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Conserved domains on  [gi|755509397|ref|XP_011248513|]
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receptor-type tyrosine-protein phosphatase U isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1256-1462 6.96e-150

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: 453.60  E-value: 6.96e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1415
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 755509397 1416 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
951-1171 1.24e-146

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: 444.88  E-value: 1.24e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYWP 1027
Cdd:cd14632     1 YINANYID------GYHRSNHFIATQG-------------PKQEMVYDFWRMVWQEHCSSIVMITKLVEVgrvKCSKYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVI 1107
Cdd:cd14632    62 DDSDTYGDIKITLLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVV 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509397 1108 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1171
Cdd:cd14632   142 HCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
31-194 5.41e-54

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: 185.62  E-value: 5.41e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397     31 FLAGCTFEEASdpvvPCEFSQAQYDDFQWEQVRIHP---GTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSEN-DTH 106
Cdd:smart00137    2 SPGNCDFEEGS----TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTH 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    107 CVQFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDHKGYIGLDD 186
Cdd:smart00137   78 CLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDD 153

                    ....*...
gi 755509397    187 ILLFSYPC 194
Cdd:smart00137  154 ILLSNGPC 161
fn3 pfam00041
Fibronectin type III domain;
502-585 1.43e-13

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.44  E-value: 1.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   502 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTS 580
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*
gi 755509397   581 KGFGQ 585
Cdd:pfam00041   79 GGEGP 83
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
355-632 1.14e-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: 69.26  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  355 LDPDTEYEISVLLTrpGDGGTGRPGPPlISRTKCAEPTRAPKGLAFAEIQARQLTLQWEP------LGYNVtrchtyavs 428
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRV--------- 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  429 lcYRYTLGGSHNQTIREcVKmergASRYTIKNLLPFRNIHVRLILTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 506
Cdd:COG3401   267 --YRSNSGDGPFTKVAT-VT----TTSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  507 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGfgq 585
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 755509397  586 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 632
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
fn3 pfam00041
Fibronectin type III domain;
299-373 1.97e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   299 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---NLQTYKLWHLDPDTEYEISVlLTRPGD 372
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79

                   .
gi 755509397   373 G 373
Cdd:pfam00041   80 G 80
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
204-290 7.07e-04

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


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 39.80  E-value: 7.07e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    204 GDVEVNAGQNASFQCMAAGraAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGaGVS 283
Cdd:smart00410    2 PSVTVKEGESVTLSCEASG--SPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78

                    ....*..
gi 755509397    284 NFAELIV 290
Cdd:smart00410   79 SGTTLTV 85
 
Name Accession Description Interval E-value
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1256-1462 6.96e-150

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: 453.60  E-value: 6.96e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1415
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 755509397 1416 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
951-1171 1.24e-146

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: 444.88  E-value: 1.24e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYWP 1027
Cdd:cd14632     1 YINANYID------GYHRSNHFIATQG-------------PKQEMVYDFWRMVWQEHCSSIVMITKLVEVgrvKCSKYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVI 1107
Cdd:cd14632    62 DDSDTYGDIKITLLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVV 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509397 1108 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1171
Cdd:cd14632   142 HCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
926-1167 5.37e-94

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 303.01  E-value: 5.37e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   926 RQEPVSAYDRHHVKLHPmlADPDADYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQ 1005
Cdd:pfam00102    6 RYKDVLPYDHTRVKLTG--DPGPSDYINASYID------GYKKPKKYIATQG-------------PLPNTVEDFWRMVWE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  1006 EQCASIVMITKLVE---VKCSRYWP---EDSDMYGDIKITLVKTET-LAEYVVRTFALERRGYSARHEVRQFHFTAWPEH 1078
Cdd:pfam00102   65 EKVTIIVMLTELEEkgrEKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDH 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  1079 GVPYHATGLLAFIRRVKASTP-PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQ 1157
Cdd:pfam00102  145 GVPESPNSLLDLLRKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQ 224
                          250
                   ....*....|
gi 755509397  1158 YIFIHDAILE 1167
Cdd:pfam00102  225 YIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
901-1167 2.67e-91

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 296.11  E-value: 2.67e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    901 GFKQEYE----------SFFEG-WDATKKKDklkggRQEPVSAYDRHHVKLHPMLADPDaDYISANYIDirinrqGYHRS 969
Cdd:smart00194    1 GLEEEFEkldrlkpddeSCTVAaFPENRDKN-----RYKDVLPYDHTRVKLKPPPGEGS-DYINASYID------GPNGP 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    970 NHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWPEDSDM---YGDIKITLVKT 1043
Cdd:smart00194   69 KAYIATQG-------------PLPSTVEDFWRMVWEQKVTVIVMLTELVEkgrEKCAQYWPDEEGEpltYGDITVTLKSV 135
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1044 ETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLD 1123
Cdd:smart00194  136 EKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAID 215
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....
gi 755509397   1124 VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:smart00194  216 ILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1199-1462 1.30e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 280.31  E-value: 1.30e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1199 QLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPL 1278
Cdd:smart00194    1 GLEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1279 QSTTPDFWRLVYDYGCTSIVMLNQLNqSNSAWPCLQYWPEPGR--QQYGLMEVEFVSGTANEDLVSRVFRVQNSSrlQEG 1356
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELV-EKGREKCAQYWPDEEGepLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSE 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1357 HLLVRHFQFLRWSaYRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAA 1436
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233
                           250       260
                    ....*....|....*....|....*.
gi 755509397   1437 KTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1227-1462 1.03e-71

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 239.45  E-value: 1.03e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  1227 NRDKNRSMDVLPPDRCLPFLiSSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1306
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  1307 NSAwPCLQYWPEP--GRQQYGLMEVEFVSGTANE-DLVSRVFRVQNSSRlQEGHLlVRHFQFLRWSAyRDTPDSRKAFLH 1383
Cdd:pfam00102   80 GRE-KCAQYWPEEegESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGS-EETRT-VKHFHYTGWPD-HGVPESPNSLLD 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397  1384 LLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:pfam00102  156 LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
31-194 5.41e-54

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: 185.62  E-value: 5.41e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397     31 FLAGCTFEEASdpvvPCEFSQAQYDDFQWEQVRIHP---GTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSEN-DTH 106
Cdd:smart00137    2 SPGNCDFEEGS----TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTH 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    107 CVQFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDHKGYIGLDD 186
Cdd:smart00137   78 CLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDD 153

                    ....*...
gi 755509397    187 ILLFSYPC 194
Cdd:smart00137  154 ILLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
35-195 3.04e-50

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: 174.86  E-value: 3.04e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    35 CTFEEASDpvvpCEFSQAQYDDFQWEQVRIH-PGTRTPED----LPHGAYLMVNASQHAPGQRAHIIFQTLSENDT-HCV 108
Cdd:pfam00629    1 CDFEDGNL----CGWTQDSSDDFDWERVSGPsVKTGPSSDhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   109 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFwPNEYQVLFEALISPDHKGYIGLDDIL 188
Cdd:pfam00629   77 RFWYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDIS 152

                   ....*..
gi 755509397   189 LFSYPCA 195
Cdd:pfam00629  153 LSSGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
35-194 1.44e-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: 167.17  E-value: 1.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   35 CTFEEAsdpvvPCEFSQAQYDDFQWEQVRIHPGTR-TPEDLPH----GAYLMVNASQHAPGQRAHIIFQTLSEN-DTHCV 108
Cdd:cd06263     1 CDFEDG-----LCGWTQDSTDDFDWTRVSGSTPSPgTPPDHTHgtgsGHYLYVESSSGREGQKARLLSPLLPPPrSSHCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  109 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWpNEYQVLFEALISPDHKGYIGLDDIL 188
Cdd:cd06263    76 SFWYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDIS 151

                  ....*.
gi 755509397  189 LFSYPC 194
Cdd:cd06263   152 LSPGPC 157
PHA02738 PHA02738
hypothetical protein; Provisional
950-1165 8.19e-38

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 145.07  E-value: 8.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  950 DYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYW 1026
Cdd:PHA02738   76 DYINANYVD------GFEYKKKFICGQA-------------PTRQTCYDFYRMLWMEHVQIIVMLCKKKEngrEKCFPYW 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1027 P--EDSDM-YGDIKITLVKTETLAEYVVRTFALERrGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA------- 1096
Cdd:PHA02738  137 SdvEQGSIrFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQcqkelaq 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1097 ---------STPPdagPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1165
Cdd:PHA02738  216 eslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
947-1161 8.33e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 123.66  E-value: 8.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  947 PDADYISANYIDIRINRQgyhrsnhFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE-----VK 1021
Cdd:COG5599    61 ANLGYLNANYIQVIGNHR-------YIATQY-------------PLEEQLEDFFQMLFDNNTPVLVVLASDDEiskpkVK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1022 CSRYWPEDSDmYG--DIKITLVKTETLAEYV-VRTFALERRGYSAR-HEVRQFHFTAWPEHGVPyHATGLLAFIRRVKAS 1097
Cdd:COG5599   121 MPVYFRQDGE-YGkyEVSSELTESIQLRDGIeARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKK 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1098 ---TPPDAGPIVIHCSAGTGRTGCYIVLDVMLDM--AECEGVVDIYNCVKTL-CSRRVNMIQTEEQYIFI 1161
Cdd:COG5599   199 ekiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMrTSRNGGMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
1225-1464 6.43e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.01  E-value: 6.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1225 PRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1304
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1305 QSNSAWPCLQYW--PEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLlvRHFQFLRWSAYrDTPDSRKAFL 1382
Cdd:PHA02747  129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI--SHFQCSEWFED-ETPSDHPDFI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1383 HLLAEVDKWQAESGDGRT---------VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQY 1453
Cdd:PHA02747  206 KFIKIIDINRKKSGKLFNpkdallcpiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285
                         250
                  ....*....|....
gi 755509397 1454 HF---CYDVALEYL 1464
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
fn3 pfam00041
Fibronectin type III domain;
502-585 1.43e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.44  E-value: 1.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   502 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTS 580
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*
gi 755509397   581 KGFGQ 585
Cdd:pfam00041   79 GGEGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
492-593 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 755509397  492 DVPGGIAAESLTftplEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPA-VNVPGPrrtisklrNETYHVFSNLHPGTT 570
Cdd:cd00063     2 SPPTNLRVTDVT----STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeVEVTPG--------SETSYTLTGLKPGTE 69
                          90       100
                  ....*....|....*....|....
gi 755509397  571 YLFSVRARTSKGFGQAA-LTEITT 593
Cdd:cd00063    70 YEFRVRAVNGGGESPPSeSVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
355-632 1.14e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.26  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  355 LDPDTEYEISVLLTrpGDGGTGRPGPPlISRTKCAEPTRAPKGLAFAEIQARQLTLQWEP------LGYNVtrchtyavs 428
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRV--------- 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  429 lcYRYTLGGSHNQTIREcVKmergASRYTIKNLLPFRNIHVRLILTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 506
Cdd:COG3401   267 --YRSNSGDGPFTKVAT-VT----TTSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  507 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGfgq 585
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 755509397  586 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 632
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
494-584 2.94e-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: 2.94e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    494 PGGIAAESLTftplEDMIFLKWEEPQEPNGL--ITQYEISYQSIESSDPAVNVPGprrtisklrNETYHVFSNLHPGTTY 571
Cdd:smart00060    4 PSNLRVTDVT----STSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTP---------SSTSYTLTGLKPGTEY 70
                            90
                    ....*....|...
gi 755509397    572 LFSVRARTSKGFG 584
Cdd:smart00060   71 EFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
299-373 1.97e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   299 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---NLQTYKLWHLDPDTEYEISVlLTRPGD 372
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79

                   .
gi 755509397   373 G 373
Cdd:pfam00041   80 G 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
394-489 3.31e-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: 44.02  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  394 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCyrytlgGSHNQTIRECVKMERGASRYTIKNLLPFRNIHVRLIL 473
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR------EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76
                          90
                  ....*....|....*..
gi 755509397  474 TNPEGR-KEGKEVTFQT 489
Cdd:cd00063    77 VNGGGEsPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
294-365 1.33e-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: 1.33e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509397    294 PTPIAPPQLLRAGPTYLIIQ-LNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQT-YKLWHLDPDTEYEISV 365
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1373-1455 3.36e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 42.27  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1373 DTPDSRKAFLHLLAEVDKWQAEsgDGRTVVHCLNGGGRSGTFCACatVLeMIRCHSLVDvffAAKTLRNYKPNMVETMDQ 1452
Cdd:COG2453    58 FGAPDDEQLQEAVDFIDEALRE--GKKVLVHCRGGIGRTGTVAAA--YL-VLLGLSAEE---ALARVRAARPGAVETPAQ 129

                  ...
gi 755509397 1453 YHF 1455
Cdd:COG2453   130 RAF 132
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
204-290 7.07e-04

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 39.80  E-value: 7.07e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    204 GDVEVNAGQNASFQCMAAGraAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGaGVS 283
Cdd:smart00410    2 PSVTVKEGESVTLSCEASG--SPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78

                    ....*..
gi 755509397    284 NFAELIV 290
Cdd:smart00410   79 SGTTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
394-479 1.87e-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: 38.75  E-value: 1.87e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    394 APKGLAFAEIQARQLTLQWEPLGYNVTRChtYAVSLCYRYTLGGSHNQTirecVKMERGASRYTIKNLLPFRNIHVRLIL 473
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIVGYRVEYREEGSEWKE----VNVTPSSTSYTLTGLKPGTEYEFRVRA 76

                    ....*.
gi 755509397    474 TNPEGR 479
Cdd:smart00060   77 VNGAGE 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
322-386 8.90e-03

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: 37.09  E-value: 8.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397  322 DGPIVRKEIEYRMA-RGPWAEV--HAVNLQTYKLWHLDPDTEYEISVLLTRpgDGGTGRPGPPLISRT 386
Cdd:cd00063    28 GGPITGYVVEYREKgSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVN--GGGESPPSESVTVTT 93
 
Name Accession Description Interval E-value
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1256-1462 6.96e-150

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: 453.60  E-value: 6.96e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1415
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 755509397 1416 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
951-1171 1.24e-146

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: 444.88  E-value: 1.24e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYWP 1027
Cdd:cd14632     1 YINANYID------GYHRSNHFIATQG-------------PKQEMVYDFWRMVWQEHCSSIVMITKLVEVgrvKCSKYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVI 1107
Cdd:cd14632    62 DDSDTYGDIKITLLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVV 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509397 1108 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1171
Cdd:cd14632   142 HCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
951-1170 5.61e-135

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: 413.93  E-value: 5.61e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYWP 1027
Cdd:cd14555     1 YINANYID------GYHRPNHYIATQG-------------PMQETVYDFWRMVWQENSASIVMVTNLVEVgrvKCSRYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVI 1107
Cdd:cd14555    62 DDTEVYGDIKVTLVETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVV 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755509397 1108 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1170
Cdd:cd14555   142 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
886-1170 6.48e-128

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: 397.88  E-value: 6.48e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  886 DLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDiri 961
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGqsapWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  962 nrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYWPEDSDMYGDIKI 1038
Cdd:cd14633    78 ---GYHRPNHYIATQG-------------PMQETIYDFWRMVWHENTASIIMVTNLVEVgrvKCCKYWPDDTEIYKDIKV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1039 TLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGC 1118
Cdd:cd14633   142 TLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGC 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1119 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1170
Cdd:cd14633   222 FIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
1256-1458 1.56e-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: 374.82  E-value: 1.56e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSnsAWPCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPK--DQSCPQYWPDEGSGTYGPIQVEFVSTT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1415
Cdd:cd14556    79 IDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFC 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 755509397 1416 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1458
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
938-1170 2.11e-113

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: 355.87  E-value: 2.11e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  938 VKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKL 1017
Cdd:cd14631     2 VILQPVEDDPSSDYINANYID------GYQRPSHYIATQG-------------PVHETVYDFWRMIWQEQSACIVMVTNL 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1018 VEV---KCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV 1094
Cdd:cd14631    63 VEVgrvKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755509397 1095 KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1170
Cdd:cd14631   143 KLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
930-1171 1.25e-106

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: 338.15  E-value: 1.25e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  930 VSAYDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCA 1009
Cdd:cd14630    12 IISYDHSRVRLQLLDGDPHSDYINANYID------GYHRPRHYIATQG-------------PMQETVKDFWRMIWQENSA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1010 SIVMITKLVEV---KCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATG 1086
Cdd:cd14630    73 SVVMVTNLVEVgrvKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1087 LLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1166
Cdd:cd14630   153 LLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232

                  ....*
gi 755509397 1167 EACLC 1171
Cdd:cd14630   233 EACLC 237
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
930-1171 7.49e-102

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: 325.12  E-value: 7.49e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  930 VSAYDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCA 1009
Cdd:cd14553    12 VIAYDHSRVILQPIEGVPGSDYINANYCD------GYRKQNAYIATQG-------------PLPETFGDFWRMVWEQRSA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1010 SIVMITKLVE---VKCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHAT 1085
Cdd:cd14553    73 TIVMMTKLEErsrVKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1086 GLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1165
Cdd:cd14553   153 PFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232

                  ....*.
gi 755509397 1166 LEACLC 1171
Cdd:cd14553   233 LEAVTC 238
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
926-1167 5.37e-94

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 303.01  E-value: 5.37e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   926 RQEPVSAYDRHHVKLHPmlADPDADYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQ 1005
Cdd:pfam00102    6 RYKDVLPYDHTRVKLTG--DPGPSDYINASYID------GYKKPKKYIATQG-------------PLPNTVEDFWRMVWE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  1006 EQCASIVMITKLVE---VKCSRYWP---EDSDMYGDIKITLVKTET-LAEYVVRTFALERRGYSARHEVRQFHFTAWPEH 1078
Cdd:pfam00102   65 EKVTIIVMLTELEEkgrEKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDH 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  1079 GVPYHATGLLAFIRRVKASTP-PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQ 1157
Cdd:pfam00102  145 GVPESPNSLLDLLRKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQ 224
                          250
                   ....*....|
gi 755509397  1158 YIFIHDAILE 1167
Cdd:pfam00102  225 YIFLYDAILE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
885-1171 2.19e-92

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: 300.03  E-value: 2.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  885 ADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDir 960
Cdd:cd14626     1 SDLADNIERLKANDGLKFSQEYESIDPGqqftWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYID-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  961 inrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP-EDSDMYGDI 1036
Cdd:cd14626    79 ----GYRKQNAYIATQG-------------PLPETLSDFWRMVWEQRTATIVMMTRLEEksrVKCDQYWPiRGTETYGMI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1037 KITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRT 1116
Cdd:cd14626   142 QVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRT 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1117 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1171
Cdd:cd14626   222 GCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
901-1167 2.67e-91

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 296.11  E-value: 2.67e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    901 GFKQEYE----------SFFEG-WDATKKKDklkggRQEPVSAYDRHHVKLHPMLADPDaDYISANYIDirinrqGYHRS 969
Cdd:smart00194    1 GLEEEFEkldrlkpddeSCTVAaFPENRDKN-----RYKDVLPYDHTRVKLKPPPGEGS-DYINASYID------GPNGP 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    970 NHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWPEDSDM---YGDIKITLVKT 1043
Cdd:smart00194   69 KAYIATQG-------------PLPSTVEDFWRMVWEQKVTVIVMLTELVEkgrEKCAQYWPDEEGEpltYGDITVTLKSV 135
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1044 ETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLD 1123
Cdd:smart00194  136 EKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAID 215
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....
gi 755509397   1124 VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:smart00194  216 ILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
1256-1462 1.45e-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: 1.45e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNqsnSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD---AAQLCMQYWPEKTSCCYGPIQVEFVSAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGT 1413
Cdd:cd14634    78 IDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSGT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755509397 1414 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
879-1172 5.81e-88

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: 288.17  E-value: 5.81e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  879 HPAVRVADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISA 954
Cdd:cd14624     1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGqqftWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  955 NYIDirinrqGYHRSNHFIATQGDLaqgqapsappgpkPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP-EDS 1030
Cdd:cd14624    81 NYID------GYRKQNAYIATQGAL-------------PETFGDFWRMIWEQRSATVVMMTKLEErsrVKCDQYWPsRGT 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1031 DMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCS 1110
Cdd:cd14624   142 ETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCS 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1111 AGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCG 1172
Cdd:cd14624   222 AGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
1256-1462 1.10e-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: 283.84  E-value: 1.10e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSawpCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGT 1413
Cdd:cd14636    78 MDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEEcdEGEGRTIIHCLNGGGRSGM 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755509397 1414 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14636   158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
879-1171 1.06e-86

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: 284.29  E-value: 1.06e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  879 HPAVRVADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISA 954
Cdd:cd14625     1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGqqftWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  955 NYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP-EDS 1030
Cdd:cd14625    81 NYID------GYRKQNAYIATQG-------------PLPETFGDFWRMVWEQRSATVVMMTKLEEksrIKCDQYWPsRGT 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1031 DMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCS 1110
Cdd:cd14625   142 ETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCS 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755509397 1111 AGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1171
Cdd:cd14625   222 AGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1199-1462 1.30e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 280.31  E-value: 1.30e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1199 QLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPL 1278
Cdd:smart00194    1 GLEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1279 QSTTPDFWRLVYDYGCTSIVMLNQLNqSNSAWPCLQYWPEPGR--QQYGLMEVEFVSGTANEDLVSRVFRVQNSSrlQEG 1356
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELV-EKGREKCAQYWPDEEGepLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSE 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1357 HLLVRHFQFLRWSaYRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAA 1436
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233
                           250       260
                    ....*....|....*....|....*.
gi 755509397   1437 KTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
951-1163 1.89e-84

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: 274.55  E-value: 1.89e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP 1027
Cdd:cd00047     1 YINASYID------GYRGPKEYIATQG-------------PLPNTVEDFWRMVWEQKVSVIVMLTNLVEkgrEKCERYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSDM---YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGP 1104
Cdd:cd00047    62 EEGGKpleYGDITVTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGP 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1105 IVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1163
Cdd:cd00047   142 IVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
1256-1462 4.24e-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: 270.79  E-value: 4.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNqsnSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVD---PAQLCPQYWPENGVHRHGPIQVEFVSAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGT 1413
Cdd:cd14635    78 LEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755509397 1414 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14635   158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
951-1163 9.76e-83

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: 269.61  E-value: 9.76e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP 1027
Cdd:cd14549     1 YINANYVD------GYNKARAYIATQG-------------PLPSTFDDFWRMVWEQNSAIIVMITNLVErgrRKCDQYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 ED-SDMYGDIKITLVKTETLAEYVVRTFAL------ERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP 1100
Cdd:cd14549    62 KEgTETYGNIQVTLLSTEVLATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPP 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755509397 1101 DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1163
Cdd:cd14549   142 GAGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
933-1162 5.51e-78

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: 256.90  E-value: 5.51e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  933 YDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIV 1012
Cdd:cd14548     8 YDHSRVKLIPINEEEGSDYINANYI------PGYNSPREFIATQG-------------PLPGTKDDFWRMVWEQNSHTIV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1013 MITKLVE---VKCSRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFALERRGYSarHEVRQFHFTAWPEHGVPYHATGL 1087
Cdd:cd14548    69 MLTQCMEkgrVKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLERGDEV--RSVRQFHFTAWPDHGVPEAPDSL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1088 LAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:cd14548   147 LRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1227-1462 1.03e-71

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 239.45  E-value: 1.03e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  1227 NRDKNRSMDVLPPDRCLPFLiSSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1306
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  1307 NSAwPCLQYWPEP--GRQQYGLMEVEFVSGTANE-DLVSRVFRVQNSSRlQEGHLlVRHFQFLRWSAyRDTPDSRKAFLH 1383
Cdd:pfam00102   80 GRE-KCAQYWPEEegESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGS-EETRT-VKHFHYTGWPD-HGVPESPNSLLD 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397  1384 LLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:pfam00102  156 LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
875-1176 3.97e-66

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: 226.06  E-value: 3.97e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  875 TGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESF-----FEGWDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDA 949
Cdd:cd14621     1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALpacpiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  950 DYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYW 1026
Cdd:cd14621    81 DYINASFIN------GYQEKNKFIAAQG-------------PKEETVNDFWRMIWEQNTATIVMVTNLKErkeCKCAQYW 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1027 PEDSD-MYGDIKITLVKTETLAEYVVRTFALERRG----YSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPD 1101
Cdd:cd14621   142 PDQGCwTYGNIRVSVEDVTVLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQY 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1102 AGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTI 1176
Cdd:cd14621   222 AGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
930-1170 9.50e-65

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: 221.06  E-value: 9.50e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  930 VSAYDRHHVKLHPmLADPDA---DYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQE 1006
Cdd:cd17667    36 ILAYDHSRVKLRP-LPGKDSkhsDYINANYVD------GYNKAKAYIATQG-------------PLKSTFEDFWRMIWEQ 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1007 QCASIVMITKLVEV---KCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALER-----------RGYSARHEVRQFH 1071
Cdd:cd17667    96 NTGIIVMITNLVEKgrrKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYH 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1072 FTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNM 1151
Cdd:cd17667   176 YTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYL 255
                         250
                  ....*....|....*....
gi 755509397 1152 IQTEEQYIFIHDAILEACL 1170
Cdd:cd17667   256 VQTEEQYIFIHDALLEAIL 274
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
933-1167 8.22e-64

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: 216.73  E-value: 8.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  933 YDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIV 1012
Cdd:cd14620     7 YDHSRVILSQLDGIPCSDYINASYID------GYKEKNKFIAAQG-------------PKQETVNDFWRMVWEQKSATIV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1013 MITKLVEVK---CSRYWPEDSD-MYGDIKITLVKTETLAEYVVRTFALERR---GYSARHEVRQFHFTAWPEHGVPYHAT 1085
Cdd:cd14620    68 MLTNLKERKeekCYQYWPDQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1086 GLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1165
Cdd:cd14620   148 GMLKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227

                  ..
gi 755509397 1166 LE 1167
Cdd:cd14620   228 LE 229
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
938-1162 3.85e-61

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 208.79  E-value: 3.85e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  938 VKLHPMLADPDADYISANYIdirinrQGY-HRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITK 1016
Cdd:cd14547    14 VCLPSVDDDPLSSYINANYI------RGYdGEEKAYIATQG-------------PLPNTVADFWRMVWQEKTPIIVMITN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1017 LVE--VKCSRYWPEDSDM-YGDIKITLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRR 1093
Cdd:cd14547    75 LTEakEKCAQYWPEEENEtYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509397 1094 VK--ASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIyncVKTLCSRRVN---MIQTEEQYIFIH 1162
Cdd:cd14547   153 VEeaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDV---LGIVCQLRLDrggMVQTAEQYEFVH 223
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
914-1162 3.88e-61

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: 210.68  E-value: 3.88e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  914 DATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKP 993
Cdd:cd14543    22 LCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMD------GYKQKNAYIATQG-------------PLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  994 EMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRTFALERRGYSARHEV 1067
Cdd:cd14543    83 KTYSDFWRMVWEQKVLVIVMTTRVVErgrVKCGQYWPLEEGSslrYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1068 RQFHFTAWPEHGVPYHATGLLAFI--------RRVKASTPPDAG-----PIVIHCSAGTGRTGCYIVLDVMLDMAECEGV 1134
Cdd:cd14543   163 THFQFTSWPDFGVPSSAAALLDFLgevrqqqaLAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGT 242
                         250       260
                  ....*....|....*....|....*...
gi 755509397 1135 VDIYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:cd14543   243 LNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
951-1162 3.97e-61

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: 207.84  E-value: 3.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP 1027
Cdd:cd14551     1 YINASYID------GYQEKNKFIAAQG-------------PKDETVNDFWRMIWEQGSATIVMVTNLKErkeKKCSQYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSD-MYGDIKITLVKTETLAEYVVRTFALERR----GYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDA 1102
Cdd:cd14551    62 DQGCwTYGNLRVRVEDTVVLVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRA 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1103 GPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:cd14551   142 GPIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
926-1167 2.16e-60

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: 206.98  E-value: 2.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  926 RQEPVSAYDRHHVKLhPMLADPDADYISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQ 1005
Cdd:cd14615     2 RYNNVLPYDISRVKL-SVQSHSTDDYINANYM------PGYNSKKEFIAAQG-------------PLPNTVKDFWRMVWE 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1006 EQCASIVMITKLVE---VKCSRYWPED-SDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVP 1081
Cdd:cd14615    62 KNVYAIVMLTKCVEqgrTKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVP 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1082 YHATGLLAF---IRRVKASTPPDaGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQY 1158
Cdd:cd14615   142 ETTDLLINFrhlVREYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQY 220

                  ....*....
gi 755509397 1159 IFIHDAILE 1167
Cdd:cd14615   221 VFLNQCALD 229
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
926-1167 8.75e-60

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 205.51  E-value: 8.75e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  926 RQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQ 1005
Cdd:cd14619     2 RFRNVLPYDWSRVPLKPIHEEPGSDYINANYM------PGYWSSQEFIATQG-------------PLPQTVGDFWRMIWE 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1006 EQCASIVMITKLVE---VKCSRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGV 1080
Cdd:cd14619    63 QQSSTIVMLTNCMEagrVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1081 PYHATGLLAFIRRVKA--STPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQY 1158
Cdd:cd14619   143 PSSTDTLLAFRRLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQY 222

                  ....*....
gi 755509397 1159 IFIHDAILE 1167
Cdd:cd14619   223 VFLHQCILD 231
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
951-1166 5.23e-59

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: 202.13  E-value: 5.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYWP 1027
Cdd:cd17668     1 YINANYVD------GYNKPKAYIAAQG-------------PLKSTAEDFWRMIWEHNVEVIVMITNLVEKgrrKCDQYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 -EDSDMYGDIKITLVKTETLAEYVVRTFALE--------RRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAST 1098
Cdd:cd17668    62 aDGSEEYGNFLVTQKSVQVLAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAK 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1099 PPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1166
Cdd:cd17668   142 RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
933-1162 9.09e-59

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: 202.07  E-value: 9.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  933 YDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGDLaqgqapsapPGPKPemiyDFWRMVWQEQCASIV 1012
Cdd:cd14617     9 YDSTRVKLSNVDDDPCSDYINASYI------PGNNFRREYIATQGPL---------PGTKD----DFWKMVWEQNVHNIV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1013 MITKLVE---VKCSRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFAL--ERRGYSARHeVRQFHFTAWPEHGVPYHAT 1085
Cdd:cd14617    70 MVTQCVEkgrVKCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcsEEQLDAPRL-VRHFHYTVWPDHGVPETTQ 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1086 GLLAFIRRVK--ASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:cd14617   149 SLIQFVRTVRdyINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
933-1165 3.10e-57

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: 198.84  E-value: 3.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  933 YDRHHVKLHPmlADPD---ADYISANYIDIRiNRQGYHRSNH--FIATQGDLAQgqapsappgpkpeMIYDFWRMVWQEQ 1007
Cdd:cd14544    13 FDHTRVILKD--RDPNvpgSDYINANYIRNE-NEGPTTDENAktYIATQGCLEN-------------TVSDFWSMVWQEN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1008 CASIVMITKLVEV---KCSRYWPED--SDMYGDIKITLVKTETLAEYVVRTFALER--RGYSARhEVRQFHFTAWPEHGV 1080
Cdd:cd14544    77 SRVIVMTTKEVERgknKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKldQGDPIR-EIWHYQYLSWPDHGV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1081 PYHATGLLAFIRRV--KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRVNMIQTE 1155
Cdd:cd14544   156 PSDPGGVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTE 235
                         250
                  ....*....|
gi 755509397 1156 EQYIFIHDAI 1165
Cdd:cd14544   236 AQYKFIYVAV 245
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
951-1163 3.87e-57

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: 196.70  E-value: 3.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDIrinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP 1027
Cdd:cd18533     1 YINASYITL-----PGTSSKRYIATQG-------------PLPATIGDFWKMIWQNNVGVIVMLTPLVEngrEKCDQYWP 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSDM--YGDIKITLVKTETLAE--YVVRTFALeRRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA--STPPD 1101
Cdd:cd18533    63 SGEYEgeYGDLTVELVSEEENDDggFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASL 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755509397 1102 AGPIVIHCSAGTGRTGCYIVLDVMLDMAE--------CEGVVD-IYNCVKTLCSRRVNMIQTEEQYIFIHD 1163
Cdd:cd18533   142 DPPIIVHCSAGVGRTGTFIALDSLLDELKrglsdsqdLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
926-1166 9.00e-57

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


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 196.70  E-value: 9.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  926 RQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQ 1005
Cdd:cd14618     2 RYPHVLPYDHSRVRLSQLGGEPHSDYINANFI------PGYTSPQEFIATQG-------------PLKKTIEDFWRLVWE 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1006 EQCASIVMITKLVE---VKCSRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGV 1080
Cdd:cd14618    63 QQVCNIIMLTVGMEngrVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGI 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1081 PYHATGLLAFIRRVKA--STPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQY 1158
Cdd:cd14618   143 PESTSSLMAFRELVREhvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQY 222

                  ....*...
gi 755509397 1159 IFIHDAIL 1166
Cdd:cd14618   223 IFLHSCIL 230
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
951-1168 1.35e-56

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: 195.29  E-value: 1.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDIRINRQGYHrsnhFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP 1027
Cdd:cd14538     1 YINASHIRIPVGGDTYH----YIACQG-------------PLPNTTGDFWQMVWEQKSEVIAMVTQDVEggkVKCHRYWP 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSD----MYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTppDAG 1103
Cdd:cd14538    64 DSLNkpliCGGRLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSG 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1104 PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1168
Cdd:cd14538   142 PIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
951-1162 8.45e-56

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: 192.73  E-value: 8.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP 1027
Cdd:cd14557     1 YINASYID------GFKEPRKYIAAQG-------------PKDETVDDFWRMIWEQKSTVIVMVTRCEEgnrNKCAQYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 ---EDSDMYGDIKITLVKTETLAEYVVRTFAL--ERRGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDA 1102
Cdd:cd14557    62 smeEGSRAFGDVVVKINEEKICPDYIIRKLNInnKKEKGSGR-EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFS 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1103 GPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:cd14557   141 GPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
930-1162 2.12e-55

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: 192.43  E-value: 2.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  930 VSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCA 1009
Cdd:cd14616     6 IKPYNNNRVKLIADAGVPGSDYINASYI------SGYLCPNEFIATQG-------------PLPGTVGDFWRMVWETRAK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1010 SIVMITKLVE---VKCSRYWPEDSD---MYGDIKITLVKTETLAEYVVRTFALERRGYSARheVRQFHFTAWPEHGVPYH 1083
Cdd:cd14616    67 TIVMLTQCFEkgrIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPEHGVPES 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1084 ATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:cd14616   145 SAPLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
1256-1458 2.87e-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: 190.96  E-value: 2.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQ--QYGLMEVEFVS 1333
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGRE-KCERYWPEEGGKplEYGDITVTLVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1334 GTANEDLVSRVFRVQNSSrlQEGHLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGT 1413
Cdd:cd00047    80 EEELSDYTIRTLELSPKG--CSESREVTHLHYTGWPD-HGVPSSPEDLLALVRRVRKEA-RKPNGPIVVHCSAGVGRTGT 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 755509397 1414 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1458
Cdd:cd00047   156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
933-1166 1.58e-54

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


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 190.87  E-value: 1.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  933 YDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIV 1012
Cdd:cd14614    24 YDFSRVKLVSMHEEEGSDYINANYI------PGYNSPQEYIATQG-------------PLPETRNDFWKMVLQQKSQIIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1013 MITKLVE---VKCSRYWP--EDSDMYGDIKITLVKTETLAEYVVRTFaleRRGYS-ARHEVRQFHFTAWPEHGVPY--HA 1084
Cdd:cd14614    85 MLTQCNEkrrVKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREF---RVSYAdEVQDVMHFNYTAWPDHGVPTanAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1085 TGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDA 1164
Cdd:cd14614   162 ESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQC 241

                  ..
gi 755509397 1165 IL 1166
Cdd:cd14614   242 VQ 243
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
31-194 5.41e-54

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: 185.62  E-value: 5.41e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397     31 FLAGCTFEEASdpvvPCEFSQAQYDDFQWEQVRIHP---GTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSEN-DTH 106
Cdd:smart00137    2 SPGNCDFEEGS----TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTH 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    107 CVQFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDHKGYIGLDD 186
Cdd:smart00137   78 CLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDD 153

                    ....*...
gi 755509397    187 ILLFSYPC 194
Cdd:smart00137  154 ILLSNGPC 161
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
933-1166 7.87e-54

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: 188.50  E-value: 7.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  933 YDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIV 1012
Cdd:cd14554    18 YESTRVCLQPIRGVEGSDYINASFID------GYRQRGAYIATQG-------------PLAETTEDFWRMLWEHNSTIIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1013 MITKLVEV---KCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLL 1088
Cdd:cd14554    79 MLTKLREMgreKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1089 AFIRRVKASTPP--DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1166
Cdd:cd14554   159 DFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
950-1168 1.42e-53

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: 186.77  E-value: 1.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  950 DYISANYIDIRINRQGYhrSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYW 1026
Cdd:cd14541     1 DYINANYVNMEIPGSGI--VNRYIAAQG-------------PLPNTCADFWQMVWEQKSTLIVMLTTLVErgrVKCHQYW 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1027 PE--DSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGP 1104
Cdd:cd14541    66 PDlgETMQFGNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEP 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509397 1105 IVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1168
Cdd:cd14541   146 TVVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
951-1163 5.31e-52

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: 181.82  E-value: 5.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEVK---CSRYWP 1027
Cdd:cd14558     1 YINASFID------GYWGPKSLIATQG-------------PLPDTIADFWQMIFQKKVKVIVMLTELKEGDqeqCAQYWG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAG---- 1103
Cdd:cd14558    62 DEKKTYGDIEVELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgr 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1104 --PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1163
Cdd:cd14558   142 svPIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
951-1165 2.96e-51

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: 179.77  E-value: 2.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGDLAQgqapsappgpkpeMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYWP 1027
Cdd:cd14552     1 YINASFID------GYRQKDAYIATQGPLDH-------------TVEDFWRMIWEWKSCSIVMLTEIKERsqnKCAQYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSDM-YGDIKITLVKTETLAEYVVRTFALER-RGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRV-KASTPPDAGP 1104
Cdd:cd14552    62 EDGSVsSGDITVELKDQTDYEDYTLRDFLVTKgKGGSTR-TVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHP 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755509397 1105 IVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1165
Cdd:cd14552   141 ITVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
35-195 3.04e-50

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: 174.86  E-value: 3.04e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    35 CTFEEASDpvvpCEFSQAQYDDFQWEQVRIH-PGTRTPED----LPHGAYLMVNASQHAPGQRAHIIFQTLSENDT-HCV 108
Cdd:pfam00629    1 CDFEDGNL----CGWTQDSSDDFDWERVSGPsVKTGPSSDhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   109 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFwPNEYQVLFEALISPDHKGYIGLDDIL 188
Cdd:pfam00629   77 RFWYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDIS 152

                   ....*..
gi 755509397   189 LFSYPCA 195
Cdd:pfam00629  153 LSSGPCP 159
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
1256-1459 4.52e-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: 4.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEI-KERSQNKCAQYWPEDGSVSSGDITVELKDQT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNSsrlQEGHL-LVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTF 1414
Cdd:cd14552    80 DYEDYTLRDFLVTKG---KGGSTrTVRQFHFHGWPEV-GIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTF 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 755509397 1415 CACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDV 1459
Cdd:cd14552   156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
1222-1461 6.44e-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: 177.33  E-value: 6.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1222 ALLPRNRDKNRSMDVLPPDR---CLPFLISSDGdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1298
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYEStrvCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1299 MLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAyRDTPDSR 1378
Cdd:cd14554    79 MLTKLREMGRE-KCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRT--VRQFQFTDWPE-QGVPKSG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1379 KAFLHLLAEVDKWQAESG-DGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd14554   155 EGFIDFIGQVHKTKEQFGqEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234

                  ....
gi 755509397 1458 DVAL 1461
Cdd:cd14554   235 RAAL 238
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
926-1165 1.92e-49

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: 176.36  E-value: 1.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  926 RQEPVSAYDRHHVKLHPM-LADPDADYISANYI--DIRINRQGYHRSNHFIATQGDLAQgqapsappgpkpeMIYDFWRM 1002
Cdd:cd14605     7 RYKNILPFDHTRVVLHDGdPNEPVSDYINANIImpEFETKCNNSKPKKSYIATQGCLQN-------------TVNDFWRM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1003 VWQEQCASIVMITKLVE---VKCSRYWPEDSDM--YGDIKITLVKTETLAEYVVRTFALERRGY-SARHEVRQFHFTAWP 1076
Cdd:cd14605    74 VFQENSRVIVMTTKEVErgkSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGQgNTERTVWQYHFRTWP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1077 EHGVPYHATGLLAFIRRV--KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRVNM 1151
Cdd:cd14605   154 DHGVPSDPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGM 233
                         250
                  ....*....|....
gi 755509397 1152 IQTEEQYIFIHDAI 1165
Cdd:cd14605   234 VQTEAQYRFIYMAV 247
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
950-1165 1.30e-48

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: 172.11  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  950 DYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYW 1026
Cdd:cd14622     1 DYINASFID------GYRQKDYFIATQG-------------PLAHTVEDFWRMVWEWKCHTIVMLTELQEReqeKCVQYW 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1027 P-EDSDMYGDIKITLvKTETLAEYV-VRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV-KASTPPDAG 1103
Cdd:cd14622    62 PsEGSVTHGEITIEI-KNDTLLETIsIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNH 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1104 PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1165
Cdd:cd14622   141 PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
946-1165 3.47e-48

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 173.12  E-value: 3.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  946 DPDADYISANYIdirinrQGY-HRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV--KC 1022
Cdd:cd14613    51 DPLSSYINANYI------RGYgGEEKVYIATQG-------------PTVNTVGDFWRMVWQERSPIIVMITNIEEMneKC 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1023 SRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---STP 1099
Cdd:cd14613   112 TEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEarqQAE 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1100 PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIyncVKTLCSRRVN---MIQTEEQYIFIHDAI 1165
Cdd:cd14613   190 PNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDI---LRTTCQLRLDrggMIQTCEQYQFVHHVL 255
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
880-1167 1.38e-47

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: 172.61  E-value: 1.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  880 PAVRVADLLQHINQMKTAEGY-GFKQEYESFFEGWDATKK-------KDKLKGgRQEPVSAYDRHHVKLHPMLADPDADY 951
Cdd:cd14628     4 PARNLYAYIQKLTQIETGENVtGMELEFKRLASSKAHTSRfisanlpCNKFKN-RLVNIMPYESTRVCLQPIRGVEGSDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  952 ISANYIDirinrqGYHRSNHFIATQGDLAqgqapsappgpkpEMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYWP- 1027
Cdd:cd14628    83 INASFID------GYRQQKAYIATQGPLA-------------ETTEDFWRMLWEHNSTIVVMLTKLREMgreKCHQYWPa 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP--DAGPI 1105
Cdd:cd14628   144 ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPI 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1106 VIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14628   224 SVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
35-194 1.44e-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: 167.17  E-value: 1.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   35 CTFEEAsdpvvPCEFSQAQYDDFQWEQVRIHPGTR-TPEDLPH----GAYLMVNASQHAPGQRAHIIFQTLSEN-DTHCV 108
Cdd:cd06263     1 CDFEDG-----LCGWTQDSTDDFDWTRVSGSTPSPgTPPDHTHgtgsGHYLYVESSSGREGQKARLLSPLLPPPrSSHCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  109 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWpNEYQVLFEALISPDHKGYIGLDDIL 188
Cdd:cd06263    76 SFWYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDIS 151

                  ....*.
gi 755509397  189 LFSYPC 194
Cdd:cd06263   152 LSPGPC 157
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
946-1162 1.62e-47

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: 170.79  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  946 DPDADYISANYIdirinrQGYH-RSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV--KC 1022
Cdd:cd14612    41 EEEGSYINANYI------RGYDgKEKAYIATQG-------------PMLNTVSDFWEMVWQEECPIIVMITKLKEKkeKC 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1023 SRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS--TPP 1100
Cdd:cd14612   102 VHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESrqTAA 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1101 DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:cd14612   180 SPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
1256-1458 6.29e-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: 6.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWpCLQYWPEpGRQQYGLMEVEFVSGT 1335
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQ-CAQYWGD-EKKTYGDIEVELKDTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNSSRLQegHLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAE--SGDGRT---VVHCLNGGGR 1410
Cdd:cd14558    79 KSPTYTVRVFEITHLKRKD--SRTVYQYQYHKWKG-EELPEKPKDLVDMIKSIKQKLPYknSKHGRSvpiVVHCSDGSSR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 755509397 1411 SGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1458
Cdd:cd14558   156 TGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
945-1167 6.69e-47

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: 168.30  E-value: 6.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  945 ADPDADYISANYIDirinrqGYHRSNhfiatqgdlaqgqAPSAPPGPKPEMIYDFWRMVWQEQCASIVMITKLVE---VK 1021
Cdd:cd14623    20 GEENTDYVNASFID------GYRQKD-------------SYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErgqEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1022 CSRYWPEDSDM-YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP 1100
Cdd:cd14623    81 CAQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1101 DAG-PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14623   161 SGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
930-1167 1.28e-46

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: 169.53  E-value: 1.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  930 VSAYDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGDLAqgqapsappgpkpEMIYDFWRMVWQEQCA 1009
Cdd:cd14627    62 IMPYETTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLA-------------ETTEDFWRMLWENNST 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1010 SIVMITKLVEV---KCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHAT 1085
Cdd:cd14627   123 IVVMLTKLREMgreKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1086 GLLAFIRRVKASTPP--DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1163
Cdd:cd14627   203 GFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282

                  ....
gi 755509397 1164 AILE 1167
Cdd:cd14627   283 AALE 286
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
1255-1463 1.49e-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: 1.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1255 NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSG 1334
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTEL-QEREQEKCVQYWPSEGSVTHGEITIEIKND 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1335 TANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTF 1414
Cdd:cd14622    80 TLLETISIRDFLVTYNQEKQT--RLVRQFHFHGWPEI-GIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTF 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755509397 1415 CACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEY 1463
Cdd:cd14622   157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
919-1166 2.20e-46

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: 166.93  E-value: 2.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  919 KDKLKGGRQEPVSAYDRHHVKLhpmlaDPDADYISANYIDIRINRQGYHrsnhFIATQGdlaqgqapsappgPKPEMIYD 998
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFIKMPVGDEEFV----YIACQG-------------PLPTTVAD 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  999 FWRMVWQEQCASIVMITKLVE---VKCSRYWPED---SDMYGD-IKITLVKTETLAEYVVRTFALERRGYSARHEVRQFH 1071
Cdd:cd14597    59 FWQMVWEQKSTVIAMMTQEVEggkIKCQRYWPEIlgkTTMVDNrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLN 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1072 FTAWPEHGVPYHATGLLAFI---RRVKAStppdaGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRR 1148
Cdd:cd14597   139 FTAWPDHDTPSQPEQLLTFIsymRHIHKS-----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQR 213
                         250
                  ....*....|....*...
gi 755509397 1149 VNMIQTEEQYIFIHDAIL 1166
Cdd:cd14597   214 HGMVQTEDQYIFCYQVIL 231
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
930-1167 1.41e-45

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: 166.82  E-value: 1.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  930 VSAYDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGDLAqgqapsappgpkpEMIYDFWRMVWQEQCA 1009
Cdd:cd14629    62 IMPYELTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLA-------------ETTEDFWRMLWEHNST 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1010 SIVMITKLVEV---KCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHAT 1085
Cdd:cd14629   123 IVVMLTKLREMgreKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGE 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1086 GLLAFIRRVKASTPP--DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1163
Cdd:cd14629   203 GFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYR 282

                  ....
gi 755509397 1164 AILE 1167
Cdd:cd14629   283 AALE 286
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
946-1162 1.99e-45

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


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 163.94  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  946 DPDADYISANYIdirinrQGYH-RSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV--KC 1022
Cdd:cd14611    25 DSLSTYINANYI------RGYGgKEKAFIATQG-------------PMINTVNDFWQMVWQEDSPVIVMITKLKEKneKC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1023 SRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALeRRGYSARHeVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS--TPP 1100
Cdd:cd14611    86 VLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTL-KQGSQSRS-VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDrlASP 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1101 DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:cd14611   164 GRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
1251-1462 3.77e-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: 3.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1251 GDPN-NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEV 1329
Cdd:cd14623    20 GEENtDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE-KCAQYWPSDGSVSYGDITI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1330 EFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGG 1409
Cdd:cd14623    99 ELKKEEECESYTVRDLLVTNTRENKSRQ--IRQFHFHGWPEV-GIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAG 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755509397 1410 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14623   176 RTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
903-1167 7.07e-45

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: 163.90  E-value: 7.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  903 KQEYESFFEGWDATKKKDKLKGgRQEPVSAYDRHHVKLHPmlADPD---ADYISANYIDIRINRQGyHRSNHFIATQGDL 979
Cdd:cd14606     1 KQEVKNLHQRLEGQRPENKSKN-RYKNILPFDHSRVILQG--RDSNipgSDYINANYVKNQLLGPD-ENAKTYIASQGCL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  980 AQgqapsappgpkpeMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWPE--DSDMYGDIKITLVKTETLAEYVVRTF 1054
Cdd:cd14606    77 EA-------------TVNDFWQMAWQENSRVIVMTTREVEkgrNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1055 ALE--RRGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRV--KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAE 1130
Cdd:cd14606   144 QVSplDNGELIR-EIWHYQYLSWPDHGVPSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIS 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 755509397 1131 CEGV---VDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14606   223 TKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQ 262
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
1174-1464 9.50e-45

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: 164.14  E-value: 9.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1174 TTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLnsVTPPLDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISSD 1250
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYETtrvCLQPIRGVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1251 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1330
Cdd:cd14627    80 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1331 FVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAESG-DGRTVVHCLNGGG 1409
Cdd:cd14627   157 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVG 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1410 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1464
Cdd:cd14627   234 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
1174-1468 1.42e-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: 163.75  E-value: 1.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1174 TTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISSD 1250
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKA--HTSRFISANLPCNKFKNRLVNIMPYEStrvCLQPIRGVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1251 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1330
Cdd:cd14628    79 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1331 FVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAESG-DGRTVVHCLNGGG 1409
Cdd:cd14628   156 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVG 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1410 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEALE 1468
Cdd:cd14628   233 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFD 291
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
1198-1457 1.95e-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: 162.53  E-value: 1.95e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1198 SQLREEFQTLnSVTPPLDVEECSiaLLPRNRDKNRSMDVLPPDRCLPFLISSDGDPN-NYINAALTDSYTRSAAFIVTLH 1276
Cdd:cd14543     3 RGIYEEYEDI-RREPPAGTFLCS--LAPANQEKNRYGDVLCLDQSRVKLPKRNGDERtDYINANFMDGYKQKNAYIATQG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1277 PLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWP--EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQ 1354
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVE-RGRVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1355 EghLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEV------------DKWQAESGDGRTVVHCLNGGGRSGTFCA---CAT 1419
Cdd:cd14543   159 S--RQVTHFQFTSWPDF-GVPSSAAALLDFLGEVrqqqalavkamgDRWKGHPPGPPIVVHCSAGIGRTGTFCTldiCLS 235
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 755509397 1420 VLEMIRchsLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd14543   236 QLEDVG---TLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
951-1162 2.40e-44

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: 159.90  E-value: 2.40e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYWP 1027
Cdd:cd14542     1 YINANFI------KGVSGSKAYIATQG-------------PLPNTVLDFWRMIWEYNVQVIVMACREFEMgkkKCERYWP 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSDM---YGDIKITLVKTETLAE-YVVRTFALERRgySARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAG 1103
Cdd:cd14542    62 EEGEEqlqFGPFKISLEKEKRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDV 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1104 PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVD---IYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:cd14542   140 PICVHCSAGCGRTGTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
950-1167 8.21e-44

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: 158.57  E-value: 8.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  950 DYISANYIDIRINRQGYhrSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYW 1026
Cdd:cd14601     1 DYINANYINMEIPSSSI--INRYIACQG-------------PLPNTCSDFWQMTWEQGSSMVVMLTTQVErgrVKCHQYW 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1027 PE--DSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGP 1104
Cdd:cd14601    66 PEpsGSSSYGGFQVTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEP 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755509397 1105 IVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14601   146 VVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
1174-1464 8.41e-44

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: 161.43  E-value: 8.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1174 TTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISSD 1250
Cdd:cd14629     2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKA--HTSRFISANLPCNKFKNRLVNIMPYELtrvCLQPIRGVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1251 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1330
Cdd:cd14629    80 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1331 FVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAESG-DGRTVVHCLNGGG 1409
Cdd:cd14629   157 PMAEYNMPQYILREFKVTDARDGQS--RTIRQFQFTDWPE-QGVPKTGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVG 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1410 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1464
Cdd:cd14629   234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
902-1167 1.29e-43

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: 159.99  E-value: 1.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  902 FKQEYESFFEgwdATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGdlaq 981
Cdd:cd14603    14 FKADYVCSTV---AGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFI------KGVDGSRAYIATQG---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  982 gqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEV---KCSRYWPEDSD--MYGDIKITLVKTETL-AEYVVRTFA 1055
Cdd:cd14603    81 ---------PLSHTVLDFWRMIWQYGVKVILMACREIEMgkkKCERYWAQEQEplQTGPFTITLVKEKRLnEEVILRTLK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1056 LERRGYSarHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVV 1135
Cdd:cd14603   152 VTFQKES--RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIP 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 755509397 1136 D---IYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14603   230 PdfsIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
926-1160 1.54e-43

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: 158.71  E-value: 1.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  926 RQEPVSAYDRHHVKLHpmLADPDADYISANYIDI-RINRQgyhrsnhFIATQGdlaqgqapsappgPKPEMIYDFWRMVW 1004
Cdd:cd14545     3 RYRDRDPYDHDRSRVK--LKQGDNDYINASLVEVeEAKRS-------YILTQG-------------PLPNTSGHFWQMVW 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1005 QEQCASIVMITKLVE---VKCSRYWP-EDSDMYG----DIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWP 1076
Cdd:cd14545    61 EQNSKAVIMLNKLMEkgqIKCAQYWPqGEGNAMIfedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWP 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1077 EHGVPYHATGLLAFIRRVK--ASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV--VDIYNCVKTLCSRRVNMI 1152
Cdd:cd14545   141 DFGVPESPAAFLNFLQKVResGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLI 220

                  ....*...
gi 755509397 1153 QTEEQYIF 1160
Cdd:cd14545   221 QTPDQLRF 228
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
951-1168 5.69e-43

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: 156.06  E-value: 5.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDIRINRQGYHrsnhFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP 1027
Cdd:cd14596     1 YINASYITMPVGEEELF----YIATQG-------------PLPSTIDDFWQMVWENRSDVIAMMTREVErgkVKCHRYWP 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 EDSD---MYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTppDAGP 1104
Cdd:cd14596    64 ETLQepmELENYQLRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGP 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509397 1105 IVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1168
Cdd:cd14596   142 IVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
968-1167 1.61e-42

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: 154.91  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  968 RSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWPED-SDMYGDIKITLVKT 1043
Cdd:cd14546    13 RNPAYIATQG-------------PLPHTIADFWQMIWEQGCVVIVMLTRLQEngvKQCARYWPEEgSEVYHIYEVHLVSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1044 ETLAE-YVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVL 1122
Cdd:cd14546    80 HIWCDdYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 755509397 1123 DVMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14546   160 DMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
926-1167 3.90e-41

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: 151.92  E-value: 3.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  926 RQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQ 1005
Cdd:cd14602     3 RYKDILPYDHSRVELSLITSDEDSDYINANFI------KGVYGPRAYIATQG-------------PLSTTLLDFWRMIWE 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1006 EQCASIVMITKLVEV---KCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRTfaLERRGYSARHEVRQFHFTAWPEHG 1079
Cdd:cd14602    64 YSVLIIVMACMEFEMgkkKCERYWAEPGEMqleFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHD 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1080 VPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAEcEGVV----DIYNCVKTLCSRRVNMIQTE 1155
Cdd:cd14602   142 VPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTK 220
                         250
                  ....*....|..
gi 755509397 1156 EQYIFIHDAILE 1167
Cdd:cd14602   221 EQYELVYNAVIE 232
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
914-1167 7.12e-41

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: 152.88  E-value: 7.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  914 DATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIdirINRQGyhRSNHFIATQGdlaqgqapsappgPKP 993
Cdd:cd14609    35 STAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPI---IEHDP--RMPAYIATQG-------------PLS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  994 EMIYDFWRMVWQEQCASIVMITKLVE--VK-CSRYWP-EDSDMYGDIKITLVKTETLAE-YVVRTFALERRGYSARHEVR 1068
Cdd:cd14609    97 HTIADFWQMVWENGCTVIVMLTPLVEdgVKqCDRYWPdEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1069 QFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSR 1147
Cdd:cd14609   177 QFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQ 256
                         250       260
                  ....*....|....*....|
gi 755509397 1148 RVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14609   257 RPGMVRTKDQFEFALTAVAE 276
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
917-1165 7.27e-41

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: 153.16  E-value: 7.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  917 KKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMI 996
Cdd:cd14604    53 EKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFI------KGVYGPKAYIATQG-------------PLANTV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  997 YDFWRMVWQEQCASIVMITKLVEV---KCSRYWP---EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSarHEVRQF 1070
Cdd:cd14604   114 IDFWRMIWEYNVAIIVMACREFEMgrkKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET--RRLYQF 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1071 HFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDV---MLDMAECEGVVDIYNCVKTLCSR 1147
Cdd:cd14604   192 HYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQ 271
                         250
                  ....*....|....*...
gi 755509397 1148 RVNMIQTEEQYIFIHDAI 1165
Cdd:cd14604   272 RHSAVQTKEQYELVHRAI 289
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
917-1167 2.60e-40

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: 150.98  E-value: 2.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  917 KKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinRQGYHRSNHFIATQGdlaqgqapsappgPKPEMI 996
Cdd:cd14610    40 QREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI-----MDHDPRNPAYIATQG-------------PLPATV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  997 YDFWRMVWQEQCASIVMITKLVE---VKCSRYWP-EDSDMYGDIKITLVKTETLAE-YVVRTFALERRGYSARHEVRQFH 1071
Cdd:cd14610   102 ADFWQMVWESGCVVIVMLTPLAEngvKQCYHYWPdEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVTQFH 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1072 FTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSRRVN 1150
Cdd:cd14610   182 FLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEHLRDQRPG 261
                         250
                  ....*....|....*..
gi 755509397 1151 MIQTEEQYIFIHDAILE 1167
Cdd:cd14610   262 MVQTKEQFEFALTAVAE 278
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
926-1176 1.73e-39

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: 148.64  E-value: 1.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  926 RQEPVSAYDRHHVKLHpmlaDPDADYISANYIDIRINRQGYhrsnhfIATQGdlaqgqapsappgPKPEMIYDFWRMVWQ 1005
Cdd:cd14608    30 RYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSY------ILTQG-------------PLPNTCGHFWEMVWE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1006 EQCASIVMITKLVE---VKCSRYWP--EDSDMY---GDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPE 1077
Cdd:cd14608    87 QKSRGVVMLNRVMEkgsLKCAQYWPqkEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1078 HGVPYHATGLLAFIRRVK--ASTPPDAGPIVIHCSAGTGRTGCYIVLD---VMLDMAECEGVVDIYNCVKTLCSRRVNMI 1152
Cdd:cd14608   167 FGVPESPASFLNFLFKVResGSLSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLI 246
                         250       260
                  ....*....|....*....|....*.
gi 755509397 1153 QTEEQYIFIHDAILEAC--LCGETTI 1176
Cdd:cd14608   247 QTADQLRFSYLAVIEGAkfIMGDSSV 272
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
951-1163 3.08e-39

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 145.24  E-value: 3.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEVK--CSRYWPE 1028
Cdd:cd14556     1 YINAALLD------SYKQPAAFIVTQH-------------PLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDqsCPQYWPD 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1029 D-SDMYGDIKITLVkTETLAEYVV-RTFALER--RGYSARHEVRQFHFTAWPEHG-VPYHATGLLAFIRRV-KASTPPDA 1102
Cdd:cd14556    62 EgSGTYGPIQVEFV-STTIDEDVIsRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGE 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755509397 1103 GPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1163
Cdd:cd14556   141 GPIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
951-1167 2.96e-38

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: 142.98  E-value: 2.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDIRINrqgyHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP 1027
Cdd:cd14540     1 YINASHITATVG----GKQRFYIAAQG-------------PLQNTVGDFWQMVWEQGVYLVVMVTAEEEggrEKCFRYWP 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 -----EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA------ 1096
Cdd:cd14540    64 tlggeHDALTFGEYKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtn 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755509397 1097 ------STPPdagPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14540   144 qdvaghNRNP---PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
1192-1467 5.46e-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: 5.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1192 DPQSNSSQLREEFQTLNSVTPPLDVeeCSIALLPRNRDKNRSMDVLPPDRCLPFL-ISSDGDPNNYINAA-LTDSYTRSA 1269
Cdd:cd14610    11 DHLKNKNRLEKEWEALCAYQAEPNA--TNVAQREENVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASpIMDHDPRNP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1270 AFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFVSGTA-NEDLVSRVFRVQ 1348
Cdd:cd14610    89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAE-NGVKQCYHYWPDEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1349 NssrLQEGHL-LVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAesgdGRT---VVHCLNGGGRSGTFCACATVL-EM 1423
Cdd:cd14610   168 N---LQTNETrTVTQFHFLSWND-QGVPASTRSLLDFRRKVNKCYR----GRScpiIVHCSDGAGRSGTYILIDMVLnKM 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 755509397 1424 IRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEAL 1467
Cdd:cd14610   240 AKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
PHA02738 PHA02738
hypothetical protein; Provisional
950-1165 8.19e-38

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 145.07  E-value: 8.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  950 DYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYW 1026
Cdd:PHA02738   76 DYINANYVD------GFEYKKKFICGQA-------------PTRQTCYDFYRMLWMEHVQIIVMLCKKKEngrEKCFPYW 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1027 P--EDSDM-YGDIKITLVKTETLAEYVVRTFALERrGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA------- 1096
Cdd:PHA02738  137 SdvEQGSIrFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQcqkelaq 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1097 ---------STPPdagPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1165
Cdd:PHA02738  216 eslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
1227-1462 9.64e-38

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


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 142.15  E-value: 9.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1227 NRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQ 1305
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPgSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL-E 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1306 SNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRV--QNSSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLH 1383
Cdd:cd14553    82 ERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKRE----VRQFQFTAWPDH-GVPEHPTPFLA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1384 LLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14553   157 FLRRV-KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
926-1166 1.37e-37

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: 143.07  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  926 RQEPVSAYDRHHVKLhpmlaDPDADYISANYIDIRInrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQ 1005
Cdd:cd14600    45 RYKDVLPYDATRVVL-----QGNEDYINASYVNMEI--PSANIVNKYIATQG-------------PLPHTCAQFWQVVWE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1006 EQCASIVMITKLVE---VKCSRYWPEDSDM--YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGV 1080
Cdd:cd14600   105 QKLSLIVMLTTLTErgrTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGV 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1081 PYHATGLLAFIRRVKaSTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIF 1160
Cdd:cd14600   185 PDDSSDFLEFVNYVR-SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKF 263

                  ....*.
gi 755509397 1161 IHDAIL 1166
Cdd:cd14600   264 VCEAIL 269
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
951-1162 1.51e-37

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: 140.29  E-value: 1.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDIriNRQGYHRSnhFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE----VKCSRYW 1026
Cdd:cd17658     1 YINASLVET--PASESLPK--FIATQG-------------PLPHTFEDFWEMVIQQRCPVIIMLTRLVDnystAKCADYF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1027 P---EDSDMYGDIKITLVKTETLAEyvvrtfALERRGYSARH--------EVRQFHFTAWPEHGVPYHATGLLAFIRRVk 1095
Cdd:cd17658    64 PaeeNESREFGRISVTNKKLKHSQH------SITLRVLEVQYieseepplSVLHIQYPEWPDHGVPKDTRSVRELLKRL- 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755509397 1096 ASTPPDAGPIVIHCSAGTGRTGCYIVLDVML------DMAecegVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:cd17658   137 YGIPPSAGPIVVHCSAGIGRTGAYCTIHNTIrrilegDMS----AVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
1232-1455 3.33e-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: 140.18  E-value: 3.33e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1232 RSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAW 1310
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCME-KGRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1311 PCLQYWPEPGRQQ-YGLMEVEFVSGTANEDLVSRVFRVQNSSRlqegHLLVRHFQFLRWSAYR--DTPDSRKAFLHLLAE 1387
Cdd:cd14548    80 KCDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKLERGDE----VRSVRQFHFTAWPDHGvpEAPDSLLRFVRLVRD 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1388 vdkwQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1455
Cdd:cd14548   156 ----YIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
972-1163 1.40e-36

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: 137.52  E-value: 1.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  972 FIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMI---TKLVEVKCSRYWPED---SDMYGDIKITLVKTET 1045
Cdd:cd14539    17 FIATQA-------------PLPGTAADFWLMVYEQQVSVIVMLvseQENEKQKVHRYWPTErgqALVYGAITVSLQSVRT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1046 LAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---STPPDAGPIVIHCSAGTGRTGCY-IV 1121
Cdd:cd14539    84 TPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCSSGVGRTGAFcLL 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 755509397 1122 LDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1163
Cdd:cd14539   164 YAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
1222-1455 9.35e-36

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: 136.56  E-value: 9.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1222 ALLPRNRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML 1300
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEgSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1301 NQLNQSNSAwPCLQYWP---EPgrQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSAYR-DTPD 1376
Cdd:cd14614    87 TQCNEKRRV-KCDHYWPfteEP--VAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHGvPTAN 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1377 SRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1455
Cdd:cd14614   160 AAESILQFVQMV-RQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
926-1165 1.32e-35

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: 136.63  E-value: 1.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  926 RQEPVSAYDRHHVKLHPMladpDADYISANYIDIRINRQGYhrsnhfIATQGdlaqgqapsappgPKPEMIYDFWRMVWQ 1005
Cdd:cd14607    29 RYRDVSPYDHSRVKLQNT----ENDYINASLVVIEEAQRSY------ILTQG-------------PLPNTCCHFWLMVWQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1006 EQCASIVMITKLVE---VKCSRYWPEDSD---MYGD--IKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPE 1077
Cdd:cd14607    86 QKTKAVVMLNRIVEkdsVKCAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1078 HGVPYHATGLLAFIRRVK--ASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEG--VVDIYNCVKTLCSRRVNMIQ 1153
Cdd:cd14607   166 FGVPESPASFLNFLFKVResGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQ 245
                         250
                  ....*....|..
gi 755509397 1154 TEEQYIFIHDAI 1165
Cdd:cd14607   246 TPDQLRFSYMAV 257
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
1256-1457 3.81e-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: 133.22  E-value: 3.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPClqYWPEPGRQQYG------LMEV 1329
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTD-NELNEDEPI--YWPTKEKPLECetfkvtLSGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1330 EFVSGTANEDLVSRVFRVQNSsrlQEGHLL-VRHFQFLRWSAyRDTPDSrkAFLHLLAEVDKWqAESGDGRTVVHCLNGG 1408
Cdd:cd14550    78 DHSCLSNEIRLIVRDFILEST---QDDYVLeVRQFQCPSWPN-PCSPIH--TVFELINTVQEW-AQQRDGPIVVHDRYGG 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 755509397 1409 GRSGTFCACATVL-EMIRCHSlVDVFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd14550   151 VQAATFCALTTLHqQLEHESS-VDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
1256-1458 4.31e-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: 133.25  E-value: 4.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRR-KCDQYWPKEGTETYGNIQVTLLSTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQN----SSRLQEGHLLVRHFQFLRWSAYrDTPDSRkafLHLLAEVDKWQAES--GDGRTVVHCLNGGG 1409
Cdd:cd14549    80 VLATYTVRTFSLKNlklkKVKGRSSERVVYQYHYTQWPDH-GVPDYT---LPVLSFVRKSSAANppGAGPIVVHCSAGVG 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755509397 1410 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1458
Cdd:cd14549   156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1066-1167 4.72e-35

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 129.40  E-value: 4.72e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1066 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP--PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECE-GVVDIYNCVK 1142
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 755509397   1143 TLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1066-1167 4.72e-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: 129.40  E-value: 4.72e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1066 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP--PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECE-GVVDIYNCVK 1142
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 755509397   1143 TLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
1256-1457 3.03e-34

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 131.03  E-value: 3.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAA-LTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSG 1334
Cdd:cd14546     1 YINAStIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRL-QENGVKQCARYWPEEGSEVYHIYEVHLVSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1335 TA-NEDLVSRVFRVQNssrLQEGHL-LVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKwqaeSGDGRT---VVHCLNGGG 1409
Cdd:cd14546    80 HIwCDDYLVRSFYLKN---LQTSETrTVTQFHFLSWPD-EGIPASAKPLLEFRRKVNK----SYRGRScpiVVHCSDGAG 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755509397 1410 RSGTFCACATVLE-MIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd14546   152 RTGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
1231-1461 4.38e-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: 131.22  E-value: 4.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1231 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqLNQSNSA 1309
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLT-VGMENGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1310 WPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYR--DTPDSRKAFLHLLA 1386
Cdd:cd14618    80 VLCDHYWPsESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERR--VKHLHYTAWPDHGipESTSSLMAFRELVR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1387 EvdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1461
Cdd:cd14618   158 E--HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
1192-1467 5.47e-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: 5.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1192 DPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRClPFLISSDGDPN--NYINAA-LTDSYTRS 1268
Cdd:cd14609     9 DHLRNRDRLAKEWQALCAYQA--EPNTCSTAQGEANVKKNRNPDFVPYDHA-RIKLKAESNPSrsDYINASpIIEHDPRM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1269 AAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFVSGTA-NEDLVSRVFRV 1347
Cdd:cd14609    86 PAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVE-DGVKQCDRYWPDEGSSLYHIYEVNLVSEHIwCEDFLVRSFYL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1348 QNsSRLQEGHLLVRhFQFLRWSAyRDTPDSRKAFLHLLAEVDKwqaeSGDGRT---VVHCLNGGGRSGTFCACATVL-EM 1423
Cdd:cd14609   165 KN-VQTQETRTLTQ-FHFLSWPA-EGIPSSTRPLLDFRRKVNK----CYRGRScpiIVHCSDGAGRTGTYILIDMVLnRM 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 755509397 1424 IRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEAL 1467
Cdd:cd14609   238 AKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
1227-1462 6.43e-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: 6.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1227 NRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQ 1305
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSVDGVPgSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRL-E 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1306 SNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRV--QNSSRLQEghllVRHFQFLRWSAY--RDTPDSRKAF 1381
Cdd:cd14626   120 EKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALykNGSSEKRE----VRQFQFMAWPDHgvPEYPTPILAF 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1382 LHLLAEVDKWQAesgdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1461
Cdd:cd14626   196 LRRVKACNPPDA----GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271

                  .
gi 755509397 1462 E 1462
Cdd:cd14626   272 E 272
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
1231-1462 7.45e-34

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 130.71  E-value: 7.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1231 NRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAw 1310
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1311 PCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYR--DTPDSRKAFLHLLAEV 1388
Cdd:cd14615    80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRT--VRHFHFTSWPDHGvpETTDLLINFRHLVREY 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509397 1389 DKwqAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14615   158 MK--QNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
1227-1462 5.81e-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: 5.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1227 NRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQ 1305
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1306 SNSAwPCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQN--SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLH 1383
Cdd:cd14630    83 VGRV-KCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKkgYHEIRE----IRQFHFTSWPDH-GVPCYATGLLG 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1384 LLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14630   156 FVRQV-KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
1228-1457 2.52e-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: 126.35  E-value: 2.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1228 RDKNRSMDVLPPDRCLPFLISSDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSN 1307
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD---NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1308 SAwPCLQYWPEPGRQQYGL----MEVEFVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAYrDTPDSRKAFLH 1383
Cdd:cd14545    78 QI-KCAQYWPQGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDF-GVPESPAAFLN 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755509397 1384 LLAEV-DKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL--VDVFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd14545   154 FLQKVrESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
1176-1462 9.27e-32

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 126.36  E-value: 9.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1176 IPVNEFkATYREMIRIDpqsNSSQLREEFQTLNsvtpPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDG-DPN 1254
Cdd:cd14625     4 IPISEL-AEHTERLKAN---DNLKLSQEYESID----PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1255 NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSG 1334
Cdd:cd14625    76 DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKL-EEKSRIKCDQYWPSRGTETYGMIQVTLLDT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1335 TANEDLVSRVFRVQN--SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGdGRTVVHCLNGGGRSG 1412
Cdd:cd14625   155 IELATFCVRTFSLHKngSSEKRE----VRQFQFTAWPDH-GVPEYPTPFLAFLRRVKTCNPPDA-GPIVVHCSAGVGRTG 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 755509397 1413 TFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14625   229 CFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
1235-1462 1.61e-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: 123.90  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1235 DVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCL 1313
Cdd:cd14620     3 NILPYDHSRVILSQLDGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE-KCY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1314 QYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQnsSRLQEGH---LLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdK 1390
Cdd:cd14620    82 QYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ--PQLPDGCkapRLVTQLHFTSWPDF-GVPFTPIGMLKFLKKV-K 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1391 WQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14620   158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
1219-1462 2.81e-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: 2.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1219 CSIALLPRNRDKNRSMDVLPPDRCLPFLISSDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1298
Cdd:cd14608    17 CRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED---NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1299 MLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVS----RVFRVQNSSRLQEGHLLvrHFQFLRWSAYrDT 1374
Cdd:cd14608    94 MLNRVMEKGSL-KCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSyytvRQLELENLTTQETREIL--HFHYTTWPDF-GV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1375 PDSRKAFLHLLAEVdkwqAESGD-----GRTVVHCLNGGGRSGTFC---ACATVLEMIRCHSLVDVFFAAKTLRNYKPNM 1446
Cdd:cd14608   170 PESPASFLNFLFKV----RESGSlspehGPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGL 245
                         250
                  ....*....|....*.
gi 755509397 1447 VETMDQYHFCYDVALE 1462
Cdd:cd14608   246 IQTADQLRFSYLAVIE 261
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
1200-1463 3.91e-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: 3.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1200 LREEFQTLNSVtpPLDVEeCSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPN-NYINAALTDSYTRSAAFIVTLHPL 1278
Cdd:cd14621    28 FREEFNALPAC--PIQAT-CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDsDYINASFINGYQEKNKFIAAQGPK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1279 QSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRL--QEG 1356
Cdd:cd14621   105 EETVNDFWRMIWEQNTATIVMVTNLKERKEC-KCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVtnKKP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1357 HLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAA 1436
Cdd:cd14621   184 QRLITQFHFTSWPDF-GVPFTPIGMLKFLKKVKNCNPQYA-GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFV 261
                         250       260
                  ....*....|....*....|....*..
gi 755509397 1437 KTLRNYKPNMVETMDQYHFCYDVALEY 1463
Cdd:cd14621   262 SRIRAQRCQMVQTDMQYVFIYQALLEH 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
947-1161 8.33e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 123.66  E-value: 8.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  947 PDADYISANYIDIRINRQgyhrsnhFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE-----VK 1021
Cdd:COG5599    61 ANLGYLNANYIQVIGNHR-------YIATQY-------------PLEEQLEDFFQMLFDNNTPVLVVLASDDEiskpkVK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1022 CSRYWPEDSDmYG--DIKITLVKTETLAEYV-VRTFALERRGYSAR-HEVRQFHFTAWPEHGVPyHATGLLAFIRRVKAS 1097
Cdd:COG5599   121 MPVYFRQDGE-YGkyEVSSELTESIQLRDGIeARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKK 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1098 ---TPPDAGPIVIHCSAGTGRTGCYIVLDVMLDM--AECEGVVDIYNCVKTL-CSRRVNMIQTEEQYIFI 1161
Cdd:COG5599   199 ekiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMrTSRNGGMVQTSEQLDVL 268
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
1256-1462 8.65e-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: 8.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGrQQYGLMEVEFVSGT 1335
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRV-KCSKYWPDDS-DTYGDIKITLLKTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNssRLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGTFC 1415
Cdd:cd14632    79 TLAEYSVRTFALER--RGYSARHEVKQFHFTSWPEH-GVPYHATGLLAFIRRV-KASTPPDAGPVVVHCSAGAGRTGCYI 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 755509397 1416 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14632   155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
1256-1457 9.01e-31

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: 120.79  E-value: 9.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKE-RKEKKCSQYWPDQGCWTYGNLRVRVEDTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNSSRL--QEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGT 1413
Cdd:cd14551    80 VLVDYTTRKFCIQKVNRGigEKRVRLVTQFHFTSWPDF-GVPFTPIGMLKFLKKV-KSANPPRAGPIVVHCSAGVGRTGT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 755509397 1414 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
1256-1458 1.52e-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: 120.43  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAA-LTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQ-YGLMEVEFVS 1333
Cdd:cd18533     1 YINASyITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVE-NGREKCDQYWPSGEYEGeYGDLTVELVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1334 GTANED--LVSRVFRVQNSsrlQEGHLLVRHFQFLRWSAYRdTPDSRKAFLHLLAEVDKW-QAESGDGRTVVHCLNGGGR 1410
Cdd:cd18533    80 EEENDDggFIVREFELSKE---DGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLIKLKRELnDSASLDPPIIVHCSAGVGR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755509397 1411 SGTFCACATVLEMIRCHSLVD---------VFFAAKTLRNYKPNMVETMDQYHFCYD 1458
Cdd:cd18533   156 TGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
1256-1462 1.73e-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: 120.02  E-value: 1.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEpGRQQYGLMEVEFVSGT 1335
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRV-KCSRYWPD-DTEVYGDIKVTLVETE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQNS--SRLQEghllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGT 1413
Cdd:cd14555    79 PLAEYVVRTFALERRgyHEIRE----VRQFHFTGWPDH-GVPYHATGLLGFIRRV-KASNPPSAGPIVVHCSAGAGRTGC 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755509397 1414 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14555   153 YIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
926-1167 2.72e-30

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: 122.03  E-value: 2.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  926 RQEPVSAYDRHHVKLHPMLADPDAdYISANYIDIRINRQGYHrsnhFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQ 1005
Cdd:cd14599    43 RIREVVPYEENRVELVPTKENNTG-YINASHIKVTVGGEEWH----YIATQG-------------PLPHTCHDFWQMVWE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1006 EQCASIVMITKLVE---VKCSRYWPE-----DSDMYGDIKITL-VKTETLAeYVVRTFALERRGYSARHEVRQFHFTAWP 1076
Cdd:cd14599   105 QGVNVIAMVTAEEEggrSKSHRYWPKlgskhSSATYGKFKVTTkFRTDSGC-YATTGLKVKHLLSGQERTVWHLQYTDWP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1077 EHGVPYHATGLLAF---IRRVKASTPP--DAG-----PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCS 1146
Cdd:cd14599   184 DHGCPEEVQGFLSYleeIQSVRRHTNSmlDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLRE 263
                         250       260
                  ....*....|....*....|.
gi 755509397 1147 RRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14599   264 QRMFMIQTIAQYKFVYQVLIQ 284
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
951-1161 2.83e-30

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: 119.35  E-value: 2.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE-VKCSRYWPED 1029
Cdd:cd14550     1 YINASYL------QGYRRSNEFIITQH-------------PLEHTIKDFWQMIWDHNSQTIVMLTDNELnEDEPIYWPTK 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1030 SDM--YGDIKITLVKTETL-----AEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDA 1102
Cdd:cd14550    62 EKPleCETFKVTLSGEDHSclsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRD 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509397 1103 GPIVIH-----CSAGTgrtgcYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFI 1161
Cdd:cd14550   140 GPIVVHdryggVQAAT-----FCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
1224-1462 3.65e-30

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 121.76  E-value: 3.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1224 LPRNRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQ 1302
Cdd:cd14624    44 LEVNKPKNRYANVIAYDHSRVLLSAIEGIPgSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1303 LnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRV--QNSSRLQEghllVRHFQFLRWSAYrDTPDSRKA 1380
Cdd:cd14624   124 L-EERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALykNGSSEKRE----VRQFQFTAWPDH-GVPEHPTP 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1381 FLHLLAEVDKWQAESGdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVA 1460
Cdd:cd14624   198 FLAFLRRVKTCNPPDA-GPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276

                  ..
gi 755509397 1461 LE 1462
Cdd:cd14624   277 LE 278
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
1256-1458 6.10e-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: 118.64  E-value: 6.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAA-FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLnQLNQSNSAWPCLQYWPEPGRQQ--YGLMEVEFV 1332
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVML-VSEQENEKQKVHRYWPTERGQAlvYGAITVSLQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1333 SGTANEDLVSRVFRVQNssRLQEGHLLVRHFQFLRWSAYRdTPDSRKAFLHLLAEVDKW--QAESGDGRTVVHCLNGGGR 1410
Cdd:cd14539    80 SVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHylQQRSLQTPIVVHCSSGVGR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755509397 1411 SGTFCAC-ATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1458
Cdd:cd14539   157 TGAFCLLyAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
902-1167 2.00e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 120.11  E-value: 2.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  902 FKQEYESFFEG------WDATKKKDkLKGGRQEPVSAYDRHHVKLHpmLADPDADYISANYIDirinrqGYHRSNHFIAT 975
Cdd:PHA02742   28 LKEEHEHIMQEivafscNESLELKN-MKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVD------GHNAKGRFICT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  976 QGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYW---PEDSDMYGDIKITLVKTETLAEY 1049
Cdd:PHA02742   99 QA-------------PLEETALDFWQAIFQDQVRVIVMITKIMEdgkEACYPYWmphERGKATHGEFKIKTKKIKSFRNY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1050 VVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV-----------KASTPPDAGPIVIHCSAGTGRTGC 1118
Cdd:PHA02742  166 AVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVKEPPILVHCSAGLDRAGA 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 755509397 1119 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:PHA02742  246 FCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
1221-1457 3.18e-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: 118.14  E-value: 3.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1221 IALLPRNRDKNRSMDVLPPDRCLPFLISSDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML 1300
Cdd:cd14607    18 VAKYPENRNRNRYRDVSPYDHSRVKLQNTE---NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1301 NQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVS----RVFRVQNssrLQEGHL-LVRHFQFLRWSAYrDTP 1375
Cdd:cd14607    95 NRIVEKDSV-KCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSyytvHLLQLEN---INSGETrTISHFHYTTWPDF-GVP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1376 DSRKAFLHLLAEVdkwqAESG-----DGRTVVHCLNGGGRSGTFCACATVLEMIRCHS--LVDVFFAAKTLRNYKPNMVE 1448
Cdd:cd14607   170 ESPASFLNFLFKV----RESGslspeHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQ 245

                  ....*....
gi 755509397 1449 TMDQYHFCY 1457
Cdd:cd14607   246 TPDQLRFSY 254
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
1256-1457 3.23e-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: 116.41  E-value: 3.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAAL--TDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQ--YGLMEVEF 1331
Cdd:cd17658     1 YINASLveTPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAKCADYFPAEENESreFGRISVTN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1332 VS-GTANEDLVSRVFRVQNsSRLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdkWQAESGDGRTVVHCLNGGGR 1410
Cdd:cd17658    81 KKlKHSQHSITLRVLEVQY-IESEEPPLSVLHIQYPEWPDH-GVPKDTRSVRELLKRL--YGIPPSAGPIVVHCSAGIGR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755509397 1411 SGTFCACATVLEMIRCHSL--VDVFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd17658   157 TGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
1225-1457 1.27e-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: 116.85  E-value: 1.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1225 PRNRDKNRSMDVLPPDR---CLPFLISSDGdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1301
Cdd:cd14603    28 KENVKKNRYKDILPYDQtrvILSLLQEEGH--SDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMAC 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1302 QlNQSNSAWPCLQYWP-EPGRQQYGLMEVEFVSGT-ANEDLVSRVFRV--QNSSRlqeghlLVRHFQFLRWSAyRDTPDS 1377
Cdd:cd14603   106 R-EIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKVtfQKESR------SVSHFQYMAWPD-HGIPDS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1378 RKAFLHLLAEVDKWQAESGDgRTVVHCLNGGGRSGTFCACATV-----LEMIRCH-SLVDVFFaakTLRNYKPNMVETMD 1451
Cdd:cd14603   178 PDCMLAMIELARRLQGSGPE-PLCVHCSAGCGRTGVICTVDYVrqlllTQRIPPDfSIFDVVL---EMRKQRPAAVQTEE 253

                  ....*.
gi 755509397 1452 QYHFCY 1457
Cdd:cd14603   254 QYEFLY 259
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
1227-1465 2.32e-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: 115.64  E-value: 2.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1227 NRDKNRSMDVLPPDRCLpfLISSDGDPN----NYINAaltdSYTRSAA-----------FIVTLHPLQSTTPDFWRLVYD 1291
Cdd:cd14544     1 NKGKNRYKNILPFDHTR--VILKDRDPNvpgsDYINA----NYIRNENegpttdenaktYIATQGCLENTVSDFWSMVWQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1292 YGCTSIVML-NQLNQSNSAwpCLQYWPEPGRQ-QYGLMEVEFVSGTANEDLVSRVFRVqnsSRLQEGHLL--VRHFQFLR 1367
Cdd:cd14544    75 ENSRVIVMTtKEVERGKNK--CVRYWPDEGMQkQYGPYRVQNVSEHDTTDYTLRELQV---SKLDQGDPIreIWHYQYLS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1368 WSAYrDTPDSRKAFLHLLAEVDKWQAESGD-GRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYK 1443
Cdd:cd14544   150 WPDH-GVPSDPGGVLNFLEDVNQRQESLPHaGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQR 228
                         250       260
                  ....*....|....*....|..
gi 755509397 1444 PNMVETMDQYHFCYDVALEYLE 1465
Cdd:cd14544   229 SGMVQTEAQYKFIYVAVAQYIE 250
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
913-1162 2.68e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 117.02  E-value: 2.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  913 WDATKKKDKLKGGRQEPVSAYDRHHVKLHPMlADPDADYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPK 992
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWID------GFEDDKKFIATQG-------------PF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  993 PEMIYDFWRMVWQEQCASIVMI--TKLV--EVKCSRYW--PEDSDM-YGDIKITLVKTETLAEYVVRTFALERRGYSARH 1065
Cdd:PHA02747  103 AETCADFWKAVWQEHCSIIVMLtpTKGTngEEKCYQYWclNEDGNIdMEDFRIETLKTSVRAKYILTLIEITDKILKDSR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1066 EVRQFHFTAWPEHGVPYHATGLLAFI------RRVKAS--TPPDA--GPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVV 1135
Cdd:PHA02747  183 KISHFQCSEWFEDETPSDHPDFIKFIkiidinRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAI 262
                         250       260
                  ....*....|....*....|....*..
gi 755509397 1136 DIYNCVKTLCSRRVNMIQTEEQYIFIH 1162
Cdd:PHA02747  263 CLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
1214-1459 3.28e-28

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 115.34  E-value: 3.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1214 LDVEECSIALLPRnrdKNRSMDVLPPDRCLPFLISSD-GDP-NNYINAALTDSY-TRSAAFIVTLHPLQSTTPDFWRLVY 1290
Cdd:cd14613    15 VDPKEYDIPGLVR---KNRYKTILPNPHSRVCLTSPDqDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVW 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1291 DYGCTSIVMLNQLNQSNSAwpCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSA 1370
Cdd:cd14613    92 QERSPIIVMITNIEEMNEK--CTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITLKSGGEERG----LKHYWYTSWPD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1371 YRdTPDSRKAFLHLLAEVD--KWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVE 1448
Cdd:cd14613   165 QK-TPDNAPPLLQLVQEVEeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQ 243
                         250
                  ....*....|.
gi 755509397 1449 TMDQYHFCYDV 1459
Cdd:cd14613   244 TCEQYQFVHHV 254
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
1231-1457 4.92e-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: 113.86  E-value: 4.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1231 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSA 1309
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1310 wPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLqEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEV 1388
Cdd:cd14617    81 -KCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQL-DAPRLVRHFHYTVWPDH-GVPETTQSLIQFVRTV 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1389 -DKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd14617   158 rDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
1227-1465 5.18e-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: 5.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1227 NRDKNRSMDVLPPDRCLpfLISSDGDPN----NYINA--ALTDSYTRS------AAFIVTLHPLQSTTPDFWRLVYDYGC 1294
Cdd:cd14605     2 NKNKNRYKNILPFDHTR--VVLHDGDPNepvsDYINAniIMPEFETKCnnskpkKSYIATQGCLQNTVNDFWRMVFQENS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1295 TSIVMLNQLNQSNSAwPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVqnsSRLQEGHL--LVRHFQFLRWSAY 1371
Cdd:cd14605    80 RVIVMTTKEVERGKS-KCVKYWPdEYALKEYGVMRVRNVKESAAHDYILRELKL---SKVGQGNTerTVWQYHFRTWPDH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1372 rDTPDSRKAFLHLLAEVD-KWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYKPNMV 1447
Cdd:cd14605   156 -GVPSDPGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMV 234
                         250
                  ....*....|....*...
gi 755509397 1448 ETMDQYHFCYDVALEYLE 1465
Cdd:cd14605   235 QTEAQYRFIYMAVQHYIE 252
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
951-1167 5.86e-28

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: 113.53  E-value: 5.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDIRINRQGYHrsnhFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVE---VKCSRYWP 1027
Cdd:cd14598     1 YINASHIKVTVGGKEWD----YIATQG-------------PLQNTCQDFWQMVWEQGVAIIAMVTAEEEggrEKSFRYWP 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 -----EDSDMYGDIKITL-VKTETLAeYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFI-------RRV 1094
Cdd:cd14598    64 rlgsrHNTVTYGRFKITTrFRTDSGC-YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLeeiqsvrRHT 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1095 KASTPPDAG--PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14598   143 NSTIDPKSPnpPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
1231-1455 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 755509397 1231 NRSMDVLPPDR---CLPfliSSDGDP-NNYINAaltdSYTR-----SAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1301
Cdd:cd14547     1 NRYKTILPNEHsrvCLP---SVDDDPlSSYINA----NYIRgydgeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMIT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1302 QLNQSNSAwpCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSAYRdTPDSRKAF 1381
Cdd:cd14547    74 NLTEAKEK--CAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRY----LKHYWYTSWPDHK-TPEAAQPL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1382 LHLLAEVDKW-QAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1455
Cdd:cd14547   147 LSLVQEVEEArQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
1224-1457 7.23e-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: 7.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1224 LPRNRDKNRSMDVLP-PDR--CLPFLISSDgDPNNYINAALTDSYT-RSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVM 1299
Cdd:cd14612    12 IPGHASKDRYKTILPnPQSrvCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1300 LNQLNQSNSAwpCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQnssrLQEGHLLVRHFQFLRWSAYRdTPDSRK 1379
Cdd:cd14612    91 ITKLKEKKEK--CVHYWPEK-EGTYGRFEIRVQDMKECDGYTIRDLTIQ----LEEESRSVKHYWFSSWPDHQ-TPESAG 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1380 AFLHLLAEVDKW-QAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd14612   163 PLLRLVAEVEESrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
991-1167 1.01e-27

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 112.04  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  991 PKPEMIYDFWRMVWQEQCASIVMITKLVEVK-CSRYWPEDSD-MYGDIKITLVKTETLAEYVVRTF-----ALERRGYSA 1063
Cdd:cd14634    22 PLPNTVADFWRLVFDYNCSSVVMLNEMDAAQlCMQYWPEKTScCYGPIQVEFVSADIDEDIISRIFricnmARPQDGYRI 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1064 rheVRQFHFTAWPEH-GVPYHATGLLAFIRRV-KASTPPDA--GPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYN 1139
Cdd:cd14634   102 ---VQHLQYIGWPAYrDTPPSKRSILKVVRRLeKWQEQYDGreGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFH 178
                         170       180
                  ....*....|....*....|....*...
gi 755509397 1140 CVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14634   179 TVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
1256-1461 1.87e-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: 1.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqlNQSNSAWPCLQYWP---EPGRQQ---YGLMEV 1329
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLP--DGQNMAEDEFVYWPnkdEPINCEtfkVTLIAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1330 EFVSGTANEDLVSRVFRVQNSsrlQEGHLL-VRHFQFLRWSayrdTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGG 1408
Cdd:cd17669    79 EHKCLSNEEKLIIQDFILEAT---QDDYVLeVRHFQCPKWP----NPDSPISKTFELISIIKEEAANRDGPMIVHDEHGG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755509397 1409 GRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1461
Cdd:cd17669   152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
1256-1461 1.95e-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: 1.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML--NQ-LNQSNSAwpclqYWPEpgRQQ--------Y 1324
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQgLAEDEFV-----YWPS--REEsmnceaftV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1325 GLMEVEFVSGTANEDLVSRVFRVQNSsrlQEGHLL-VRHFQFLRWSayrdTPDSRKAFLHLLAEVDKWQAESGDGRTVVH 1403
Cdd:cd17670    74 TLISKDRLCLSNEEQIIIHDFILEAT---QDDYVLeVRHFQCPKWP----NPDAPISSTFELINVIKEEALTRDGPTIVH 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1404 CLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1461
Cdd:cd17670   147 DEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
1225-1462 2.99e-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: 2.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1225 PRNRDKNRSMDVLPPDRC---LPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1301
Cdd:cd17667    25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1302 QLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNS--SRLQEGHLLVRH-------FQFLRWsayr 1372
Cdd:cd17667   105 NLVEKGRR-KCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTkvKKGQKGNPKGRQnertviqYHYTQW---- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1373 dtPDS--RKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVE 1448
Cdd:cd17667   180 --PDMgvPEYALPVLTFVRRSSAArtPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQ 257
                         250
                  ....*....|....
gi 755509397 1449 TMDQYHFCYDVALE 1462
Cdd:cd17667   258 TEEQYIFIHDALLE 271
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
1230-1457 3.44e-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: 111.16  E-value: 3.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1230 KNRSMDVLPPDRCLPFL--ISSDGDPNNYINAALTDSYT-RSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1306
Cdd:cd14611     2 KNRYKTILPNPHSRVCLkpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1307 NSAwpCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSAYRdTPDSRKAFLHLLA 1386
Cdd:cd14611    82 NEK--CVLYWPEK-RGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRS----VKHYWYTSWPDHK-TPDSAQPLLQLML 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1387 EVDKWQAES-GDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd14611   154 DVEEDRLASpGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1256-1455 4.47e-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: 110.50  E-value: 4.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAA----FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPG-RQQYGLMEVE 1330
Cdd:cd14541     2 YINANYVNMEIPGSGivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRV-KCHQYWPDLGeTMQFGNLQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1331 FVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDgRTVVHCLNGGGR 1410
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERH--ITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRVGMVE-PTVVHCSAGIGR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 755509397 1411 SGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1455
Cdd:cd14541   157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
1231-1464 4.57e-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: 111.13  E-value: 4.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1231 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSA 1309
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPgSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME-AGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1310 WPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNssRLQEGHLLVRHFQFLRWSAY--RDTPDSRKAFLHLLA 1386
Cdd:cd14619    80 VKCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQ--VEEQKTLSVRHFHFTAWPDHgvPSSTDTLLAFRRLLR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1387 EVDKWQAESGDgrTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1464
Cdd:cd14619   158 QWLDQTMSGGP--TVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
951-1167 6.35e-27

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: 109.73  E-value: 6.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEVK-CSRYWPED 1029
Cdd:cd14636     1 YINAALMD------SYRQPAAFIVTQH-------------PLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQgCPQYWPEE 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1030 SDM-YGDIKITLVKTETLAEYVVRTFAL-----ERRGYSArheVRQFHFTAWPEH-GVPYHATGLLAFIRRV---KASTP 1099
Cdd:cd14636    62 GMLrYGPIQVECMSCSMDCDVISRIFRIcnltrPQEGYLM---VQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECD 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1100 PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14636   139 EGEGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
1256-1464 1.93e-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: 108.62  E-value: 1.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAaltdSYTR------SAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWPEPGRQQ---YGL 1326
Cdd:cd14538     1 YINA----SHIRipvggdTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQ-DVEGGKVKCHRYWPDSLNKPlicGGR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1327 MEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAesgDGRTVVHCLN 1406
Cdd:cd14538    76 LEVSLEKYQSLQDFVIRRISLRDKETGEVHH--ITHLNFTTWPDH-GTPQSADPLLRFIRYMRRIHN---SGPIVVHCSA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1407 GGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1464
Cdd:cd14538   150 GIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
951-1167 2.12e-26

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 108.46  E-value: 2.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATqgdlaqgqapsapPGPKPEMIYDFWRMVWQEQCASIVMITKLVEVK----CSRYW 1026
Cdd:cd14637     1 YINAALTD------SYTRSAAFIVT-------------LHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNsawpCLQYW 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1027 PEDS-DMYGDIKITLVKTETLAEYVVRTFALER--RGYSARHEVRQFHFTAW-PEHGVPYHATGLLAFIRRV-KASTPPD 1101
Cdd:cd14637    62 PEPGlQQYGPMEVEFVSGSADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESG 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755509397 1102 AGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14637   142 EGRTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
1227-1462 2.36e-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: 110.52  E-value: 2.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1227 NRDKNRSMDVLPPDRCLPFLISSDGDPN-NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQ 1305
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETSsDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1306 SNSAwPCLQYWPEpGRQQYGLMEVEFVSGTANEDLVSRVFRVQN--SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLH 1383
Cdd:cd14633   120 VGRV-KCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFAVEKrgVHEIRE----IRQFHFTGWPDH-GVPYHATGLLG 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1384 LLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14633   193 FVRQV-KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
1250-1462 1.03e-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: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1250 DGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGrQQYGLME 1328
Cdd:cd14631     8 EDDPsSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRV-KCYKYWPDDT-EVYGDFK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1329 VEFVSGTANEDLVSRVFRVQNS--SRLQEghllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLN 1406
Cdd:cd14631    86 VTCVEMEPLAEYVVRTFTLERRgyNEIRE----VKQFHFTGWPDH-GVPYHATGLLSFIRRV-KLSNPPSAGPIVVHCSA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755509397 1407 GGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:cd14631   160 GAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
1231-1455 3.04e-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: 105.76  E-value: 3.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1231 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSA 1309
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1310 wPCLQYWPEPGR--QQYGLMEVEFVSGTANEDLVSRVFRVQnssrlQEGH-LLVRHFQFLRWSAYrDTPDSRKAFLHLLA 1386
Cdd:cd14616    81 -RCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKIE-----RHGDyMMVRQCNFTSWPEH-GVPESSAPLIHFVK 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509397 1387 EVDKWQAESgDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1455
Cdd:cd14616   154 LVRASRAHD-NTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
1225-1464 6.43e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.01  E-value: 6.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1225 PRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1304
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1305 QSNSAWPCLQYW--PEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLlvRHFQFLRWSAYrDTPDSRKAFL 1382
Cdd:PHA02747  129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI--SHFQCSEWFED-ETPSDHPDFI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1383 HLLAEVDKWQAESGDGRT---------VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQY 1453
Cdd:PHA02747  206 KFIKIIDINRKKSGKLFNpkdallcpiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285
                         250
                  ....*....|....
gi 755509397 1454 HF---CYDVALEYL 1464
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
1256-1458 7.22e-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: 7.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGT 1335
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPADGSEEYGNFLVTQKSVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1336 ANEDLVSRVFRVQN------SSRLQEGHLLVRHFQFLRWsayrdtPDS--RKAFLHLLAEVDKWQA--ESGDGRTVVHCL 1405
Cdd:cd17668    80 VLAYYTVRNFTLRNtkikkgSQKGRPSGRVVTQYHYTQW------PDMgvPEYTLPVLTFVRKASYakRHAVGPVVVHCS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755509397 1406 NGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1458
Cdd:cd17668   154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1255-1464 2.40e-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: 102.92  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1255 NYINAALTDSYTRsaaFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWP----EPGRQQYGLMEVE 1330
Cdd:cd14540     5 SHITATVGGKQRF---YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTA-EEEGGREKCFRYWPtlggEHDALTFGEYKVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1331 FVSGTANEDLVSRVFRVQNSSRLQegHLLVRHFQFLRWsAYRDTPDSRKAFLHLLAEVDK-----WQAESGDGR---TVV 1402
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQ--SRTVWHLQYTDW-PDHGCPEDVSGFLDFLEEINSvrrhtNQDVAGHNRnppTLV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1403 HCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1464
Cdd:cd14540   158 HCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
951-1167 5.76e-24

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: 101.30  E-value: 5.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEVK-CSRYWPED 1029
Cdd:cd14635     1 YINAALMD------SYKQPSAFIVTQH-------------PLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQlCPQYWPEN 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1030 S-DMYGDIKITLVKTETLAEYVVRTFAL--ERRGYSARHEVRQFHFTAWPEH-GVPYHATGLLAFIRRV-KASTPPDAGP 1104
Cdd:cd14635    62 GvHRHGPIQVEFVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdKWQEEYNGGE 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1105 --IVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1167
Cdd:cd14635   142 grTVVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
1256-1465 8.23e-24

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


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 100.98  E-value: 8.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAaltdSYTRSAA------FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGL--M 1327
Cdd:cd14596     1 YINA----SYITMPVgeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKV-KCHRYWPETLQEPMELenY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1328 EVEFVSGTANEDLVSRVFR-VQNSSrlQEGHLlVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAEsgdGRTVVHCLN 1406
Cdd:cd14596    76 QLRLENYQALQYFIIRIIKlVEKET--GENRL-IKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT---GPIVVHCSA 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1407 GGGRSGTFCACATVLEMIR---CHSLVDVffaAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1465
Cdd:cd14596   149 GIGRAGVLICVDVLLSLIEkdlSFNIKDI---VREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
1256-1457 8.63e-24

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: 8.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWPEPGRQ--QYGLMEVEFVS 1333
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACR-EFEMGKKKCERYWPEEGEEqlQFGPFKISLEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1334 GTA-NEDLVSRVFRV--QNSSRlqeghlLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGR 1410
Cdd:cd14542    80 EKRvGPDFLIRTLKVtfQKESR------TVYQFHYTAWPD-HGVPSSVDPILDLVRLVRDYQ-GSEDVPICVHCSAGCGR 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 755509397 1411 SGTFCACATVLEMIRCHSLVD---VFFAAKTLRNYKPNMVETMDQYHFCY 1457
Cdd:cd14542   152 TGTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
1227-1464 1.60e-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: 101.06  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1227 NRDKNRSMDVLPPDRCLPFLissdGDPNNYINAALTDSYTRSAAF--IVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1304
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1305 QSNSAwPCLQYWPEPGRQQYGL---MEVEFVSGTANEDLVSRVFRVQNssrLQEGHllVRHFQFLRWSAYRD--TPDSRK 1379
Cdd:cd14597    79 EGGKI-KCQRYWPEILGKTTMVdnrLQLTLVRMQQLKNFVIRVLELED---IQTRE--VRHITHLNFTAWPDhdTPSQPE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1380 AFLHLLAEVDKWQAEsgdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDV 1459
Cdd:cd14597   153 QLLTFISYMRHIHKS---GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229

                  ....*
gi 755509397 1460 ALEYL 1464
Cdd:cd14597   230 ILYVL 234
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
1256-1453 2.66e-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: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEP--GRQQYGLMEVEFVS 1333
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRN-KCAQYWPSMeeGSRAFGDVVVKINE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1334 GTANEDLVSRVFRVQNSSRLQEGHlLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGT 1413
Cdd:cd14557    80 EKICPDYIIRKLNINNKKEKGSGR-EVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN-NFFSGPIVVHCSAGVGRTGT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 755509397 1414 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQY 1453
Cdd:cd14557   157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
946-1165 3.98e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 102.03  E-value: 3.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  946 DPDADYISANYIDirinrqGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKL--VEVKCS 1023
Cdd:PHA02746   95 DNAENYIHANFVD------GFKEANKFICAQG-------------PKEDTSEDFFKLISEHESQVIVSLTDIddDDEKCF 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1024 RYW--PEDSDM-YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---- 1096
Cdd:PHA02746  156 ELWtkEEDSELaFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqae 235
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1097 ------STPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1165
Cdd:PHA02746  236 likqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
1188-1455 4.59e-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: 100.69  E-value: 4.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1188 MIRIDPQSNSSQLREEFQTLNSVTPPLDVeecSIALLPRNRDKNRSMDVLPPDRCLPFLISSDgdpnNYINAALTDSYTR 1267
Cdd:cd14600     4 MAQLKKGLESGTVLIQFEQLYRKKPGLAI---TCAKLPQNMDKNRYKDVLPYDATRVVLQGNE----DYINASYVNMEIP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1268 SAA----FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGR-QQYGLMEVEFVSGTANEDLVS 1342
Cdd:cd14600    77 SANivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRT-KCHQYWPDPPDvMEYGGFRVQCHSEDCTIAYVF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1343 RVFRVQNSSRLQEghLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDgrTVVHCLNGGGRSGTFCACATVLE 1422
Cdd:cd14600   156 REMLLTNTQTGEE--RTVTHLQYVAWPDH-GVPDDSSDFLEFVNYVRSKRVENEP--VLVHCSAGIGRTGVLVTMETAMC 230
                         250       260       270
                  ....*....|....*....|....*....|...
gi 755509397 1423 MIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1455
Cdd:cd14600   231 LTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKF 263
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1360-1462 1.15e-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: 93.96  E-value: 1.15e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1360 VRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQ-AESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL-VDVFFAAK 1437
Cdd:smart00012    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 755509397   1438 TLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1360-1462 1.15e-22

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 93.96  E-value: 1.15e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   1360 VRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQ-AESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL-VDVFFAAK 1437
Cdd:smart00404    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 755509397   1438 TLRNYKPNMVETMDQYHFCYDVALE 1462
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
1230-1462 1.96e-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: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1230 KNRSMDVLPPDRCLP--FLISSDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSN 1307
Cdd:cd14602     1 KNRYKDILPYDHSRVelSLITSDED-SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1308 SAwPCLQYWPEPGRQ--QYGLMEVEFVSGTANEDLVSRVFRVQnssrLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLL 1385
Cdd:cd14602    80 KK-KCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIRTLKVK----FNSETRTIYQFHYKNWPDH-DVPSSIDPILELI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1386 AEVDKWQAESgDGRTVVHCLNGGGRSGTFCACATVLEMIR------CHSlvdVFFAAKTLRNYKPNMVETMDQYHFCYDV 1459
Cdd:cd14602   154 WDVRCYQEDD-SVPICIHCSAGCGRTGVICAIDYTWMLLKdgiipeNFS---VFSLIQEMRTQRPSLVQTKEQYELVYNA 229

                  ...
gi 755509397 1460 ALE 1462
Cdd:cd14602   230 VIE 232
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
1225-1466 3.77e-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: 98.03  E-value: 3.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1225 PRNRDKNRSMDVLPPDRCLpfLISSDGDPN---------NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCT 1295
Cdd:cd14606    16 PENKSKNRYKNILPFDHSR--VILQGRDSNipgsdyinaNYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1296 SIVMLNQLNQSNSAwPCLQYWPEPGRQ-QYGLMEVEFVSGTANEDLVSRVFRV---QNSSRLQEGHllvrHFQFLRWSAY 1371
Cdd:cd14606    94 VIVMTTREVEKGRN-KCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVsplDNGELIREIW----HYQYLSWPDH 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1372 rDTPDSRKAFLHLLAEVDKWQAE-SGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYKPNMV 1447
Cdd:cd14606   169 -GVPSEPGGVLSFLDQINQRQESlPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMV 247
                         250
                  ....*....|....*....
gi 755509397 1448 ETMDQYHFCYDVALEYLEA 1466
Cdd:cd14606   248 QTEAQYKFIYVAIAQFIET 266
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
951-1166 9.75e-22

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: 95.06  E-value: 9.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMIT---KLVEVKCSrYWP 1027
Cdd:cd17669     1 YINASYI------MGYYQSNEFIITQH-------------PLLHTIKDFWRMIWDHNAQLIVMLPdgqNMAEDEFV-YWP 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 -EDSDMYGD-IKITLVKTETLA-----EYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPP 1100
Cdd:cd17669    61 nKDEPINCEtFKVTLIAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAAN 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755509397 1101 DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1166
Cdd:cd17669   139 RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
1247-1463 2.92e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 96.64  E-value: 2.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1247 ISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwpCLQYWPEPgrQQYGL 1326
Cdd:PHA02746   91 VTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEK--CFELWTKE--EDSEL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1327 MEVEFVSGTAN--EDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAE---------S 1395
Cdd:PHA02746  167 AFGRFVAKILDiiEELSFTKTRLMITDKISDTSREIHHFWFPDWPDN-GIPTGMAEFLELINKVNEEQAElikqadndpQ 245
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1396 GDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYdVALEY 1463
Cdd:PHA02746  246 TLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCY-KALKY 312
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
1255-1465 3.05e-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: 93.86  E-value: 3.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1255 NYINAALTDSyTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEP-GRQQYGLMEVEFVS 1333
Cdd:cd14601     6 NYINMEIPSS-SIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRV-KCHQYWPEPsGSSSYGGFQVTCHS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1334 GTANEDLVSRVFRVQNSSRLQEGHLLvrHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAeSGDGRTVVHCLNGGGRSGT 1413
Cdd:cd14601    84 EEGNPAYVFREMTLTNLEKNESRPLT--QIQYIAWPDH-GVPDDSSDFLDFVCLVRNKRA-GKDEPVVVHCSAGIGRTGV 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755509397 1414 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1465
Cdd:cd14601   160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
951-1166 3.48e-21

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 93.20  E-value: 3.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  951 YISANYIdirinrQGYHRSNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITK---LVEVKcSRYWP 1027
Cdd:cd17670     1 YINASYI------MGYYRSNEFIITQH-------------PLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAEDE-FVYWP 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1028 --EDSDMYGDIKITLVKTETLA-----EYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPP 1100
Cdd:cd17670    61 srEESMNCEAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALT 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755509397 1101 DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1166
Cdd:cd17670   139 RDGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
1220-1465 1.02e-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: 94.29  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1220 SIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAA--FIVTLHPLQSTTPDFWRLVYDYGCTSI 1297
Cdd:cd14599    31 TTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1298 VMLNQLNQSNSAwPCLQYWPEPGRQQYglmevefvSGTANEDLVSRVFRVQN----SSRLQEGHLL------VRHFQFLR 1367
Cdd:cd14599   111 AMVTAEEEGGRS-KSHRYWPKLGSKHS--------SATYGKFKVTTKFRTDSgcyaTTGLKVKHLLsgqertVWHLQYTD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1368 WSAYrDTPDSRKAFLHLLAEVDKWQ---------AESGDGRTVVHCLNGGGRSGTFCACATvleMIRC---HSLVDVFFA 1435
Cdd:cd14599   182 WPDH-GCPEEVQGFLSYLEEIQSVRrhtnsmldsTKNCNPPIVVHCSAGVGRTGVVILTEL---MIGClehNEKVEVPVM 257
                         250       260       270
                  ....*....|....*....|....*....|
gi 755509397 1436 AKTLRNYKPNMVETMDQYHFCYDVALEYLE 1465
Cdd:cd14599   258 LRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PHA02738 PHA02738
hypothetical protein; Provisional
1226-1465 7.89e-20

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 92.30  E-value: 7.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1226 RNRDKNRSMDVLPPDRCLPFLiSSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQ 1305
Cdd:PHA02738   48 KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK-KK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1306 SNSAWPCLQYWP--EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQN-SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFL 1382
Cdd:PHA02738  126 ENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDgTSATQT----VTHFNFTAWPDH-DVPKNTSEFL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1383 HLLAEVDKWQAE-------SGDGRT-----VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETM 1450
Cdd:PHA02738  201 NFVLEVRQCQKElaqeslqIGHNRLqpppiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIP 280
                         250
                  ....*....|....*
gi 755509397 1451 DQYHFCYDVALEYLE 1465
Cdd:PHA02738  281 FQYFFCYRAVKRYVN 295
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
1219-1463 4.34e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 86.59  E-value: 4.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1219 CSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1298
Cdd:PHA02742   44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDGG-DDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1299 MLNQLNQSNSAwPCLQYW--PEPGRQQYGLMEVefvsgtanEDLVSRVFRVQNSSRLQ-----EGHLL-VRHFQFLRWSa 1370
Cdd:PHA02742  123 MITKIMEDGKE-ACYPYWmpHERGKATHGEFKI--------KTKKIKSFRNYAVTNLCltdtnTGASLdIKHFAYEDWP- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1371 YRDTPDSRKAFLHLLAEVDKWQAE-----SGDGRT-----VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLR 1440
Cdd:PHA02742  193 HGGLPRDPNKFLDFVLAVREADLKadvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLR 272
                         250       260
                  ....*....|....*....|...
gi 755509397 1441 NYKPNMVETMDQYHFCYDVALEY 1463
Cdd:PHA02742  273 KQRHNCLSLPQQYIFCYFIVLIF 295
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
1227-1453 2.65e-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: 2.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1227 NRDKNRSMDVLPPD--RCLPFLISSDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1304
Cdd:cd14604    57 NVKKNRYKDILPFDhsRVKLTLKTSSQD-SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1305 QSNSAwPCLQYWPEPGRQ--QYGLMEVEFVSGTANEDLVSRVFRV--QNSSRlqeghlLVRHFQFLRWSAYrDTPDSRKA 1380
Cdd:cd14604   136 EMGRK-KCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLLefQNETR------RLYQFHYVNWPDH-DVPSSFDS 207
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755509397 1381 FLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYKPNMVETMDQY 1453
Cdd:cd14604   208 ILDMISLMRKYQ-EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 282
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
1256-1465 4.62e-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: 4.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1256 YINAALTDSYTRSAA--FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqLNQSNSAWPCLQYWPEPGRQQYGLMEVEFvs 1333
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVT-AEEEGGREKSFRYWPRLGSRHNTVTYGRF-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1334 gtaneDLVSRvFRVQN----SSRLQEGHLL------VRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQ--------AES 1395
Cdd:cd14598    78 -----KITTR-FRTDSgcyaTTGLKIKHLLtgqertVWHLQYTDWPEH-GCPEDLKGFLSYLEEIQSVRrhtnstidPKS 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1396 GDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1465
Cdd:cd14598   151 PNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
fn3 pfam00041
Fibronectin type III domain;
502-585 1.43e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.44  E-value: 1.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   502 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTS 580
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*
gi 755509397   581 KGFGQ 585
Cdd:pfam00041   79 GGEGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
492-593 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 755509397  492 DVPGGIAAESLTftplEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPA-VNVPGPrrtisklrNETYHVFSNLHPGTT 570
Cdd:cd00063     2 SPPTNLRVTDVT----STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeVEVTPG--------SETSYTLTGLKPGTE 69
                          90       100
                  ....*....|....*....|....
gi 755509397  571 YLFSVRARTSKGFGQAA-LTEITT 593
Cdd:cd00063    70 YEFRVRAVNGGGESPPSeSVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
355-632 1.14e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.26  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  355 LDPDTEYEISVLLTrpGDGGTGRPGPPlISRTKCAEPTRAPKGLAFAEIQARQLTLQWEP------LGYNVtrchtyavs 428
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRV--------- 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  429 lcYRYTLGGSHNQTIREcVKmergASRYTIKNLLPFRNIHVRLILTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 506
Cdd:COG3401   267 --YRSNSGDGPFTKVAT-VT----TTSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  507 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGfgq 585
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 755509397  586 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 632
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
494-584 2.94e-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: 2.94e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    494 PGGIAAESLTftplEDMIFLKWEEPQEPNGL--ITQYEISYQSIESSDPAVNVPGprrtisklrNETYHVFSNLHPGTTY 571
Cdd:smart00060    4 PSNLRVTDVT----STSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTP---------SSTSYTLTGLKPGTEY 70
                            90
                    ....*....|...
gi 755509397    572 LFSVRARTSKGFG 584
Cdd:smart00060   71 EFRVRAVNGAGEG 83
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
947-1158 3.27e-10

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 61.65  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  947 PDADYISANYIDIRINrqgyhrsNHFIATQGdlaqgqapsappgPKPEMIYDFWRMVWQEQCASIVMITKLVEVKCsRYW 1026
Cdd:cd14559    13 PVGKNLNANRVQIGNK-------NVAIACQY-------------PKNEQLEDHLKMLADNRTPCLVVLASNKDIQR-KGL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1027 PE---DSDMYGdiKITLVKTETLAEYVVRTFA-----LERRGYSARHEVRQFHFTAWPEHG-VPYHATGLLAfiRRVKAS 1097
Cdd:cd14559    72 PPyfrQSGTYG--SVTVKSKKTGKDELVDGLKadmynLKITDGNKTITIPVVHVTNWPDHTaISSEGLKELA--DLVNKS 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755509397 1098 T----------------PPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTlcSRRVNMIQTEEQY 1158
Cdd:cd14559   148 AeekrnfykskgssainDKNKLLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVSDMRT--SRNGKMVQKDEQL 222
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
999-1165 7.80e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 61.91  E-value: 7.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  999 FWRMVWQEQCASIVMITKLVEVKC-SRYWPEDSD---MYGDIKITLVKTETLAEYVVRTFALERRGYSARhEVRQFHFTA 1074
Cdd:PHA02740  107 FLQALSDNKVQIIVLISRHADKKCfNQFWSLKEGcviTSDKFQIETLEIIIKPHFNLTLLSLTDKFGQAQ-KISHFQYTA 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1075 WPEHGVPYHATGLLAFIRRVKA--------STPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCS 1146
Cdd:PHA02740  186 WPADGFSHDPDAFIDFFCNIDDlcadlekhKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQ 265
                         170
                  ....*....|....*....
gi 755509397 1147 RRVNMIQTEEQYIFIHDAI 1165
Cdd:PHA02740  266 KKYGCMNCLDDYVFCYHLI 284
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
1362-1458 3.68e-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: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1362 HFQFLRWSAYRDTPDSRKAFLHLLAEVDKwQAESGDGRTVVHCLNGGGRSGTFCACATVlemirCHSLVDVFFAAKTLR- 1440
Cdd:cd14494    22 DSRFLKQLGVTTIVDLTLAMVDRFLEVLD-QAEKPGEPVLVHCKAGVGRTGTLVACYLV-----LLGGMSAEEAVRIVRl 95
                          90
                  ....*....|....*...
gi 755509397 1441 NYKPNMVETMDQYHFCYD 1458
Cdd:cd14494    96 IRPGGIPQTIEQLDFLIK 113
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
1257-1465 1.07e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 55.36  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1257 INAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWpclQYWpepgrqqyglmevefvsgTA 1336
Cdd:PHA02740   79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFN---QFW------------------SL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1337 NEDLV--SRVFRVQNSSRLQEGH----LLV-----------RHFQFLRWSA--YRDTPDSRKAFL----HLLAEVDKWQA 1393
Cdd:PHA02740  138 KEGCVitSDKFQIETLEIIIKPHfnltLLSltdkfgqaqkiSHFQYTAWPAdgFSHDPDAFIDFFcnidDLCADLEKHKA 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755509397 1394 ESGDGRTVVHCLNGGGRSGTFCA---CATVLEMIRCHSLVDVFfaaKTLRNYKPNMVETMDQYHFCYDVALEYLE 1465
Cdd:PHA02740  218 DGKIAPIIIDCIDGISSSAVFCVfdiCATEFDKTGMLSIANAL---KKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
1063-1163 2.97e-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: 52.74  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1063 ARHEVRQFHFtAWPEHGVPyhATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTG----CYIVLdvMLDMAECEgvvdiy 1138
Cdd:cd14506    73 MRAGIYFYNF-GWKDYGVP--SLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGvliaCYLVY--ALRMSADQ------ 141
                          90       100
                  ....*....|....*....|....*
gi 755509397 1139 nCVKTLCSRRVNMIQTEEQYIFIHD 1163
Cdd:cd14506   142 -AIRLVRSKRPNSIQTRGQVLCVRE 165
fn3 pfam00041
Fibronectin type III domain;
299-373 1.97e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397   299 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---NLQTYKLWHLDPDTEYEISVlLTRPGD 372
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79

                   .
gi 755509397   373 G 373
Cdd:pfam00041   80 G 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
394-489 3.31e-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: 44.02  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397  394 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCyrytlgGSHNQTIRECVKMERGASRYTIKNLLPFRNIHVRLIL 473
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR------EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76
                          90
                  ....*....|....*..
gi 755509397  474 TNPEGR-KEGKEVTFQT 489
Cdd:cd00063    77 VNGGGEsPPSESVTVTT 93
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
1366-1458 4.83e-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: 4.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1366 LRWSAY--RD--TPDSRKAFLHLLAEVDkwQAESGDGRTVVHCLNGGGRSGTFCACAtvleMIRCHSLVDVFFAAKTLRN 1441
Cdd:cd14505    73 ITWHHLpiPDggVPSDIAQWQELLEELL--SALENGKKVLIHCKGGLGRTGLIAACL----LLELGDTLDPEQAIAAVRA 146
                          90
                  ....*....|....*..
gi 755509397 1442 YKPNMVETMDQYHFCYD 1458
Cdd:cd14505   147 LRPGAIQTPKQENFLHQ 163
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
294-365 1.33e-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: 1.33e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509397    294 PTPIAPPQLLRAGPTYLIIQ-LNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQT-YKLWHLDPDTEYEISV 365
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
1087-1163 3.33e-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: 3.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397 1087 LLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAEC-EGVVDIYNcvktlCSRRVNMIQTEEQYIFIHD 1163
Cdd:cd14494    41 MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSaEEAVRIVR-----LIRPGGIPQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1373-1455 3.36e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 42.27  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1373 DTPDSRKAFLHLLAEVDKWQAEsgDGRTVVHCLNGGGRSGTFCACatVLeMIRCHSLVDvffAAKTLRNYKPNMVETMDQ 1452
Cdd:COG2453    58 FGAPDDEQLQEAVDFIDEALRE--GKKVLVHCRGGIGRTGTVAAA--YL-VLLGLSAEE---ALARVRAARPGAVETPAQ 129

                  ...
gi 755509397 1453 YHF 1455
Cdd:COG2453   130 RAF 132
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
204-290 7.07e-04

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 39.80  E-value: 7.07e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    204 GDVEVNAGQNASFQCMAAGraAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGaGVS 283
Cdd:smart00410    2 PSVTVKEGESVTLSCEASG--SPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78

                    ....*..
gi 755509397    284 NFAELIV 290
Cdd:smart00410   79 SGTTLTV 85
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
1382-1417 1.32e-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: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755509397 1382 LHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCAC 1417
Cdd:cd14497    80 LEIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICA 115
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
394-479 1.87e-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: 38.75  E-value: 1.87e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397    394 APKGLAFAEIQARQLTLQWEPLGYNVTRChtYAVSLCYRYTLGGSHNQTirecVKMERGASRYTIKNLLPFRNIHVRLIL 473
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIVGYRVEYREEGSEWKE----VNVTPSSTSYTLTGLKPGTEYEFRVRA 76

                    ....*.
gi 755509397    474 TNPEGR 479
Cdd:smart00060   77 VNGAGE 82
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1063-1163 2.78e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.57  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509397 1063 ARHEVRQFHFtAWPEHGVPyHATGLLAFIRRVKASTPPDaGPIVIHCSAGTGRTGCyiVLdVMLDMAECEGVVDIYNCVK 1142
Cdd:COG2453    44 EEAGLEYLHL-PIPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGT--VA-AAYLVLLGLSAEEALARVR 117
                          90       100
                  ....*....|....*....|.
gi 755509397 1143 tlcSRRVNMIQTEEQYIFIHD 1163
Cdd:COG2453   118 ---AARPGAVETPAQRAFLER 135
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
1398-1453 3.32e-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: 3.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755509397 1398 GRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKpnMVETMDQY 1453
Cdd:cd14559   169 LLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVSDMRTSRNGK--MVQKDEQL 222
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
1105-1163 7.38e-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: 38.78  E-value: 7.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755509397 1105 IVIHCSAGTGRTG----CyivldVMLDMAECEGVVDIYNCVKTLcsrRVNMIQTEEQYIFIHD 1163
Cdd:cd14505   109 VLIHCKGGLGRTGliaaC-----LLLELGDTLDPEQAIAAVRAL---RPGAIQTPKQENFLHQ 163
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
322-386 8.90e-03

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: 37.09  E-value: 8.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755509397  322 DGPIVRKEIEYRMA-RGPWAEV--HAVNLQTYKLWHLDPDTEYEISVLLTRpgDGGTGRPGPPLISRT 386
Cdd:cd00063    28 GGPITGYVVEYREKgSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVN--GGGESPPSESVTVTT 93
 
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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