
Cdd:cd14620    87 QGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVNPVHAGP 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1081 VVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14620   167 IVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1203-1438 3.64e-72

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 240.99  E-value: 3.64e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  1203 NRDKNRSMDVLPPDRCLPFLvSTDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLhQS 1282
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL-EE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  1283 NSAWPCPQYWPEP--GRQQYGLMEVEFVSGTADE-DLVARVFRVQNISRMQEghLLVRHFQFLRWSAyRDTPDSKKAFLH 1359
Cdd:pfam00102   79 KGREKCAQYWPEEegESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEET--RTVKHFHYTGWPD-HGVPESPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675  1360 LLAAVDKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:pfam00102  156 LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 925-1143 1.21e-71

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: 239.33  E-value: 1.21e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLhPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 1004
Cdd:cd14615     9 YDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1005 D-SDMYGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAF---IRRVKASTPPDaGP 1080
Cdd:cd14615    88 KqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlVREYMKQNPPN-SP 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1081 VVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14615   167 ILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 906-1138 1.43e-71

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: 240.73  E-value: 1.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  906 DATKKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIV 985
Cdd:cd14543    22 LCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  986 MITKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATG 1062
Cdd:cd14543   102 MTTRVVERGRVKCGQYWPLEEGSslrYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAAA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1063 LLAFI--------RRVKASTPPDAG-----PVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQ 1129
Cdd:cd14543   182 LLDFLgevrqqqaLAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQ 261


                  ....*....
gi 300795675 1130 TEEQYIFIH 1138
Cdd:cd14543   262 TPDQYYFCY 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 925-1143 7.49e-70

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: 234.01  E-value: 7.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 1004
Cdd:cd14619     9 YDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRVKCEHYWPL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1005 DSD--MYGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA--STPPDAGP 1080
Cdd:cd14619    89 DYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQwlDQTMSGGP 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1081 VVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14619   169 TVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 925-1138 1.17e-68

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: 230.58  E-value: 1.17e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 1004
Cdd:cd14617     9 YDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1005 DSD--MYGDIKITLVKTETLAEYVVRSFAL--ERRGYSARHeVRQFHFTAWPEHGVPYHATGLLAFIRRVK--ASTPPDA 1078
Cdd:cd14617    89 DQDslYYGDLIVQMLSESVLPEWTIREFKIcsEEQLDAPRL-VRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRTPGS 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1079 GPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14617   168 GPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 929-1138 1.56e-68

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: 229.98  E-value: 1.56e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  929 RVKLHPMLGDPDADYINANYIDGY-HRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEvGRVKCSRYWPEDSD 1007
Cdd:cd14547    13 RVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AKEKCAQYWPEEEN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1008 M-YGDIKITLVKTETLAEYVVRSFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVK--ASTPPDAGPVVIH 1084
Cdd:cd14547    92 EtYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEeaRQTEPHRGPIVVH 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300795675 1085 CSAGTGRTGCYIVLDVMLDMAECEGVVDIyncVKTLCSRRVN---MIQTEEQYIFIH 1138
Cdd:cd14547   170 CSAGIGRTGCFIATSIGCQQLREEGVVDV---LGIVCQLRLDrggMVQTAEQYEFVH 223
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 943-1142 1.72e-68

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: 229.48  E-value: 1.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTET 1021
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1022 LAEYVVRSFALE--------RRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTG 1093
Cdd:cd17668    81 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1094 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd17668   161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 943-1138 5.76e-68

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: 227.49  E-value: 5.76e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD-MYGDIKITLVKTET 1021
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1022 LAEYVVRSFALERR----GYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIV 1097
Cdd:cd14551    81 LVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 300795675 1098 LDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14551   161 IDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 925-1138 5.54e-66

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: 222.86  E-value: 5.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 1004
Cdd:cd14616     9 YNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCHQYWPE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1005 DSD---MYGDIKITLVKTETLAEYVVRSFALERRGYSARheVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPV 1081
Cdd:cd14616    89 DNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPEHGVPESSAPLIHFVKLVRASRAHDNTPM 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300795675 1082 VIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14616   167 IVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 925-1142 5.91e-66

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: 222.90  E-value: 5.91e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 1004
Cdd:cd14618     9 YDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRVLCDHYWPS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1005 DSD--MYGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA--STPPDAGP 1080
Cdd:cd14618    89 ESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREhvQATKGKGP 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795675 1081 VVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd14618   169 TLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 925-1142 2.56e-65

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: 221.24  E-value: 2.56e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP- 1003
Cdd:cd14554    18 YESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPa 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1004 EDSDMYGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP--DAGPV 1081
Cdd:cd14554    98 ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQEGPI 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795675 1082 VIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd14554   178 TVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 943-1138 7.32e-65

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: 218.54  E-value: 7.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP---EDSDMYGDIKITLVKT 1019
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1020 ETLAEYVVRSFAL--ERRGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIV 1097
Cdd:cd14557    81 KICPDYIIRKLNInnKKEKGSGR-EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 300795675 1098 LDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14557   160 IDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 943-1139 2.16e-64

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 217.50  E-value: 2.16e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYID-GYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDM--YGDIKITLVKT 1019
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgeYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1020 ETLAE--YVVRSFALeRRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA--STPPDAGPVVIHCSAGTGRTGCY 1095
Cdd:cd18533    81 EENDDggFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1096 IVLDVMLDMAE--------CEGVVD-IYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd18533   160 IALDSLLDELKrglsdsqdLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 925-1142 2.69e-63

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: 215.91  E-value: 2.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP- 1003
Cdd:cd14614    24 YDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPf 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1004 -EDSDMYGDIKITLVKTETLAEYVVRSFaleRRGYS-ARHEVRQFHFTAWPEHGVPY--HATGLLAFIRRVKASTPPDAG 1079
Cdd:cd14614   104 tEEPVAYGDITVEMLSEEEQPDWAIREF---RVSYAdEVQDVMHFNYTAWPDHGVPTanAAESILQFVQMVRQQAVKSKG 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1080 PVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd14614   181 PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 925-1141 4.17e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 215.40  E-value: 4.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPmlGDPD---ADYINANYI-----DGYHRSNH--FIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVG 994
Cdd:cd14544    13 FDHTRVILKD--RDPNvpgSDYINANYIrneneGPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVIVMTTKEVERG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  995 RVKCSRYWPED--SDMYGDIKITLVKTETLAEYVVRSFALER--RGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRV 1070
Cdd:cd14544    91 KNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKldQGDPIR-EIWHYQYLSWPDHGVPSDPGGVLNFLEDV 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795675 1071 --KASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14544   170 nqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAV 245
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 943-1144 1.94e-62

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 211.85  E-value: 1.94e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYI------DGYHrsnhFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD----MYGDI 1012
Cdd:cd14538     1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNkpliCGGRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1013 KITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTppDAGPVVIHCSAGTGRT 1092
Cdd:cd14538    77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300795675 1093 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1144
Cdd:cd14538   155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 942-1144 6.47e-61

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: 207.57  E-value: 6.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  942 DYINANYID----GYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE--DSDMYGDIKIT 1015
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1016 LVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCY 1095
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1096 IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1144
Cdd:cd14541   161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 943-1139 7.57e-60

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


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 204.16  E-value: 7.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETL 1022
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1023 AEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAG------PVVIHCSAGTGRTGCYI 1096
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGSSRTGIFC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 300795675 1097 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14558   161 ALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 872-1143 8.50e-59

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: 204.97  E-value: 8.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  872 PAVRVADLLQHINQMKTAEGY-GFKQEYESFFEGWDATKK-------KDKVKGGRQEPMPaYDRHRVKLHPMLGDPDADY 943
Cdd:cd14628     4 PARNLYAYIQKLTQIETGENVtGMELEFKRLASSKAHTSRfisanlpCNKFKNRLVNIMP-YESTRVCLQPIRGVEGSDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  944 INANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETL 1022
Cdd:cd14628    83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPaERSARYQYFVVDPMAEYNM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1023 AEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP--DAGPVVIHCSAGTGRTGCYIVLDV 1100
Cdd:cd14628   163 PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSI 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 300795675 1101 MLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14628   243 VLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 943-1141 2.19e-58

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: 200.19  E-value: 2.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDM-YGDIKITLVKTET 1021
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1022 LAEYVVRSFALER-RGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRV-KASTPPDAGPVVIHCSAGTGRTGCYIVLD 1099
Cdd:cd14552    81 YEDYTLRDFLVTKgKGGSTR-TVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCALS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 300795675 1100 VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14552   160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 922-1143 1.45e-57

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: 201.11  E-value: 1.45e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  922 MPaYDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRY 1001
Cdd:cd14627    63 MP-YETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQY 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1002 WP-EDSDMYGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP--DA 1078
Cdd:cd14627   142 WPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQD 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795675 1079 GPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14627   222 GPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 925-1143 1.29e-56

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: 196.03  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 1004
Cdd:cd14623     8 YEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1005 DSDM-YGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAG-PVV 1082
Cdd:cd14623    88 DGSVsYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNhPIT 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795675 1083 IHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14623   168 VHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 922-1143 1.74e-56

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: 198.03  E-value: 1.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  922 MPaYDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRY 1001
Cdd:cd14629    63 MP-YELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQY 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1002 WP-EDSDMYGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP--DA 1078
Cdd:cd14629   142 WPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQfgQD 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795675 1079 GPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14629   222 GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 911-1141 3.90e-56

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: 195.62  E-value: 3.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  911 KDKVKGGRQEPMPaYDRHRVKLHPmlGDPD---ADYINANYIDGYHRSN--------HFIATQGPKPEMVYDFWRMVWQE 979
Cdd:cd14605     1 ENKNKNRYKNILP-FDHTRVVLHD--GDPNepvSDYINANIIMPEFETKcnnskpkkSYIATQGCLQNTVNDFWRMVFQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  980 HCSSIVMITKLVEVGRVKCSRYWPEDSDM--YGDIKITLVKTETLAEYVVRSFALERRGY-SARHEVRQFHFTAWPEHGV 1056
Cdd:cd14605    78 NSRVIVMTTKEVERGKSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGQgNTERTVWQYHFRTWPDHGV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1057 PYHATGLLAFIRRV--KASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRVNMIQTE 1131
Cdd:cd14605   158 PSDPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTE 237

                         250
                  ....*....|
gi 300795675 1132 EQYIFIHDAI 1141
Cdd:cd14605   238 AQYRFIYMAV 247
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 942-1141 4.41e-56

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: 193.68  E-value: 4.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  942 DYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLvKTE 1020
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPsEGSVTHGEITIEI-KND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1021 TLAEYV-VRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV-KASTPPDAGPVVIHCSAGTGRTGCYIVL 1098
Cdd:cd14622    80 TLLETIsIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 300795675 1099 DVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 929-1141 8.43e-56

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: 194.70  E-value: 8.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  929 RVKL-HPMLGDPDADYINANYIDGY-HRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSRYWPEDS 1006
Cdd:cd14613    41 RVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWPEEQ 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1007 DMYGDIKITLVKTETLAEYVVRSFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---STPPDAGPVVI 1083
Cdd:cd14613   120 VTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEarqQAEPNCGPVIV 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795675 1084 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIyncVKTLCSRRVN---MIQTEEQYIFIHDAI 1141
Cdd:cd14613   198 HCSAGIGRTGCFIATSICCKQLRNEGVVDI---LRTTCQLRLDrggMIQTCEQYQFVHHVL 255
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1232-1434 3.77e-55

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: 190.57  E-value: 3.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQ--QYGLMEVEFVS 1309
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGRE-KCERYWPEEGGKplEYGDITVTLVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1310 GTADEDLVARVFRVQNISRMQEghLLVRHFQFLRWSAyRDTPDSKKAFLHLLAAVDKWQaESGDGRTIVHCLNGGGRSGT 1389
Cdd:cd00047    80 EEELSDYTIRTLELSPKGCSES--REVTHLHYTGWPD-HGVPSSPEDLLALVRRVRKEA-RKPNGPIVVHCSAGVGRTGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795675 1390 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYD 1434
Cdd:cd00047   156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 938-1138 5.06e-55

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: 192.36  E-value: 5.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  938 DPDADYINANYIDGYH-RSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEvGRVKCSRYWPEDSDMYGDIKITL 1016
Cdd:cd14612    41 EEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE-KKEKCVHYWPEKEGTYGRFEIRV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1017 VKTETLAEYVVRSFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPVVIHCSAGTGRTGC 1094
Cdd:cd14612   120 QDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESrqTAASPGPIVVHCSAGIGRTGC 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 300795675 1095 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14612   198 FIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 22-186 6.95e-55

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


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 188.32  E-value: 6.95e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675     22 TPAAGCTFEEtsdpAVPCEYSQAQYDDFQWEQVRIHPGTRAP---ADLPHGSYLVVNASQHAPGQRAHVIFQSLSEN-DT 97
Cdd:smart00137    1 TSPGNCDFEE----GSTCGWHQDSNDDGHWERVSSATGIPGPnrdHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675     98 HCVQFSYFLYsrdGHSPGTLGIYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALVSPDRRGYMGLD 177
Cdd:smart00137   77 HCLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALD 152


                    ....*....
gi 300795675    178 DILLLSYPC 186
Cdd:smart00137  153 DILLSNGPC 161
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 911-1142 6.41e-53

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: 185.80  E-value: 6.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  911 KDKVKGGRQEPMPAYDRHRVklhpMLGDpDADYINANYIDGYHRSNHF--IATQGPKPEMVYDFWRMVWQEHCSSIVMIT 988
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRV----PLGD-EGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  989 KLVEVGRVKCSRYWPED---SDMYGD-IKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLL 1064
Cdd:cd14597    76 QEVEGGKIKCQRYWPEIlgkTTMVDNrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1065 AFI---RRVKAStppdaGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14597   156 TFIsymRHIHKS-----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                  .
gi 300795675 1142 L 1142
Cdd:cd14597   231 L 231
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 943-1138 6.95e-53

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: 184.16  E-value: 6.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKT 1019
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEqlqFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1020 ETLAE-YVVRSFALERRgySARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVL 1098
Cdd:cd14542    81 KRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 300795675 1099 DVMLDMAECEGVVD---IYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14542   159 DYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 894-1143 4.59e-52

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: 184.26  E-value: 4.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  894 FKQEYESFFEgwdATKKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFW 973
Cdd:cd14603    14 FKADYVCSTV---AGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFW 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  974 RMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD--MYGDIKITLVKTETL-AEYVVRSFALERRGYSarHEVRQFHFTA 1050
Cdd:cd14603    91 RMIWQYGVKVILMACREIEMGKKKCERYWAQEQEplQTGPFTITLVKEKRLnEEVILRTLKVTFQKES--RSVSHFQYMA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1051 WPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVD---IYNCVKTLCSRRVNM 1127
Cdd:cd14603   169 WPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAA 248

                         250
                  ....*....|....*.
gi 300795675 1128 IQTEEQYIFIHDAILE 1143
Cdd:cd14603   249 VQTEEQYEFLYHTVAQ 264
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 929-1138 1.06e-51

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: 181.65  E-value: 1.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  929 RVKLHPM-LGDPDADYINANYIDGYH-RSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSRYWPEDS 1006
Cdd:cd14611    15 RVCLKPKnSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1007 DMYGDIKITLVKTETLAEYVVRSFALeRRGYSARHeVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPVVIH 1084
Cdd:cd14611    94 GIYGKVEVLVNSVKECDNYTIRNLTL-KQGSQSRS-VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDrlASPGRGPVVVH 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300795675 1085 CSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14611   172 CSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 895-1143 1.72e-51

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: 182.77  E-value: 1.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  895 KQEYESFFEGWDATKKKDKVKGGRQEPMPaYDRHRVKLHPmlGDPD---ADYINANYIDGY-----HRSNHFIATQGPKP 966
Cdd:cd14606     1 KQEVKNLHQRLEGQRPENKSKNRYKNILP-FDHSRVILQG--RDSNipgSDYINANYVKNQllgpdENAKTYIASQGCLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  967 EMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE--DSDMYGDIKITLVKTETLAEYVVRSFALE--RRGYSARhE 1042
Cdd:cd14606    78 ATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSplDNGELIR-E 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1043 VRQFHFTAWPEHGVPYHATGLLAFIRRV--KASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCV 1117
Cdd:cd14606   157 IWHYQYLSWPDHGVPSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTI 236

                         250       260
                  ....*....|....*....|....*.
gi 300795675 1118 KTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14606   237 QMVRAQRSGMVQTEAQYKFIYVAIAQ 262
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1232-1435 1.08e-50

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: 177.85  E-value: 1.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLhQSNSAWPCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEI-KERSQNKCAQYWPEDGSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNisrMQEGHL-LVRHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQAESGDGRTIVHCLNGGGRSGTF 1390
Cdd:cd14552    80 DYEDYTLRDFLVTK---GKGGSTrTVRQFHFHGWPEV-GIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTF 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795675 1391 CACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDV 1435
Cdd:cd14552   156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 942-1143 2.29e-50

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: 177.44  E-value: 2.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  942 DYINANYIDGYHRS----NHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE--DSDMYGDIKIT 1015
Cdd:cd14601     1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1016 LVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCY 1095
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 300795675 1096 IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14601   161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 925-1143 2.73e-50

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: 178.11  E-value: 2.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 1004
Cdd:cd14602    10 YDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGKKKCERYWAE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1005 DSDM---YGDIKITLVKTETLAEYVVRSfaLERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPV 1081
Cdd:cd14602    90 PGEMqleFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPI 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795675 1082 VIHCSAGTGRTGCYIVLDVMLDMAEcEGVV----DIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14602   168 CIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1198-1437 2.81e-50

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: 178.10  E-value: 2.81e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1198 ALLPRNRDKNRSMDVLPPDR---CLPFLVSTDGdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1274
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYEStrvCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1275 MLNQLHQSNSAwPCPQYWPEPGRQQYGLMEVEFVSGTADEDLVARVFRVQNISRMQEGHllVRHFQFLRWSAyRDTPDSK 1354
Cdd:cd14554    79 MLTKLREMGRE-KCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRT--VRQFQFTDWPE-QGVPKSG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1355 KAFLHLLAAVDKWQAESG-DGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCY 1433
Cdd:cd14554   155 EGFIDFIGQVHKTKEQFGqEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234


                  ....
gi 300795675 1434 DVAL 1437
Cdd:cd14554   235 RAAL 238
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 943-1143 3.51e-50

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: 176.87  E-value: 3.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYI-DGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPED-SDMYGDIKITLVKTE 1020
Cdd:cd14546     1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVHLVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1021 TLAE-YVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLD 1099
Cdd:cd14546    81 IWCDdYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795675 1100 VMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14546   161 MVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 909-1141 3.94e-50

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: 180.13  E-value: 3.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  909 KKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMIT 988
Cdd:cd14604    53 EKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMAC 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  989 KLVEVGRVKCSRYWP---EDSDMYGDIKITLVKTETLAEYVVRSFALERRGYSarHEVRQFHFTAWPEHGVPYHATGLLA 1065
Cdd:cd14604   133 REFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET--RRLYQFHYVNWPDHDVPSSFDSILD 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675 1066 FIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDV---MLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14604   211 MISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 906-1143 1.85e-49

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: 177.54  E-value: 1.85e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  906 DATKKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPDADYINAN-YIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSI 984
Cdd:cd14609    35 STAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  985 VMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAE-YVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATG 1062
Cdd:cd14609   115 VMLTPLVEDGVKQCDRYWPdEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRP 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1063 LLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14609   195 LLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAV 274


                  ..
gi 300795675 1142 LE 1143
Cdd:cd14609   275 AE 276
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 27-187 2.69e-49

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


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 172.16  E-value: 2.69e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    27 CTFEETSDpavpCEYSQAQYDDFQWEQVRIHPGTRAPA-----DLPHGSYLVVNASQHAPGQRAHVIFQSLSENDT-HCV 100
Cdd:pfam00629    1 CDFEDGNL----CGWTQDSSDDFDWERVSGPSVKTGPSsdhtqGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   101 QFSYFLYsrdGHSPGTLGIYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFwPNEYQVLFEALVSPDRRGYMGLDDIL 180
Cdd:pfam00629   77 RFWYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDIS 152


                   ....*..
gi 300795675   181 LLSYPCA 187
Cdd:pfam00629  153 LSSGPCP 159
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 943-1144 3.27e-49

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: 173.78  E-value: 3.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYI-----DGYHRsnhFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD---MYGDIKI 1014
Cdd:cd14596     1 YINASYItmpvgEEELF---YIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQepmELENYQL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1015 TLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTppDAGPVVIHCSAGTGRTGC 1094
Cdd:cd14596    78 RLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAGV 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 300795675 1095 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1144
Cdd:cd14596   156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 924-1136 5.56e-49

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: 174.12  E-value: 5.56e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  924 AYDRHRVKLHpmlgDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP 1003
Cdd:cd14545    11 DHDRSRVKLK----QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKCAQYWP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1004 -EDSDMYG----DIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVK--ASTPP 1076
Cdd:cd14545    87 qGEGNAMIfedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVResGSLSS 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795675 1077 DAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGV--VDIYNCVKTLCSRRVNMIQTEEQYIF 1136
Cdd:cd14545   167 DVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 909-1143 7.56e-49

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: 175.63  E-value: 7.56e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  909 KKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPDADYINANYI-DGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMI 987
Cdd:cd14610    40 QREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVML 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  988 TKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAE-YVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLA 1065
Cdd:cd14610   120 TPLAENGVKQCYHYWPdEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLD 199

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675 1066 FIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14610   200 FRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1232-1434 3.02e-47

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: 167.95  E-value: 3.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAWpCPQYWPEpGRQQYGLMEVEFVSGT 1311
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQ-CAQYWGD-EKKTYGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNISRMQegHLLVRHFQFLRWSAyRDTPDSKKAFLHLLAAVDKWQAE--SGDGRT---IVHCLNGGGR 1386
Cdd:cd14558    79 KSPTYTVRVFEITHLKRKD--SRTVYQYQYHKWKG-EELPEKPKDLVDMIKSIKQKLPYknSKHGRSvpiVVHCSDGSSR 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 300795675 1387 SGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYD 1434
Cdd:cd14558   156 TGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1231-1439 1.15e-46

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: 166.72  E-value: 1.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1231 NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLhQSNSAWPCPQYWPEPGRQQYGLMEVEFVSG 1310
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTEL-QEREQEKCVQYWPSEGSVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1311 TADEDLVARVFRVQNISRMQEghLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQAESGDGRTIVHCLNGGGRSGTF 1390
Cdd:cd14622    80 TLLETISIRDFLVTYNQEKQT--RLVRQFHFHGWPEI-GIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1391 CACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALEY 1439
Cdd:cd14622   157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PHA02738 PHA02738
hypothetical protein; Provisional
 905-1141 1.22e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 170.49  E-value: 1.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  905 WDATKKKDKVKggRQEPMPAYDRHRVKLhPMLGDpDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSI 984
Cdd:PHA02738   43 FNAEKKNRKLN--RYLDAVCFDHSRVIL-PAERN-RGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQII 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  985 VMITKLVEVGRVKCSRYWP--EDSDM-YGDIKITLVKTETLAEYvVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHAT 1061
Cdd:PHA02738  119 VMLCKKKENGREKCFPYWSdvEQGSIrFGKFKITTTQVETHPHY-VKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTS 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1062 GLLAFIRRVKA----------------STPPdagPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRV 1125
Cdd:PHA02738  198 EFLNFVLEVRQcqkelaqeslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRY 274

                         250
                  ....*....|....*.
gi 300795675 1126 NMIQTEEQYIFIHDAI 1141
Cdd:PHA02738  275 YSLFIPFQYFFCYRAV 290
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 27-186 2.54e-46

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


Pssm-ID: 99706  Cd Length: 157  Bit Score: 163.70  E-value: 2.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   27 CTFEETsdpavPCEYSQAQYDDFQWEQVRIHPGTRAPADL-----PHGSYLVVNASQHAPGQRAHVIFQSLSEN-DTHCV 100
Cdd:cd06263     1 CDFEDG-----LCGWTQDSTDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  101 QFSYFLYsrdGHSPGTLGIYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWpNEYQVLFEALVSPDRRGYMGLDDIL 180
Cdd:cd06263    76 SFWYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDIS 151


                  ....*.
gi 300795675  181 LLSYPC 186
Cdd:cd06263   152 LSPGPC 157
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1227-1438 2.82e-46

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: 166.37  E-value: 2.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1227 GDPN-NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQQYGLMEV 1305
Cdd:cd14623    20 GEENtDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE-KCAQYWPSDGSVSYGDITI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1306 EFVSGTADEDLVARVFRVQNISRMQEGHllVRHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQAESGDGRTIVHCLNGGG 1385
Cdd:cd14623    99 ELKKEEECESYTVRDLLVTNTRENKSRQ--IRQFHFHGWPEV-GIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAG 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1386 RSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14623   176 RTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 943-1139 4.16e-46

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: 164.89  E-value: 4.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSRYWPED-SDMYGDIKITLVkTET 1021
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWPDEgSGTYGPIQVEFV-STT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1022 LAEYVV-RSFALER--RGYSARHEVRQFHFTAWPEHG-VPYHATGLLAFIRRV-KASTPPDAGPVVIHCSAGTGRTGCYI 1096
Cdd:cd14556    79 IDEDVIsRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 300795675 1097 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 918-1152 4.70e-46

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 167.51  E-value: 4.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  918 RQEPMPAYDRHRVKLHpmlgDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVK 997
Cdd:cd14608    30 RYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  998 CSRYWP--EDSDMY---GDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVK- 1071
Cdd:cd14608   106 CAQYWPqkEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRe 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1072 -ASTPPDAGPVVIHCSAGTGRTGCYIVLD---VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEAC-- 1145
Cdd:cd14608   186 sGSLSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAkf 265


                  ....*..
gi 300795675 1146 LCGETTI 1152
Cdd:cd14608   266 IMGDSSV 272
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 925-1142 3.74e-45

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: 164.64  E-value: 3.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLhpmlgDPDADYINANYID----GYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSR 1000
Cdd:cd14600    52 YDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1001 YWPEDSDM--YGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKaSTPPDA 1078
Cdd:cd14600   127 YWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVR-SKRVEN 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795675 1079 GPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd14600   206 EPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 943-1143 1.06e-44

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: 161.47  E-value: 1.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGY--HRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-----EDSDMYGDIKIT 1015
Cdd:cd14540     1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggeHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1016 LVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA------------STPPdagPVVI 1083
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtnqdvaghNRNP---PTLV 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1084 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14540   158 HCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1150-1440 2.78e-44

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 162.98  E-value: 2.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1150 TTIPVSEFKATYKEMIRIDPQSNSSQLREEFQTLnsVTPPLDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLVSTD 1226
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYETtrvCLQPIRGVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1227 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQQYGLMEVE 1306
Cdd:cd14627    80 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1307 FVSGTADEDLVARVFRVQNISRMQEghLLVRHFQFLRWSAyRDTPDSKKAFLHLLAAVDKWQAESG-DGRTIVHCLNGGG 1385
Cdd:cd14627   157 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVG 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 300795675 1386 RSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALEYL 1440
Cdd:cd14627   234 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1150-1440 4.71e-44

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 162.21  E-value: 4.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1150 TTIPVSEFKATYKEMIRIDPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLVSTD 1226
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKA--HTSRFISANLPCNKFKNRLVNIMPYEStrvCLQPIRGVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1227 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQQYGLMEVE 1306
Cdd:cd14628    79 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1307 FVSGTADEDLVARVFRVQNISRMQEghLLVRHFQFLRWSAyRDTPDSKKAFLHLLAAVDKWQAESG-DGRTIVHCLNGGG 1385
Cdd:cd14628   156 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVG 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 300795675 1386 RSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALEYL 1440
Cdd:cd14628   233 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 943-1139 1.85e-43

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 157.16  E-value: 1.85e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGY-HRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPED---SDMYGDIKITLVK 1018
Cdd:cd14539     1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1019 TETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---STPPDAGPVVIHCSAGTGRTGCY 1095
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795675 1096 -IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14539   161 cLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1150-1440 2.95e-43

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 159.89  E-value: 2.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1150 TTIPVSEFKATYKEMIRIDPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLVSTD 1226
Cdd:cd14629     2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKA--HTSRFISANLPCNKFKNRLVNIMPYELtrvCLQPIRGVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1227 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQQYGLMEVE 1306
Cdd:cd14629    80 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1307 FVSGTADEDLVARVFRVQNISRMQEghLLVRHFQFLRWSAyRDTPDSKKAFLHLLAAVDKWQAESG-DGRTIVHCLNGGG 1385
Cdd:cd14629   157 PMAEYNMPQYILREFKVTDARDGQS--RTIRQFQFTDWPE-QGVPKTGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVG 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 300795675 1386 RSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALEYL 1440
Cdd:cd14629   234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1174-1433 9.03e-43

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: 157.91  E-value: 9.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1174 SQLREEFQTLnSVTPPLDVEECSiaLLPRNRDKNRSMDVLPPDRCLPFLVSTDGDPN-NYINAALTDSYTRSAAFIVTLH 1252
Cdd:cd14543     3 RGIYEEYEDI-RREPPAGTFLCS--LAPANQEKNRYGDVLCLDQSRVKLPKRNGDERtDYINANFMDGYKQKNAYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1253 PLQSTTPDFWRLVYDYGCTSIVMLNQLHQsNSAWPCPQYWP--EPGRQQYGLMEVEFVSGTADEDLVARVFRVQNISRMQ 1330
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVE-RGRVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1331 EghLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAV------------DKWQAESGDGRTIVHCLNGGGRSGTFCA---CAT 1395
Cdd:cd14543   159 S--RQVTHFQFTSWPDF-GVPSSAAALLDFLGEVrqqqalavkamgDRWKGHPPGPPIVVHCSAGIGRTGTFCTldiCLS 235

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 300795675 1396 VLEMIRchnLVDVFFAAKTLRNYKPNMVETLDQYHFCY 1433
Cdd:cd14543   236 QLEDVG---TLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 943-1138 9.98e-43

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 155.31  E-value: 9.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNH--FIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVE-VGRVKCSRYWP---EDSDMYGDIKITL 1016
Cdd:cd17658     1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPaeeNESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1017 VKTETlaeyvvRSFALERRGYSARH--------EVRQFHFTAWPEHGVPYHATGLLAFIRRVkASTPPDAGPVVIHCSAG 1088
Cdd:cd17658    81 KKLKH------SQHSITLRVLEVQYieseepplSVLHIQYPEWPDHGVPKDTRSVRELLKRL-YGIPPSAGPIVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300795675 1089 TGRTGCYIVLDVML------DMAecegVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd17658   154 IGRTGAYCTIHNTIrrilegDMS----AVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 918-1141 7.50e-41

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: 151.66  E-value: 7.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  918 RQEPMPAYDRHRVKLHPMlgdpDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVK 997
Cdd:cd14607    29 RYRDVSPYDHSRVKLQNT----ENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKDSVK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  998 CSRYWPEDSD---MYGD--IKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVK- 1071
Cdd:cd14607   105 CAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRe 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1072 -ASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEG--VVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14607   185 sGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1232-1433 2.01e-38

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: 142.85  E-value: 2.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSawpCPQYWPEPGRQQYG------LMEV 1305
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNED---EPIYWPTKEKPLECetfkvtLSGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1306 EFVSGTADEDLVARVFRVQNIsrmQEGHLL-VRHFQFLRWSAyRDTPDSKkaFLHLLAAVDKWqAESGDGRTIVHCLNGG 1384
Cdd:cd14550    78 DHSCLSNEIRLIVRDFILEST---QDDYVLeVRQFQCPSWPN-PCSPIHT--VFELINTVQEW-AQQRDGPIVVHDRYGG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1385 GRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCY 1433
Cdd:cd14550   151 VQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 923-1143 4.08e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 145.53  E-value: 4.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  923 PAYDRHRVKLHpmLGDPDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYW 1002
Cdd:PHA02742   62 PCFDRNRVILK--IEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYW 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1003 ---PEDSDMYGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV--------- 1070
Cdd:PHA02742  140 mphERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVreadlkadv 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795675 1071 --KASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:PHA02742  220 diKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1203-1438 4.14e-38

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: 143.31  E-value: 4.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1203 NRDKNRSMDVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLhQ 1281
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPgSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL-E 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1282 SNSAWPCPQYWPEPGRQQYGLMEVEFVSGTadeDLVARVFRVQNISRMQEGHLL-VRHFQFLRWSAYrDTPDSKKAFLHL 1360
Cdd:cd14553    82 ERSRVKCDQYWPTRGTETYGLIQVTLLDTV---ELATYTVRTFALHKNGSSEKReVRQFQFTAWPDH-GVPEHPTPFLAF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300795675 1361 LAAVdKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14553   158 LRRV-KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1208-1431 8.83e-38

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: 141.72  E-value: 8.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1208 RSMDVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQsNSAW 1286
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCME-KGRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1287 PCPQYWPEPGRQQ-YGLMEVEFVSGTADEDLVARVFRVQNISRmqegHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAVD 1365
Cdd:cd14548    80 KCDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKLERGDE----VRSVRQFHFTAWPDH-GVPEAPDSLLRFVRLVR 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795675 1366 KWQAESGdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHF 1431
Cdd:cd14548   155 DYIKQEK-GPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 905-1138 1.59e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 143.99  E-value: 1.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  905 WDATKKKDKVKGGRQEPMPAYDRHRVKLHPMLGDPdADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSI 984
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  985 VMITKLVEV-GRVKCSRYW--PEDSDM-YGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHA 1060
Cdd:PHA02747  122 VMLTPTKGTnGEEKCYQYWclNEDGNIdMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDH 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1061 TGLLAFI------RRVKAS--TPPDA--GPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQT 1130
Cdd:PHA02747  202 PDFIKFIkiidinRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMN 281


                  ....*...
gi 300795675 1131 EEQYIFIH 1138
Cdd:PHA02747  282 FDDYLFIQ 289
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 925-1143 2.07e-37

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: 142.83  E-value: 2.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  925 YDRHRVKLHPMLGDPDAdYINANYIDGYHRSN--HFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYW 1002
Cdd:cd14599    50 YEENRVELVPTKENNTG-YINASHIKVTVGGEewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYW 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1003 PE-----DSDMYGDIKITL-VKTETLAeYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAF---IRRVKAS 1073
Cdd:cd14599   129 PKlgskhSSATYGKFKVTTkFRTDSGC-YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYleeIQSVRRH 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795675 1074 TPP--DAG-----PVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14599   208 TNSmlDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1168-1431 2.23e-37

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: 142.50  E-value: 2.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1168 DPQSNSSQLREEFQTLNSVTPPLDVeeCSIALLPRNRDKNRSMDVLPPDRCLPFL-VSTDGDPNNYINAA-LTDSYTRSA 1245
Cdd:cd14610    11 DHLKNKNRLEKEWEALCAYQAEPNA--TNVAQREENVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASpIMDHDPRNP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1246 AFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQsNSAWPCPQYWPEPGRQQYGLMEVEFVSGTA-DEDLVARVFRVQ 1324
Cdd:cd14610    89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAE-NGVKQCYHYWPDEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1325 NISRMQEghLLVRHFQFLRWSAyRDTPDSKKAFLHLLAAVDKWQAesgdGRT---IVHCLNGGGRSGTFCACATVL-EMI 1400
Cdd:cd14610   168 NLQTNET--RTVTQFHFLSWND-QGVPASTRSLLDFRRKVNKCYR----GRScpiIVHCSDGAGRSGTYILIDMVLnKMA 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 300795675 1401 RCHNLVDVFFAAKTLRNYKPNMVETLDQYHF 1431
Cdd:cd14610   241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 943-1137 7.99e-36

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: 135.14  E-value: 7.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCsrYWPEDSDM--YGDIKITLVKTE 1020
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPleCETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1021 TL-----AEYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPVVIH-----CSAGTg 1090
Cdd:cd14550    79 HSclsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHdryggVQAAT- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300795675 1091 rtgcYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFI 1137
Cdd:cd14550   156 ----FCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1232-1434 9.31e-36

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: 135.17  E-value: 9.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRR-KCDQYWPKEGTETYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNI----SRMQEGHLLVRHFQFLRWSAYrDTPDSKkafLHLLAAVDKWQAES--GDGRTIVHCLNGGG 1385
Cdd:cd14549    80 VLATYTVRTFSLKNLklkkVKGRSSERVVYQYHYTQWPDH-GVPDYT---LPVLSFVRKSSAANppGAGPIVVHCSAGVG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1386 RSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYD 1434
Cdd:cd14549   156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1198-1431 1.73e-35

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: 135.79  E-value: 1.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1198 ALLPRNRDKNRSMDVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML 1276
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEgSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1277 NQLHQSNSAwPCPQYWP---EPgrQQYGLMEVEFVSGTADEDLVARVFRVQNISRMQEghllVRHFQFLRWSAYR-DTPD 1352
Cdd:cd14614    87 TQCNEKRRV-KCDHYWPfteEP--VAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHGvPTAN 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675 1353 SKKAFLHLLAAVdKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHF 1431
Cdd:cd14614   160 AAESILQFVQMV-RQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1042-1143 7.62e-35

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 128.63  E-value: 7.62e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1042 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP--PDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECE-GVVDIYNCVK 1118
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 300795675   1119 TLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1042-1143 7.62e-35

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: 128.63  E-value: 7.62e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1042 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP--PDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECE-GVVDIYNCVK 1118
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 300795675   1119 TLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1168-1431 9.51e-35

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: 134.78  E-value: 9.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1168 DPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRC-LPFLVSTDGDPNNYINAA-LTDSYTRSA 1245
Cdd:cd14609     9 DHLRNRDRLAKEWQALCAYQA--EPNTCSTAQGEANVKKNRNPDFVPYDHArIKLKAESNPSRSDYINASpIIEHDPRMP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1246 AFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQsNSAWPCPQYWPEPGRQQYGLMEVEFVSGTA-DEDLVARVFRVQ 1324
Cdd:cd14609    87 AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVE-DGVKQCDRYWPDEGSSLYHIYEVNLVSEHIwCEDFLVRSFYLK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1325 NIsRMQEGHLLVRhFQFLRWSAyRDTPDSKKAFLHLLAAVDKwqaeSGDGRT---IVHCLNGGGRSGTFCACATVL-EMI 1400
Cdd:cd14609   166 NV-QTQETRTLTQ-FHFLSWPA-EGIPSSTRPLLDFRRKVNK----CYRGRScpiIVHCSDGAGRTGTYILIDMVLnRMA 238

                         250       260       270
                  ....*....|....*....|....*....|.
gi 300795675 1401 RCHNLVDVFFAAKTLRNYKPNMVETLDQYHF 1431
Cdd:cd14609   239 KGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1203-1438 1.35e-34

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: 134.39  E-value: 1.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1203 NRDKNRSMDVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQ 1281
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSVDGVPgSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1282 sNSAWPCPQYWPEPGRQQYGLMEVEFVSGTADEDLVARVFRVQNISRMQEGHllVRHFQFLRWSAY--RDTPDSKKAFLH 1359
Cdd:cd14626   121 -KSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKRE--VRQFQFMAWPDHgvPEYPTPILAFLR 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675 1360 LLAAVDKWQAesgdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14626   198 RVKACNPPDA----GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1232-1433 1.43e-34

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: 131.80  E-value: 1.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAA-LTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLhQSNSAWPCPQYWPEPGRQQYGLMEVEFVSG 1310
Cdd:cd14546     1 YINAStIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRL-QENGVKQCARYWPEEGSEVYHIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1311 TA-DEDLVARVFRVQNIsRMQEGHlLVRHFQFLRWSAyRDTPDSKKAFLHLLAAVDKwqaeSGDGRT---IVHCLNGGGR 1386
Cdd:cd14546    80 HIwCDDYLVRSFYLKNL-QTSETR-TVTQFHFLSWPD-EGIPASAKPLLEFRRKVNK----SYRGRScpiVVHCSDGAGR 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 300795675 1387 SGTFCACATVLE-MIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCY 1433
Cdd:cd14546   153 TGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1207-1438 2.26e-34

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: 132.25  E-value: 2.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1207 NRSMDVLPPDRCLPFLVSTDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAw 1286
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1287 PCPQYWPEPGRQQYGLMEVEFVSGTADEDLVARVFRVQNISRMQEGHllVRHFQFLRWSAYR--DTPDSKKAFLHLLAav 1364
Cdd:cd14615    80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRT--VRHFHFTSWPDHGvpETTDLLINFRHLVR-- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795675 1365 DKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14615   156 EYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 943-1143 3.72e-34

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


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 131.25  E-value: 3.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNH--FIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-----EDSDMYGDIKIT 1015
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1016 L-VKTETLAeYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFI-------RRVKASTPPDAG--PVVIHC 1085
Cdd:cd14598    81 TrFRTDSGC-YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLeeiqsvrRHTNSTIDPKSPnpPVLVHC 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 300795675 1086 SAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14598   160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1207-1437 7.88e-34

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: 130.45  E-value: 7.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1207 NRSMDVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqLHQSNSA 1285
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLT-VGMENGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1286 WPCPQYWP-EPGRQQYGLMEVEFVSGTADEDLVARVFRVQNISRMQEGHllVRHFQFLRWSAYR--DTPDSKKAFLHLla 1362
Cdd:cd14618    80 VLCDHYWPsESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERR--VKHLHYTAWPDHGipESTSSLMAFREL-- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795675 1363 AVDKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVAL 1437
Cdd:cd14618   156 VREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
939-1137 8.96e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 132.14  E-value: 8.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  939 PDADYINANYIDGYhRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVG--RVKCSRYWPEDSDmYG--DIKI 1014
Cdd:COG5599    61 ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGE-YGkyEVSS 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1015 TLVKTETLAEYV-VRSFALERRGYSAR-HEVRQFHFTAWPEHGVPyHATGLLAFIRRVKAS---TPPDAGPVVIHCSAGT 1089
Cdd:COG5599   139 ELTESIQLRDGIeARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKekiKDPDKLLPVVHCRAGV 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 300795675 1090 GRTGCYIVLDVMLDM--AECEGVVDIYNCVKTL-CSRRVNMIQTEEQYIFI 1137
Cdd:COG5599   218 GRTGTLIACLALSKSinALVQITLSVEEIVIDMrTSRNGGMVQTSEQLDVL 268
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 943-1143 9.90e-34

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: 129.37  E-value: 9.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLvEVGRVkCSRYWPEDSD-MYGDIKITLVKTET 1021
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQL-CMQYWPEKTScCYGPIQVEFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1022 LAEYVVRSF-----ALERRGYSArheVRQFHFTAWPEH-GVPYHATGLLAFIRRV-KASTPPDA--GPVVIHCSAGTGRT 1092
Cdd:cd14634    79 DEDIISRIFricnmARPQDGYRI---VQHLQYIGWPAYrDTPPSKRSILKVVRRLeKWQEQYDGreGRTVVHCLNGGGRS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 300795675 1093 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14634   156 GTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1204-1433 2.41e-33

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: 129.05  E-value: 2.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1204 RDKNRSMDVLPPDRCLPFLVSTDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSN 1283
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD---NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1284 SAwPCPQYWPEPGRQQYGL----MEVEFVSGTADEDLVARVFRVQNI----SRMqeghllVRHFQFLRWSAYrDTPDSKK 1355
Cdd:cd14545    78 QI-KCAQYWPQGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLktqeTRE------VLHFHYTTWPDF-GVPESPA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1356 AFLHLLAAV-DKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNL--VDVFFAAKTLRNYKPNMVETLDQYHFC 1432
Cdd:cd14545   150 AFLNFLQKVrESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFS 229


                  .
gi 300795675 1433 Y 1433
Cdd:cd14545   230 Y 230
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 943-1143 1.57e-32

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: 125.91  E-value: 1.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGrvKCSRYWPEDSDM-YGDIKITLVKTET 1021
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWPEEGMLrYGPIQVECMSCSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1022 LAEYVVRSFAL-----ERRGYSArheVRQFHFTAWPEH-GVPYHATGLLAFIRRV---KASTPPDAGPVVIHCSAGTGRT 1092
Cdd:cd14636    79 DCDVISRIFRIcnltrPQEGYLM---VQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECDEGEGRTIIHCLNGGGRS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 300795675 1093 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14636   156 GMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1152-1438 4.71e-32

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: 127.13  E-value: 4.71e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1152 IPVSEFkATYKEMIRIDpqsNSSQLREEFQTLNsvtpPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLVSTDG-DPN 1230
Cdd:cd14625     4 IPISEL-AEHTERLKAN---DNLKLSQEYESID----PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1231 NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQsNSAWPCPQYWPEPGRQQYGLMEVEFVSG 1310
Cdd:cd14625    76 DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEE-KSRIKCDQYWPSRGTETYGMIQVTLLDT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1311 TADEDLVARVFRVQNISRMQEGHllVRHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQAESGdGRTIVHCLNGGGRSGTF 1390
Cdd:cd14625   155 IELATFCVRTFSLHKNGSSEKRE--VRQFQFTAWPDH-GVPEYPTPFLAFLRRVKTCNPPDA-GPIVVHCSAGVGRTGCF 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 300795675 1391 CACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14625   231 IVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1176-1442 4.95e-32

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: 127.45  E-value: 4.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1176 LREEFQTLNSVtpPLDVEeCSIALLPRNRDKNRSMDVLPPDRCLPFLVSTDGDPN-NYINAALTDSYTRSAAFIVTLHPL 1254
Cdd:cd14621    28 FREEFNALPAC--PIQAT-CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDsDYINASFINGYQEKNKFIAAQGPK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1255 QSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQQYGLMEVEFVSGTADEDLVARVFRVQNISRM--QEG 1332
Cdd:cd14621   105 EETVNDFWRMIWEQNTATIVMVTNLKERKEC-KCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVtnKKP 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1333 HLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQAESGdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAA 1412
Cdd:cd14621   184 QRLITQFHFTSWPDF-GVPFTPIGMLKFLKKVKNCNPQYA-GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFV 261

                         250       260       270
                  ....*....|....*....|....*....|.
gi 300795675 1413 KTLRNYKPNMVETLDQYHFCYDVALE-YLEG 1442
Cdd:cd14621   262 SRIRAQRCQMVQTDMQYVFIYQALLEhYLYG 292
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1203-1438 5.19e-32

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: 125.52  E-value: 5.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1203 NRDKNRSMDVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQ 1281
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1282 SNSAwPCPQYWPEPgRQQYGLMEVEFVSGTADEDLVARVFRVQnisrmQEGHLLVRHFQFLRWSAYRD--TPDSKKAFLH 1359
Cdd:cd14630    83 VGRV-KCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQ-----KKGYHEIREIRQFHFTSWPDhgVPCYATGLLG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675 1360 LLAAVdKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14630   156 FVRQV-KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 943-1143 1.39e-31

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: 123.48  E-value: 1.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRV-KCSRYWPEDS-DMYGDIKITLVKTE 1020
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGlQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1021 TLAEYVVRSFALER--RGYSARHEVRQFHFTAW-PEHGVPYHATGLLAFIRRV-KASTPPDAGPVVIHCSAGTGRTGCYI 1096
Cdd:cd14637    81 ADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGGRSGTYC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300795675 1097 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1211-1438 5.35e-31

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: 122.36  E-value: 5.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1211 DVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCP 1289
Cdd:cd14620     3 NILPYDHSRVILSQLDGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE-KCY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1290 QYWPEPGRQQYGLMEVEFVSGTADEDLVARVFRVQ-NISRMQEGHLLVRHFQFLRWSAYRD--TPDSKKAFLHLLAAVDK 1366
Cdd:cd14620    82 QYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQpQLPDGCKAPRLVTQLHFTSWPDFGVpfTPIGMLKFLKKVKSVNP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795675 1367 WQAesgdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14620   162 VHA----GPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1195-1442 5.97e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 123.98  E-value: 5.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1195 CSIALLPRNRDKNRSMDVLPPDRCLPFLVSTDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1274
Cdd:cd14608    17 CRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED---NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1275 MLNQLHQSNSAwPCPQYWPEPGRQQYGLMEVEFVSGTADEDL----VARVFRVQNISRMQEGHLLvrHFQFLRWSAYrDT 1350
Cdd:cd14608    94 MLNRVMEKGSL-KCAQYWPQKEEKEMIFEDTNLKLTLISEDIksyyTVRQLELENLTTQETREIL--HFHYTTWPDF-GV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1351 PDSKKAFLHLLAAVdkwqAESGD-----GRTIVHCLNGGGRSGTFC---ACATVLEMIRCHNLVDVFFAAKTLRNYKPNM 1422
Cdd:cd14608   170 PESPASFLNFLFKV----RESGSlspehGPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGL 245

                         250       260
                  ....*....|....*....|
gi 300795675 1423 VETLDQYHFCYdvaLEYLEG 1442
Cdd:cd14608   246 IQTADQLRFSY---LAVIEG 262
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 943-1143 1.06e-30

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: 120.95  E-value: 1.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKlVEVGRVkCSRYWPEDS-DMYGDIKITLVKTET 1021
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWPENGvHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1022 LAEYVVRSFAL--ERRGYSARHEVRQFHFTAWPEH-GVPYHATGLLAFIRRV-KASTPPDAGP--VVIHCSAGTGRTGCY 1095
Cdd:cd14635    79 EEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdKWQEEYNGGEgrTVVHCLNGGGRSGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 300795675 1096 IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14635   159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1232-1433 1.12e-30

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 120.40  E-value: 1.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQsNSAWPCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKE-RKEKKCSQYWPDQGCWTYGNLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNISRM--QEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAVdKWQAESGDGRTIVHCLNGGGRSGT 1389
Cdd:cd14551    80 VLVDYTTRKFCIQKVNRGigEKRVRLVTQFHFTSWPDF-GVPFTPIGMLKFLKKV-KSANPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 300795675 1390 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCY 1433
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1232-1438 1.24e-30

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: 120.54  E-value: 1.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGrQQYGLMEVEFVSGT 1311
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRV-KCSKYWPDDS-DTYGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNisRMQEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAVdKWQAESGDGRTIVHCLNGGGRSGTFC 1391
Cdd:cd14632    79 TLAEYSVRTFALER--RGYSARHEVKQFHFTSWPEH-GVPYHATGLLAFIRRV-KASTPPDAGPVVVHCSAGAGRTGCYI 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300795675 1392 ACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14632   155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1232-1434 4.79e-30

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: 118.89  E-value: 4.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAA-LTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQsNSAWPCPQYWPEPGRQQ-YGLMEVEFVS 1309
Cdd:cd18533     1 YINASyITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVE-NGREKCDQYWPSGEYEGeYGDLTVELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1310 GTADEDLVArVFRVQNISRMQEGHLLVRHFQFLRWSAYRdTPDSKKAFLHLLAAVDKW-QAESGDGRTIVHCLNGGGRSG 1388
Cdd:cd18533    80 EEENDDGGF-IVREFELSKEDGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLIKLKRELnDSASLDPPIIVHCSAGVGRTG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 300795675 1389 TFCACATVLEMI-RCHNLVD--------VFFAAKTLRNYKPNMVETLDQYHFCYD 1434
Cdd:cd18533   158 TFIALDSLLDELkRGLSDSQdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1200-1438 5.82e-30

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 120.99  E-value: 5.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1200 LPRNRDKNRSMDVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQ 1278
Cdd:cd14624    44 LEVNKPKNRYANVIAYDHSRVLLSAIEGIPgSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1279 LHQsNSAWPCPQYWPEPGRQQYGLMEVEFVSGTADEDLVARVFRVQNISRMQEGHllVRHFQFLRWSAYrDTPDSKKAFL 1358
Cdd:cd14624   124 LEE-RSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKRE--VRQFQFTAWPDH-GVPEHPTPFL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1359 HLLAAVDKWQAESGdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14624   200 AFLRRVKTCNPPDA-GPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1197-1433 7.29e-30

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: 120.07  E-value: 7.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1197 IALLPRNRDKNRSMDVLPPDRCLPFLVSTDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML 1276
Cdd:cd14607    18 VAKYPENRNRNRYRDVSPYDHSRVKLQNTE---NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1277 NQLHQSNSAwPCPQYWPEPGRQQYGLMEVEFVSGTADEDL----VARVFRVQNI----SRMqeghllVRHFQFLRWSAYr 1348
Cdd:cd14607    95 NRIVEKDSV-KCAQYWPTDEEEVLSFKETGFSVKLLSEDVksyyTVHLLQLENInsgeTRT------ISHFHYTTWPDF- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1349 DTPDSKKAFLHLLAAVdkwqAESG-----DGRTIVHCLNGGGRSGTFCACATVLEMIRCHN--LVDVFFAAKTLRNYKPN 1421
Cdd:cd14607   167 GVPESPASFLNFLFKV----RESGslspeHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMG 242

                         250
                  ....*....|..
gi 300795675 1422 MVETLDQYHFCY 1433
Cdd:cd14607   243 LIQTPDQLRFSY 254
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1232-1438 1.21e-29

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: 117.71  E-value: 1.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEpGRQQYGLMEVEFVSGT 1311
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRV-KCSRYWPD-DTEVYGDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQN--ISRMQEghllVRHFQFLRWSAYrDTPDSKKAFLHLLAAVdKWQAESGDGRTIVHCLNGGGRSGT 1389
Cdd:cd14555    79 PLAEYVVRTFALERrgYHEIRE----VRQFHFTGWPDH-GVPYHATGLLGFIRRV-KASNPPSAGPIVVHCSAGAGRTGC 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1390 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14555   153 YIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1232-1433 1.48e-29

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 117.57  E-value: 1.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAAL--TDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAWPCPQYWPEPGRQQ--YGLMEVEF 1307
Cdd:cd17658     1 YINASLveTPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAKCADYFPAEENESreFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1308 VS-GTADEDLVARVFRVQNIsRMQEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAVdkWQAESGDGRTIVHCLNGGGR 1386
Cdd:cd17658    81 KKlKHSQHSITLRVLEVQYI-ESEEPPLSVLHIQYPEWPDH-GVPKDTRSVRELLKRL--YGIPPSAGPIVVHCSAGIGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1387 SGTFCACATVLEMIRCHNL--VDVFFAAKTLRNYKPNMVETLDQYHFCY 1433
Cdd:cd17658   157 TGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1232-1437 5.00e-29

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: 115.86  E-value: 5.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHqsNSAWPCPQYWP---EPGRQQ---YGLMEV 1305
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQ--NMAEDEFVYWPnkdEPINCEtfkVTLIAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1306 EFVSGTADEDLVARVFRVQnisRMQEGHLL-VRHFQFLRWSayrdTPDSKKAFLHLLAAVDKWQAESGDGRTIVHCLNGG 1384
Cdd:cd17669    79 EHKCLSNEEKLIIQDFILE---ATQDDYVLeVRHFQCPKWP----NPDSPISKTFELISIIKEEAANRDGPMIVHDEHGG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1385 GRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVAL 1437
Cdd:cd17669   152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 910-1141 1.12e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 118.59  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  910 KKDKVKGGRQEPMPAYDRHRVKLHPM-------LGDPD------------ADYINANYIDGYHRSNHFIATQGPKPEMVY 970
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINAHeslkmfdVGDSDgkkievtsednaENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  971 DFWRMVWQEHCSSIVMITKlVEVGRVKCSRYW--PEDSDM-YGDIKITLVKTETLAEYVVRSFALERRGYSARHEVRQFH 1047
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELaFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1048 FTAWPEHGVPYHATGLLAFIRRVKA----------STPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCV 1117
Cdd:PHA02746  207 FPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIV 286

                         250       260
                  ....*....|....*....|....
gi 300795675 1118 KTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:PHA02746  287 LKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1190-1435 3.12e-28

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: 115.34  E-value: 3.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1190 LDVEECSIALLPRnrdKNRSMDVLPPDRCLPFLVSTD-GDP-NNYINAALTDSY-TRSAAFIVTLHPLQSTTPDFWRLVY 1266
Cdd:cd14613    15 VDPKEYDIPGLVR---KNRYKTILPNPHSRVCLTSPDqDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVW 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1267 DYGCTSIVMLNQLHQSNSAwpCPQYWPEPgRQQYGLMEVEFVSGTADEDLVARVFRVQniSRMQEGHLlvRHFQFLRWSA 1346
Cdd:cd14613    92 QERSPIIVMITNIEEMNEK--CTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITLK--SGGEERGL--KHYWYTSWPD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1347 YRdTPDSKKAFLHLLAAVD--KWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVE 1424
Cdd:cd14613   165 QK-TPDNAPPLLQLVQEVEeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQ 243

                         250
                  ....*....|.
gi 300795675 1425 TLDQYHFCYDV 1435
Cdd:cd14613   244 TCEQYQFVHHV 254
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1207-1431 4.42e-28

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: 113.65  E-value: 4.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1207 NRSMDVLPPDRCLPFLVSTDGDP-NNYINAaltdSYTR-----SAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLH 1280
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPlSSYINA----NYIRgydgeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1281 QSNSAwpCPQYWPEPGRQQYGLMEVEFVSGTADEDlvarvFRVQNISRMQEGHLL-VRHFQFLRWSAYRdTPDSKKAFLH 1359
Cdd:cd14547    77 EAKEK--CAQYWPEEENETYGDFEVTVQSVKETDG-----YTVRKLTLKYGGEKRyLKHYWYTSWPDHK-TPEAAQPLLS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1360 LLAAVDKW-QAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHF 1431
Cdd:cd14547   149 LVQEVEEArQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1232-1437 8.46e-28

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 112.46  E-value: 8.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML--NQ-LHQSNSAwpcpqYWPEpgRQQ--------Y 1300
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQgLAEDEFV-----YWPS--REEsmnceaftV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1301 GLMEVEFVSGTADEDLVARVFRVQnisRMQEGHLL-VRHFQFLRWSayrdTPDSKKAFLHLLAAVDKWQAESGDGRTIVH 1379
Cdd:cd17670    74 TLISKDRLCLSNEEQIIIHDFILE---ATQDDYVLeVRHFQCPKWP----NPDAPISSTFELINVIKEEALTRDGPTIVH 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 300795675 1380 CLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVAL 1437
Cdd:cd17670   147 DEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1232-1434 8.78e-28

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: 112.09  E-value: 8.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAA-FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLnQLHQSNSAWPCPQYWPEPGRQQ--YGLMEVEFV 1308
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVML-VSEQENEKQKVHRYWPTERGQAlvYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1309 SGTADEDLVARVFRVQNisRMQEGHLLVRHFQFLRWSAYRdTPDSKKAFLHLLAAVDKW--QAESGDGRTIVHCLNGGGR 1386
Cdd:cd14539    80 SVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHylQQRSLQTPIVVHCSSGVGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300795675 1387 SGTFCAC-ATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYD 1434
Cdd:cd14539   157 TGAFCLLyAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 943-1142 8.98e-28

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 112.39  E-value: 8.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSrYWP-EDSDMYGD-IKITLVKTE 1020
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPnKDEPINCEtFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1021 TLA-----EYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCY 1095
Cdd:cd17669    80 HKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTAGTF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300795675 1096 IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd17669   158 CALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1207-1433 1.21e-27

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: 112.70  E-value: 1.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1207 NRSMDVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSA 1285
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1286 wPCPQYWP-EPGRQQYGLMEVEFVSGTADEDLVARVFRVQNISRMqEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAV 1364
Cdd:cd14617    81 -KCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQL-DAPRLVRHFHYTVWPDH-GVPETTQSLIQFVRTV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1365 -DKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCY 1433
Cdd:cd14617   158 rDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1207-1440 1.35e-27

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: 112.67  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1207 NRSMDVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQsNSA 1285
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPgSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME-AGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1286 WPCPQYWP-EPGRQQYGLMEVEFVSGTADEDLVARVFRVQNIsrMQEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAV 1364
Cdd:cd14619    80 VKCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQV--EEQKTLSVRHFHFTAWPDH-GVPSSTDTLLAFRRLL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300795675 1365 DKW--QAESGdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALEYL 1440
Cdd:cd14619   157 RQWldQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1201-1438 2.52e-27

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 113.21  E-value: 2.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1201 PRNRDKNRSMDVLPPDRC---LPFLVSTDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1277
Cdd:cd17667    25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1278 QLHQSNSAwPCPQYWPEPGRQQYGLMEVEFVSGTADEDLVARVFRVQN--ISRMQEGHLLVRH-------FQFLRWsayr 1348
Cdd:cd17667   105 NLVEKGRR-KCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkVKKGQKGNPKGRQnertviqYHYTQW---- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1349 dtPDS--KKAFLHLLAAVDKWQAE--SGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVE 1424
Cdd:cd17667   180 --PDMgvPEYALPVLTFVRRSSAArtPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQ 257

                         250
                  ....*....|....
gi 300795675 1425 TLDQYHFCYDVALE 1438
Cdd:cd17667   258 TEEQYIFIHDALLE 271
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 943-1142 2.69e-27

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 110.92  E-value: 2.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  943 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITK---LVEVGRVkcsrYWP--EDSDMYGDIKITLV 1017
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAEDEFV----YWPsrEESMNCEAFTVTLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1018 KTETLA-----EYVVRSFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPVVIHCSAGTGRT 1092
Cdd:cd17670    77 SKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEFGAVSA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 300795675 1093 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd17670   155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1201-1433 4.30e-27

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: 112.23  E-value: 4.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1201 PRNRDKNRSMDVLPPDR---CLPFLVSTDGdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1277
Cdd:cd14603    28 KENVKKNRYKDILPYDQtrvILSLLQEEGH--SDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMAC 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1278 QlHQSNSAWPCPQYWP-EPGRQQYGLMEVEFVSGT-ADEDLVARVFRV--QNISRMqeghllVRHFQFLRWSAyRDTPDS 1353
Cdd:cd14603   106 R-EIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKVtfQKESRS------VSHFQYMAWPD-HGIPDS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1354 KKAFLHLLAAVDKWQAESGDgRTIVHCLNGGGRSGTFCACATV-----LEMIRCHnlVDVFFAAKTLRNYKPNMVETLDQ 1428
Cdd:cd14603   178 PDCMLAMIELARRLQGSGPE-PLCVHCSAGCGRTGVICTVDYVrqlllTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQ 254


                  ....*
gi 300795675 1429 YHFCY 1433
Cdd:cd14603   255 YEFLY 259
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1203-1441 6.91e-27

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: 111.26  E-value: 6.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1203 NRDKNRSMDVLPPDRCLpfLVSTDGDPN----NYINA--ALTDSYTRS------AAFIVTLHPLQSTTPDFWRLVYDYGC 1270
Cdd:cd14605     2 NKNKNRYKNILPFDHTR--VVLHDGDPNepvsDYINAniIMPEFETKCnnskpkKSYIATQGCLQNTVNDFWRMVFQENS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1271 TSIVMLNQLHQSNSAwPCPQYWP-EPGRQQYGLMEVEFVSGTADEDLVARVFRvqnISRMQEGHL--LVRHFQFLRWSAY 1347
Cdd:cd14605    80 RVIVMTTKEVERGKS-KCVKYWPdEYALKEYGVMRVRNVKESAAHDYILRELK---LSKVGQGNTerTVWQYHFRTWPDH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1348 rDTPDSKKAFLHLLAAVD-KWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNL---VDVFFAAKTLRNYKPNMV 1423
Cdd:cd14605   156 -GVPSDPGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMV 234

                         250
                  ....*....|....*...
gi 300795675 1424 ETLDQYHFCYDVALEYLE 1441
Cdd:cd14605   235 QTEAQYRFIYMAVQHYIE 252
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1203-1441 6.97e-27

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: 111.02  E-value: 6.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1203 NRDKNRSMDVLPPDRCLPFLvsTDGDPN----NYINAaltdSYTRSAA-----------FIVTLHPLQSTTPDFWRLVYD 1267
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVIL--KDRDPNvpgsDYINA----NYIRNENegpttdenaktYIATQGCLENTVSDFWSMVWQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1268 YGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQ-QYGLMEVEFVSGTADEDLVARVFrvqNISRMQEGHLL--VRHFQFLRW 1344
Cdd:cd14544    75 ENSRVIVMTTKEVERGKN-KCVRYWPDEGMQkQYGPYRVQNVSEHDTTDYTLREL---QVSKLDQGDPIreIWHYQYLSW 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1345 SAYrDTPDSKKAFLHLLAAVDKWQAESGD-GRTIVHCLNGGGRSGTFCACATVLEMIRCHNL---VDVFFAAKTLRNYKP 1420
Cdd:cd14544   151 PDH-GVPSDPGGVLNFLEDVNQRQESLPHaGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRS 229

                         250       260
                  ....*....|....*....|.
gi 300795675 1421 NMVETLDQYHFCYDVALEYLE 1441
Cdd:cd14544   230 GMVQTEAQYKFIYVAVAQYIE 250
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1207-1431 1.70e-26

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: 109.23  E-value: 1.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1207 NRSMDVLPPDRCLPFLVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSA 1285
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1286 wPCPQYWPEPGR--QQYGLMEVEFVSGTADEDLVARVFRVQnisrmQEGH-LLVRHFQFLRWSAYrDTPDSKKAFLHLLA 1362
Cdd:cd14616    81 -RCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKIE-----RHGDyMMVRQCNFTSWPEH-GVPESSAPLIHFVK 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675 1363 AVDKWQAESgDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHF 1431
Cdd:cd14616   154 LVRASRAHD-NTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1232-1440 3.68e-26

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: 107.85  E-value: 3.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAaltdSYTR------SAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQQ---YGL 1302
Cdd:cd14538     1 YINA----SHIRipvggdTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKV-KCHRYWPDSLNKPlicGGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1303 MEVEFVSGTADEDLVARVFRVQNISRMQEGHllVRHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQAesgDGRTIVHCLN 1382
Cdd:cd14538    76 LEVSLEKYQSLQDFVIRRISLRDKETGEVHH--ITHLNFTTWPDH-GTPQSADPLLRFIRYMRRIHN---SGPIVVHCSA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675 1383 GGGRSGTFCACATVLEMIRcHNL-VDVFFAAKTLRNYKPNMVETLDQYHFCYDVALEYL 1440
Cdd:cd14538   150 GIGRTGVLITIDVALGLIE-RDLpFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1203-1438 5.62e-26

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: 109.36  E-value: 5.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1203 NRDKNRSMDVLPPDRCLPFLVSTDGDPN-NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQ 1281
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETSsDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1282 SNSAwPCPQYWPEpGRQQYGLMEVEFVSGTADEDLVARVFRVQN--ISRMQEghllVRHFQFLRWSAYrDTPDSKKAFLH 1359
Cdd:cd14633   120 VGRV-KCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFAVEKrgVHEIRE----IRQFHFTGWPDH-GVPYHATGLLG 192

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675 1360 LLAAVdKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14633   193 FVRQV-KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1200-1433 8.69e-26

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: 108.00  E-value: 8.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1200 LPRNRDKNRSMDVLP-PDR--CLPFLVSTDgDPNNYINAALTDSYT-RSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVM 1275
Cdd:cd14612    12 IPGHASKDRYKTILPnPQSrvCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1276 LNQLHQSNSAwpCPQYWPEPgRQQYGLMEVEFVSGTADEDLVARVFRVQnisrMQEGHLLVRHFQFLRWSAYRdTPDSKK 1355
Cdd:cd14612    91 ITKLKEKKEK--CVHYWPEK-EGTYGRFEIRVQDMKECDGYTIRDLTIQ----LEEESRSVKHYWFSSWPDHQ-TPESAG 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795675 1356 AFLHLLAAVDKW-QAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCY 1433
Cdd:cd14612   163 PLLRLVAEVEESrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1232-1431 9.97e-26

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: 106.64  E-value: 9.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAA----FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPG-RQQYGLMEVE 1306
Cdd:cd14541     2 YINANYVNMEIPGSGivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRV-KCHQYWPDLGeTMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1307 FVSGTADEDLVARVFRVQNISRMQEGHllVRHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQAESGDgRTIVHCLNGGGR 1386
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERH--ITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRVGMVE-PTVVHCSAGIGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795675 1387 SGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHF 1431
Cdd:cd14541   157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1232-1434 2.82e-25

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: 105.06  E-value: 2.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPADGSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1312 ADEDLVARVFRVQNiSRMQEG-------HLLVRHFQFLRWsayrdtPDS--KKAFLHLLAAVDKWQA--ESGDGRTIVHC 1380
Cdd:cd17668    80 VLAYYTVRNFTLRN-TKIKKGsqkgrpsGRVVTQYHYTQW------PDMgvPEYTLPVLTFVRKASYakRHAVGPVVVHC 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300795675 1381 LNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYD 1434
Cdd:cd17668   153 SAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1222-1438 3.48e-25

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: 105.10  E-value: 3.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1222 LVSTDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGrQQY 1300
Cdd:cd14631     4 LQPVEDDPsSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRV-KCYKYWPDDT-EVY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1301 GLMEVEFVSGTADEDLVARVFRVQ--NISRMQEghllVRHFQFLRWSAYrDTPDSKKAFLHLLAAVdKWQAESGDGRTIV 1378
Cdd:cd14631    82 GDFKVTCVEMEPLAEYVVRTFTLErrGYNEIRE----VKQFHFTGWPDH-GVPYHATGLLSFIRRV-KLSNPPSAGPIVV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1379 HCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:cd14631   156 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1206-1433 3.63e-25

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: 105.39  E-value: 3.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1206 KNRSMDVLPPDRCLPFLVSTDGDP--NNYINAALTDSYT-RSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQS 1282
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDslSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1283 NSAwpCPQYWPEPgRQQYGLMEVEFVSGTADEDLVARVFRVQNISRMQEghllVRHFQFLRWSAYRdTPDSKKAFLHLLA 1362
Cdd:cd14611    82 NEK--CVLYWPEK-RGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRS----VKHYWYTSWPDHK-TPDSAQPLLQLML 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795675 1363 AVDKWQAES-GDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCY 1433
Cdd:cd14611   154 DVEEDRLASpGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1203-1440 1.01e-24

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: 104.53  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1203 NRDKNRSMDVLPPDRCLPFLvstdGDPNNYINAALTDSYTRSAAF--IVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLH 1280
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1281 QSNSAwPCPQYWPEPGRQQYGL---MEVEFVSGTADEDLVARVFRVQNISRMQEGHllVRHFQFLRWSAYrDTPDSKKAF 1357
Cdd:cd14597    79 EGGKI-KCQRYWPEILGKTTMVdnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRH--ITHLNFTAWPDH-DTPSQPEQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1358 LHLLAAVDKWQAEsgdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVAL 1437
Cdd:cd14597   155 LTFISYMRHIHKS---GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231


                  ...
gi 300795675 1438 EYL 1440
Cdd:cd14597   232 YVL 234
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1232-1441 1.08e-24

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: 103.29  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAaltdSYTRSAA------FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGRQQYGL--M 1303
Cdd:cd14596     1 YINA----SYITMPVgeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKV-KCHRYWPETLQEPMELenY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1304 EVEFVSGTADEDLVARVFRVQNiSRMQEGHLlVRHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQAEsgdGRTIVHCLNG 1383
Cdd:cd14596    76 QLRLENYQALQYFIIRIIKLVE-KETGENRL-IKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT---GPIVVHCSAG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795675 1384 GGRSGTFCACATVLEMIR---CHNLVDVffaAKTLRNYKPNMVETLDQYHFCYDVALEYLE 1441
Cdd:cd14596   150 IGRAGVLICVDVLLSLIEkdlSFNIKDI---VREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1201-1440 1.48e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 103.16  E-value: 1.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1201 PRNRDKNRSMDVLPPDRCLPFLVSTDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLH 1280
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1281 QSNSAWPCPQYW--PEPGRQQYGLMEVEFVSGTADEDLVARVFRVQNISRMQEGHLlvRHFQFLRWSAYrDTPDSKKAFL 1358
Cdd:PHA02747  129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI--SHFQCSEWFED-ETPSDHPDFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1359 HLLAAVDKWQAESGDGRT---------IVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQY 1429
Cdd:PHA02747  206 KFIKIIDINRKKSGKLFNpkdallcpiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                         250
                  ....*....|....
gi 300795675 1430 HF---CYDVALEYL 1440
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1164-1431 2.21e-23

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: 101.47  E-value: 2.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1164 MIRIDPQSNSSQLREEFQTLNSVTPPLDVeecSIALLPRNRDKNRSMDVLPPDRCLpflVSTDGDpNNYINAALTDSYTR 1243
Cdd:cd14600     4 MAQLKKGLESGTVLIQFEQLYRKKPGLAI---TCAKLPQNMDKNRYKDVLPYDATR---VVLQGN-EDYINASYVNMEIP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1244 SAA----FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEPGR-QQYGLMEVEFVSgtadEDL-V 1317
Cdd:cd14600    77 SANivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRT-KCHQYWPDPPDvMEYGGFRVQCHS----EDCtI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1318 ARVFRVQNISRMQEG-HLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQAESGDgrTIVHCLNGGGRSGTFCACATV 1396
Cdd:cd14600   152 AYVFREMLLTNTQTGeERTVTHLQYVAWPDH-GVPDDSSDFLEFVNYVRSKRVENEP--VLVHCSAGIGRTGVLVTMETA 228

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 300795675 1397 LEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHF 1431
Cdd:cd14600   229 MCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKF 263
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1336-1438 2.88e-23

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 95.89  E-value: 2.88e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1336 VRHFQFLRWSAyRDTPDSKKAFLHLLAAVDKWQ-AESGDGRTIVHCLNGGGRSGTFCACATVLEMIR-CHNLVDVFFAAK 1413
Cdd:smart00404    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 300795675   1414 TLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1336-1438 2.88e-23

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: 95.89  E-value: 2.88e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   1336 VRHFQFLRWSAyRDTPDSKKAFLHLLAAVDKWQ-AESGDGRTIVHCLNGGGRSGTFCACATVLEMIR-CHNLVDVFFAAK 1413
Cdd:smart00012    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 300795675   1414 TLRNYKPNMVETLDQYHFCYDVALE 1438
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1232-1429 8.61e-23

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: 97.59  E-value: 8.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEP--GRQQYGLMEVEFVS 1309
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRN-KCAQYWPSMeeGSRAFGDVVVKINE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1310 GTADEDLVARVFRVQNiSRMQEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQaESGDGRTIVHCLNGGGRSGT 1389
Cdd:cd14557    80 EKICPDYIIRKLNINN-KKEKGSGREVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN-NFFSGPIVVHCSAGVGRTGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 300795675 1390 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQY 1429
Cdd:cd14557   157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1231-1440 9.33e-23

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: 98.30  E-value: 9.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1231 NYINAALTDSYTRsaaFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlHQSNSAWPCPQYWP----EPGRQQYGLMEVE 1306
Cdd:cd14540     5 SHITATVGGKQRF---YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTA-EEEGGREKCFRYWPtlggEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1307 FVSGTADEDLVARVFRVQNISRMQegHLLVRHFQFLRWsAYRDTPDSKKAFLHLLAAVDK-----WQAESGDGR---TIV 1378
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQ--SRTVWHLQYTDW-PDHGCPEDVSGFLDFLEEINSvrrhtNQDVAGHNRnppTLV 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795675 1379 HCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALEYL 1440
Cdd:cd14540   158 HCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1232-1433 1.78e-22

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: 96.72  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlHQSNSAWPCPQYWPEPGRQ--QYGLMEVEFVS 1309
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACR-EFEMGKKKCERYWPEEGEEqlQFGPFKISLEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1310 GTA-DEDLVARVFRVQnisRMQEGHlLVRHFQFLRWSAyRDTPDSKKAFLHLLAAVDKWQaESGDGRTIVHCLNGGGRSG 1388
Cdd:cd14542    80 EKRvGPDFLIRTLKVT---FQKESR-TVYQFHYTAWPD-HGVPSSVDPILDLVRLVRDYQ-GSEDVPICVHCSAGCGRTG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 300795675 1389 TFCACATVLEMIRCHNLVD---VFFAAKTLRNYKPNMVETLDQYHFCY 1433
Cdd:cd14542   154 TICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1201-1441 3.30e-21

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: 94.95  E-value: 3.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1201 PRNRDKNRSMDVLPPDRCLPFLvsTDGDPN---------NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCT 1271
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVIL--QGRDSNipgsdyinaNYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1272 SIVMLNQLHQSNSAwPCPQYWPEPGRQ-QYGLMEVEFVSGTADEDLVARVFRVQNISRmQEGHLLVRHFQFLRWSAYrDT 1350
Cdd:cd14606    94 VIVMTTREVEKGRN-KCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLDN-GELIREIWHYQYLSWPDH-GV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1351 PDSKKAFLHLLAAVDKWQAE-SGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNL---VDVFFAAKTLRNYKPNMVETL 1426
Cdd:cd14606   171 PSEPGGVLSFLDQINQRQESlPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTE 250

                         250
                  ....*....|....*
gi 300795675 1427 DQYHFCYDVALEYLE 1441
Cdd:cd14606   251 AQYKFIYVAIAQFIE 265
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1231-1441 6.44e-21

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: 92.70  E-value: 6.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1231 NYINAALTDSyTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwPCPQYWPEP-GRQQYGLMEVEFVS 1309
Cdd:cd14601     6 NYINMEIPSS-SIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRV-KCHQYWPEPsGSSSYGGFQVTCHS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1310 GTADEDLVARVFRVQNISRMQEGHLLvrHFQFLRWSAYrDTPDSKKAFLHLLAAVDKWQAeSGDGRTIVHCLNGGGRSGT 1389
Cdd:cd14601    84 EEGNPAYVFREMTLTNLEKNESRPLT--QIQYIAWPDH-GVPDDSSDFLDFVCLVRNKRA-GKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300795675 1390 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALEYLE 1441
Cdd:cd14601   160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1206-1438 8.50e-21

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: 92.98  E-value: 8.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1206 KNRSMDVLPPDRC---LPFLVS-TDGDpnnYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQ 1281
Cdd:cd14602     1 KNRYKDILPYDHSrveLSLITSdEDSD---YINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1282 SNSAwPCPQYWPEPGRQ--QYGLMEVEFVSGTADEDLVARVFRVQnisrMQEGHLLVRHFQFLRWSAYrDTPDSKKAFLH 1359
Cdd:cd14602    78 MGKK-KCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIRTLKVK----FNSETRTIYQFHYKNWPDH-DVPSSIDPILE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1360 LLAAVDKWQAEsgDGRTI-VHCLNGGGRSGTFCACATVLEMIRcHNLVDVFFAAKTL----RNYKPNMVETLDQYHFCYD 1434
Cdd:cd14602   152 LIWDVRCYQED--DSVPIcIHCSAGCGRTGVICAIDYTWMLLK-DGIIPENFSVFSLiqemRTQRPSLVQTKEQYELVYN 228


                  ....
gi 300795675 1435 VALE 1438
Cdd:cd14602   229 AVIE 232
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1196-1441 3.29e-20

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 92.75  E-value: 3.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1196 SIALLPRNRDKNRSMDVLPPDRCLPFLVSTDGDPNNYINAALTDSYTRSAA--FIVTLHPLQSTTPDFWRLVYDYGCTSI 1273
Cdd:cd14599    31 TTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1274 VMLNQLHQSNSAwPCPQYWPEPGRQQYglmevefvSGTADEDLVARVFRVQNISRMQEG----HLL------VRHFQFLR 1343
Cdd:cd14599   111 AMVTAEEEGGRS-KSHRYWPKLGSKHS--------SATYGKFKVTTKFRTDSGCYATTGlkvkHLLsgqertVWHLQYTD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1344 WSAYrDTPDSKKAFLHLLA---AVDKWQAESGDGRT------IVHCLNGGGRSGTFCACATvleMIRC--HN-LVDVFFA 1411
Cdd:cd14599   182 WPDH-GCPEEVQGFLSYLEeiqSVRRHTNSMLDSTKncnppiVVHCSAGVGRTGVVILTEL---MIGCleHNeKVEVPVM 257

                         250       260       270
                  ....*....|....*....|....*....|
gi 300795675 1412 AKTLRNYKPNMVETLDQYHFCYDVALEYLE 1441
Cdd:cd14599   258 LRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1204-1439 3.83e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 93.17  E-value: 3.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1204 RDKNRSMDVLPPDRCLPFLVSTDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSN 1283
Cdd:PHA02746   73 HESLKMFDVGDSDGKKIEVTSEDNA-ENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDD 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1284 SAwpCPQYWPEPgrQQYGLMEVEFVSGTAD--EDLVARVFRVQNISRMQEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLL 1361
Cdd:PHA02746  152 EK--CFELWTKE--EDSELAFGRFVAKILDiiEELSFTKTRLMITDKISDTSREIHHFWFPDWPDN-GIPTGMAEFLELI 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1362 AAVDKWQAE---------SGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFC 1432
Cdd:PHA02746  227 NKVNEEQAElikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFC 306


                  ....*..
gi 300795675 1433 YdVALEY 1439
Cdd:PHA02746  307 Y-KALKY 312
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1195-1439 8.63e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 88.91  E-value: 8.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1195 CSIALLPRNRDKNRSMDVLPPDRCLPFLVSTDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1274
Cdd:PHA02742   44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDGG-DDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1275 MLNQLHQSNSAwPCPQYW--PEPGRQQYGLMEVefvsgtadEDLVARVFRVQNISRMQ-----EGHLL-VRHFQFLRWSa 1346
Cdd:PHA02742  123 MITKIMEDGKE-ACYPYWmpHERGKATHGEFKI--------KTKKIKSFRNYAVTNLCltdtnTGASLdIKHFAYEDWP- 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1347 YRDTPDSKKAFLHLLAAVDKWQAE-----SGDGRT-----IVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLR 1416
Cdd:PHA02742  193 HGGLPRDPNKFLDFVLAVREADLKadvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLR 272

                         250       260
                  ....*....|....*....|...
gi 300795675 1417 NYKPNMVETLDQYHFCYDVALEY 1439
Cdd:PHA02742  273 KQRHNCLSLPQQYIFCYFIVLIF 295
PHA02738 PHA02738
hypothetical protein; Provisional
 1202-1441 3.19e-18

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 87.67  E-value: 3.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1202 RNRDKNRSMDVLPPDRCLPFLvSTDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlHQ 1281
Cdd:PHA02738   48 KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK-KK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1282 SNSAWPCPQYWP--EPGRQQYGLMEVEFVSGTADEDLVARVFRVQN-ISRMQEghllVRHFQFLRWSAYrDTPDSKKAFL 1358
Cdd:PHA02738  126 ENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDgTSATQT----VTHFNFTAWPDH-DVPKNTSEFL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1359 HLLAAVDKWQAE-------SGDGRT-----IVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETL 1426
Cdd:PHA02738  201 NFVLEVRQCQKElaqeslqIGHNRLqpppiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIP 280

                         250
                  ....*....|....*
gi 300795675 1427 DQYHFCYDVALEYLE 1441
Cdd:PHA02738  281 FQYFFCYRAVKRYVN 295
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1203-1429 9.40e-18

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: 85.75  E-value: 9.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1203 NRDKNRSMDVLPPDRC-LPFLVSTDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQ 1281
Cdd:cd14604    57 NVKKNRYKDILPFDHSrVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1282 SNSAwPCPQYWPEPGRQ--QYGLMEVEFVSGTADEDLVARVFRV--QNISRMqeghllVRHFQFLRWSAYrDTPDSKKAF 1357
Cdd:cd14604   137 MGRK-KCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLLefQNETRR------LYQFHYVNWPDH-DVPSSFDSI 208

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795675 1358 LHLLAAVDKWQaESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNL---VDVFFAAKTLRNYKPNMVETLDQY 1429
Cdd:cd14604   209 LDMISLMRKYQ-EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 282
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1232-1441 2.02e-15

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: 76.94  E-value: 2.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1232 YINAALTDSYTRSAA--FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqLHQSNSAWPCPQYWPEPGRQQ----YGLMEV 1305
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVT-AEEEGGREKSFRYWPRLGSRHntvtYGRFKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1306 EFVSGTADEDLVARVFRVQNISRMQEghLLVRHFQFLRWSAYrDTPDSKKAFLHLL---AAVDKWQAESGDGRT-----I 1377
Cdd:cd14598    80 TTRFRTDSGCYATTGLKIKHLLTGQE--RTVWHLQYTDWPEH-GCPEDLKGFLSYLeeiQSVRRHTNSTIDPKSpnppvL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795675 1378 VHCLNGGGRSGTFCACATvleMIRC--HN-LVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALEYLE 1441
Cdd:cd14598   157 VHCSAGVGRTGVVILSEI---MIACleHNeMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 939-1134 1.52e-14

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 74.74  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  939 PDADYINANY--IDGYHRsnhFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDmYGdiKITL 1016
Cdd:cd14559    13 PVGKNLNANRvqIGNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGT-YG--SVTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1017 VKTETLAEYVVRSFA-----LERRGYSARHEVRQFHFTAWPEHG-VPYHATGLLAfiRRVKAST---------------- 1074
Cdd:cd14559    87 KSKKTGKDELVDGLKadmynLKITDGNKTITIPVVHVTNWPDHTaISSEGLKELA--DLVNKSAeekrnfykskgssain 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1075 PPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTlcSRRVNMIQTEEQY 1134
Cdd:cd14559   165 DKNKLLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVSDMRT--SRNGKMVQKDEQL 222
fn3 pfam00041
Fibronectin type III domain;
494-577 3.01e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 3.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   494 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSVESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTG 572
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*
gi 300795675   573 KGFGQ 577
Cdd:pfam00041   79 GGEGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 484-585 1.18e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.91  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  484 DVPGGIAAESLTftplEDMIFLKWEEPQEPNGLITQYEISYQSVESSDPA-VNVPGPrrtisklrNETYHVFSNLHPGTT 562
Cdd:cd00063     2 SPPTNLRVTDVT----STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeVEVTPG--------SETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....
gi 300795675  563 YLFSVRARTGKGFGQAA-LTEITT 585
Cdd:cd00063    70 YEFRVRAVNGGGESPPSeSVTVTT 93
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 921-1141 2.43e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 69.61  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  921 PMPAYDRHRVKLHPmlgdpDADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEvgrVKC-S 999
Cdd:PHA02740   61 HITRLLHRRIKLFN-----DEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD---KKCfN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1000 RYWPEDSD---MYGDIKITLVKTETLAEYVVRSFALERRGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---- 1072
Cdd:PHA02740  133 QFWSLKEGcviTSDKFQIETLEIIIKPHFNLTLLSLTDKFGQAQ-KISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcad 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1073 ----STPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:PHA02740  212 lekhKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
347-624 2.41e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 68.11  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  347 LDPDTEYEISVLLTrpGDGGTGRPGPPlVSRTKCAEPMRAPKGLAFAEIQARQLTLQWEP------LGYNVTRCHTYSVS 420
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRVYRSNSGDGP 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  421 LCyhyTLGSSHNqtvrecvkmergvSRYTIKNLLPYRNVHVRLVLTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 498
Cdd:COG3401   276 FT---KVATVTT-------------TSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  499 LEDM-IFLKWEEPQEPNglITQYEIsYQSVESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTGKGfgq 577
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 300795675  578 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 624
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 486-576 2.47e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.39  E-value: 2.47e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    486 PGGIAAESLTftplEDMIFLKWEEPQEPNGL--ITQYEISYQSVESSDPAVNVPGprrtisklrNETYHVFSNLHPGTTY 563
Cdd:smart00060    4 PSNLRVTDVT----STSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTP---------SSTSYTLTGLKPGTEY 70

                            90
                    ....*....|...
gi 300795675    564 LFSVRARTGKGFG 576
Cdd:smart00060   71 EFRVRAVNGAGEG 83
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1233-1441 1.74e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 54.59  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1233 INAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLHQSNSAwpcPQYWpepgrqqyglmevefvSGTA 1312
Cdd:PHA02740   79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCF---NQFW----------------SLKE 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1313 DEDLVARVFRVQNISRMQEGH----LLV-----------RHFQFLRWSA--YRDTPDskkAFLHLLAAVD-------KWQ 1368
Cdd:PHA02740  140 GCVITSDKFQIETLEIIIKPHfnltLLSltdkfgqaqkiSHFQYTAWPAdgFSHDPD---AFIDFFCNIDdlcadleKHK 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1369 AESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETLDQYHFCYDVALEYLE 1441
Cdd:PHA02740  217 ADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1039-1139 2.05e-07

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: 53.12  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1039 ARHEVRQFHFtAWPEHGVPyhATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTG----CYIVLdvMLDMAECEgvvdiy 1114
Cdd:cd14506    73 MRAGIYFYNF-GWKDYGVP--SLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGvliaCYLVY--ALRMSADQ------ 141

                          90       100
                  ....*....|....*....|....*
gi 300795675 1115 nCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14506   142 -AIRLVRSKRPNSIQTRGQVLCVRE 165
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 386-481 2.95e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675  386 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYSVSLCyhytlgSSHNQTVRECVKMERGVSRYTIKNLLPYRNVHVRLVL 465
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR------EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*..
gi 300795675  466 TNPEGR-KEGKEVTFQT 481
Cdd:cd00063    77 VNGGGEsPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
291-365 3.65e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   291 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---SLQTYKLWHLDPDTEYEISVlLTRPGD 364
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 300795675   365 G 365
Cdd:pfam00041   80 G 80
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1322-1434 8.06e-06

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 46.19  E-value: 8.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1322 RVQNISRMQEGHLLVR-HFQFLRWSAYRD----TPDSKKAFLHLLAavdkwQAESGDGRTIVHCLNGGGRSGTFCACATV 1396
Cdd:cd14494     5 DPLRLIAGALPLSPLEaDSRFLKQLGVTTivdlTLAMVDRFLEVLD-----QAEKPGEPVLVHCKAGVGRTGTLVACYLV 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 300795675 1397 lemirCHNLVDVFFAAKTLR-NYKPNMVETLDQYHFCYD 1434
Cdd:cd14494    80 -----LLGGMSAEEAVRIVRlIRPGGIPQTIEQLDFLIK 113
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 286-357 1.86e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.45  E-value: 1.86e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795675    286 PTPIAPPQLLRAGPTYLIIQ-LNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVSLQT-YKLWHLDPDTEYEISV 357
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1063-1139 3.21e-04

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 41.57  E-value: 3.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300795675 1063 LLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAEC-EGVVDIYNcvktlCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14494    41 MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSaEEAVRIVR-----LIRPGGIPQTIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1342-1434 3.77e-04

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: 42.64  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1342 LRWSAY--RD--TPDSKKAFLHLLaavdKW--QAESGDGRTIVHCLNGGGRSGTFCACAtvleMIRCHNLVDVFFAAKTL 1415
Cdd:cd14505    73 ITWHHLpiPDggVPSDIAQWQELL----EEllSALENGKKVLIHCKGGLGRTGLIAACL----LLELGDTLDPEQAIAAV 144

                          90
                  ....*....|....*....
gi 300795675 1416 RNYKPNMVETLDQYHFCYD 1434
Cdd:cd14505   145 RALRPGAIQTPKQENFLHQ 163
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 386-471 6.08e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.91  E-value: 6.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    386 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYSVSLCYHYTLGSSHNQTVREcvkmerGVSRYTIKNLLPYRNVHVRLVL 465
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP------SSTSYTLTGLKPGTEYEFRVRA 76


                    ....*.
gi 300795675    466 TNPEGR 471
Cdd:smart00060   77 VNGAGE 82
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1039-1139 7.74e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 41.11  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675 1039 ARHEVRQFHFtAWPEHGVPyHATGLLAFIRRVKASTPPDaGPVVIHCSAGTGRTGCyiVLdVMLDMAECEGVVDIYNCVK 1118
Cdd:COG2453    44 EEAGLEYLHL-PIPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGT--VA-AAYLVLLGLSAEEALARVR 117

                          90       100
                  ....*....|....*....|.
gi 300795675 1119 tlcSRRVNMIQTEEQYIFIHD 1139
Cdd:COG2453   118 ---AARPGAVETPAQRAFLER 135
fn3 pfam00041
Fibronectin type III domain;
386-467 1.00e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.32  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675   386 APKGLAFAEIQARQLTLQWEP--------LGYNVTRCHTYSVSLCYHYTLGSSHNqtvrecvkmergvsRYTIKNLLPYR 457
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgngpiTGYEVEYRPKNSGEPWNEITVPGTTT--------------SVTLTGLKPGT 67

                           90
                   ....*....|
gi 300795675   458 NVHVRLVLTN 467
Cdd:pfam00041   68 EYEVRVQAVN 77
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1081-1139 3.52e-03

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 39.94  E-value: 3.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795675 1081 VVIHCSAGTGRTG----CyivldVMLDMAECEGVVDIYNCVKTLcsrRVNMIQTEEQYIFIHD 1139
Cdd:cd14505   109 VLIHCKGGLGRTGliaaC-----LLLELGDTLDPEQAIAAVRAL---RPGAIQTPKQENFLHQ 163
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 196-282 3.57e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 37.87  E-value: 3.57e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795675    196 GDVEVNAGQNASFQCmaAGRAAEAERFLLQRQSGALVPAAGVRHISHRRFLATFPLVAVSREDQDLYRCVSQAPRGaGVS 275
Cdd:smart00410    2 PSVTVKEGESVTLSC--EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78


                    ....*..
gi 300795675    276 NFAELIV 282
Cdd:smart00410   79 SGTTLTV 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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