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Conserved domains on  [gi|1958774396|ref|XP_038965082|]
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receptor-type tyrosine-protein phosphatase U isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 937-1147 9.96e-154

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


The actual alignment was detected with superfamily member cd14632:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 205  Bit Score: 463.37  E-value: 9.96e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDMYGDIKITL 1016
Cdd:cd14632      1 YINANYID------GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1017 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYI 1096
Cdd:cd14632     75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958774396 1097 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14632    155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1232-1438 2.97e-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: 451.67  E-value: 2.97e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1391
Cdd:cd14637     81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958774396 1392 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14637    161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 20-180 1.48e-53

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: 184.47  E-value: 1.48e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396    20 GCTFEEASdpvvPCEFSQAQYDDFQWEQVRIHP---GTRTPADLPHGAYLMVNASQHAPGQRAHIIFQTLSEN-DTHCVQ 95
Cdd:smart00137    5 NCDFEEGS----TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396    96 FSYFLFsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDHKGYIGLDDILL 175
Cdd:smart00137   81 FWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 1958774396   176 FSHPC 180
Cdd:smart00137  157 SNGPC 161
fn3 pfam00041
Fibronectin type III domain;
488-571 1.16e-13

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 1.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  488 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLQPGTTYLFSVRARTS 566
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*
gi 1958774396  567 KGFGQ 571
Cdd:pfam00041   79 GGEGP 83
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
341-618 3.80e-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: 67.72  E-value: 3.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  341 LDPDTEYEISVLLTrpGDGGTGRPGPPLlSRTKCAEPTRAPKGLAFAEIQARQLTLQWEP------LGYNVTRCHTYAVS 414
Cdd:COG3401    199 IEPGTTYYYRVAAT--DTGGESAPSNEV-SVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRVYRSNSGDGP 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  415 lcyhYTLGGSHNQTirecvkmergasRYTIKNLLPFRNVHVRLILTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 492
Cdd:COG3401    276 ----FTKVATVTTT------------SYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  493 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLQPGTTYLFSVRARTSKGfgq 571
Cdd:COG3401    338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958774396  572 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 618
Cdd:COG3401    405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
fn3 pfam00041
Fibronectin type III domain;
285-359 2.49e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  285 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---NLQTYKLWHLDPDTEYEISVlLTRPGD 358
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 1958774396  359 G 359
Cdd:pfam00041   80 G 80
 
Name Accession Description Interval E-value
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 937-1147 9.96e-154

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: 463.37  E-value: 9.96e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDMYGDIKITL 1016
Cdd:cd14632      1 YINANYID------GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1017 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYI 1096
Cdd:cd14632     75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958774396 1097 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14632    155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1232-1438 2.97e-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: 451.67  E-value: 2.97e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1391
Cdd:cd14637     81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958774396 1392 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14637    161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
912-1143 1.68e-99

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.03  E-value: 1.68e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  912 RQEPVSAYDRHRVKLHPmlGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLV 991
Cdd:pfam00102    6 RYKDVLPYDHTRVKLTG--DPGPSDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  992 EVGRVKCSRYWP---EDSDMYGDIKITLVKTET-LAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFI 1067
Cdd:pfam00102   78 EKGREKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1068 RRVKASTP-PDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
887-1143 2.82e-98

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 315.75  E-value: 2.82e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   887 GFKQEYESFFEGWD-------ATKKKDKLKSgRQEPVSAYDRHRVKLHPMLGDPDaDYISANYIDirinrqGYHRSNHFI 959
Cdd:smart00194    1 GLEEEFEKLDRLKPddesctvAAFPENRDKN-RYKDVLPYDHTRVKLKPPPGEGS-DYINASYID------GPNGPKAYI 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   960 ATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRTFALERRG 1036
Cdd:smart00194   73 ATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEVTNTG 152

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1037 YSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNC 1116
Cdd:smart00194  153 CSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232

                           250       260
                    ....*....|....*....|....*..
gi 1958774396  1117 VKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1175-1438 2.77e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 279.16  E-value: 2.77e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1175 QLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPL 1254
Cdd:smart00194    1 GLEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1255 QSTTPDFWRLVYDYGCTSIVMLNQLNqSNSAWPCLQYWPEPGR--QQYGLMEVEFVSGTANEDLVSRVFRVQNSSrlQEG 1332
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELV-EKGREKCAQYWPDEEGepLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1333 HLLVRHFQFLRWSaYRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAA 1412
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 1958774396  1413 KTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1203-1438 2.20e-71

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 238.68  E-value: 2.20e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1203 NRDKNRSMDVLPPDRCLPFLiSSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1282
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1283 NSAwPCLQYWPEP--GRQQYGLMEVEFVSGTANE-DLVSRVFRVQNSSRlQEGHLlVRHFQFLRWSAyRDTPDSRKAFLH 1359
Cdd:pfam00102   80 GRE-KCAQYWPEEegESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGS-EETRT-VKHFHYTGWPD-HGVPESPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1360 LLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:pfam00102  156 LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 20-180 1.48e-53

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: 184.47  E-value: 1.48e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396    20 GCTFEEASdpvvPCEFSQAQYDDFQWEQVRIHP---GTRTPADLPHGAYLMVNASQHAPGQRAHIIFQTLSEN-DTHCVQ 95
Cdd:smart00137    5 NCDFEEGS----TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396    96 FSYFLFsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDHKGYIGLDDILL 175
Cdd:smart00137   81 FWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 1958774396   176 FSHPC 180
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 21-181 4.50e-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: 171.78  E-value: 4.50e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   21 CTFEEASDpvvpCEFSQAQYDDFQWEQVRIH-PGTRTPAD----LPHGAYLMVNASQHAPGQRAHIIFQTLSENDT-HCV 94
Cdd:pfam00629    1 CDFEDGNL----CGWTQDSSDDFDWERVSGPsVKTGPSSDhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   95 QFSYFLFsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFwPNEYQVLFEALISPDHKGYIGLDDIL 174
Cdd:pfam00629   77 RFWYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDIS 152


                   ....*..
gi 1958774396  175 LFSHPCA 181
Cdd:pfam00629  153 LSSGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 21-180 2.30e-47

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: 166.78  E-value: 2.30e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   21 CTFEEAsdpvvPCEFSQAQYDDFQWEQVRIHPGTR-TPADLPH----GAYLMVNASQHAPGQRAHIIFQTLSEN-DTHCV 94
Cdd:cd06263      1 CDFEDG-----LCGWTQDSTDDFDWTRVSGSTPSPgTPPDHTHgtgsGHYLYVESSSGREGQKARLLSPLLPPPrSSHCL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   95 QFSYFLFsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWpNEYQVLFEALISPDHKGYIGLDDIL 174
Cdd:cd06263     76 SFWYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDIS 151


                   ....*.
gi 1958774396  175 LFSHPC 180
Cdd:cd06263    152 LSPGPC 157
PHA02738 PHA02738
hypothetical protein; Provisional
 899-1141 2.17e-42

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 158.16  E-value: 2.17e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  899 WDATKKKDKLKsgRQEPVSAYDRHRVKLhPMLGDpDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQ 978
Cdd:PHA02738    43 FNAEKKNRKLN--RYLDAVCFDHSRVIL-PAERN-RGDYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWM 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  979 EQCVSVVMISKLVEVGRVKCSRYWP--EDSDM-YGDIKITLVKTETLAEYVVRTFALErRGYSARHEVRQFHFTAWPEHG 1055
Cdd:PHA02738   113 EHVQIIVMLCKKKENGREKCFPYWSdvEQGSIrFGKFKITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHD 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1056 VPYHATGLLAFIRRVKA----------------STPPdagPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKT 1119
Cdd:PHA02738   192 VPKNTSEFLNFVLEVRQcqkelaqeslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSS 268

                          250       260
                   ....*....|....*....|..
gi 1958774396 1120 LCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:PHA02738   269 IRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
933-1137 5.29e-32

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 127.13  E-value: 5.29e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  933 PDADYISANYIDIRINRQgyhrsnhFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVG--RVKCSRYWPEDSDmYG 1010
Cdd:COG5599     61 ANLGYLNANYIQVIGNHR-------YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGE-YG 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1011 --DIKITLVKTETLAEYV-VRTFALERRGYSAR-HEVRQFHFTAWPEHGVPyHATGLLAFIRRVKAS---TPPDAGPVVI 1083
Cdd:COG5599    133 kyEVSSELTESIQLRDGIeARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKekiKDPDKLLPVV 211

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1084 HCSAGTGRTGCYIVLDVMLDM--AECEGVVDIYNCVKTL-CSRRVNMIQTEEQYIFI 1137
Cdd:COG5599    212 HCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMrTSRNGGMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1201-1440 6.31e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.01  E-value: 6.31e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1201 PRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1280
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1281 QSNSAWPCLQYW--PEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLlvRHFQFLRWSAYrDTPDSRKAFL 1358
Cdd:PHA02747   129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI--SHFQCSEWFED-ETPSDHPDFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1359 HLLAEVDKWQAESGDGRT---------VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQY 1429
Cdd:PHA02747   206 KFIKIIDINRKKSGKLFNpkdallcpiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                          250
                   ....*....|....
gi 1958774396 1430 HF---CYDVALEYL 1440
Cdd:PHA02747   286 LFiqpGYEVLHYFL 299
fn3 pfam00041
Fibronectin type III domain;
488-571 1.16e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 1.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  488 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLQPGTTYLFSVRARTS 566
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*
gi 1958774396  567 KGFGQ 571
Cdd:pfam00041   79 GGEGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 478-579 2.18e-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: 67.14  E-value: 2.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  478 DVPGGIAAESLTftplEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPA-VNVPGPrrtisklrNETYHVFSNLQPGTT 556
Cdd:cd00063      2 SPPTNLRVTDVT----STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeVEVTPG--------SETSYTLTGLKPGTE 69

                           90       100
                   ....*....|....*....|....
gi 1958774396  557 YLFSVRARTSKGFGQAA-LTEITT 579
Cdd:cd00063     70 YEFRVRAVNGGGESPPSeSVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
341-618 3.80e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.72  E-value: 3.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  341 LDPDTEYEISVLLTrpGDGGTGRPGPPLlSRTKCAEPTRAPKGLAFAEIQARQLTLQWEP------LGYNVTRCHTYAVS 414
Cdd:COG3401    199 IEPGTTYYYRVAAT--DTGGESAPSNEV-SVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRVYRSNSGDGP 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  415 lcyhYTLGGSHNQTirecvkmergasRYTIKNLLPFRNVHVRLILTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 492
Cdd:COG3401    276 ----FTKVATVTTT------------SYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  493 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLQPGTTYLFSVRARTSKGfgq 571
Cdd:COG3401    338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958774396  572 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 618
Cdd:COG3401    405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 480-570 2.92e-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: 58.01  E-value: 2.92e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   480 PGGIAAESLTftplEDMIFLKWEEPQEPNGL--ITQYEISYQSIESSDPAVNVPGprrtisklrNETYHVFSNLQPGTTY 557
Cdd:smart00060    4 PSNLRVTDVT----STSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTP---------SSTSYTLTGLKPGTEY 70

                            90
                    ....*....|...
gi 1958774396   558 LFSVRARTSKGFG 570
Cdd:smart00060   71 EFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
285-359 2.49e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  285 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---NLQTYKLWHLDPDTEYEISVlLTRPGD 358
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 1958774396  359 G 359
Cdd:pfam00041   80 G 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 380-475 2.63e-05

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: 44.41  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  380 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCyhytlgGSHNQTIRECVKMERGASRYTIKNLLPFRNVHVRLIL 459
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR------EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                           90
                   ....*....|....*..
gi 1958774396  460 TNPEGR-KEGKEVTFQT 475
Cdd:cd00063     77 VNGGGEsPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 280-351 1.70e-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: 41.83  E-value: 1.70e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774396   280 PTPIAPPQLLRAGPTYLIIQ-LNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQT-YKLWHLDPDTEYEISV 351
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1349-1431 2.98e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 42.65  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1349 DTPDSRKAFLHLLAEVDKWQAEsgDGRTVVHCLNGGGRSGTFCACatVLeMIRCHSLVDvffAAKTLRNYKPNMVETMDQ 1428
Cdd:COG2453     58 FGAPDDEQLQEAVDFIDEALRE--GKKVLVHCRGGIGRTGTVAAA--YL-VLLGLSAEE---ALARVRAARPGAVETPAQ 129


                   ...
gi 1958774396 1429 YHF 1431
Cdd:COG2453    130 RAF 132
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 380-465 1.12e-03

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: 39.52  E-value: 1.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   380 APKGLAFAEIQARQLTLQWEPLGYNVTRChtYAVslcyHYTLGGSHNQTIRECVKMERGASRYTIKNLLPFRNVHVRLIL 459
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIV----GYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76


                    ....*.
gi 1958774396   460 TNPEGR 465
Cdd:smart00060   77 VNGAGE 82
 
Name Accession Description Interval E-value
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 937-1147 9.96e-154

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: 463.37  E-value: 9.96e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDMYGDIKITL 1016
Cdd:cd14632      1 YINANYID------GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1017 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYI 1096
Cdd:cd14632     75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958774396 1097 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14632    155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1232-1438 2.97e-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: 451.67  E-value: 2.97e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1391
Cdd:cd14637     81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958774396 1392 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14637    161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 937-1146 1.01e-140

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: 428.95  E-value: 1.01e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDMYGDIKITL 1016
Cdd:cd14555      1 YINANYID------GYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1017 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYI 1096
Cdd:cd14555     75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYI 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1097 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1146
Cdd:cd14555    155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 872-1146 7.02e-136

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: 418.68  E-value: 7.02e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  872 DLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPDADYISANYIDiri 947
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGqsapWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  948 nrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETLAEYVV 1027
Cdd:cd14633     78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1028 RTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAEC 1107
Cdd:cd14633    155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958774396 1108 EGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1146
Cdd:cd14633    235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 923-1146 1.70e-120

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: 375.13  E-value: 1.70e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  923 RVKLHPMLGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYW 1002
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYID------GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1003 PEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVV 1082
Cdd:cd14631     75 PDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIV 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774396 1083 IHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1146
Cdd:cd14631    155 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1232-1434 7.45e-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: 372.51  E-value: 7.45e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSnsAWPCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPK--DQSCPQYWPDEGSGTYGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1391
Cdd:cd14556     79 IDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958774396 1392 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1434
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 916-1147 1.31e-114

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: 359.72  E-value: 1.31e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  916 VSAYDRHRVKLHPMLGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGR 995
Cdd:cd14630     12 IISYDHSRVRLQLLDGDPHSDYINANYID------GYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVGR 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  996 VKCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP 1075
Cdd:cd14630     86 VKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFLNP 165

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958774396 1076 PDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14630    166 PDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 916-1147 2.33e-107

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: 339.76  E-value: 2.33e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  916 VSAYDRHRVKLHPMLGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGR 995
Cdd:cd14553     12 VIAYDHSRVILQPIEGVPGSDYINANYCD------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSR 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  996 VKCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAST 1074
Cdd:cd14553     86 VKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKACN 165

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774396 1075 PPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14553    166 PPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
912-1143 1.68e-99

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.03  E-value: 1.68e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  912 RQEPVSAYDRHRVKLHPmlGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLV 991
Cdd:pfam00102    6 RYKDVLPYDHTRVKLTG--DPGPSDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  992 EVGRVKCSRYWP---EDSDMYGDIKITLVKTET-LAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFI 1067
Cdd:pfam00102   78 EKGREKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1068 RRVKASTP-PDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 871-1147 2.35e-98

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: 316.59  E-value: 2.35e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  871 ADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPDADYISANYIDir 946
Cdd:cd14626      1 SDLADNIERLKANDGLKFSQEYESIDPGqqftWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYID-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  947 inrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAEY 1025
Cdd:cd14626     79 ----GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPiRGTETYGMIQVTLLDTVELATY 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1026 VVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMA 1105
Cdd:cd14626    155 SVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1958774396 1106 ECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14626    235 KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
887-1143 2.82e-98

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 315.75  E-value: 2.82e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   887 GFKQEYESFFEGWD-------ATKKKDKLKSgRQEPVSAYDRHRVKLHPMLGDPDaDYISANYIDirinrqGYHRSNHFI 959
Cdd:smart00194    1 GLEEEFEKLDRLKPddesctvAAFPENRDKN-RYKDVLPYDHTRVKLKPPPGEGS-DYINASYID------GPNGPKAYI 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   960 ATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRTFALERRG 1036
Cdd:smart00194   73 ATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEVTNTG 152

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1037 YSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNC 1116
Cdd:smart00194  153 CSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232

                           250       260
                    ....*....|....*....|....*..
gi 1958774396  1117 VKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 865-1148 3.07e-93

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: 302.81  E-value: 3.07e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  865 HPAVRVADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPDADYISA 940
Cdd:cd14624      1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGqqftWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  941 NYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKT 1019
Cdd:cd14624     81 NYID------GYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPsRGTETYGLIQVTLLDT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1020 ETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLD 1099
Cdd:cd14624    155 VELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1100 VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCG 1148
Cdd:cd14624    235 AMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 865-1147 1.71e-92

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: 300.47  E-value: 1.71e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  865 HPAVRVADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPDADYISA 940
Cdd:cd14625      1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGqqftWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  941 NYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKT 1019
Cdd:cd14625     81 NYID------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPsRGTETYGMIQVTLLDT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1020 ETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLD 1099
Cdd:cd14625    155 IELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1958774396 1100 VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1147
Cdd:cd14625    235 AMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1232-1438 1.33e-90

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: 291.93  E-value: 1.33e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNqsnSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD---AAQLCMQYWPEKTSCCYGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGT 1389
Cdd:cd14634     78 IDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1390 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14634    158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 937-1139 1.68e-88

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 285.72  E-value: 1.68e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDM---YGDIK 1013
Cdd:cd00047      1 YINASYID------GYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKpleYGDIT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1014 ITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTG 1093
Cdd:cd00047     75 VTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958774396 1094 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd00047    155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1232-1438 1.83e-87

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: 283.07  E-value: 1.83e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSawpCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGT 1389
Cdd:cd14636     78 MDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEEcdEGEGRTIIHCLNGGGRSGM 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1390 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14636    158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 937-1139 4.61e-87

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: 281.93  E-value: 4.61e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPED-SDMYGDIKIT 1015
Cdd:cd14549      1 YINANYVD------GYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1016 LVKTETLAEYVVRTFAL------ERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGT 1089
Cdd:cd14549     75 LLSTEVLATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGV 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1090 GRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14549    155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1175-1438 2.77e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 279.16  E-value: 2.77e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1175 QLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPL 1254
Cdd:smart00194    1 GLEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1255 QSTTPDFWRLVYDYGCTSIVMLNQLNqSNSAWPCLQYWPEPGR--QQYGLMEVEFVSGTANEDLVSRVFRVQNSSrlQEG 1332
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELV-EKGREKCAQYWPDEEGepLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1333 HLLVRHFQFLRWSaYRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAA 1412
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 1958774396  1413 KTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 919-1138 3.34e-83

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: 271.92  E-value: 3.34e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  919 YDRHRVKLHPMLGDPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKC 998
Cdd:cd14548      8 YDHSRVKLIPINEEEGSDYINANYI------PGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  999 SRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFALERRGYSarHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP 1076
Cdd:cd14548     82 DHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLERGDEV--RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958774396 1077 DAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14548    160 EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1232-1438 8.30e-83

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: 270.02  E-value: 8.30e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNqsnSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVD---PAQLCPQYWPENGVHRHGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGT 1389
Cdd:cd14635     78 LEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1390 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14635    158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 916-1146 1.59e-71

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: 240.71  E-value: 1.59e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  916 VSAYDRHRVKLHPMLG--DPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEV 993
Cdd:cd17667     36 ILAYDHSRVKLRPLPGkdSKHSDYINANYVD------GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEK 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  994 GRVKCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALER-----------RGYSARHEVRQFHFTAWPEHGVPYHAT 1061
Cdd:cd17667    110 GRRKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYAL 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1062 GLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd17667    190 PVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 269


                   ....*
gi 1958774396 1142 LEACL 1146
Cdd:cd17667    270 LEAIL 274
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1203-1438 2.20e-71

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 238.68  E-value: 2.20e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1203 NRDKNRSMDVLPPDRCLPFLiSSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1282
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1283 NSAwPCLQYWPEP--GRQQYGLMEVEFVSGTANE-DLVSRVFRVQNSSRlQEGHLlVRHFQFLRWSAyRDTPDSRKAFLH 1359
Cdd:pfam00102   80 GRE-KCAQYWPEEegESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGS-EETRT-VKHFHYTGWPD-HGVPESPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1360 LLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:pfam00102  156 LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 861-1152 9.78e-71

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: 239.16  E-value: 9.78e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  861 TGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESF-----FEGWDATKKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPDA 935
Cdd:cd14621      1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALpacpiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  936 DYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSD-MYGDIKI 1014
Cdd:cd14621     81 DYINASFIN------GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCwTYGNIRV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1015 TLVKTETLAEYVVRTFALERRG----YSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTG 1090
Cdd:cd14621    155 SVEDVTVLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVG 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958774396 1091 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTI 1152
Cdd:cd14621    235 RTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 919-1143 5.86e-68

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: 228.67  E-value: 5.86e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  919 YDRHRVKLHPMLGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKC 998
Cdd:cd14620      7 YDHSRVILSQLDGIPCSDYINASYID------GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  999 SRYWPEDSD-MYGDIKITLVKTETLAEYVVRTFALERR---GYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAST 1074
Cdd:cd14620     81 YQYWPDQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVN 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1075 PPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14620    161 PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 900-1138 1.13e-67

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: 229.56  E-value: 1.13e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  900 DATKKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQE 979
Cdd:cd14543     22 LCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMD------GYKQKNAYIATQGPLPKTYSDFWRMVWEQ 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  980 QCVSVVMISKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGV 1056
Cdd:cd14543     96 KVLVIVMTTRVVERGRVKCGQYWPLEEGSslrYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGV 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1057 PYHATGLLAFI--------RRVKASTPPDAG-----PVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSR 1123
Cdd:cd14543    176 PSSAAALLDFLgevrqqqaLAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQ 255

                          250
                   ....*....|....*
gi 1958774396 1124 RVNMIQTEEQYIFIH 1138
Cdd:cd14543    256 RAFSIQTPDQYYFCY 270
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 912-1143 1.12e-66

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: 225.08  E-value: 1.12e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  912 RQEPVSAYDRHRVKLhPMLGDPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLV 991
Cdd:cd14615      2 RYNNVLPYDISRVKL-SVQSHSTDDYINANYM------PGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  992 EVGRVKCSRYWPED-SDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAF---I 1067
Cdd:cd14615     75 EQGRTKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlV 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774396 1068 RRVKASTPPDaGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14615    155 REYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 912-1143 3.67e-65

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 220.92  E-value: 3.67e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  912 RQEPVSAYDRHRVKLHPMLGDPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLV 991
Cdd:cd14619      2 RFRNVLPYDWSRVPLKPIHEEPGSDYINANYM------PGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCM 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  992 EVGRVKCSRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRR 1069
Cdd:cd14619     76 EAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRL 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774396 1070 VKA--STPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14619    156 LRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 937-1142 2.98e-64

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: 217.15  E-value: 2.98e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWP-EDSDMYGDIKIT 1015
Cdd:cd17668      1 YINANYVD------GYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1016 LVKTETLAEYVVRTFALE--------RRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSA 1087
Cdd:cd17668     75 QKSVQVLAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958774396 1088 GTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd17668    155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 937-1138 4.35e-64

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: 216.32  E-value: 4.35e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSD-MYGDIKIT 1015
Cdd:cd14551      1 YINASYID------GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1016 LVKTETLAEYVVRTFALERR----GYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGR 1091
Cdd:cd14551     75 VEDTVVLVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGR 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958774396 1092 TGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14551    155 TGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 919-1138 5.29e-64

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: 217.09  E-value: 5.29e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  919 YDRHRVKLHPMLGDPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKC 998
Cdd:cd14617      9 YDSTRVKLSNVDDDPCSDYINASYI------PGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKC 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  999 SRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFAL--ERRGYSARHeVRQFHFTAWPEHGVPYHATGLLAFIRRVK--A 1072
Cdd:cd14617     83 DHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcsEEQLDAPRL-VRHFHYTVWPDHGVPETTQSLIQFVRTVRdyI 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774396 1073 STPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14617    162 NRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 923-1138 2.19e-63

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: 215.34  E-value: 2.19e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  923 RVKLHPMLGDPDADYISANYIdirinrQGY-HRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEvGRVKCSRY 1001
Cdd:cd14547     13 RVCLPSVDDDPLSSYINANYI------RGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AKEKCAQY 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1002 WPEDSDM-YGDIKITLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVK--ASTPPDA 1078
Cdd:cd14547     86 WPEEENEtYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEeaRQTEPHR 163

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774396 1079 GPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIyncVKTLCSRRVN---MIQTEEQYIFIH 1138
Cdd:cd14547    164 GPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDV---LGIVCQLRLDrggMVQTAEQYEFVH 223
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 912-1142 5.32e-63

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: 214.42  E-value: 5.32e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  912 RQEPVSAYDRHRVKLHPMLGDPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLV 991
Cdd:cd14618      2 RYPHVLPYDHSRVRLSQLGGEPHSDYINANFI------PGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGM 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  992 EVGRVKCSRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRR 1069
Cdd:cd14618     76 ENGRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFREL 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774396 1070 VKA--STPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd14618    156 VREhvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 916-1138 8.56e-62

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: 210.53  E-value: 8.56e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  916 VSAYDRHRVKLHPMLGDPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGR 995
Cdd:cd14616      6 IKPYNNNRVKLIADAGVPGSDYINASYI------SGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  996 VKCSRYWPEDSD---MYGDIKITLVKTETLAEYVVRTFALERRGYSARheVRQFHFTAWPEHGVPYHATGLLAFIRRVKA 1072
Cdd:cd14616     80 IRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774396 1073 STPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14616    158 SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 937-1139 1.67e-61

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: 209.41  E-value: 1.67e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDIrinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDM--YGDIKI 1014
Cdd:cd18533      1 YINASYITL-----PGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgeYGDLTV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1015 TLVKTETLAE--YVVRTFALeRRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA--STPPDAGPVVIHCSAGTG 1090
Cdd:cd18533     76 ELVSEEENDDggFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774396 1091 RTGCYIVLDVMLDMAE--------CEGVVD-IYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd18533    155 RTGTFIALDSLLDELKrglsdsqdLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 919-1141 2.04e-61

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: 210.78  E-value: 2.04e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  919 YDRHRVKLHPmlGDPD---ADYISANYIDIRiNRQGYHRSNH--FIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEV 993
Cdd:cd14544     13 FDHTRVILKD--RDPNvpgSDYINANYIRNE-NEGPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVIVMTTKEVER 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  994 GRVKCSRYWPED--SDMYGDIKITLVKTETLAEYVVRTFALER--RGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRR 1069
Cdd:cd14544     90 GKNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKldQGDPIR-EIWHYQYLSWPDHGVPSDPGGVLNFLED 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1070 V--KASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14544    169 VnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAV 245
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 937-1144 1.59e-60

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: 206.46  E-value: 1.59e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDIRINRQGYHrsnhFIATQGPKPEMIYDFWRMVWqEQCVSVV-MISKLVEVGRVKCSRYWPEDSD----MYGD 1011
Cdd:cd14538      1 YINASHIRIPVGGDTYH----YIACQGPLPNTTGDFWQMVW-EQKSEVIaMVTQDVEGGKVKCHRYWPDSLNkpliCGGR 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1012 IKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTppDAGPVVIHCSAGTGR 1091
Cdd:cd14538     76 LEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGR 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958774396 1092 TGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1144
Cdd:cd14538    154 TGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 919-1142 1.62e-60

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: 207.76  E-value: 1.62e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  919 YDRHRVKLHPMLGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKC 998
Cdd:cd14554     18 YESTRVCLQPIRGVEGSDYINASFID------GYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGREKC 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  999 SRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP- 1076
Cdd:cd14554     92 HQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQf 171

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1077 -DAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd14554    172 gQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 937-1138 3.53e-60

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: 205.06  E-value: 3.53e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWP---EDSDMYGDIK 1013
Cdd:cd14557      1 YINASYID------GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1014 ITLVKTETLAEYVVRTFAL--ERRGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGR 1091
Cdd:cd14557     75 VKINEEKICPDYIIRKLNInnKKEKGSGR-EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958774396 1092 TGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14557    154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 936-1144 1.03e-58

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: 201.40  E-value: 1.03e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  936 DYISANYIDIRINRQGYhrSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPE--DSDMYGDIK 1013
Cdd:cd14541      1 DYINANYVNMEIPGSGI--VNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQFGNLQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1014 ITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTG 1093
Cdd:cd14541     79 ITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958774396 1094 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1144
Cdd:cd14541    159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 919-1142 1.75e-58

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


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 202.04  E-value: 1.75e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  919 YDRHRVKLHPMLGDPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKC 998
Cdd:cd14614     24 YDFSRVKLVSMHEEEGSDYINANYI------PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKC 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  999 SRYWP--EDSDMYGDIKITLVKTETLAEYVVRTFaleRRGYS-ARHEVRQFHFTAWPEHGVPY--HATGLLAFIRRVKAS 1073
Cdd:cd14614     98 DHYWPftEEPVAYGDITVEMLSEEEQPDWAIREF---RVSYAdEVQDVMHFNYTAWPDHGVPTanAAESILQFVQMVRQQ 174

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1074 TPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd14614    175 AVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 937-1139 5.31e-56

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: 193.38  E-value: 5.31e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDMYGDIKITL 1016
Cdd:cd14558      1 YINASFID------GYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVEL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1017 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAG------PVVIHCSAGTG 1090
Cdd:cd14558     75 KDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGSS 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1091 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14558    155 RTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1232-1434 4.31e-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: 4.31e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQ--QYGLMEVEFVS 1309
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGRE-KCERYWPEEGGKplEYGDITVTLVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1310 GTANEDLVSRVFRVQNSSrlQEGHLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGT 1389
Cdd:cd00047     80 EEELSDYTIRTLELSPKG--CSESREVTHLHYTGWPD-HGVPSSPEDLLALVRRVRKEA-RKPNGPIVVHCSAGVGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958774396 1390 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1434
Cdd:cd00047    156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 912-1141 5.16e-55

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: 192.54  E-value: 5.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  912 RQEPVSAYDRHRVKLHPmlGDPD---ADYISANYI--DIRINRQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVM 986
Cdd:cd14605      7 RYKNILPFDHTRVVLHD--GDPNepvSDYINANIImpEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVM 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  987 ISKLVEVGRVKCSRYWPEDSDM--YGDIKITLVKTETLAEYVVRTFALERRGY-SARHEVRQFHFTAWPEHGVPYHATGL 1063
Cdd:cd14605     85 TTKEVERGKSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGQgNTERTVWQYHFRTWPDHGVPSDPGGV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1064 LAFIRRV--KASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14605    165 LDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQYRFIY 244


                   ...
gi 1958774396 1139 DAI 1141
Cdd:cd14605    245 MAV 247
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 866-1143 1.40e-54

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: 192.64  E-value: 1.40e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  866 PAVRVADLLQHINQMKTAEGY-GFKQEYESFFEGWDATKK-------KDKLKSgRQEPVSAYDRHRVKLHPMLGDPDADY 937
Cdd:cd14628      4 PARNLYAYIQKLTQIETGENVtGMELEFKRLASSKAHTSRfisanlpCNKFKN-RLVNIMPYESTRVCLQPIRGVEGSDY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  938 ISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWP-EDSDMYGDIKITL 1016
Cdd:cd14628     83 INASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPaERSARYQYFVVDP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1017 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP--DAGPVVIHCSAGTGRTGC 1094
Cdd:cd14628    157 MAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGV 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1095 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14628    237 FITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 937-1141 1.49e-54

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: 189.02  E-value: 1.49e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDM-YGDIKIT 1015
Cdd:cd14552      1 YINASFID------GYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1016 LVKTETLAEYVVRTFALER-RGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRV-KASTPPDAGPVVIHCSAGTGRTG 1093
Cdd:cd14552     75 LKDQTDYEDYTLRDFLVTKgKGGSTR-TVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958774396 1094 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14552    154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 20-180 1.48e-53

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: 184.47  E-value: 1.48e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396    20 GCTFEEASdpvvPCEFSQAQYDDFQWEQVRIHP---GTRTPADLPHGAYLMVNASQHAPGQRAHIIFQTLSEN-DTHCVQ 95
Cdd:smart00137    5 NCDFEEGS----TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396    96 FSYFLFsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDHKGYIGLDDILL 175
Cdd:smart00137   81 FWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 1958774396   176 FSHPC 180
Cdd:smart00137  157 SNGPC 161
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 916-1143 1.59e-53

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: 189.56  E-value: 1.59e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  916 VSAYDRHRVKLHPMLGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGR 995
Cdd:cd14627     62 IMPYETTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGR 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  996 VKCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAST 1074
Cdd:cd14627    136 EKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTK 215

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774396 1075 PP--DAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14627    216 EQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 919-1143 3.64e-53

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: 186.02  E-value: 3.64e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  919 YDRHRVKLHPMLGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKC 998
Cdd:cd14623      8 YEFNRVIIPVKRGEENTDYVNASFID------GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  999 SRYWPEDSDM-YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPD 1077
Cdd:cd14623     82 AQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQS 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1078 AG-PVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14623    162 GNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 916-1143 4.15e-52

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: 185.31  E-value: 4.15e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  916 VSAYDRHRVKLHPMLGDPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGR 995
Cdd:cd14629     62 IMPYELTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGR 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  996 VKCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAST 1074
Cdd:cd14629    136 EKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTK 215

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774396 1075 PP--DAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14629    216 EQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 905-1142 8.68e-52

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: 182.34  E-value: 8.68e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  905 KDKLKSGRQEPVSAYDRHRVklhpMLGDpDADYISANYIDIRINRQGYHrsnhFIATQGPKPEMIYDFWRMVWQEQCVSV 984
Cdd:cd14597      1 KENRKKNRYKNILPYDTTRV----PLGD-EGGYINASFIKMPVGDEEFV----YIACQGPLPTTVADFWQMVWEQKSTVI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  985 VMISKLVEVGRVKCSRYWPED---SDMYGD-IKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHA 1060
Cdd:cd14597     72 AMMTQEVEGGKIKCQRYWPEIlgkTTMVDNrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1061 TGLLAFI---RRVKAStppdaGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFI 1137
Cdd:cd14597    152 EQLLTFIsymRHIHKS-----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFC 226


                   ....*
gi 1958774396 1138 HDAIL 1142
Cdd:cd14597    227 YQVIL 231
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 936-1141 1.29e-51

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: 180.97  E-value: 1.29e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  936 DYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWP-EDSDMYGDIKI 1014
Cdd:cd14622      1 DYINASFID------GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPsEGSVTHGEITI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1015 TLvKTETLAEYV-VRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV-KASTPPDAGPVVIHCSAGTGRT 1092
Cdd:cd14622     75 EI-KNDTLLETIsIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRT 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1093 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14622    154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 923-1141 1.34e-50

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: 180.06  E-value: 1.34e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  923 RVKL-HPMLGDPDADYISANYIdirinrQGY-HRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRvKCSR 1000
Cdd:cd14613     41 RVCLtSPDQDDPLSSYINANYI------RGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEMNE-KCTE 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1001 YWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---STPPD 1077
Cdd:cd14613    114 YWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEarqQAEPN 191

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1078 AGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIyncVKTLCSRRVN---MIQTEEQYIFIHDAI 1141
Cdd:cd14613    192 CGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDI---LRTTCQLRLDrggMIQTCEQYQFVHHVL 255
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 937-1138 2.45e-50

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: 176.84  E-value: 2.45e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDM---YGDIK 1013
Cdd:cd14542      1 YINANFI------KGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEqlqFGPFK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1014 ITLVKTETLAE-YVVRTFALERRgySARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRT 1092
Cdd:cd14542     75 ISLEKEKRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRT 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1093 GCYIVLDVMLDMAECEGVVD---IYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14542    153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1232-1435 4.44e-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: 176.31  E-value: 4.44e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEI-KERSQNKCAQYWPEDGSVSSGDITVELKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNSsrlQEGHL-LVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTF 1390
Cdd:cd14552     80 DYEDYTLRDFLVTKG---KGGSTrTVRQFHFHGWPEV-GIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTF 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958774396 1391 CACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDV 1435
Cdd:cd14552    156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 905-1138 5.85e-50

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: 177.72  E-value: 5.85e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  905 KDKLKSGRQEPVSaydrhRVKL-HPMLGDPDADYISANYIdirinrQGYH-RSNHFIATQGPKPEMIYDFWRMVWQEQCV 982
Cdd:cd14612     18 KDRYKTILPNPQS-----RVCLrRAGSQEEEGSYINANYI------RGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  983 SVVMISKLVEvGRVKCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATG 1062
Cdd:cd14612     87 IIVMITKLKE-KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGP 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774396 1063 LLAFIRRVKAS--TPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14612    164 LLRLVAEVEESrqTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1198-1437 8.94e-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: 176.56  E-value: 8.94e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1198 ALLPRNRDKNRSMDVLPPDR---CLPFLISSDGdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1274
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYEStrvCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1275 MLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAyRDTPDSR 1354
Cdd:cd14554     79 MLTKLREMGRE-KCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRT--VRQFQFTDWPE-QGVPKSG 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1355 KAFLHLLAEVDKWQAESG-DGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd14554    155 EGFIDFIGQVHKTKEQFGqEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234


                   ....
gi 1958774396 1434 DVAL 1437
Cdd:cd14554    235 RAAL 238
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 916-1136 1.06e-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: 176.43  E-value: 1.06e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  916 VSAYDRHRVKLHpmlgDPDADYISANYIDI-RINRQgyhrsnhFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVG 994
Cdd:cd14545      9 PYDHDRSRVKLK----QGDNDYINASLVEVeEAKRS-------YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  995 RVKCSRYWP-EDSDMYG----DIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRR 1069
Cdd:cd14545     78 QIKCAQYWPqGEGNAMIfedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQK 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774396 1070 VK--ASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGV--VDIYNCVKTLCSRRVNMIQTEEQYIF 1136
Cdd:cd14545    158 VResGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 888-1143 1.21e-49

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: 177.32  E-value: 1.21e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  888 FKQEYESFFEgwdATKKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPDADYISANYIdirinrQGYHRSNHFIATQGPKPE 967
Cdd:cd14603     14 FKADYVCSTV---AGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFI------KGVDGSRAYIATQGPLSH 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  968 MIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSD--MYGDIKITLVKTETL-AEYVVRTFALERRGYSarHEVR 1044
Cdd:cd14603     85 TVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEplQTGPFTITLVKEKRLnEEVILRTLKVTFQKES--RSVS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1045 QFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVD---IYNCVKTLC 1121
Cdd:cd14603    163 HFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMR 242

                          250       260
                   ....*....|....*....|..
gi 1958774396 1122 SRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14603    243 KQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 936-1143 1.85e-49

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: 174.75  E-value: 1.85e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  936 DYISANYIDIRINRQGYhrSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPE--DSDMYGDIK 1013
Cdd:cd14601      1 DYINANYINMEIPSSSI--INRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1014 ITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTG 1093
Cdd:cd14601     79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1094 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14601    159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 889-1143 2.66e-49

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: 176.61  E-value: 2.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  889 KQEYESFFEGWDATKKKDKLKSgRQEPVSAYDRHRVKLHPmlGDPD---ADYISANYIDIRINRQGyHRSNHFIATQGPK 965
Cdd:cd14606      1 KQEVKNLHQRLEGQRPENKSKN-RYKNILPFDHSRVILQG--RDSNipgSDYINANYVKNQLLGPD-ENAKTYIASQGCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  966 PEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPE--DSDMYGDIKITLVKTETLAEYVVRTFALE--RRGYSARh 1041
Cdd:cd14606     77 EATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSplDNGELIR- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1042 EVRQFHFTAWPEHGVPYHATGLLAFIRRV--KASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNC 1116
Cdd:cd14606    156 EIWHYQYLSWPDHGVPSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKT 235

                          250       260
                   ....*....|....*....|....*..
gi 1958774396 1117 VKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14606    236 IQMVRAQRSGMVQTEAQYKFIYVAIAQ 262
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 21-181 4.50e-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: 171.78  E-value: 4.50e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   21 CTFEEASDpvvpCEFSQAQYDDFQWEQVRIH-PGTRTPAD----LPHGAYLMVNASQHAPGQRAHIIFQTLSENDT-HCV 94
Cdd:pfam00629    1 CDFEDGNL----CGWTQDSSDDFDWERVSGPsVKTGPSSDhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   95 QFSYFLFsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFwPNEYQVLFEALISPDHKGYIGLDDIL 174
Cdd:pfam00629   77 RFWYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDIS 152


                   ....*..
gi 1958774396  175 LFSHPCA 181
Cdd:pfam00629  153 LSSGPCP 159
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 905-1138 5.24e-48

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: 171.25  E-value: 5.24e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  905 KDKLKSGRQEPVSaydrhRVKLHPM-LGDPDADYISANYIdirinrQGYH-RSNHFIATQGPKPEMIYDFWRMVWQEQCV 982
Cdd:cd14611      2 KNRYKTILPNPHS-----RVCLKPKnSNDSLSTYINANYI------RGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  983 SVVMISKLVEVGRvKCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALeRRGYSARHeVRQFHFTAWPEHGVPYHATG 1062
Cdd:cd14611     71 VIVMITKLKEKNE-KCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTL-KQGSQSRS-VKHYWYTSWPDHKTPDSAQP 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774396 1063 LLAFIRRVKAS--TPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd14611    148 LLQLMLDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 912-1143 1.36e-47

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: 170.41  E-value: 1.36e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  912 RQEPVSAYDRHRVKLHPMLGDPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLV 991
Cdd:cd14602      3 RYKDILPYDHSRVELSLITSDEDSDYINANFI------KGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  992 EVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRTfaLERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIR 1068
Cdd:cd14602     77 EMGKKKCERYWAEPGEMqleFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1069 RVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAEcEGVV----DIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14602    155 DVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 21-180 2.30e-47

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: 166.78  E-value: 2.30e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   21 CTFEEAsdpvvPCEFSQAQYDDFQWEQVRIHPGTR-TPADLPH----GAYLMVNASQHAPGQRAHIIFQTLSEN-DTHCV 94
Cdd:cd06263      1 CDFEDG-----LCGWTQDSTDDFDWTRVSGSTPSPgTPPDHTHgtgsGHYLYVESSSGREGQKARLLSPLLPPPrSSHCL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   95 QFSYFLFsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWpNEYQVLFEALISPDHKGYIGLDDIL 174
Cdd:cd06263     76 SFWYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDIS 151


                   ....*.
gi 1958774396  175 LFSHPC 180
Cdd:cd06263    152 LSPGPC 157
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 954-1143 2.33e-47

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: 168.78  E-value: 2.33e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  954 RSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPED-SDMYGDIKITLVKTETLAE-YVVRTFA 1031
Cdd:cd14546     13 RNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVHLVSEHIWCDdYLVRSFY 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1032 LERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLD-MAECEGV 1110
Cdd:cd14546     93 LKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILIDMVLNrMAKGAKE 172

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1958774396 1111 VDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14546    173 IDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 903-1141 2.77e-47

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: 171.65  E-value: 2.77e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  903 KKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCV 982
Cdd:cd14604     53 EKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFI------KGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  983 SVVMISKLVEVGRVKCSRYWP---EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSarHEVRQFHFTAWPEHGVPYH 1059
Cdd:cd14604    127 IIVMACREFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET--RRLYQFHYVNWPDHDVPSS 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1060 ATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDV---MLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIF 1136
Cdd:cd14604    205 FDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYEL 284


                   ....*
gi 1958774396 1137 IHDAI 1141
Cdd:cd14604    285 VHRAI 289
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 937-1144 3.03e-47

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 168.39  E-value: 3.03e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDIRINRQGYHrsnhFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSD---MYGDIK 1013
Cdd:cd14596      1 YINASYITMPVGEEELF----YIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQepmELENYQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1014 ITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTppDAGPVVIHCSAGTGRTG 1093
Cdd:cd14596     77 LRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958774396 1094 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1144
Cdd:cd14596    155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1232-1434 6.17e-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: 167.18  E-value: 6.17e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWpCLQYWPEpGRQQYGLMEVEFVSGT 1311
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQ-CAQYWGD-EKKTYGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNSSRLQegHLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAE--SGDGRT---VVHCLNGGGR 1386
Cdd:cd14558     79 KSPTYTVRVFEITHLKRKD--SRTVYQYQYHKWKG-EELPEKPKDLVDMIKSIKQKLPYknSKHGRSvpiVVHCSDGSSR 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958774396 1387 SGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 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 1.47e-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: 166.33  E-value: 1.47e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1231 NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSG 1310
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTEL-QEREQEKCVQYWPSEGSVTHGEITIEIKND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1311 TANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTF 1390
Cdd:cd14622     80 TLLETISIRDFLVTYNQEKQT--RLVRQFHFHGWPEI-GIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTF 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1391 CACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEY 1439
Cdd:cd14622    157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 912-1152 1.53e-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: 169.05  E-value: 1.53e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  912 RQEPVSAYDRHRVKLHpmlgDPDADYISANYIDIRINRQGYhrsnhfIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLV 991
Cdd:cd14608     30 RYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSY------ILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVM 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  992 EVGRVKCSRYWP--EDSDMY---GDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAF 1066
Cdd:cd14608    100 EKGSLKCAQYWPqkEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNF 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1067 IRRVK--ASTPPDAGPVVIHCSAGTGRTGCYIVLD---VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14608    180 LFKVResGSLSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAV 259

                          250
                   ....*....|...
gi 1958774396 1142 LEAC--LCGETTI 1152
Cdd:cd14608    260 IEGAkfIMGDSSV 272
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 900-1143 3.23e-46

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: 168.29  E-value: 3.23e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  900 DATKKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPDADYISANYIdirINRQGyhRSNHFIATQGPKPEMIYDFWRMVWQE 979
Cdd:cd14609     35 STAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPI---IEHDP--RMPAYIATQGPLSHTIADFWQMVWEN 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  980 QCVSVVMISKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAE-YVVRTFALERRGYSARHEVRQFHFTAWPEHGVP 1057
Cdd:cd14609    110 GCTVIVMLTPLVEDGVKQCDRYWPdEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIP 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1058 YHATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIF 1136
Cdd:cd14609    190 SSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269


                   ....*..
gi 1958774396 1137 IHDAILE 1143
Cdd:cd14609    270 ALTAVAE 276
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 903-1143 3.97e-46

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: 167.93  E-value: 3.97e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  903 KKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPDADYISANYIdirinRQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCV 982
Cdd:cd14610     40 QREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI-----MDHDPRNPAYIATQGPLPATVADFWQMVWESGCV 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  983 SVVMISKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAE-YVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHA 1060
Cdd:cd14610    115 VIVMLTPLAENGVKQCYHYWPdEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPAST 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1061 TGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14610    195 RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                   ....
gi 1958774396 1140 AILE 1143
Cdd:cd14610    275 AVAE 278
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1227-1438 3.70e-45

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: 163.29  E-value: 3.70e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1227 GDPN-NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEV 1305
Cdd:cd14623     20 GEENtDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE-KCAQYWPSDGSVSYGDITI 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1306 EFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGG 1385
Cdd:cd14623     99 ELKKEEECESYTVRDLLVTNTRENKSRQ--IRQFHFHGWPEV-GIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAG 175

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958774396 1386 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14623    176 RTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1150-1440 1.42e-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: 163.75  E-value: 1.42e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1150 TTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLnsVTPPLDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISSD 1226
Cdd:cd14627      2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYETtrvCLQPIRGVE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1227 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1306
Cdd:cd14627     80 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1307 FVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAESG-DGRTVVHCLNGGG 1385
Cdd:cd14627    157 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVG 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958774396 1386 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 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 ...
 1150-1444 2.27e-44

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 162.98  E-value: 2.27e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1150 TTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISSD 1226
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKA--HTSRFISANLPCNKFKNRLVNIMPYEStrvCLQPIRGVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1227 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1306
Cdd:cd14628     79 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1307 FVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAESG-DGRTVVHCLNGGG 1385
Cdd:cd14628    156 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVG 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1386 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEALE 1444
Cdd:cd14628    233 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFD 291
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1174-1433 3.61e-44

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 161.76  E-value: 3.61e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1174 SQLREEFQTLnSVTPPLDVEECSiaLLPRNRDKNRSMDVLPPDRCLPFLISSDGDPN-NYINAALTDSYTRSAAFIVTLH 1252
Cdd:cd14543      3 RGIYEEYEDI-RREPPAGTFLCS--LAPANQEKNRYGDVLCLDQSRVKLPKRNGDERtDYINANFMDGYKQKNAYIATQG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1253 PLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWP--EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQ 1330
Cdd:cd14543     80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVE-RGRVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1331 EghLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEV------------DKWQAESGDGRTVVHCLNGGGRSGTFCA---CAT 1395
Cdd:cd14543    159 S--RQVTHFQFTSWPDF-GVPSSAAALLDFLGEVrqqqalavkamgDRWKGHPPGPPIVVHCSAGIGRTGTFCTldiCLS 235

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1958774396 1396 VLEMIRchsLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd14543    236 QLEDVG---TLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 903-1142 5.46e-44

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: 161.56  E-value: 5.46e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  903 KKKDKLKSGRQEPVSAYDRHRVKLhpmlgDPDADYISANYIDIRInrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCV 982
Cdd:cd14600     36 KLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNMEI--PSANIVNKYIATQGPLPHTCAQFWQVVWEQKLS 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  983 SVVMISKLVEVGRVKCSRYWPEDSDM--YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHA 1060
Cdd:cd14600    109 LIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDS 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1061 TGLLAFIRRVKaSTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDA 1140
Cdd:cd14600    189 SDFLEFVNYVR-SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267


                   ..
gi 1958774396 1141 IL 1142
Cdd:cd14600    268 IL 269
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1150-1440 1.32e-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: 161.05  E-value: 1.32e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1150 TTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISSD 1226
Cdd:cd14629      2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKA--HTSRFISANLPCNKFKNRLVNIMPYELtrvCLQPIRGVE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1227 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1306
Cdd:cd14629     80 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1307 FVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAESG-DGRTVVHCLNGGG 1385
Cdd:cd14629    157 PMAEYNMPQYILREFKVTDARDGQS--RTIRQFQFTDWPE-QGVPKTGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVG 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958774396 1386 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1440
Cdd:cd14629    234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 937-1143 1.76e-42

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: 154.92  E-value: 1.76e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDIRINrqgyHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWP-----EDSDMYGD 1011
Cdd:cd14540      1 YINASHITATVG----GKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggeHDALTFGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1012 IKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA------------STPPdag 1079
Cdd:cd14540     77 YKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtnqdvaghNRNP--- 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774396 1080 PVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14540    154 PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PHA02738 PHA02738
hypothetical protein; Provisional
 899-1141 2.17e-42

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 158.16  E-value: 2.17e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  899 WDATKKKDKLKsgRQEPVSAYDRHRVKLhPMLGDpDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQ 978
Cdd:PHA02738    43 FNAEKKNRKLN--RYLDAVCFDHSRVIL-PAERN-RGDYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWM 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  979 EQCVSVVMISKLVEVGRVKCSRYWP--EDSDM-YGDIKITLVKTETLAEYVVRTFALErRGYSARHEVRQFHFTAWPEHG 1055
Cdd:PHA02738   113 EHVQIIVMLCKKKENGREKCFPYWSdvEQGSIrFGKFKITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHD 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1056 VPYHATGLLAFIRRVKA----------------STPPdagPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKT 1119
Cdd:PHA02738   192 VPKNTSEFLNFVLEVRQcqkelaqeslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSS 268

                          250       260
                   ....*....|....*....|..
gi 1958774396 1120 LCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:PHA02738   269 IRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 937-1139 6.27e-42

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: 152.95  E-value: 6.27e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRvKCSRYWPED-SDMYGDIKIT 1015
Cdd:cd14556      1 YINAALLD------SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWPDEgSGTYGPIQVE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1016 LVkTETLAEYVV-RTFALER--RGYSARHEVRQFHFTAWPEHG-VPYHATGLLAFIRRV-KASTPPDAGPVVIHCSAGTG 1090
Cdd:cd14556     74 FV-STTIDEDVIsRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVG 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1091 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14556    153 RSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 912-1141 2.28e-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: 153.20  E-value: 2.28e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  912 RQEPVSAYDRHRVKLHPMlgdpDADYISANYIDIRINRQGYhrsnhfIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLV 991
Cdd:cd14607     29 RYRDVSPYDHSRVKLQNT----ENDYINASLVVIEEAQRSY------ILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  992 EVGRVKCSRYWPEDSD---MYGD--IKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAF 1066
Cdd:cd14607     99 EKDSVKCAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNF 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1067 IRRVK--ASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEG--VVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:cd14607    179 LFKVResGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 958-1139 7.48e-40

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: 147.15  E-value: 7.48e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  958 FIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPED---SDMYGDIKITLVKTETLAEYVVRTFALER 1034
Cdd:cd14539     17 FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAITVSLQSVRTTPTHVERIISIQH 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1035 RGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---STPPDAGPVVIHCSAGTGRTGCY-IVLDVMLDMAECEGV 1110
Cdd:cd14539     97 KDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCSSGVGRTGAFcLLYAAVQEIEAGNGI 176

                          170       180
                   ....*....|....*....|....*....
gi 1958774396 1111 VDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14539    177 PDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 937-1138 8.21e-39

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: 144.14  E-value: 8.21e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDIriNRQGYHRSnhFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVE-VGRVKCSRYWP---EDSDMYGDI 1012
Cdd:cd17658      1 YINASLVET--PASESLPK--FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPaeeNESREFGRI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1013 KITLVKTETLAEyvvrtfALERRGYSARH--------EVRQFHFTAWPEHGVPYHATGLLAFIRRVkASTPPDAGPVVIH 1084
Cdd:cd17658     77 SVTNKKLKHSQH------SITLRVLEVQYieseepplSVLHIQYPEWPDHGVPKDTRSVRELLKRL-YGIPPSAGPIVVH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1085 CSAGTGRTGCYIVLDVML------DMAecegVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1138
Cdd:cd17658    150 CSAGIGRTGAYCTIHNTIrrilegDMS----AVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1168-1443 5.35e-38

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: 144.43  E-value: 5.35e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1168 DPQSNSSQLREEFQTLNSVTPPLDVeeCSIALLPRNRDKNRSMDVLPPDRCLPFL-ISSDGDPNNYINAA-LTDSYTRSA 1245
Cdd:cd14610     11 DHLKNKNRLEKEWEALCAYQAEPNA--TNVAQREENVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASpIMDHDPRNP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1246 AFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFVSGTA-NEDLVSRVFRVQ 1324
Cdd:cd14610     89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAE-NGVKQCYHYWPDEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1325 NssrLQEGHL-LVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAesgdGRT---VVHCLNGGGRSGTFCACATVL-EM 1399
Cdd:cd14610    168 N---LQTNETrTVTQFHFLSWND-QGVPASTRSLLDFRRKVNKCYR----GRScpiIVHCSDGAGRSGTYILIDMVLnKM 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1958774396 1400 IRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEAL 1443
Cdd:cd14610    240 AKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1203-1438 1.39e-37

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: 141.77  E-value: 1.39e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1203 NRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQ 1281
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPgSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL-E 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1282 SNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRV--QNSSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLH 1359
Cdd:cd14553     82 ERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKRE----VRQFQFTAWPDH-GVPEHPTPFLA 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1360 LLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14553    157 FLRRV-KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1208-1431 5.78e-37

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: 139.41  E-value: 5.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1208 RSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAW 1286
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCME-KGRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1287 PCLQYWPEPGRQQ-YGLMEVEFVSGTANEDLVSRVFRVQNSSRlqegHLLVRHFQFLRWSAYR--DTPDSRKAFLHLLAE 1363
Cdd:cd14548     80 KCDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKLERGDE----VRSVRQFHFTAWPDHGvpEAPDSLLRFVRLVRD 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774396 1364 vdkwQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1431
Cdd:cd14548    156 ----YIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 906-1143 2.37e-36

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: 139.75  E-value: 2.37e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  906 DKLKSGRQEPVSAYDRHRVKLHPMLGDPDAdYISANYIDIRINRQGYHrsnhFIATQGPKPEMIYDFWRMVWqEQCVSVV 985
Cdd:cd14599     37 ENAERNRIREVVPYEENRVELVPTKENNTG-YINASHIKVTVGGEEWH----YIATQGPLPHTCHDFWQMVW-EQGVNVI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  986 -MISKLVEVGRVKCSRYWPE-----DSDMYGDIKITL-VKTETLAeYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPY 1058
Cdd:cd14599    111 aMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTkFRTDSGC-YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPE 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1059 HATGLLAF---IRRVKASTPP--DAG-----PVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMI 1128
Cdd:cd14599    190 EVQGFLSYleeIQSVRRHTNSmlDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMI 269

                          250
                   ....*....|....*
gi 1958774396 1129 QTEEQYIFIHDAILE 1143
Cdd:cd14599    270 QTIAQYKFVYQVLIQ 284
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1198-1431 1.59e-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: 136.17  E-value: 1.59e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1198 ALLPRNRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML 1276
Cdd:cd14614      7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEgSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1277 NQLNQSNSAwPCLQYWP---EPgrQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSAYR-DTPD 1352
Cdd:cd14614     87 TQCNEKRRV-KCDHYWPfteEP--VAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHGvPTAN 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1353 SRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1431
Cdd:cd14614    160 AAESILQFVQMV-RQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1232-1433 4.81e-35

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 132.83  E-value: 4.81e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPClqYWPEPGRQQYG------LMEV 1305
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTD-NELNEDEPI--YWPTKEKPLECetfkvtLSGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1306 EFVSGTANEDLVSRVFRVQNSsrlQEGHLL-VRHFQFLRWSAyRDTPDSrkAFLHLLAEVDKWqAESGDGRTVVHCLNGG 1384
Cdd:cd14550     78 DHSCLSNEIRLIVRDFILEST---QDDYVLeVRQFQCPSWPN-PCSPIH--TVFELINTVQEW-AQQRDGPIVVHDRYGG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1385 GRSGTFCACATVL-EMIRCHSlVDVFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd14550    151 VQAATFCALTTLHqQLEHESS-VDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1232-1434 5.23e-35

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: 132.86  E-value: 5.23e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRR-KCDQYWPKEGTETYGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQN----SSRLQEGHLLVRHFQFLRWSAYrDTPDSRkafLHLLAEVDKWQAES--GDGRTVVHCLNGGG 1385
Cdd:cd14549     80 VLATYTVRTFSLKNlklkKVKGRSSERVVYQYHYTQWPDH-GVPDYT---LPVLSFVRKSSAANppGAGPIVVHCSAGVG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1386 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1434
Cdd:cd14549    156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1042-1143 8.90e-35

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 128.63  E-value: 8.90e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1042 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP--PDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECE-GVVDIYNCVK 1118
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1958774396  1119 TLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1042-1143 8.90e-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: 8.90e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1042 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP--PDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECE-GVVDIYNCVK 1118
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1958774396  1119 TLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 888-1143 9.12e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 135.51  E-value: 9.12e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  888 FKQEYESFFEG------WDATKKKDkLKSGRQEPVSAYDRHRVKLHpmLGDPDADYISANYIDirinrqGYHRSNHFIAT 961
Cdd:PHA02742    28 LKEEHEHIMQEivafscNESLELKN-MKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVD------GHNAKGRFICT 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  962 QGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYW---PEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYS 1038
Cdd:PHA02742    99 QAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmphERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTG 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1039 ARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV-----------KASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAEC 1107
Cdd:PHA02742   179 ASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNE 258

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1958774396 1108 EGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:PHA02742   259 RAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1232-1433 4.63e-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: 130.64  E-value: 4.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAA-LTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSG 1310
Cdd:cd14546      1 YINAStIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRL-QENGVKQCARYWPEEGSEVYHIYEVHLVSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1311 TA-NEDLVSRVFRVQNssrLQEGHL-LVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKwqaeSGDGRT---VVHCLNGGG 1385
Cdd:cd14546     80 HIwCDDYLVRSFYLKN---LQTSETrTVTQFHFLSWPD-EGIPASAKPLLEFRRKVNK----SYRGRScpiVVHCSDGAG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1386 RSGTFCACATVLE-MIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd14546    152 RTGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1168-1443 5.36e-34

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: 132.85  E-value: 5.36e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1168 DPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRClPFLISSDGDPN--NYINAA-LTDSYTRS 1244
Cdd:cd14609      9 DHLRNRDRLAKEWQALCAYQA--EPNTCSTAQGEANVKKNRNPDFVPYDHA-RIKLKAESNPSrsDYINASpIIEHDPRM 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1245 AAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFVSGTA-NEDLVSRVFRV 1323
Cdd:cd14609     86 PAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVE-DGVKQCDRYWPDEGSSLYHIYEVNLVSEHIwCEDFLVRSFYL 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1324 QNsSRLQEGHLLVRhFQFLRWSAyRDTPDSRKAFLHLLAEVDKwqaeSGDGRT---VVHCLNGGGRSGTFCACATVL-EM 1399
Cdd:cd14609    165 KN-VQTQETRTLTQ-FHFLSWPA-EGIPSSTRPLLDFRRKVNK----CYRGRScpiIVHCSDGAGRTGTYILIDMVLnRM 237

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1958774396 1400 IRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEAL 1443
Cdd:cd14609    238 AKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1203-1438 6.31e-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: 132.47  E-value: 6.31e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1203 NRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQ 1281
Cdd:cd14626     41 NKPKNRYANVIAYDHSRVILTSVDGVPgSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRL-E 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1282 SNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRV--QNSSRLQEghllVRHFQFLRWSAY--RDTPDSRKAF 1357
Cdd:cd14626    120 EKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALykNGSSEKRE----VRQFQFMAWPDHgvPEYPTPILAF 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1358 LHLLAEVDKWQAesgdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1437
Cdd:cd14626    196 LRRVKACNPPDA----GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271


                   .
gi 1958774396 1438 E 1438
Cdd:cd14626    272 E 272
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1207-1437 8.60e-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: 8.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1207 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqLNQSNSA 1285
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLT-VGMENGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1286 WPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYR--DTPDSRKAFLHLLA 1362
Cdd:cd14618     80 VLCDHYWPsESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERR--VKHLHYTAWPDHGipESTSSLMAFRELVR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774396 1363 EvdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1437
Cdd:cd14618    158 E--HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1207-1438 1.21e-33

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: 129.94  E-value: 1.21e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1207 NRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAw 1286
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1287 PCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYR--DTPDSRKAFLHLLAEV 1364
Cdd:cd14615     80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRT--VRHFHFTSWPDHGvpETTDLLINFRHLVREY 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774396 1365 DKwqAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14615    158 MK--QNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 937-1143 5.15e-33

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


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 127.78  E-value: 5.15e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDIRINRQGYHrsnhFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWP-----EDSDMYGD 1011
Cdd:cd14598      1 YINASHIKVTVGGKEWD----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1012 IKITL-VKTETLAeYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFI-------RRVKASTPPDAG--PV 1081
Cdd:cd14598     77 FKITTrFRTDSGC-YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLeeiqsvrRHTNSTIDPKSPnpPV 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958774396 1082 VIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14598    156 LVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1203-1438 7.39e-33

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: 128.22  E-value: 7.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1203 NRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQ 1281
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1282 SNSAwPCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQN--SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLH 1359
Cdd:cd14630     83 VGRV-KCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKkgYHEIRE----IRQFHFTSWPDH-GVPCYATGLLG 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1360 LLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14630    156 FVRQV-KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 899-1138 2.08e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 128.97  E-value: 2.08e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  899 WDATKKKDKLKSGRQEPVSAYDRHRVKLHPMLGDPdADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQ 978
Cdd:PHA02747    43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWID------GFEDDKKFIATQGPFAETCADFWKAVWQ 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  979 EQCVSVVMISKLVEV-GRVKCSRYW--PEDSDM-YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEH 1054
Cdd:PHA02747   116 EHCSIIVMLTPTKGTnGEEKCYQYWclNEDGNIdMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFED 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1055 GVPYHATGLLAFI------RRVKAS--TPPDA--GPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRR 1124
Cdd:PHA02747   196 ETPSDHPDFIKFIkiidinRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQR 275

                          250
                   ....*....|....
gi 1958774396 1125 VNMIQTEEQYIFIH 1138
Cdd:PHA02747   276 HAGIMNFDDYLFIQ 289
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1204-1433 3.33e-32

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 125.97  E-value: 3.33e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1204 RDKNRSMDVLPPDRCLPFLISSDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSN 1283
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGD---NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1284 SAwPCLQYWPEPGRQQYGL----MEVEFVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAYrDTPDSRKAFLH 1359
Cdd:cd14545     78 QI-KCAQYWPQGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDF-GVPESPAAFLN 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1360 LLAEV-DKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL--VDVFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd14545    154 FLQKVrESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 937-1137 3.66e-32

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: 124.74  E-value: 3.66e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCsrYWPEDSDM--YGDIKI 1014
Cdd:cd14550      1 YINASYL------QGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPleCETFKV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1015 TLVKTETL-----AEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPVVIH----- 1084
Cdd:cd14550     73 TLSGEDHSclsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHdrygg 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958774396 1085 CSAGTgrtgcYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFI 1137
Cdd:cd14550    151 VQAAT-----FCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
933-1137 5.29e-32

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 127.13  E-value: 5.29e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  933 PDADYISANYIDIRINRQgyhrsnhFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVG--RVKCSRYWPEDSDmYG 1010
Cdd:COG5599     61 ANLGYLNANYIQVIGNHR-------YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGE-YG 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1011 --DIKITLVKTETLAEYV-VRTFALERRGYSAR-HEVRQFHFTAWPEHGVPyHATGLLAFIRRVKAS---TPPDAGPVVI 1083
Cdd:COG5599    133 kyEVSSELTESIQLRDGIeARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKekiKDPDKLLPVV 211

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1084 HCSAGTGRTGCYIVLDVMLDM--AECEGVVDIYNCVKTL-CSRRVNMIQTEEQYIFI 1137
Cdd:COG5599    212 HCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMrTSRNGGMVQTSEQLDVL 268
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1152-1438 1.03e-31

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: 126.36  E-value: 1.03e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1152 IPVNEFkATYREMIRIDpqsNSSQLREEFQTLNsvtpPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDG-DPN 1230
Cdd:cd14625      4 IPISEL-AEHTERLKAN---DNLKLSQEYESID----PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1231 NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSG 1310
Cdd:cd14625     76 DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKL-EEKSRIKCDQYWPSRGTETYGMIQVTLLDT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1311 TANEDLVSRVFRVQN--SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGdGRTVVHCLNGGGRSG 1388
Cdd:cd14625    155 IELATFCVRTFSLHKngSSEKRE----VRQFQFTAWPDH-GVPEYPTPFLAFLRRVKTCNPPDA-GPIVVHCSAGVGRTG 228

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1389 TFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14625    229 CFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1211-1438 1.88e-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: 123.51  E-value: 1.88e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1211 DVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCL 1289
Cdd:cd14620      3 NILPYDHSRVILSQLDGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE-KCY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1290 QYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQnsSRLQEGH---LLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdK 1366
Cdd:cd14620     82 QYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ--PQLPDGCkapRLVTQLHFTSWPDF-GVPFTPIGMLKFLKKV-K 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958774396 1367 WQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14620    158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1195-1438 2.76e-31

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


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 124.75  E-value: 2.76e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1195 CSIALLPRNRDKNRSMDVLPPDRCLPFLISSDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1274
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED---NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1275 MLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVS----RVFRVQNSSRLQEGHLLvrHFQFLRWSAYrDT 1350
Cdd:cd14608     94 MLNRVMEKGSL-KCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSyytvRQLELENLTTQETREIL--HFHYTTWPDF-GV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1351 PDSRKAFLHLLAEVdkwqAESGD-----GRTVVHCLNGGGRSGTFC---ACATVLEMIRCHSLVDVFFAAKTLRNYKPNM 1422
Cdd:cd14608    170 PESPASFLNFLFKV----RESGSlspehGPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGL 245

                          250
                   ....*....|....*.
gi 1958774396 1423 VETMDQYHFCYDVALE 1438
Cdd:cd14608    246 IQTADQLRFSYLAVIE 261
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1176-1439 4.06e-31

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: 124.75  E-value: 4.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1176 LREEFQTLNSVtpPLDVEeCSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPN-NYINAALTDSYTRSAAFIVTLHPL 1254
Cdd:cd14621     28 FREEFNALPAC--PIQAT-CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDsDYINASFINGYQEKNKFIAAQGPK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1255 QSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRL--QEG 1332
Cdd:cd14621    105 EETVNDFWRMIWEQNTATIVMVTNLKERKEC-KCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVtnKKP 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1333 HLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAA 1412
Cdd:cd14621    184 QRLITQFHFTSWPDF-GVPFTPIGMLKFLKKVKNCNPQYA-GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFV 261

                          250       260
                   ....*....|....*....|....*..
gi 1958774396 1413 KTLRNYKPNMVETMDQYHFCYDVALEY 1439
Cdd:cd14621    262 SRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1232-1438 8.49e-31

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: 120.93  E-value: 8.49e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGrQQYGLMEVEFVSGT 1311
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRV-KCSKYWPDDS-DTYGDIKITLLKTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNssRLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGTFC 1391
Cdd:cd14632     79 TLAEYSVRTFALER--RGYSARHEVKQFHFTSWPEH-GVPYHATGLLAFIRRV-KASTPPDAGPVVVHCSAGAGRTGCYI 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958774396 1392 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14632    155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1232-1433 1.26e-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: 1.26e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKE-RKEKKCSQYWPDQGCWTYGNLRVRVEDTV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNSSRL--QEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGT 1389
Cdd:cd14551     80 VLVDYTTRKFCIQKVNRGigEKRVRLVTQFHFTSWPDF-GVPFTPIGMLKFLKKV-KSANPPRAGPIVVHCSAGVGRTGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958774396 1390 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd14551    158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1232-1438 2.18e-30

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: 119.64  E-value: 2.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEpGRQQYGLMEVEFVSGT 1311
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRV-KCSRYWPD-DTEVYGDIKVTLVETE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQNS--SRLQEghllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGT 1389
Cdd:cd14555     79 PLAEYVVRTFALERRgyHEIRE----VRQFHFTGWPDH-GVPYHATGLLGFIRRV-KASNPPSAGPIVVHCSAGAGRTGC 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1390 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14555    153 YIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1232-1434 2.49e-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: 119.66  E-value: 2.49e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAA-LTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQ-YGLMEVEFVS 1309
Cdd:cd18533      1 YINASyITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVE-NGREKCDQYWPSGEYEGeYGDLTVELVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1310 GTANED--LVSRVFRVQNSsrlQEGHLLVRHFQFLRWSAYRdTPDSRKAFLHLLAEVDKW-QAESGDGRTVVHCLNGGGR 1386
Cdd:cd18533     80 EEENDDggFIVREFELSKE---DGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLIKLKRELnDSASLDPPIIVHCSAGVGR 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1387 SGTFCACATVLEMIRCHSLVD---------VFFAAKTLRNYKPNMVETMDQYHFCYD 1434
Cdd:cd18533    156 TGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1200-1438 4.06e-30

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 121.76  E-value: 4.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1200 LPRNRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQ 1278
Cdd:cd14624     44 LEVNKPKNRYANVIAYDHSRVLLSAIEGIPgSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1279 LnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRV--QNSSRLQEghllVRHFQFLRWSAYrDTPDSRKA 1356
Cdd:cd14624    124 L-EERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALykNGSSEKRE----VRQFQFTAWPDH-GVPEHPTP 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1357 FLHLLAEVDKWQAESGdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVA 1436
Cdd:cd14624    198 FLAFLRRVKTCNPPDA-GPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276


                   ..
gi 1958774396 1437 LE 1438
Cdd:cd14624    277 LE 278
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1232-1434 9.70e-30

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: 117.87  E-value: 9.70e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAA-FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLnQLNQSNSAWPCLQYWPEPGRQQ--YGLMEVEFV 1308
Cdd:cd14539      1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVML-VSEQENEKQKVHRYWPTERGQAlvYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1309 SGTANEDLVSRVFRVQNssRLQEGHLLVRHFQFLRWSAYRdTPDSRKAFLHLLAEVDKW--QAESGDGRTVVHCLNGGGR 1386
Cdd:cd14539     80 SVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHylQQRSLQTPIVVHCSSGVGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1387 SGTFCAC-ATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1434
Cdd:cd14539    157 TGAFCLLyAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 937-1143 1.08e-29

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: 117.81  E-value: 1.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLvEVGRVkCSRYWPEDSD-MYGDIKIT 1015
Cdd:cd14634      1 YINAALMD------SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQL-CMQYWPEKTScCYGPIQVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1016 LVKTETLAEYVVRTF-----ALERRGYSArheVRQFHFTAWPEH-GVPYHATGLLAFIRRV-KASTPPDA--GPVVIHCS 1086
Cdd:cd14634     73 FVSADIDEDIISRIFricnmARPQDGYRI---VQHLQYIGWPAYrDTPPSKRSILKVVRRLeKWQEQYDGreGRTVVHCL 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1087 AGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14634    150 NGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 937-1143 2.54e-29

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: 116.66  E-value: 2.54e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGrvKCSRYWPEDSDM-YGDIKIT 1015
Cdd:cd14636      1 YINAALMD------SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWPEEGMLrYGPIQVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1016 LVKTETLAEYVVRTFAL-----ERRGYSArheVRQFHFTAWPEH-GVPYHATGLLAFIRRV---KASTPPDAGPVVIHCS 1086
Cdd:cd14636     73 CMSCSMDCDVISRIFRIcnltrPQEGYLM---VQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECDEGEGRTIIHCL 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774396 1087 AGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14636    150 NGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1232-1433 4.36e-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: 116.02  E-value: 4.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAAL--TDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQ--YGLMEVEF 1307
Cdd:cd17658      1 YINASLveTPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAKCADYFPAEENESreFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1308 VS-GTANEDLVSRVFRVQNsSRLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdkWQAESGDGRTVVHCLNGGGR 1386
Cdd:cd17658     81 KKlKHSQHSITLRVLEVQY-IESEEPPLSVLHIQYPEWPDH-GVPKDTRSVRELLKRL--YGIPPSAGPIVVHCSAGIGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958774396 1387 SGTFCACATVLEMIRCHSL--VDVFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd17658    157 TGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1197-1433 5.59e-29

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: 117.37  E-value: 5.59e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1197 IALLPRNRDKNRSMDVLPPDRCLPFLISSDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML 1276
Cdd:cd14607     18 VAKYPENRNRNRYRDVSPYDHSRVKLQNTE---NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1277 NQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVS----RVFRVQNSSRLQEghLLVRHFQFLRWSAYrDTPD 1352
Cdd:cd14607     95 NRIVEKDSV-KCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSyytvHLLQLENINSGET--RTISHFHYTTWPDF-GVPE 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1353 SRKAFLHLLAEVdkwqAESG-----DGRTVVHCLNGGGRSGTFCACATVLEMIRCHS--LVDVFFAAKTLRNYKPNMVET 1425
Cdd:cd14607    171 SPASFLNFLFKV----RESGslspeHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQT 246


                   ....*...
gi 1958774396 1426 MDQYHFCY 1433
Cdd:cd14607    247 PDQLRFSY 254
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 937-1143 1.63e-28

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: 114.62  E-value: 1.63e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRV-KCSRYWPEDS-DMYGDIKI 1014
Cdd:cd14637      1 YINAALTD------SYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGlQQYGPMEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1015 TLVKTETLAEYVVRTFALER--RGYSARHEVRQFHFTAW-PEHGVPYHATGLLAFIRRV-KASTPPDAGPVVIHCSAGTG 1090
Cdd:cd14637     75 EFVSGSADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958774396 1091 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14637    155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1201-1433 1.86e-28

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: 116.08  E-value: 1.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1201 PRNRDKNRSMDVLPPDR---CLPFLISSDGdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1277
Cdd:cd14603     28 KENVKKNRYKDILPYDQtrvILSLLQEEGH--SDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMAC 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1278 QlNQSNSAWPCLQYWP-EPGRQQYGLMEVEFVSGT-ANEDLVSRVFRV--QNSSRlqeghlLVRHFQFLRWSAyRDTPDS 1353
Cdd:cd14603    106 R-EIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKVtfQKESR------SVSHFQYMAWPD-HGIPDS 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1354 RKAFLHLLAEVDKWQAESGDgRTVVHCLNGGGRSGTFCACATV-----LEMIRCH-SLVDVFFaakTLRNYKPNMVETMD 1427
Cdd:cd14603    178 PDCMLAMIELARRLQGSGPE-PLCVHCSAGCGRTGVICTVDYVrqlllTQRIPPDfSIFDVVL---EMRKQRPAAVQTEE 253


                   ....*.
gi 1958774396 1428 QYHFCY 1433
Cdd:cd14603    254 QYEFLY 259
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1203-1441 3.00e-28

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: 115.25  E-value: 3.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1203 NRDKNRSMDVLPPDRCLpfLISSDGDPN----NYINAaltdSYTRSAA-----------FIVTLHPLQSTTPDFWRLVYD 1267
Cdd:cd14544      1 NKGKNRYKNILPFDHTR--VILKDRDPNvpgsDYINA----NYIRNENegpttdenaktYIATQGCLENTVSDFWSMVWQ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1268 YGCTSIVML-NQLNQSNSAwpCLQYWPEPGRQ-QYGLMEVEFVSGTANEDLVSRVFRVqnsSRLQEGHLL--VRHFQFLR 1343
Cdd:cd14544     75 ENSRVIVMTtKEVERGKNK--CVRYWPDEGMQkQYGPYRVQNVSEHDTTDYTLRELQV---SKLDQGDPIreIWHYQYLS 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1344 WSAYrDTPDSRKAFLHLLAEVDKWQAESGD-GRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYK 1419
Cdd:cd14544    150 WPDH-GVPSDPGGVLNFLEDVNQRQESLPHaGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQR 228

                          250       260
                   ....*....|....*....|..
gi 1958774396 1420 PNMVETMDQYHFCYDVALEYLE 1441
Cdd:cd14544    229 SGMVQTEAQYKFIYVAVAQYIE 250
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1190-1435 3.61e-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: 114.96  E-value: 3.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1190 LDVEECSIALLPRnrdKNRSMDVLPPDRCLPFLISSD-GDP-NNYINAALTDSY-TRSAAFIVTLHPLQSTTPDFWRLVY 1266
Cdd:cd14613     15 VDPKEYDIPGLVR---KNRYKTILPNPHSRVCLTSPDqDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVW 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1267 DYGCTSIVMLNQLNQSNSAwpCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSA 1346
Cdd:cd14613     92 QERSPIIVMITNIEEMNEK--CTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITLKSGGEERG----LKHYWYTSWPD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1347 YRdTPDSRKAFLHLLAEVD--KWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVE 1424
Cdd:cd14613    165 QK-TPDNAPPLLQLVQEVEeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQ 243

                          250
                   ....*....|.
gi 1958774396 1425 TMDQYHFCYDV 1435
Cdd:cd14613    244 TCEQYQFVHHV 254
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1203-1441 5.09e-28

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: 114.73  E-value: 5.09e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1203 NRDKNRSMDVLPPDRCLpfLISSDGDPN----NYINA--ALTDSYTRS------AAFIVTLHPLQSTTPDFWRLVYDYGC 1270
Cdd:cd14605      2 NKNKNRYKNILPFDHTR--VVLHDGDPNepvsDYINAniIMPEFETKCnnskpkKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1271 TSIVMLNQLNQSNSAwPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVqnsSRLQEGHL--LVRHFQFLRWSAY 1347
Cdd:cd14605     80 RVIVMTTKEVERGKS-KCVKYWPdEYALKEYGVMRVRNVKESAAHDYILRELKL---SKVGQGNTerTVWQYHFRTWPDH 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1348 rDTPDSRKAFLHLLAEVD-KWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYKPNMV 1423
Cdd:cd14605    156 -GVPSDPGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMV 234

                          250
                   ....*....|....*...
gi 1958774396 1424 ETMDQYHFCYDVALEYLE 1441
Cdd:cd14605    235 QTEAQYRFIYMAVQHYIE 252
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1207-1431 6.00e-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: 113.26  E-value: 6.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1207 NRSMDVLPPDR---CLPfliSSDGDP-NNYINAaltdSYTR-----SAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1277
Cdd:cd14547      1 NRYKTILPNEHsrvCLP---SVDDDPlSSYINA----NYIRgydgeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMIT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1278 QLNQSNSAwpCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSAYRdTPDSRKAF 1357
Cdd:cd14547     74 NLTEAKEK--CAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRY----LKHYWYTSWPDHK-TPEAAQPL 146

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774396 1358 LHLLAEVDKW-QAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1431
Cdd:cd14547    147 LSLVQEVEEArQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1207-1433 7.88e-28

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: 113.09  E-value: 7.88e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1207 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSA 1285
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1286 wPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLqEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEV 1364
Cdd:cd14617     81 -KCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQL-DAPRLVRHFHYTVWPDH-GVPETTQSLIQFVRTV 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1365 -DKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd14617    158 rDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1200-1433 8.03e-28

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: 113.78  E-value: 8.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1200 LPRNRDKNRSMDVLP-PDR--CLPFLISSDgDPNNYINAALTDSYT-RSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVM 1275
Cdd:cd14612     12 IPGHASKDRYKTILPnPQSrvCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1276 LNQLNQSNSAwpCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQnssrLQEGHLLVRHFQFLRWSAYRdTPDSRK 1355
Cdd:cd14612     91 ITKLKEKKEK--CVHYWPEK-EGTYGRFEIRVQDMKECDGYTIRDLTIQ----LEEESRSVKHYWFSSWPDHQ-TPESAG 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1356 AFLHLLAEVDKW-QAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd14612    163 PLLRLVAEVEESrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1232-1437 1.83e-27

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: 111.24  E-value: 1.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqlNQSNSAWPCLQYWP---EPGRQQ---YGLMEV 1305
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLP--DGQNMAEDEFVYWPnkdEPINCEtfkVTLIAE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1306 EFVSGTANEDLVSRVFRVQNSsrlQEGHLL-VRHFQFLRWSayrdTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGG 1384
Cdd:cd17669     79 EHKCLSNEEKLIIQDFILEAT---QDDYVLeVRHFQCPKWP----NPDSPISKTFELISIIKEEAANRDGPMIVHDEHGG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958774396 1385 GRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1437
Cdd:cd17669    152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1232-1437 1.92e-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: 111.31  E-value: 1.92e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML--NQ-LNQSNSAwpclqYWPEpgRQQ--------Y 1300
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQgLAEDEFV-----YWPS--REEsmnceaftV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1301 GLMEVEFVSGTANEDLVSRVFRVQNSsrlQEGHLL-VRHFQFLRWSayrdTPDSRKAFLHLLAEVDKWQAESGDGRTVVH 1379
Cdd:cd17670     74 TLISKDRLCLSNEEQIIIHDFILEAT---QDDYVLeVRHFQCPKWP----NPDAPISSTFELINVIKEEALTRDGPTIVH 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774396 1380 CLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1437
Cdd:cd17670    147 DEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1201-1438 2.94e-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: 112.82  E-value: 2.94e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1201 PRNRDKNRSMDVLPPDRC---LPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1277
Cdd:cd17667     25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1278 QLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNS--SRLQEGHLLVRH-------FQFLRWsayr 1348
Cdd:cd17667    105 NLVEKGRR-KCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTkvKKGQKGNPKGRQnertviqYHYTQW---- 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1349 dtPDS--RKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVE 1424
Cdd:cd17667    180 --PDMgvPEYALPVLTFVRRSSAArtPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQ 257

                          250
                   ....*....|....
gi 1958774396 1425 TMDQYHFCYDVALE 1438
Cdd:cd17667    258 TEEQYIFIHDALLE 271
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1206-1433 4.72e-27

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: 110.78  E-value: 4.72e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1206 KNRSMDVLPPDRCLPFL--ISSDGDPNNYINAALTDSYT-RSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1282
Cdd:cd14611      2 KNRYKTILPNPHSRVCLkpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1283 NSAwpCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSAYRdTPDSRKAFLHLLA 1362
Cdd:cd14611     82 NEK--CVLYWPEK-RGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRS----VKHYWYTSWPDHK-TPDSAQPLLQLML 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958774396 1363 EVDKWQAES-GDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd14611    154 DVEEDRLASpGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1232-1431 5.75e-27

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: 110.11  E-value: 5.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAA----FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPG-RQQYGLMEVE 1306
Cdd:cd14541      2 YINANYVNMEIPGSGivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRV-KCHQYWPDLGeTMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1307 FVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDgRTVVHCLNGGGR 1386
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEERH--ITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRVGMVE-PTVVHCSAGIGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958774396 1387 SGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1431
Cdd:cd14541    157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1207-1440 7.31e-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: 110.75  E-value: 7.31e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1207 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSA 1285
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPgSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME-AGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1286 WPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNssRLQEGHLLVRHFQFLRWSAY--RDTPDSRKAFLHLLA 1362
Cdd:cd14619     80 VKCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQ--VEEQKTLSVRHFHFTAWPDHgvPSSTDTLLAFRRLLR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774396 1363 EVDKWQAESGDgrTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1440
Cdd:cd14619    158 QWLDQTMSGGP--TVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 937-1143 2.01e-26

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: 108.62  E-value: 2.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKlVEVGRVkCSRYWPEDS-DMYGDIKIT 1015
Cdd:cd14635      1 YINAALMD------SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWPENGvHRHGPIQVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1016 LVKTETLAEYVVRTFAL--ERRGYSARHEVRQFHFTAWPEH-GVPYHATGLLAFIRRV-KASTPPDAGP--VVIHCSAGT 1089
Cdd:cd14635     73 FVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdKWQEEYNGGEgrTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958774396 1090 GRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1143
Cdd:cd14635    153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1203-1438 2.60e-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: 110.13  E-value: 2.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1203 NRDKNRSMDVLPPDRCLPFLISSDGDPN-NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQ 1281
Cdd:cd14633     40 NRMKNRYGNIIAYDHSRVRLQPIEGETSsDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1282 SNSAwPCLQYWPEpGRQQYGLMEVEFVSGTANEDLVSRVFRVQN--SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLH 1359
Cdd:cd14633    120 VGRV-KCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFAVEKrgVHEIRE----IRQFHFTGWPDH-GVPYHATGLLG 192

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1360 LLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14633    193 FVRQV-KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1232-1440 2.68e-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: 108.23  E-value: 2.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAaltdSYTR------SAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWPEPGRQQ---YGL 1302
Cdd:cd14538      1 YINA----SHIRipvggdTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQ-DVEGGKVKCHRYWPDSLNKPlicGGR 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1303 MEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAesgDGRTVVHCLN 1382
Cdd:cd14538     76 LEVSLEKYQSLQDFVIRRISLRDKETGEVHH--ITHLNFTTWPDH-GTPQSADPLLRFIRYMRRIHN---SGPIVVHCSA 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774396 1383 GGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1440
Cdd:cd14538    150 GIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1226-1438 1.26e-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: 106.64  E-value: 1.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1226 DGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGrQQYGLME 1304
Cdd:cd14631      8 EDDPsSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRV-KCYKYWPDDT-EVYGDFK 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1305 VEFVSGTANEDLVSRVFRVQNS--SRLQEghllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLN 1382
Cdd:cd14631     86 VTCVEMEPLAEYVVRTFTLERRgyNEIRE----VKQFHFTGWPDH-GVPYHATGLLSFIRRV-KLSNPPSAGPIVVHCSA 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774396 1383 GGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:cd14631    160 GAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 904-1141 1.76e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 108.96  E-value: 1.76e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  904 KKDKLKSGRQEPVSAYDRHRVKLHPM-------LGDPD------------ADYISANYIDirinrqGYHRSNHFIATQGP 964
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVVINAHeslkmfdVGDSDgkkievtsednaENYIHANFVD------GFKEANKFICAQGP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  965 KPEMIYDFWRMVWQEQcvSVVMISkLVEVGR--VKCSRYW--PEDSDM-YGDIKITLVKTETLAEYVVRTFALERRGYSA 1039
Cdd:PHA02746   122 KEDTSEDFFKLISEHE--SQVIVS-LTDIDDddEKCFELWtkEEDSELaFGRFVAKILDIIEELSFTKTRLMITDKISDT 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1040 RHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA----------STPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEG 1109
Cdd:PHA02746   199 SREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEK 278

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1958774396 1110 VVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:PHA02746   279 EVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1207-1431 3.65e-25

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: 105.37  E-value: 3.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1207 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSA 1285
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1286 wPCLQYWPEPGR--QQYGLMEVEFVSGTANEDLVSRVFRVQnssrlQEGH-LLVRHFQFLRWSAYrDTPDSRKAFLHLLA 1362
Cdd:cd14616     81 -RCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKIE-----RHGDyMMVRQCNFTSWPEH-GVPESSAPLIHFVK 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1363 EVDKWQAESgDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1431
Cdd:cd14616    154 LVRASRAHD-NTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1201-1440 6.31e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.01  E-value: 6.31e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1201 PRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1280
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1281 QSNSAWPCLQYW--PEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLlvRHFQFLRWSAYrDTPDSRKAFL 1358
Cdd:PHA02747   129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI--SHFQCSEWFED-ETPSDHPDFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1359 HLLAEVDKWQAESGDGRT---------VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQY 1429
Cdd:PHA02747   206 KFIKIIDINRKKSGKLFNpkdallcpiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                          250
                   ....*....|....
gi 1958774396 1430 HF---CYDVALEYL 1440
Cdd:PHA02747   286 LFiqpGYEVLHYFL 299
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 937-1142 6.60e-25

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: 103.92  E-value: 6.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSrYWP-EDSDMYGD-IKI 1014
Cdd:cd17669      1 YINASYI------MGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPnKDEPINCEtFKV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1015 TLVKTETLA-----EYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPVVIHCSAGT 1089
Cdd:cd17669     74 TLIAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958774396 1090 GRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd17669    152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1232-1434 8.19e-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: 103.90  E-value: 8.19e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGT 1311
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPADGSEEYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1312 ANEDLVSRVFRVQN------SSRLQEGHLLVRHFQFLRWsayrdtPDS--RKAFLHLLAEVDKWQA--ESGDGRTVVHCL 1381
Cdd:cd17668     80 VLAYYTVRNFTLRNtkikkgSQKGRPSGRVVTQYHYTQW------PDMgvPEYTLPVLTFVRKASYakRHAVGPVVVHCS 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958774396 1382 NGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1434
Cdd:cd17668    154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1231-1440 3.62e-24

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: 102.15  E-value: 3.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1231 NYINAALTDSYTRsaaFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWP----EPGRQQYGLMEVE 1306
Cdd:cd14540      5 SHITATVGGKQRF---YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTA-EEEGGREKCFRYWPtlggEHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1307 FVSGTANEDLVSRVFRVQNSSRLQegHLLVRHFQFLRWsAYRDTPDSRKAFLHLLAEVDK-----WQAESGDGR---TVV 1378
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQ--SRTVWHLQYTDW-PDHGCPEDVSGFLDFLEEINSvrrhtNQDVAGHNRnppTLV 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958774396 1379 HCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1440
Cdd:cd14540    158 HCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 937-1142 1.02e-23

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: 100.52  E-value: 1.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  937 YISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISK---LVEVGRVkcsrYWP--EDSDMYGD 1011
Cdd:cd17670      1 YINASYI------MGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAEDEFV----YWPsrEESMNCEA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1012 IKITLVKTETLA-----EYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPVVIHCS 1086
Cdd:cd17670     71 FTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDE 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774396 1087 AGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1142
Cdd:cd17670    149 FGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1232-1433 1.08e-23

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: 100.58  E-value: 1.08e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWPEPGRQ--QYGLMEVEFVS 1309
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACR-EFEMGKKKCERYWPEEGEEqlQFGPFKISLEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1310 GTA-NEDLVSRVFRV--QNSSRlqeghlLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGR 1386
Cdd:cd14542     80 EKRvGPDFLIRTLKVtfQKESR------TVYQFHYTAWPD-HGVPSSVDPILDLVRLVRDYQ-GSEDVPICVHCSAGCGR 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1387 SGTFCACATVLEMIRCHSLVD---VFFAAKTLRNYKPNMVETMDQYHFCY 1433
Cdd:cd14542    152 TGTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1232-1441 1.28e-23

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: 100.21  E-value: 1.28e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAaltdSYTRSAA------FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGL--M 1303
Cdd:cd14596      1 YINA----SYITMPVgeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKV-KCHRYWPETLQEPMELenY 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1304 EVEFVSGTANEDLVSRVFR-VQNSSrlQEGHLlVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAEsgdGRTVVHCLN 1382
Cdd:cd14596     76 QLRLENYQALQYFIIRIIKlVEKET--GENRL-IKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT---GPIVVHCSA 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958774396 1383 GGGRSGTFCACATVLEMIR---CHSLVDVffaAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1441
Cdd:cd14596    149 GIGRAGVLICVDVLLSLIEkdlSFNIKDI---VREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1203-1440 1.68e-23

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: 100.67  E-value: 1.68e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1203 NRDKNRSMDVLPPDRCLPFLissdGDPNNYINAALTDSYTRSAAF--IVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1280
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1281 QSNSAwPCLQYWPEPGRQQYGL---MEVEFVSGTANEDLVSRVFRVQNssrLQEGHllVRHFQFLRWSAYRD--TPDSRK 1355
Cdd:cd14597     79 EGGKI-KCQRYWPEILGKTTMVdnrLQLTLVRMQQLKNFVIRVLELED---IQTRE--VRHITHLNFTAWPDhdTPSQPE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1356 AFLHLLAEVDKWQAEsgdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDV 1435
Cdd:cd14597    153 QLLTFISYMRHIHKS---GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                   ....*
gi 1958774396 1436 ALEYL 1440
Cdd:cd14597    230 ILYVL 234
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1232-1429 3.08e-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: 99.13  E-value: 3.08e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEP--GRQQYGLMEVEFVS 1309
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRN-KCAQYWPSMeeGSRAFGDVVVKINE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1310 GTANEDLVSRVFRVQNSSRLQEGHlLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGT 1389
Cdd:cd14557     80 EKICPDYIIRKLNINNKKEKGSGR-EVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN-NFFSGPIVVHCSAGVGRTGT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1958774396 1390 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQY 1429
Cdd:cd14557    157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1164-1431 6.77e-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: 100.31  E-value: 6.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1164 MIRIDPQSNSSQLREEFQTLNSVTPPLDVeecSIALLPRNRDKNRSMDVLPPDRCLPFLISSDgdpnNYINAALTDSYTR 1243
Cdd:cd14600      4 MAQLKKGLESGTVLIQFEQLYRKKPGLAI---TCAKLPQNMDKNRYKDVLPYDATRVVLQGNE----DYINASYVNMEIP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1244 SAA----FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGR-QQYGLMEVEFVSGTANEDLVS 1318
Cdd:cd14600     77 SANivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRT-KCHQYWPDPPDvMEYGGFRVQCHSEDCTIAYVF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1319 RVFRVQNSSRLQEghLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDgrTVVHCLNGGGRSGTFCACATVLE 1398
Cdd:cd14600    156 REMLLTNTQTGEE--RTVTHLQYVAWPDH-GVPDDSSDFLEFVNYVRSKRVENEP--VLVHCSAGIGRTGVLVTMETAMC 230

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1958774396 1399 MIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1431
Cdd:cd14600    231 LTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKF 263
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1336-1438 1.61e-22

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 93.58  E-value: 1.61e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1336 VRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQ-AESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL-VDVFFAAK 1413
Cdd:smart00404    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1958774396  1414 TLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1336-1438 1.61e-22

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: 93.58  E-value: 1.61e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  1336 VRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQ-AESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL-VDVFFAAK 1413
Cdd:smart00012    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1958774396  1414 TLRNYKPNMVETMDQYHFCYDVALE 1438
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1206-1438 2.20e-22

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: 97.60  E-value: 2.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1206 KNRSMDVLPPDRCLP--FLISSDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSN 1283
Cdd:cd14602      1 KNRYKDILPYDHSRVelSLITSDED-SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1284 SAwPCLQYWPEPGRQ--QYGLMEVEFVSGTANEDLVSRVFRVQnssrLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLL 1361
Cdd:cd14602     80 KK-KCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIRTLKVK----FNSETRTIYQFHYKNWPDH-DVPSSIDPILELI 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1362 AEVDKWQAESgDGRTVVHCLNGGGRSGTFCACATVLEMIR------CHSlvdVFFAAKTLRNYKPNMVETMDQYHFCYDV 1435
Cdd:cd14602    154 WDVRCYQEDD-SVPICIHCSAGCGRTGVICAIDYTWMLLKdgiipeNFS---VFSLIQEMRTQRPSLVQTKEQYELVYNA 229


                   ...
gi 1958774396 1436 ALE 1438
Cdd:cd14602    230 VIE 232
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1201-1442 4.18e-22

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: 97.64  E-value: 4.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1201 PRNRDKNRSMDVLPPDRCLpfLISSDGDPN---------NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCT 1271
Cdd:cd14606     16 PENKSKNRYKNILPFDHSR--VILQGRDSNipgsdyinaNYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1272 SIVMLNQLNQSNSAwPCLQYWPEPGRQ-QYGLMEVEFVSGTANEDLVSRVFRV---QNSSRLQEGHllvrHFQFLRWSAY 1347
Cdd:cd14606     94 VIVMTTREVEKGRN-KCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVsplDNGELIREIW----HYQYLSWPDH 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1348 rDTPDSRKAFLHLLAEVDKWQAE-SGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYKPNMV 1423
Cdd:cd14606    169 -GVPSEPGGVLSFLDQINQRQESlPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMV 247

                          250
                   ....*....|....*....
gi 1958774396 1424 ETMDQYHFCYDVALEYLEA 1442
Cdd:cd14606    248 QTEAQYKFIYVAIAQFIET 266
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1223-1439 2.86e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 96.64  E-value: 2.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1223 ISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwpCLQYWPEPgrQQYGL 1302
Cdd:PHA02746    91 VTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEK--CFELWTKE--EDSEL 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1303 MEVEFVSGTAN--EDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAE---------S 1371
Cdd:PHA02746   167 AFGRFVAKILDiiEELSFTKTRLMITDKISDTSREIHHFWFPDWPDN-GIPTGMAEFLELINKVNEEQAElikqadndpQ 245

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774396 1372 GDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYdVALEY 1439
Cdd:PHA02746   246 TLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCY-KALKY 312
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1231-1441 3.73e-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: 93.47  E-value: 3.73e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1231 NYINAALTDSyTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEP-GRQQYGLMEVEFVS 1309
Cdd:cd14601      6 NYINMEIPSS-SIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRV-KCHQYWPEPsGSSSYGGFQVTCHS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1310 GTANEDLVSRVFRVQNSSRLQEGHLLvrHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAeSGDGRTVVHCLNGGGRSGT 1389
Cdd:cd14601     84 EEGNPAYVFREMTLTNLEKNESRPLT--QIQYIAWPDH-GVPDDSSDFLDFVCLVRNKRA-GKDEPVVVHCSAGIGRTGV 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958774396 1390 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1441
Cdd:cd14601    160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1196-1441 1.15e-20

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 93.91  E-value: 1.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1196 SIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAA--FIVTLHPLQSTTPDFWRLVYDYGCTSI 1273
Cdd:cd14599     31 TTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1274 VMLNQLNQSNSAwPCLQYWPEPGRQQYglmevefvSGTANEDLVSRVFRVQN----SSRLQEGHLL------VRHFQFLR 1343
Cdd:cd14599    111 AMVTAEEEGGRS-KSHRYWPKLGSKHS--------SATYGKFKVTTKFRTDSgcyaTTGLKVKHLLsgqertVWHLQYTD 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1344 WSAYrDTPDSRKAFLHLLAEVDKWQ---------AESGDGRTVVHCLNGGGRSGTFCACATvleMIRC---HSLVDVFFA 1411
Cdd:cd14599    182 WPDH-GCPEEVQGFLSYLEEIQSVRrhtnsmldsTKNCNPPIVVHCSAGVGRTGVVILTEL---MIGClehNEKVEVPVM 257

                          250       260       270
                   ....*....|....*....|....*....|
gi 1958774396 1412 AKTLRNYKPNMVETMDQYHFCYDVALEYLE 1441
Cdd:cd14599    258 LRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PHA02738 PHA02738
hypothetical protein; Provisional
 1202-1441 1.24e-19

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 91.52  E-value: 1.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1202 RNRDKNRSMDVLPPDRCLPFLiSSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQ 1281
Cdd:PHA02738    48 KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK-KK 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1282 SNSAWPCLQYWP--EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQN-SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFL 1358
Cdd:PHA02738   126 ENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDgTSATQT----VTHFNFTAWPDH-DVPKNTSEFL 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1359 HLLAEVDKWQAE-------SGDGRT-----VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETM 1426
Cdd:PHA02738   201 NFVLEVRQCQKElaqeslqIGHNRLqpppiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIP 280

                          250
                   ....*....|....*
gi 1958774396 1427 DQYHFCYDVALEYLE 1441
Cdd:PHA02738   281 FQYFFCYRAVKRYVN 295
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1195-1439 4.26e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 86.59  E-value: 4.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1195 CSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1274
Cdd:PHA02742    44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDGG-DDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIV 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1275 MLNQLNQSNSAwPCLQYW--PEPGRQQYGLMEVefvsgtanEDLVSRVFRVQNSSRLQ-----EGHLL-VRHFQFLRWSa 1346
Cdd:PHA02742   123 MITKIMEDGKE-ACYPYWmpHERGKATHGEFKI--------KTKKIKSFRNYAVTNLCltdtnTGASLdIKHFAYEDWP- 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1347 YRDTPDSRKAFLHLLAEVDKWQAE-----SGDGRT-----VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLR 1416
Cdd:PHA02742   193 HGGLPRDPNKFLDFVLAVREADLKadvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLR 272

                          250       260
                   ....*....|....*....|...
gi 1958774396 1417 NYKPNMVETMDQYHFCYDVALEY 1439
Cdd:PHA02742   273 KQRHNCLSLPQQYIFCYFIVLIF 295
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1203-1429 2.60e-17

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: 84.21  E-value: 2.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1203 NRDKNRSMDVLPPD--RCLPFLISSDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1280
Cdd:cd14604     57 NVKKNRYKDILPFDhsRVKLTLKTSSQD-SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1281 QSNSAwPCLQYWPEPGRQ--QYGLMEVEFVSGTANEDLVSRVFRV--QNSSRlqeghlLVRHFQFLRWSAYrDTPDSRKA 1356
Cdd:cd14604    136 EMGRK-KCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLLefQNETR------RLYQFHYVNWPDH-DVPSSFDS 207

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774396 1357 FLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYKPNMVETMDQY 1429
Cdd:cd14604    208 ILDMISLMRKYQ-EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 282
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1232-1441 4.54e-16

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


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 78.86  E-value: 4.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1232 YINAALTDSYTRSAA--FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqLNQSNSAWPCLQYWPEPGRQQYGLMEVEFvs 1309
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVT-AEEEGGREKSFRYWPRLGSRHNTVTYGRF-- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1310 gtaneDLVSRvFRVQN----SSRLQEGHLL------VRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQ--------AES 1371
Cdd:cd14598     78 -----KITTR-FRTDSgcyaTTGLKIKHLLtgqertVWHLQYTDWPEH-GCPEDLKGFLSYLEEIQSVRrhtnstidPKS 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1372 GDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1441
Cdd:cd14598    151 PNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 933-1134 2.71e-14

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 73.97  E-value: 2.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  933 PDADYISANYIDIRINrqgyhrsNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVGRVKCSRYWPEDSDmYGdi 1012
Cdd:cd14559     13 PVGKNLNANRVQIGNK-------NVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGT-YG-- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1013 KITLVKTETLAEYVVRTFA-----LERRGYSARHEVRQFHFTAWPEHG-VPYHATGLLAfiRRVKAST------------ 1074
Cdd:cd14559     83 SVTVKSKKTGKDELVDGLKadmynLKITDGNKTITIPVVHVTNWPDHTaISSEGLKELA--DLVNKSAeekrnfykskgs 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774396 1075 ----PPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTlcSRRVNMIQTEEQY 1134
Cdd:cd14559    161 sainDKNKLLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVSDMRT--SRNGKMVQKDEQL 222
fn3 pfam00041
Fibronectin type III domain;
488-571 1.16e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 1.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  488 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLQPGTTYLFSVRARTS 566
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*
gi 1958774396  567 KGFGQ 571
Cdd:pfam00041   79 GGEGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 478-579 2.18e-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: 67.14  E-value: 2.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  478 DVPGGIAAESLTftplEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPA-VNVPGPrrtisklrNETYHVFSNLQPGTT 556
Cdd:cd00063      2 SPPTNLRVTDVT----STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeVEVTPG--------SETSYTLTGLKPGTE 69

                           90       100
                   ....*....|....*....|....
gi 1958774396  557 YLFSVRARTSKGFGQAA-LTEITT 579
Cdd:cd00063     70 YEFRVRAVNGGGESPPSeSVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
341-618 3.80e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.72  E-value: 3.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  341 LDPDTEYEISVLLTrpGDGGTGRPGPPLlSRTKCAEPTRAPKGLAFAEIQARQLTLQWEP------LGYNVTRCHTYAVS 414
Cdd:COG3401    199 IEPGTTYYYRVAAT--DTGGESAPSNEV-SVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRVYRSNSGDGP 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  415 lcyhYTLGGSHNQTirecvkmergasRYTIKNLLPFRNVHVRLILTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 492
Cdd:COG3401    276 ----FTKVATVTTT------------SYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  493 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLQPGTTYLFSVRARTSKGfgq 571
Cdd:COG3401    338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958774396  572 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 618
Cdd:COG3401    405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 915-1141 3.86e-11

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 65.76  E-value: 3.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  915 PVSAYDRHRVKLHPmlgdpDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCVSVVMISKLVEVg 994
Cdd:PHA02740    61 HITRLLHRRIKLFN-----DEKVLDARFVD------GYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK- 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  995 rvKC-SRYWPEDSD---MYGDIKITLVKTETLAEYVVRTFALERRGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRV 1070
Cdd:PHA02740   129 --KCfNQFWSLKEGcviTSDKFQIETLEIIIKPHFNLTLLSLTDKFGQAQ-KISHFQYTAWPADGFSHDPDAFIDFFCNI 205

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774396 1071 KA--------STPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1141
Cdd:PHA02740   206 DDlcadlekhKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 480-570 2.92e-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: 58.01  E-value: 2.92e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   480 PGGIAAESLTftplEDMIFLKWEEPQEPNGL--ITQYEISYQSIESSDPAVNVPGprrtisklrNETYHVFSNLQPGTTY 557
Cdd:smart00060    4 PSNLRVTDVT----STSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTP---------SSTSYTLTGLKPGTEY 70

                            90
                    ....*....|...
gi 1958774396   558 LFSVRARTSKGFG 570
Cdd:smart00060   71 EFRVRAVNGAGEG 83
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1338-1434 3.69e-08

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 53.12  E-value: 3.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1338 HFQFLRWSAYRDTPDSRKAFLHLLAEVDKwQAESGDGRTVVHCLNGGGRSGTFCACATVlemirCHSLVDVFFAAKTLR- 1416
Cdd:cd14494     22 DSRFLKQLGVTTIVDLTLAMVDRFLEVLD-QAEKPGEPVLVHCKAGVGRTGTLVACYLV-----LLGGMSAEEAVRIVRl 95

                           90
                   ....*....|....*...
gi 1958774396 1417 NYKPNMVETMDQYHFCYD 1434
Cdd:cd14494     96 IRPGGIPQTIEQLDFLIK 113
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1233-1441 1.05e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 55.36  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1233 INAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWpclQYWpepgrqqyglmevefvsgTA 1312
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFN---QFW------------------SL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1313 NEDLV--SRVFRVQNSSRLQEGH----LLV-----------RHFQFLRWSA--YRDTPDSRKAFL----HLLAEVDKWQA 1369
Cdd:PHA02740   138 KEGCVitSDKFQIETLEIIIKPHfnltLLSltdkfgqaqkiSHFQYTAWPAdgFSHDPDAFIDFFcnidDLCADLEKHKA 217

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774396 1370 ESGDGRTVVHCLNGGGRSGTFCA---CATVLEMIRCHSLVDVFfaaKTLRNYKPNMVETMDQYHFCYDVALEYLE 1441
Cdd:PHA02740   218 DGKIAPIIIDCIDGISSSAVFCVfdiCATEFDKTGMLSIANAL---KKVRQKKYGCMNCLDDYVFCYHLIAAYLK 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 1958774396 1039 ARHEVRQFHFtAWPEHGVPyhATGLLAFIRRVKASTPPDAGPVVIHCSAGTGRTG----CYIVLdvMLDMAECEgvvdiy 1114
Cdd:cd14506     73 MRAGIYFYNF-GWKDYGVP--SLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGvliaCYLVY--ALRMSADQ------ 141

                           90       100
                   ....*....|....*....|....*
gi 1958774396 1115 nCVKTLCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14506    142 -AIRLVRSKRPNSIQTRGQVLCVRE 165
fn3 pfam00041
Fibronectin type III domain;
285-359 2.49e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  285 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---NLQTYKLWHLDPDTEYEISVlLTRPGD 358
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 1958774396  359 G 359
Cdd:pfam00041   80 G 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 380-475 2.63e-05

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: 44.41  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  380 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCyhytlgGSHNQTIRECVKMERGASRYTIKNLLPFRNVHVRLIL 459
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR------EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                           90
                   ....*....|....*..
gi 1958774396  460 TNPEGR-KEGKEVTFQT 475
Cdd:cd00063     77 VNGGGEsPPSESVTVTT 93
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1342-1434 4.23e-05

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 45.33  E-value: 4.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1342 LRWSAY--RD--TPDSRKAFLHLLAEVDkwQAESGDGRTVVHCLNGGGRSGTFCACAtvleMIRCHSLVDVFFAAKTLRN 1417
Cdd:cd14505     73 ITWHHLpiPDggVPSDIAQWQELLEELL--SALENGKKVLIHCKGGLGRTGLIAACL----LLELGDTLDPEQAIAAVRA 146

                           90
                   ....*....|....*..
gi 1958774396 1418 YKPNMVETMDQYHFCYD 1434
Cdd:cd14505    147 LRPGAIQTPKQENFLHQ 163
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 280-351 1.70e-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: 41.83  E-value: 1.70e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774396   280 PTPIAPPQLLRAGPTYLIIQ-LNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQT-YKLWHLDPDTEYEISV 351
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1349-1431 2.98e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 42.65  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1349 DTPDSRKAFLHLLAEVDKWQAEsgDGRTVVHCLNGGGRSGTFCACatVLeMIRCHSLVDvffAAKTLRNYKPNMVETMDQ 1428
Cdd:COG2453     58 FGAPDDEQLQEAVDFIDEALRE--GKKVLVHCRGGIGRTGTVAAA--YL-VLLGLSAEE---ALARVRAARPGAVETPAQ 129


                   ...
gi 1958774396 1429 YHF 1431
Cdd:COG2453    130 RAF 132
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1063-1139 3.40e-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: 3.40e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774396 1063 LLAFIRRVKASTPPDAGPVVIHCSAGTGRTGCYIVLDVMLDMAEC-EGVVDIYNcvktlCSRRVNMIQTEEQYIFIHD 1139
Cdd:cd14494     41 MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSaEEAVRIVR-----LIRPGGIPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1039-1139 6.28e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 41.49  E-value: 6.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396 1039 ARHEVRQFHFtAWPEHGVPyHATGLLAFIRRVKASTPPDaGPVVIHCSAGTGRTGCyiVLdVMLDMAECEGVVDIYNCVK 1118
Cdd:COG2453     44 EEAGLEYLHL-PIPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGT--VA-AAYLVLLGLSAEEALARVR 117

                           90       100
                   ....*....|....*....|.
gi 1958774396 1119 tlcSRRVNMIQTEEQYIFIHD 1139
Cdd:COG2453    118 ---AARPGAVETPAQRAFLER 135
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 380-465 1.12e-03

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: 39.52  E-value: 1.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396   380 APKGLAFAEIQARQLTLQWEPLGYNVTRChtYAVslcyHYTLGGSHNQTIRECVKMERGASRYTIKNLLPFRNVHVRLIL 459
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIV----GYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76


                    ....*.
gi 1958774396   460 TNPEGR 465
Cdd:smart00060   77 VNGAGE 82
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 1358-1393 1.42e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 41.03  E-value: 1.42e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958774396 1358 LHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCAC 1393
Cdd:cd14497     80 LEIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICA 115
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1374-1429 3.27e-03

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: 40.85  E-value: 3.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774396 1374 GRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKpnMVETMDQY 1429
Cdd:cd14559    169 LLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVSDMRTSRNGK--MVQKDEQL 222
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1081-1139 3.39e-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: 3.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774396 1081 VVIHCSAGTGRTG----CyivldVMLDMAECEGVVDIYNCVKTLcsrRVNMIQTEEQYIFIHD 1139
Cdd:cd14505    109 VLIHCKGGLGRTGliaaC-----LLLELGDTLDPEQAIAAVRAL---RPGAIQTPKQENFLHQ 163
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 488-566 3.75e-03

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 38.16  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774396  488 LTFTPLEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGprRTISKLRNETYHV-FSNLQPGTTYLFSVRARTS 566
Cdd:pfam16656    6 LSLTGDSTSMTVSWVTPSAVTSPVVQYGTSSSALTSTATATSSTY--TTGDGGTGYIHRAtLTGLEPGTTYYYRVGDDNG 83
 
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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