NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568930827|ref|XP_006538729|]
View 

receptor-type tyrosine-protein phosphatase U isoform X6 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 951-1161 9.21e-155

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: 466.45  E-value: 9.21e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITL 1030
Cdd:cd14632     1 YINANYID------GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1031 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYI 1110
Cdd:cd14632    75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568930827 1111 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1161
Cdd:cd14632   155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1246-1452 7.61e-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: 7.61e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1405
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568930827 1406 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 31-194 5.37e-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: 5.37e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827     31 FLAGCTFEEASdpvvPCEFSQAQYDDFQWEQVRIHP---GTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSEN-DTH 106
Cdd:smart00137    2 SPGNCDFEEGS----TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    107 CVQFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDHKGYIGLDD 186
Cdd:smart00137   78 CLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDD 153


                    ....*...
gi 568930827    187 ILLFSYPC 194
Cdd:smart00137  154 ILLSNGPC 161
fn3 pfam00041
Fibronectin type III domain;
502-585 1.42e-13

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.44  E-value: 1.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   502 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTS 580
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*
gi 568930827   581 KGFGQ 585
Cdd:pfam00041   79 GGEGP 83
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
355-632 1.13e-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: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  355 LDPDTEYEISVLLTrpGDGGTGRPGPPlISRTKCAEPTRAPKGLAFAEIQARQLTLQWEP------LGYNVtrchtyavs 428
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRV--------- 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  429 lcYRYTLGGSHNQTIREcVKmergASRYTIKNLLPFRNIHVRLILTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 506
Cdd:COG3401   267 --YRSNSGDGPFTKVAT-VT----TTSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  507 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGfgq 585
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568930827  586 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 632
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
fn3 pfam00041
Fibronectin type III domain;
299-373 1.95e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   299 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---NLQTYKLWHLDPDTEYEISVlLTRPGD 372
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 568930827   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 7.02e-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: 7.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    204 GDVEVNAGQNASFQCMAAGraAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGaGVS 283
Cdd:smart00410    2 PSVTVKEGESVTLSCEASG--SPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78


                    ....*..
gi 568930827    284 NFAELIV 290
Cdd:smart00410   79 SGTTLTV 85
 
Name Accession Description Interval E-value
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 951-1161 9.21e-155

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: 466.45  E-value: 9.21e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITL 1030
Cdd:cd14632     1 YINANYID------GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1031 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYI 1110
Cdd:cd14632    75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568930827 1111 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1161
Cdd:cd14632   155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1246-1452 7.61e-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: 7.61e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1405
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568930827 1406 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
926-1157 3.52e-100

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 319.96  E-value: 3.52e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   926 RQEPVSAYDRHHVKLHPmlADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLV 1005
Cdd:pfam00102    6 RYKDVLPYDHTRVKLTG--DPGPSDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  1006 EVGRVKCSRYWP---EDSDMYGDIKITLVKTET-LAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFI 1081
Cdd:pfam00102   78 EKGREKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827  1082 RRVKASTP-PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
901-1157 3.29e-97

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 312.67  E-value: 3.29e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    901 GFKQEYE----------SFFEG-WDATKKKDklkggRQEPVSAYDRHHVKLHPMLADPDaDYISANYIDirinrqGYHRS 969
Cdd:smart00194    1 GLEEEFEkldrlkpddeSCTVAaFPENRDKN-----RYKDVLPYDHTRVKLKPPPGEGS-DYINASYID------GPNGP 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    970 NHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRTFAL 1046
Cdd:smart00194   69 KAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEV 148

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1047 ERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVD 1126
Cdd:smart00194  149 TNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVD 228

                           250       260       270
                    ....*....|....*....|....*....|.
gi 568930827   1127 IYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:smart00194  229 IFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1189-1452 1.87e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 279.93  E-value: 1.87e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1189 QLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPL 1268
Cdd:smart00194    1 GLEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1269 QSTTPDFWRLVYDYGCTSIVMLNQLNqSNSAWPCLQYWPEPGR--QQYGLMEVEFVSGTANEDLVSRVFRVQNSSrlQEG 1346
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELV-EKGREKCAQYWPDEEGepLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1347 HLLVRHFQFLRWSaYRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAA 1426
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 568930827   1427 KTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1217-1452 1.43e-71

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 239.07  E-value: 1.43e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  1217 NRDKNRSMDVLPPDRCLPFLiSSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1296
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  1297 NSAwPCLQYWPEP--GRQQYGLMEVEFVSGTANE-DLVSRVFRVQNSSRlQEGHLlVRHFQFLRWSAyRDTPDSRKAFLH 1373
Cdd:pfam00102   80 GRE-KCAQYWPEEegESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGS-EETRT-VKHFHYTGWPD-HGVPESPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827  1374 LLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:pfam00102  156 LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 31-194 5.37e-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: 5.37e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827     31 FLAGCTFEEASdpvvPCEFSQAQYDDFQWEQVRIHP---GTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSEN-DTH 106
Cdd:smart00137    2 SPGNCDFEEGS----TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    107 CVQFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDHKGYIGLDD 186
Cdd:smart00137   78 CLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDD 153


                    ....*...
gi 568930827    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 3.02e-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: 3.02e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    35 CTFEEASDpvvpCEFSQAQYDDFQWEQVRIH-PGTRTPED----LPHGAYLMVNASQHAPGQRAHIIFQTLSENDT-HCV 108
Cdd:pfam00629    1 CDFEDGNL----CGWTQDSSDDFDWERVSGPsVKTGPSSDhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   109 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFwPNEYQVLFEALISPDHKGYIGLDDIL 188
Cdd:pfam00629   77 RFWYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDIS 152


                   ....*..
gi 568930827   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 1.52e-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: 1.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   35 CTFEEAsdpvvPCEFSQAQYDDFQWEQVRIHPGTR-TPEDLPH----GAYLMVNASQHAPGQRAHIIFQTLSEN-DTHCV 108
Cdd:cd06263     1 CDFEDG-----LCGWTQDSTDDFDWTRVSGSTPSPgTPPDHTHgtgsGHYLYVESSSGREGQKARLLSPLLPPPrSSHCL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  109 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWpNEYQVLFEALISPDHKGYIGLDDIL 188
Cdd:cd06263    76 SFWYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDIS 151


                  ....*.
gi 568930827  189 LFSYPC 194
Cdd:cd06263   152 LSPGPC 157
PHA02738 PHA02738
hypothetical protein; Provisional
 950-1155 8.86e-44

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 162.40  E-value: 8.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  950 DYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP--EDSDM-YGDI 1026
Cdd:PHA02738   76 DYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdvEQGSIrFGKF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1027 KITLVKTETLAEYVVRTFALErRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA----------------STPP 1090
Cdd:PHA02738  150 KITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQcqkelaqeslqighnrLQPP 228

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1091 dagPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1155
Cdd:PHA02738  229 ---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
947-1151 3.98e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 133.29  E-value: 3.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  947 PDADYISANYIDIRINRQgyhrsnhFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVG--RVKCSRYWPEDSDmYG 1024
Cdd:COG5599    61 ANLGYLNANYIQVIGNHR-------YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGE-YG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1025 --DIKITLVKTETLAEYV-VRTFALERRGYSAR-HEVRQFHFTAWPEHGVPyHATGLLAFIRRVKAS---TPPDAGPIVI 1097
Cdd:COG5599   133 kyEVSSELTESIQLRDGIeARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKekiKDPDKLLPVV 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827 1098 HCSAGTGRTGCYIVLDVMLDM--AECEGVVDIYNCVKTL-CSRRVNMIQTEEQYIFI 1151
Cdd:COG5599   212 HCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMrTSRNGGMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1215-1454 6.38e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.01  E-value: 6.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1215 PRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1294
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1295 QSNSAWPCLQYW--PEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLlvRHFQFLRWSAYrDTPDSRKAFL 1372
Cdd:PHA02747  129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI--SHFQCSEWFED-ETPSDHPDFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1373 HLLAEVDKWQAESGDGRT---------VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQY 1443
Cdd:PHA02747  206 KFIKIIDINRKKSGKLFNpkdallcpiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                         250
                  ....*....|....
gi 568930827 1444 HF---CYDVALEYL 1454
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
fn3 pfam00041
Fibronectin type III domain;
502-585 1.42e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.44  E-value: 1.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   502 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTS 580
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*
gi 568930827   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 2.34e-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: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  492 DVPGGIAAESLTftplEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPA-VNVPGPrrtisklrNETYHVFSNLHPGTT 570
Cdd:cd00063     2 SPPTNLRVTDVT----STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeVEVTPG--------SETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....
gi 568930827  571 YLFSVRARTSKGFGQAA-LTEITT 593
Cdd:cd00063    70 YEFRVRAVNGGGESPPSeSVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
355-632 1.13e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.26  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  355 LDPDTEYEISVLLTrpGDGGTGRPGPPlISRTKCAEPTRAPKGLAFAEIQARQLTLQWEP------LGYNVtrchtyavs 428
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRV--------- 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  429 lcYRYTLGGSHNQTIREcVKmergASRYTIKNLLPFRNIHVRLILTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 506
Cdd:COG3401   267 --YRSNSGDGPFTKVAT-VT----TTSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  507 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGfgq 585
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568930827  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 3.07e-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: 3.07e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    494 PGGIAAESLTftplEDMIFLKWEEPQEPNGL--ITQYEISYQSIESSDPAVNVPGprrtisklrNETYHVFSNLHPGTTY 571
Cdd:smart00060    4 PSNLRVTDVT----STSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTP---------SSTSYTLTGLKPGTEY 70

                            90
                    ....*....|...
gi 568930827    572 LFSVRARTSKGFG 584
Cdd:smart00060   71 EFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
299-373 1.95e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   299 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---NLQTYKLWHLDPDTEYEISVlLTRPGD 372
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 568930827   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 3.35e-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: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  394 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCyrytlgGSHNQTIRECVKMERGASRYTIKNLLPFRNIHVRLIL 473
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR------EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*..
gi 568930827  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 1.37e-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: 1.37e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568930827    294 PTPIAPPQLLRAGPTYLIIQ-LNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQT-YKLWHLDPDTEYEISV 365
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1363-1445 3.34e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 42.27  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1363 DTPDSRKAFLHLLAEVDKWQAEsgDGRTVVHCLNGGGRSGTFCACatVLeMIRCHSLVDvffAAKTLRNYKPNMVETMDQ 1442
Cdd:COG2453    58 FGAPDDEQLQEAVDFIDEALRE--GKKVLVHCRGGIGRTGTVAAA--YL-VLLGLSAEE---ALARVRAARPGAVETPAQ 129


                  ...
gi 568930827 1443 YHF 1445
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 7.02e-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: 7.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    204 GDVEVNAGQNASFQCMAAGraAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGaGVS 283
Cdd:smart00410    2 PSVTVKEGESVTLSCEASG--SPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78


                    ....*..
gi 568930827    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 568930827    394 APKGLAFAEIQARQLTLQWEPLGYNVTRChtYAVSLCYRYTLGGSHNQTirecVKMERGASRYTIKNLLPFRNIHVRLIL 473
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIVGYRVEYREEGSEWKE----VNVTPSSTSYTLTGLKPGTEYEFRVRA 76


                    ....*.
gi 568930827    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 9.37e-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: 9.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930827  322 DGPIVRKEIEYRMA-RGPWAEV--HAVNLQTYKLWHLDPDTEYEISVLLTRpgDGGTGRPGPPLISRT 386
Cdd:cd00063    28 GGPITGYVVEYREKgSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVN--GGGESPPSESVTVTT 93
 
Name Accession Description Interval E-value
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 951-1161 9.21e-155

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: 466.45  E-value: 9.21e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITL 1030
Cdd:cd14632     1 YINANYID------GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1031 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYI 1110
Cdd:cd14632    75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568930827 1111 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1161
Cdd:cd14632   155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1246-1452 7.61e-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: 7.61e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1405
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568930827 1406 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 951-1160 8.24e-143

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


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 434.73  E-value: 8.24e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITL 1030
Cdd:cd14555     1 YINANYID------GYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1031 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYI 1110
Cdd:cd14555    75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568930827 1111 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1160
Cdd:cd14555   155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 886-1160 1.53e-135

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: 417.91  E-value: 1.53e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  886 DLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDiri 961
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGqsapWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  962 nrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITLVKTETLAEYVV 1041
Cdd:cd14633    78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1042 RTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAEC 1121
Cdd:cd14633   155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 568930827 1122 EGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1160
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 938-1160 4.54e-121

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 376.67  E-value: 4.54e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  938 VKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP 1017
Cdd:cd14631     2 VILQPVEDDPSSDYINANYID------GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1018 EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVI 1097
Cdd:cd14631    76 DDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1098 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1160
Cdd:cd14631   156 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1246-1448 1.78e-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: 374.44  E-value: 1.78e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSnsAWPCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPK--DQSCPQYWPDEGSGTYGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFC 1405
Cdd:cd14556    79 IDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568930827 1406 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1448
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 930-1161 3.33e-114

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


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 358.95  E-value: 3.33e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  930 VSAYDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGR 1009
Cdd:cd14630    12 IISYDHSRVRLQLLDGDPHSDYINANYID------GYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVGR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1010 VKCSRYWPEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP 1089
Cdd:cd14630    86 VKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFLNP 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1090 PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1161
Cdd:cd14630   166 PDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 930-1161 1.06e-107

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


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 340.91  E-value: 1.06e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  930 VSAYDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGR 1009
Cdd:cd14553    12 VIAYDHSRVILQPIEGVPGSDYINANYCD------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1010 VKCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAST 1088
Cdd:cd14553    86 VKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKACN 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1089 PPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1161
Cdd:cd14553   166 PPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
926-1157 3.52e-100

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 319.96  E-value: 3.52e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   926 RQEPVSAYDRHHVKLHPmlADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLV 1005
Cdd:pfam00102    6 RYKDVLPYDHTRVKLTG--DPGPSDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  1006 EVGRVKCSRYWP---EDSDMYGDIKITLVKTET-LAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFI 1081
Cdd:pfam00102   78 EKGREKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827  1082 RRVKASTP-PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:pfam00102  158 RKVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 885-1161 4.45e-98

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


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 315.82  E-value: 4.45e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  885 ADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDir 960
Cdd:cd14626     1 SDLADNIERLKANDGLKFSQEYESIDPGqqftWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYID-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  961 inrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAEY 1039
Cdd:cd14626    79 ----GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPiRGTETYGMIQVTLLDTVELATY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1040 VVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMA 1119
Cdd:cd14626   155 SVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568930827 1120 ECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1161
Cdd:cd14626   235 KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
901-1157 3.29e-97

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 312.67  E-value: 3.29e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    901 GFKQEYE----------SFFEG-WDATKKKDklkggRQEPVSAYDRHHVKLHPMLADPDaDYISANYIDirinrqGYHRS 969
Cdd:smart00194    1 GLEEEFEkldrlkpddeSCTVAaFPENRDKN-----RYKDVLPYDHTRVKLKPPPGEGS-DYINASYID------GPNGP 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    970 NHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRTFAL 1046
Cdd:smart00194   69 KAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEV 148

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1047 ERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVD 1126
Cdd:smart00194  149 TNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVD 228

                           250       260       270
                    ....*....|....*....|....*....|.
gi 568930827   1127 IYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:smart00194  229 IFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 879-1162 1.38e-92

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: 300.88  E-value: 1.38e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  879 HPAVRVADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISA 954
Cdd:cd14624     1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGqqftWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  955 NYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKT 1033
Cdd:cd14624    81 NYID------GYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPsRGTETYGLIQVTLLDT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1034 ETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLD 1113
Cdd:cd14624   155 VELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1114 VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCG 1162
Cdd:cd14624   235 AMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 879-1161 2.22e-92

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 300.47  E-value: 2.22e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  879 HPAVRVADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISA 954
Cdd:cd14625     1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGqqftWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  955 NYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKT 1033
Cdd:cd14625    81 NYID------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPsRGTETYGMIQVTLLDT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1034 ETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLD 1113
Cdd:cd14625   155 IELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 568930827 1114 VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1161
Cdd:cd14625   235 AMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1246-1452 1.40e-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: 1.40e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNqsnSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD---AAQLCMQYWPEKTSCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGT 1403
Cdd:cd14634    78 IDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1404 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 951-1153 2.58e-90

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: 291.11  E-value: 2.58e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDM---YGDIK 1027
Cdd:cd00047     1 YINASYID------GYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKpleYGDIT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1028 ITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTG 1107
Cdd:cd00047    75 VTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 568930827 1108 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1153
Cdd:cd00047   155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 951-1153 3.44e-89

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: 288.10  E-value: 3.44e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPED-SDMYGDIKIT 1029
Cdd:cd14549     1 YINANYVD------GYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1030 LVKTETLAEYVVRTFAL------ERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGT 1103
Cdd:cd14549    75 LLSTEVLATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGV 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568930827 1104 GRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1153
Cdd:cd14549   155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1246-1452 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 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSawpCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGT 1403
Cdd:cd14636    78 MDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEEcdEGEGRTIIHCLNGGGRSGM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1404 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14636   158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1189-1452 1.87e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 279.93  E-value: 1.87e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1189 QLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPL 1268
Cdd:smart00194    1 GLEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1269 QSTTPDFWRLVYDYGCTSIVMLNQLNqSNSAWPCLQYWPEPGR--QQYGLMEVEFVSGTANEDLVSRVFRVQNSSrlQEG 1346
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELV-EKGREKCAQYWPDEEGepLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1347 HLLVRHFQFLRWSaYRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAA 1426
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 568930827   1427 KTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 933-1152 2.28e-84

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: 275.00  E-value: 2.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  933 YDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKC 1012
Cdd:cd14548     8 YDHSRVKLIPINEEEGSDYINANYI------PGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1013 SRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFALERRGYSarHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP 1090
Cdd:cd14548    82 DHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLERGDEV--RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1091 DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1152
Cdd:cd14548   160 EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1246-1452 3.92e-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: 271.18  E-value: 3.92e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNqsnSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVD---PAQLCPQYWPENGVHRHGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYRDTPDSRKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGT 1403
Cdd:cd14635    78 LEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1404 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14635   158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1217-1452 1.43e-71

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 239.07  E-value: 1.43e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  1217 NRDKNRSMDVLPPDRCLPFLiSSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1296
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  1297 NSAwPCLQYWPEP--GRQQYGLMEVEFVSGTANE-DLVSRVFRVQNSSRlQEGHLlVRHFQFLRWSAyRDTPDSRKAFLH 1373
Cdd:pfam00102   80 GRE-KCAQYWPEEegESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGS-EETRT-VKHFHYTGWPD-HGVPESPNSLLD 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827  1374 LLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:pfam00102  156 LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 930-1160 3.50e-71

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 239.55  E-value: 3.50e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  930 VSAYDRHHVKLHPmLADPDA---DYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVE 1006
Cdd:cd17667    36 ILAYDHSRVKLRP-LPGKDSkhsDYINANYVD------GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1007 VGRVKCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALER-----------RGYSARHEVRQFHFTAWPEHGVPYHA 1074
Cdd:cd17667   109 KGRRKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYA 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1075 TGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDA 1154
Cdd:cd17667   189 LPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDA 268


                  ....*.
gi 568930827 1155 ILEACL 1160
Cdd:cd17667   269 LLEAIL 274
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 875-1166 1.36e-70

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: 238.77  E-value: 1.36e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  875 TGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESF-----FEGWDATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDA 949
Cdd:cd14621     1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALpacpiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  950 DYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSD-MYGDIKI 1028
Cdd:cd14621    81 DYINASFIN------GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCwTYGNIRV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1029 TLVKTETLAEYVVRTFALERRG----YSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTG 1104
Cdd:cd14621   155 SVEDVTVLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVG 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1105 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTI 1166
Cdd:cd14621   235 RTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 933-1157 3.59e-68

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 229.06  E-value: 3.59e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  933 YDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKC 1012
Cdd:cd14620     7 YDHSRVILSQLDGIPCSDYINASYID------GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1013 SRYWPEDSD-MYGDIKITLVKTETLAEYVVRTFALERR---GYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAST 1088
Cdd:cd14620    81 YQYWPDQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1089 PPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14620   161 PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 914-1152 1.36e-67

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


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 229.17  E-value: 1.36e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  914 DATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQE 993
Cdd:cd14543    22 LCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMD------GYKQKNAYIATQGPLPKTYSDFWRMVWEQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  994 QCASIVMITKLVEVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGV 1070
Cdd:cd14543    96 KVLVIVMTTRVVERGRVKCGQYWPLEEGSslrYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1071 PYHATGLLAFI--------RRVKASTPPDAG-----PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSR 1137
Cdd:cd14543   176 PSSAAALLDFLgevrqqqaLAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQ 255

                         250
                  ....*....|....*
gi 568930827 1138 RVNMIQTEEQYIFIH 1152
Cdd:cd14543   256 RAFSIQTPDQYYFCY 270
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 926-1157 6.33e-67

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 225.47  E-value: 6.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  926 RQEPVSAYDRHHVKLhPMLADPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLV 1005
Cdd:cd14615     2 RYNNVLPYDISRVKL-SVQSHSTDDYINANYM------PGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1006 EVGRVKCSRYWPED-SDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAF---I 1081
Cdd:cd14615    75 EQGRTKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568930827 1082 RRVKASTPPDaGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14615   155 REYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 951-1152 2.44e-66

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: 222.87  E-value: 2.44e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSD-MYGDIKIT 1029
Cdd:cd14551     1 YINASYID------GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1030 LVKTETLAEYVVRTFALERR----GYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGR 1105
Cdd:cd14551    75 VEDTVVLVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568930827 1106 TGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1152
Cdd:cd14551   155 TGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 926-1157 2.63e-66

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: 224.00  E-value: 2.63e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  926 RQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLV 1005
Cdd:cd14619     2 RFRNVLPYDWSRVPLKPIHEEPGSDYINANYM------PGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1006 EVGRVKCSRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRR 1083
Cdd:cd14619    76 EAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568930827 1084 VKA--STPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14619   156 LRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 951-1156 1.88e-65

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: 220.62  E-value: 1.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKIT 1029
Cdd:cd17668     1 YINANYVD------GYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1030 LVKTETLAEYVVRTFALE--------RRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSA 1101
Cdd:cd17668    75 QKSVQVLAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1102 GTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1156
Cdd:cd17668   155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 938-1152 5.11e-65

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: 219.96  E-value: 5.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  938 VKLHPMLADPDADYISANYIdirinrQGY-HRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEvGRVKCSRYW 1016
Cdd:cd14547    14 VCLPSVDDDPLSSYINANYI------RGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AKEKCAQYW 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1017 PEDSDM-YGDIKITLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVK--ASTPPDAG 1093
Cdd:cd14547    87 PEEENEtYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEeaRQTEPHRG 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1094 PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIyncVKTLCSRRVN---MIQTEEQYIFIH 1152
Cdd:cd14547   165 PIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDV---LGIVCQLRLDrggMVQTAEQYEFVH 223
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 933-1152 2.00e-64

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 218.63  E-value: 2.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  933 YDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKC 1012
Cdd:cd14617     9 YDSTRVKLSNVDDDPCSDYINASYI------PGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1013 SRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFAL--ERRGYSARHeVRQFHFTAWPEHGVPYHATGLLAFIRRVK--A 1086
Cdd:cd14617    83 DHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcsEEQLDAPRL-VRHFHYTVWPDHGVPETTQSLIQFVRTVRdyI 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568930827 1087 STPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1152
Cdd:cd14617   162 NRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 951-1153 2.67e-63

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: 214.42  E-value: 2.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDIrinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDM--YGDIKI 1028
Cdd:cd18533     1 YINASYITL-----PGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgeYGDLTV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1029 TLVKTETLAE--YVVRTFALeRRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA--STPPDAGPIVIHCSAGTG 1104
Cdd:cd18533    76 ELVSEEENDDggFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568930827 1105 RTGCYIVLDVMLDMAE--------CEGVVD-IYNCVKTLCSRRVNMIQTEEQYIFIHD 1153
Cdd:cd18533   155 RTGTFIALDSLLDELKrglsdsqdLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 926-1156 3.73e-63

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


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 214.81  E-value: 3.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  926 RQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLV 1005
Cdd:cd14618     2 RYPHVLPYDHSRVRLSQLGGEPHSDYINANFI------PGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1006 EVGRVKCSRYWPEDSD--MYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRR 1083
Cdd:cd14618    76 ENGRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFREL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1084 VKA--STPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1156
Cdd:cd14618   156 VREhvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 951-1158 2.69e-62

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 211.46  E-value: 2.69e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDIRINRQGYHrsnhFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSD----MYGDI 1026
Cdd:cd14538     1 YINASHIRIPVGGDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNkpliCGGRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1027 KITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTppDAGPIVIHCSAGTGRT 1106
Cdd:cd14538    77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1107 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1158
Cdd:cd14538   155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 933-1155 5.29e-62

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: 212.32  E-value: 5.29e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  933 YDRHHVKLHPmlADPD---ADYISANYIDIRiNRQGYHRSNH--FIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEV 1007
Cdd:cd14544    13 FDHTRVILKD--RDPNvpgSDYINANYIRNE-NEGPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVIVMTTKEVER 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1008 GRVKCSRYWPED--SDMYGDIKITLVKTETLAEYVVRTFALER--RGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRR 1083
Cdd:cd14544    90 GKNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKldQGDPIR-EIWHYQYLSWPDHGVPSDPGGVLNFLED 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827 1084 V--KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1155
Cdd:cd14544   169 VnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAV 245
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 930-1152 9.54e-62

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 210.53  E-value: 9.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  930 VSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGR 1009
Cdd:cd14616     6 IKPYNNNRVKLIADAGVPGSDYINASYI------SGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1010 VKCSRYWPEDSD---MYGDIKITLVKTETLAEYVVRTFALERRGYSARheVRQFHFTAWPEHGVPYHATGLLAFIRRVKA 1086
Cdd:cd14616    80 IRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568930827 1087 STPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1152
Cdd:cd14616   158 SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 951-1152 1.29e-61

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: 209.30  E-value: 1.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP---EDSDMYGDIK 1027
Cdd:cd14557     1 YINASYID------GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1028 ITLVKTETLAEYVVRTFAL--ERRGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGR 1105
Cdd:cd14557    75 VKINEEKICPDYIIRKLNInnKKEKGSGR-EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568930827 1106 TGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1152
Cdd:cd14557   154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 933-1156 5.76e-60

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 206.22  E-value: 5.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  933 YDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKC 1012
Cdd:cd14554    18 YESTRVCLQPIRGVEGSDYINASFID------GYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGREKC 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1013 SRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP- 1090
Cdd:cd14554    92 HQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQf 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827 1091 -DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1156
Cdd:cd14554   172 gQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 950-1158 5.81e-60

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: 204.87  E-value: 5.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  950 DYISANYIDIRINRQGYhrSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPE--DSDMYGDIK 1027
Cdd:cd14541     1 DYINANYVNMEIPGSGI--VNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQFGNLQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1028 ITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTG 1107
Cdd:cd14541    79 ITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568930827 1108 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1158
Cdd:cd14541   159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 933-1156 1.04e-59

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: 205.51  E-value: 1.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  933 YDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKC 1012
Cdd:cd14614    24 YDFSRVKLVSMHEEEGSDYINANYI------PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKC 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1013 SRYWP--EDSDMYGDIKITLVKTETLAEYVVRTFaleRRGYS-ARHEVRQFHFTAWPEHGVPY--HATGLLAFIRRVKAS 1087
Cdd:cd14614    98 DHYWPftEEPVAYGDITVEMLSEEEQPDWAIREF---RVSYAdEVQDVMHFNYTAWPDHGVPTanAAESILQFVQMVRQQ 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1088 TPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1156
Cdd:cd14614   175 AVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 951-1153 4.47e-57

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: 196.46  E-value: 4.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDMYGDIKITL 1030
Cdd:cd14558     1 YINASFID------GYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1031 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAG------PIVIHCSAGTG 1104
Cdd:cd14558    75 KDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGSS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1105 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1153
Cdd:cd14558   155 RTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 951-1155 4.29e-56

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: 193.64  E-value: 4.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDM-YGDIKIT 1029
Cdd:cd14552     1 YINASFID------GYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1030 LVKTETLAEYVVRTFALER-RGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRV-KASTPPDAGPIVIHCSAGTGRTG 1107
Cdd:cd14552    75 LKDQTDYEDYTLRDFLVTKgKGGSTR-TVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568930827 1108 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1155
Cdd:cd14552   154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1246-1448 3.63e-55

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


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 190.57  E-value: 3.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQ--QYGLMEVEFVS 1323
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGRE-KCERYWPEEGGKplEYGDITVTLVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1324 GTANEDLVSRVFRVQNSSrlQEGHLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGT 1403
Cdd:cd00047    80 EEELSDYTIRTLELSPKG--CSESREVTHLHYTGWPD-HGVPSSPEDLLALVRRVRKEA-RKPNGPIVVHCSAGVGRTGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568930827 1404 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1448
Cdd:cd00047   156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 926-1155 2.99e-54

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: 190.23  E-value: 2.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  926 RQEPVSAYDRHHVKLHPM-LADPDADYISANYI--DIRINRQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMIT 1002
Cdd:cd14605     7 RYKNILPFDHTRVVLHDGdPNEPVSDYINANIImpEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1003 KLVEVGRVKCSRYWPEDSDM--YGDIKITLVKTETLAEYVVRTFALERRGY-SARHEVRQFHFTAWPEHGVPYHATGLLA 1079
Cdd:cd14605    87 KEVERGKSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGQgNTERTVWQYHFRTWPDHGVPSDPGGVLD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1080 FIRRV--KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRVNMIQTEEQYIFIHDA 1154
Cdd:cd14605   167 FLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQYRFIYMA 246


                  .
gi 568930827 1155 I 1155
Cdd:cd14605   247 V 247
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 31-194 5.37e-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: 5.37e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827     31 FLAGCTFEEASdpvvPCEFSQAQYDDFQWEQVRIHP---GTRTPEDLPHGAYLMVNASQHAPGQRAHIIFQTLSEN-DTH 106
Cdd:smart00137    2 SPGNCDFEEGS----TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    107 CVQFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDHKGYIGLDD 186
Cdd:smart00137   78 CLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDD 153


                    ....*...
gi 568930827    187 ILLFSYPC 194
Cdd:smart00137  154 ILLSNGPC 161
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 880-1157 1.41e-53

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: 189.94  E-value: 1.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  880 PAVRVADLLQHINQMKTAEGY-GFKQEYESFFEGWDATKK-------KDKLKGgRQEPVSAYDRHHVKLHPMLADPDADY 951
Cdd:cd14628     4 PARNLYAYIQKLTQIETGENVtGMELEFKRLASSKAHTSRfisanlpCNKFKN-RLVNIMPYESTRVCLQPIRGVEGSDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  952 ISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITL 1030
Cdd:cd14628    83 INASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPaERSARYQYFVVDP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1031 VKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP--DAGPIVIHCSAGTGRTGC 1108
Cdd:cd14628   157 MAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGV 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1109 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14628   237 FITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 950-1155 4.47e-53

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 184.82  E-value: 4.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  950 DYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKI 1028
Cdd:cd14622     1 DYINASFID------GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPsEGSVTHGEITI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1029 TLvKTETLAEYV-VRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV-KASTPPDAGPIVIHCSAGTGRT 1106
Cdd:cd14622    75 EI-KNDTLLETIsIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRT 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1107 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1155
Cdd:cd14622   154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 930-1157 1.22e-52

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: 186.86  E-value: 1.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  930 VSAYDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGR 1009
Cdd:cd14627    62 IMPYETTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1010 VKCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAST 1088
Cdd:cd14627   136 EKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTK 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930827 1089 PP--DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14627   216 EQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 945-1157 1.48e-52

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: 184.48  E-value: 1.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  945 ADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDM-Y 1023
Cdd:cd14623    20 GEENTDYVNASFID------GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSDGSVsY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1024 GDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAG-PIVIHCSAG 1102
Cdd:cd14623    94 GDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNhPITVHCSAG 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1103 TGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14623   174 AGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 919-1156 6.83e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 182.72  E-value: 6.83e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  919 KDKLKGGRQEPVSAYDRHHVKLhpmlaDPDADYISANYIDIRINRQGYHrsnhFIATQGPKPEMIYDFWRMVWQEQCASI 998
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFIKMPVGDEEFV----YIACQGPLPTTVADFWQMVWEQKSTVI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  999 VMITKLVEVGRVKCSRYWPED---SDMYGD-IKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHA 1074
Cdd:cd14597    72 AMMTQEVEGGKIKCQRYWPEIlgkTTMVDNrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1075 TGLLAFI---RRVKAStppdaGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFI 1151
Cdd:cd14597   152 EQLLTFIsymRHIHKS-----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFC 226


                  ....*
gi 568930827 1152 HDAIL 1156
Cdd:cd14597   227 YQVIL 231
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 930-1157 1.38e-51

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: 184.16  E-value: 1.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  930 VSAYDRHHVKLHPMLADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGR 1009
Cdd:cd14629    62 IMPYELTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1010 VKCSRYWP-EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAST 1088
Cdd:cd14629   136 EKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTK 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930827 1089 PP--DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14629   216 EQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 946-1152 2.46e-51

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: 181.57  E-value: 2.46e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  946 DPDADYISANYIdirinrQGYH-RSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEvGRVKCSRYWPEDSDMYG 1024
Cdd:cd14612    41 EEEGSYINANYI------RGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE-KKEKCVHYWPEKEGTYG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1025 DIKITLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPIVIHCSAG 1102
Cdd:cd14612   114 RFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESrqTAASPGPIVVHCSAG 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568930827 1103 TGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1152
Cdd:cd14612   192 IGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 946-1155 2.51e-51

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: 181.98  E-value: 2.51e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  946 DPDADYISANYIdirinrQGY-HRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRvKCSRYWPEDSDMYG 1024
Cdd:cd14613    51 DPLSSYINANYI------RGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWPEEQVTYE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1025 DIKITLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---STPPDAGPIVIHCSA 1101
Cdd:cd14613   124 GIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEarqQAEPNCGPVIVHCSA 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827 1102 GTGRTGCYIVLDVMLDMAECEGVVDIyncVKTLCSRRVN---MIQTEEQYIFIHDAI 1155
Cdd:cd14613   202 GIGRTGCFIATSICCKQLRNEGVVDI---LRTTCQLRLDrggMIQTCEQYQFVHHVL 255
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 951-1152 1.13e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 178.00  E-value: 1.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDM---YGDIK 1027
Cdd:cd14542     1 YINANFI------KGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEqlqFGPFK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1028 ITLVKTETLAE-YVVRTFALERRgySARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRT 1106
Cdd:cd14542    75 ISLEKEKRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRT 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1107 GCYIVLDVMLDMAECEGVVD---IYNCVKTLCSRRVNMIQTEEQYIFIH 1152
Cdd:cd14542   153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 35-195 3.02e-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: 3.02e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    35 CTFEEASDpvvpCEFSQAQYDDFQWEQVRIH-PGTRTPED----LPHGAYLMVNASQHAPGQRAHIIFQTLSENDT-HCV 108
Cdd:pfam00629    1 CDFEDGNL----CGWTQDSSDDFDWERVSGPsVKTGPSSDhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   109 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFwPNEYQVLFEALISPDHKGYIGLDDIL 188
Cdd:pfam00629   77 RFWYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDIS 152


                   ....*..
gi 568930827   189 LFSYPCA 195
Cdd:pfam00629  153 LSSGPCP 159
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 950-1157 3.94e-50

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 176.67  E-value: 3.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  950 DYISANYIDIRINRQGYhrSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPE--DSDMYGDIK 1027
Cdd:cd14601     1 DYINANYINMEIPSSSI--INRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1028 ITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTG 1107
Cdd:cd14601    79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568930827 1108 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1246-1449 4.49e-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: 4.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEI-KERSQNKCAQYWPEDGSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNSsrlQEGHL-LVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTF 1404
Cdd:cd14552    80 DYEDYTLRDFLVTKG---KGGSTrTVRQFHFHGWPEV-GIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTF 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568930827 1405 CACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDV 1449
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 ...
 1212-1451 7.67e-50

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 176.95  E-value: 7.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1212 ALLPRNRDKNRSMDVLPPDR---CLPFLISSDGdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1288
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYEStrvCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1289 MLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAyRDTPDSR 1368
Cdd:cd14554    79 MLTKLREMGRE-KCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRT--VRQFQFTDWPE-QGVPKSG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1369 KAFLHLLAEVDKWQAESG-DGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd14554   155 EGFIDFIGQVHKTKEQFGqEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234


                  ....
gi 568930827 1448 DVAL 1451
Cdd:cd14554   235 RAAL 238
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 903-1157 8.16e-50

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: 177.76  E-value: 8.16e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  903 KQEYESFFEGWDATKKKDKLKGgRQEPVSAYDRHHVKLHPmlADPD---ADYISANYIDIRINRQGyHRSNHFIATQGPK 979
Cdd:cd14606     1 KQEVKNLHQRLEGQRPENKSKN-RYKNILPFDHSRVILQG--RDSNipgSDYINANYVKNQLLGPD-ENAKTYIASQGCL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  980 PEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPE--DSDMYGDIKITLVKTETLAEYVVRTFALE--RRGYSARh 1055
Cdd:cd14606    77 EATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSplDNGELIR- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1056 EVRQFHFTAWPEHGVPYHATGLLAFIRRV--KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNC 1130
Cdd:cd14606   156 EIWHYQYLSWPDHGVPSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKT 235

                         250       260
                  ....*....|....*....|....*..
gi 568930827 1131 VKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14606   236 IQMVRAQRSGMVQTEAQYKFIYVAIAQ 262
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 902-1157 1.52e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 177.32  E-value: 1.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  902 FKQEYESFFEgwdATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGPKPE 981
Cdd:cd14603    14 FKADYVCSTV---AGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFI------KGVDGSRAYIATQGPLSH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  982 MIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSD--MYGDIKITLVKTETL-AEYVVRTFALERRGYSarHEVR 1058
Cdd:cd14603    85 TVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEplQTGPFTITLVKEKRLnEEVILRTLKVTFQKES--RSVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1059 QFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVD---IYNCVKTLC 1135
Cdd:cd14603   163 HFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMR 242

                         250       260
                  ....*....|....*....|..
gi 568930827 1136 SRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14603   243 KQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 951-1158 4.29e-49

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


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 173.78  E-value: 4.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDIRINRQGYHrsnhFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSD---MYGDIK 1027
Cdd:cd14596     1 YINASYITMPVGEEELF----YIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQepmELENYQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1028 ITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTppDAGPIVIHCSAGTGRTG 1107
Cdd:cd14596    77 LRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568930827 1108 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1158
Cdd:cd14596   155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 926-1150 1.29e-48

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: 172.96  E-value: 1.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  926 RQEPVSAYDRHHVKLHpmLADPDADYISANYIDI-RINRQgyhrsnhFIATQGPKPEMIYDFWRMVWQEQCASIVMITKL 1004
Cdd:cd14545     3 RYRDRDPYDHDRSRVK--LKQGDNDYINASLVEVeEAKRS-------YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1005 VEVGRVKCSRYWP-EDSDMYG----DIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLA 1079
Cdd:cd14545    74 MEKGQIKCAQYWPqGEGNAMIfedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLN 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1080 FIRRVK--ASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV--VDIYNCVKTLCSRRVNMIQTEEQYIF 1150
Cdd:cd14545   154 FLQKVResGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 946-1152 1.45e-48

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


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 172.80  E-value: 1.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  946 DPDADYISANYIdirinrQGYH-RSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRvKCSRYWPEDSDMYG 1024
Cdd:cd14611    25 DSLSTYINANYI------RGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKRGIYG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1025 DIKITLVKTETLAEYVVRTFALeRRGYSARHeVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPIVIHCSAG 1102
Cdd:cd14611    98 KVEVLVNSVKECDNYTIRNLTL-KQGSQSRS-VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDrlASPGRGPVVVHCSAG 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568930827 1103 TGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1152
Cdd:cd14611   176 IGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 968-1157 1.22e-47

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 169.55  E-value: 1.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  968 RSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPED-SDMYGDIKITLVKTETLAE-YVVRTFA 1045
Cdd:cd14546    13 RNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVHLVSEHIWCDdYLVRSFY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1046 LERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLD-MAECEGV 1124
Cdd:cd14546    93 LKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILIDMVLNrMAKGAKE 172

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568930827 1125 VDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14546   173 IDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 35-194 1.52e-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: 1.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   35 CTFEEAsdpvvPCEFSQAQYDDFQWEQVRIHPGTR-TPEDLPH----GAYLMVNASQHAPGQRAHIIFQTLSEN-DTHCV 108
Cdd:cd06263     1 CDFEDG-----LCGWTQDSTDDFDWTRVSGSTPSPgTPPDHTHgtgsGHYLYVESSSGREGQKARLLSPLLPPPrSSHCL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  109 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWpNEYQVLFEALISPDHKGYIGLDDIL 188
Cdd:cd06263    76 SFWYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDIS 151


                  ....*.
gi 568930827  189 LFSYPC 194
Cdd:cd06263   152 LSPGPC 157
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 926-1157 2.59e-47

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 169.64  E-value: 2.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  926 RQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLV 1005
Cdd:cd14602     3 RYKDILPYDHSRVELSLITSDEDSDYINANFI------KGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1006 EVGRVKCSRYWPEDSDM---YGDIKITLVKTETLAEYVVRTfaLERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIR 1082
Cdd:cd14602    77 EMGKKKCERYWAEPGEMqleFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1083 RVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAEcEGVV----DIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14602   155 DVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 917-1155 2.62e-47

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 171.65  E-value: 2.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  917 KKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCA 996
Cdd:cd14604    53 EKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFI------KGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  997 SIVMITKLVEVGRVKCSRYWP---EDSDMYGDIKITLVKTETLAEYVVRTFALERRGYSarHEVRQFHFTAWPEHGVPYH 1073
Cdd:cd14604   127 IIVMACREFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET--RRLYQFHYVNWPDHDVPSS 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1074 ATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDV---MLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIF 1150
Cdd:cd14604   205 FDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYEL 284


                  ....*
gi 568930827 1151 IHDAI 1155
Cdd:cd14604   285 VHRAI 289
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1246-1448 6.24e-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: 6.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWpCLQYWPEpGRQQYGLMEVEFVSGT 1325
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQ-CAQYWGD-EKKTYGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNSSRLQegHLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAE--SGDGRT---VVHCLNGGGR 1400
Cdd:cd14558    79 KSPTYTVRVFEITHLKRKD--SRTVYQYQYHKWKG-EELPEKPKDLVDMIKSIKQKLPYknSKHGRSvpiVVHCSDGSSR 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568930827 1401 SGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1448
Cdd:cd14558   156 TGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1245-1453 1.48e-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: 1.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1245 NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSG 1324
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTEL-QEREQEKCVQYWPSEGSVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1325 TANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTF 1404
Cdd:cd14622    80 TLLETISIRDFLVTYNQEKQT--RLVRQFHFHGWPEI-GIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1405 CACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEY 1453
Cdd:cd14622   157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 914-1157 5.59e-46

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 167.52  E-value: 5.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  914 DATKKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIdirINRQGyhRSNHFIATQGPKPEMIYDFWRMVWQE 993
Cdd:cd14609    35 STAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPI---IEHDP--RMPAYIATQGPLSHTIADFWQMVWEN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  994 QCASIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAE-YVVRTFALERRGYSARHEVRQFHFTAWPEHGVP 1071
Cdd:cd14609   110 GCTVIVMLTPLVEDGVKQCDRYWPdEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIP 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1072 YHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIF 1150
Cdd:cd14609   190 SSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269


                  ....*..
gi 568930827 1151 IHDAILE 1157
Cdd:cd14609   270 ALTAVAE 276
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 917-1157 2.09e-45

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: 166.00  E-value: 2.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  917 KKKDKLKGGRQEPVSAYDRHHVKLHPMLADPDADYISANYIdirinRQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCA 996
Cdd:cd14610    40 QREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI-----MDHDPRNPAYIATQGPLPATVADFWQMVWESGCV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  997 SIVMITKLVEVGRVKCSRYWP-EDSDMYGDIKITLVKTETLAE-YVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHA 1074
Cdd:cd14610   115 VIVMLTPLAENGVKQCYHYWPdEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPAST 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1075 TGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1153
Cdd:cd14610   195 RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                  ....
gi 568930827 1154 AILE 1157
Cdd:cd14610   275 AVAE 278
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1241-1452 3.74e-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: 3.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1241 GDPN-NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEV 1319
Cdd:cd14623    20 GEENtDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE-KCAQYWPSDGSVSYGDITI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1320 EFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGGG 1399
Cdd:cd14623    99 ELKKEEECESYTVRDLLVTNTRENKSRQ--IRQFHFHGWPEV-GIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAG 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1400 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14623   176 RTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 926-1166 6.42e-45

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: 164.04  E-value: 6.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  926 RQEPVSAYDRHHVKLHpmlaDPDADYISANYIDIRINRQGYhrsnhfIATQGPKPEMIYDFWRMVWQEQCASIVMITKLV 1005
Cdd:cd14608    30 RYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSY------ILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVM 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1006 EVGRVKCSRYWP--EDSDMY---GDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAF 1080
Cdd:cd14608   100 EKGSLKCAQYWPqkEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1081 IRRVK--ASTPPDAGPIVIHCSAGTGRTGCYIVLD---VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1155
Cdd:cd14608   180 LFKVResGSLSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAV 259

                         250
                  ....*....|...
gi 568930827 1156 LEAC--LCGETTI 1166
Cdd:cd14608   260 IEGAkfIMGDSSV 272
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1164-1454 9.61e-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: 9.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1164 TTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLnsVTPPLDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISSD 1240
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYETtrvCLQPIRGVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1241 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1320
Cdd:cd14627    80 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1321 FVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAESG-DGRTVVHCLNGGG 1399
Cdd:cd14627   157 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVG 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1400 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1454
Cdd:cd14627   234 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1164-1458 1.44e-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: 1.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1164 TTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISSD 1240
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKA--HTSRFISANLPCNKFKNRLVNIMPYEStrvCLQPIRGVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1241 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1320
Cdd:cd14628    79 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1321 FVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAESG-DGRTVVHCLNGGG 1399
Cdd:cd14628   156 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVG 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1400 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEALE 1458
Cdd:cd14628   233 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFD 291
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1188-1447 2.01e-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: 2.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1188 SQLREEFQTLnSVTPPLDVEECSiaLLPRNRDKNRSMDVLPPDRCLPFLISSDGDPN-NYINAALTDSYTRSAAFIVTLH 1266
Cdd:cd14543     3 RGIYEEYEDI-RREPPAGTFLCS--LAPANQEKNRYGDVLCLDQSRVKLPKRNGDERtDYINANFMDGYKQKNAYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1267 PLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWP--EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQ 1344
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVE-RGRVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1345 EghLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEV------------DKWQAESGDGRTVVHCLNGGGRSGTFCA---CAT 1409
Cdd:cd14543   159 S--RQVTHFQFTSWPDF-GVPSSAAALLDFLGEVrqqqalavkamgDRWKGHPPGPPIVVHCSAGIGRTGTFCTldiCLS 235

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568930827 1410 VLEMIRchsLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd14543   236 QLEDVG---TLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 951-1157 5.12e-44

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 159.54  E-value: 5.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDIRINrqgyHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP-----EDSDMYGD 1025
Cdd:cd14540     1 YINASHITATVG----GKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggeHDALTFGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1026 IKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA------------STPPdag 1093
Cdd:cd14540    77 YKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtnqdvaghNRNP--- 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568930827 1094 PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14540   154 PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 926-1156 5.21e-44

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 161.56  E-value: 5.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  926 RQEPVSAYDRHHVKLhpmlaDPDADYISANYIDIRInrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLV 1005
Cdd:cd14600    45 RYKDVLPYDATRVVL-----QGNEDYINASYVNMEI--PSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1006 EVGRVKCSRYWPEDSDM--YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRR 1083
Cdd:cd14600   118 ERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNY 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1084 VKaSTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1156
Cdd:cd14600   198 VR-SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1164-1454 8.19e-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: 8.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1164 TTIPVNEFKATYREMIRIDPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISSD 1240
Cdd:cd14629     2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKA--HTSRFISANLPCNKFKNRLVNIMPYELtrvCLQPIRGVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1241 GdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1320
Cdd:cd14629    80 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1321 FVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAESG-DGRTVVHCLNGGG 1399
Cdd:cd14629   157 PMAEYNMPQYILREFKVTDARDGQS--RTIRQFQFTDWPE-QGVPKTGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVG 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1400 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1454
Cdd:cd14629   234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PHA02738 PHA02738
hypothetical protein; Provisional
 950-1155 8.86e-44

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 162.40  E-value: 8.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  950 DYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP--EDSDM-YGDI 1026
Cdd:PHA02738   76 DYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdvEQGSIrFGKF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1027 KITLVKTETLAEYVVRTFALErRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA----------------STPP 1090
Cdd:PHA02738  150 KITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQcqkelaqeslqighnrLQPP 228

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1091 dagPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1155
Cdd:PHA02738  229 ---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 951-1153 3.45e-42

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 153.72  E-value: 3.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRvKCSRYWPED-SDMYGDIKIT 1029
Cdd:cd14556     1 YINAALLD------SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWPDEgSGTYGPIQVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1030 LVkTETLAEYVV-RTFALER--RGYSARHEVRQFHFTAWPEHG-VPYHATGLLAFIRRV-KASTPPDAGPIVIHCSAGTG 1104
Cdd:cd14556    74 FV-STTIDEDVIsRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1105 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1153
Cdd:cd14556   153 RSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 972-1153 3.19e-41

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 151.00  E-value: 3.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  972 FIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPED---SDMYGDIKITLVKTETLAEYVVRTFALER 1048
Cdd:cd14539    17 FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAITVSLQSVRTTPTHVERIISIQH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1049 RGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---STPPDAGPIVIHCSAGTGRTGCY-IVLDVMLDMAECEGV 1124
Cdd:cd14539    97 KDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCSSGVGRTGAFcLLYAAVQEIEAGNGI 176

                         170       180
                  ....*....|....*....|....*....
gi 568930827 1125 VDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1153
Cdd:cd14539   177 PDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 951-1152 4.93e-41

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: 150.31  E-value: 4.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDIriNRQGYHRSnhFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVE-VGRVKCSRYWP---EDSDMYGDI 1026
Cdd:cd17658     1 YINASLVET--PASESLPK--FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPaeeNESREFGRI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1027 KITLVKTETlaeyvvRTFALERRGYSARH--------EVRQFHFTAWPEHGVPYHATGLLAFIRRVkASTPPDAGPIVIH 1098
Cdd:cd17658    77 SVTNKKLKH------SQHSITLRVLEVQYieseepplSVLHIQYPEWPDHGVPKDTRSVRELLKRL-YGIPPSAGPIVVH 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1099 CSAGTGRTGCYIVLDVML------DMAecegVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1152
Cdd:cd17658   150 CSAGIGRTGAYCTIHNTIrrilegDMS----AVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 926-1155 1.89e-40

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: 150.50  E-value: 1.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  926 RQEPVSAYDRHHVKLHPMladpDADYISANYIDIRINRQGYhrsnhfIATQGPKPEMIYDFWRMVWQEQCASIVMITKLV 1005
Cdd:cd14607    29 RYRDVSPYDHSRVKLQNT----ENDYINASLVVIEEAQRSY------ILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1006 EVGRVKCSRYWPEDSD---MYGD--IKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAF 1080
Cdd:cd14607    99 EKDSVKCAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNF 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1081 IRRVK--ASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEG--VVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1155
Cdd:cd14607   179 LFKVResGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1182-1457 5.41e-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: 5.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1182 DPQSNSSQLREEFQTLNSVTPPLDVeeCSIALLPRNRDKNRSMDVLPPDRCLPFL-ISSDGDPNNYINAA-LTDSYTRSA 1259
Cdd:cd14610    11 DHLKNKNRLEKEWEALCAYQAEPNA--TNVAQREENVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASpIMDHDPRNP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1260 AFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFVSGTA-NEDLVSRVFRVQ 1338
Cdd:cd14610    89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAE-NGVKQCYHYWPDEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1339 NssrLQEGHL-LVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQAesgdGRT---VVHCLNGGGRSGTFCACATVL-EM 1413
Cdd:cd14610   168 N---LQTNETrTVTQFHFLSWND-QGVPASTRSLLDFRRKVNKCYR----GRScpiIVHCSDGAGRSGTYILIDMVLnKM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568930827 1414 IRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEAL 1457
Cdd:cd14610   240 AKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1217-1452 1.04e-37

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


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 142.15  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1217 NRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQ 1295
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPgSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL-E 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1296 SNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRV--QNSSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLH 1373
Cdd:cd14553    82 ERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKRE----VRQFQFTAWPDH-GVPEHPTPFLA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1374 LLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14553   157 FLRRV-KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1222-1445 3.90e-37

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 139.80  E-value: 3.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1222 RSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAW 1300
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCME-KGRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1301 PCLQYWPEPGRQQ-YGLMEVEFVSGTANEDLVSRVFRVQNSSRlqegHLLVRHFQFLRWSAYR--DTPDSRKAFLHLLAE 1377
Cdd:cd14548    80 KCDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKLERGDE----VRSVRQFHFTAWPDHGvpEAPDSLLRFVRLVRD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930827 1378 vdkwQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1445
Cdd:cd14548   156 ----YIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 926-1157 1.54e-36

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 140.52  E-value: 1.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  926 RQEPVSAYDRHHVKLHPMLADPDAdYISANYIDIRINRQGYHrsnhFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLV 1005
Cdd:cd14599    43 RIREVVPYEENRVELVPTKENNTG-YINASHIKVTVGGEEWH----YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1006 EVGRVKCSRYWPE-----DSDMYGDIKITL-VKTETLAeYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLA 1079
Cdd:cd14599   118 EGGRSKSHRYWPKlgskhSSATYGKFKVTTkFRTDSGC-YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1080 F---IRRVKASTPP--DAG-----PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYI 1149
Cdd:cd14599   197 YleeIQSVRRHTNSmlDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYK 276


                  ....*...
gi 568930827 1150 FIHDAILE 1157
Cdd:cd14599   277 FVYQVLIQ 284
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1212-1445 9.64e-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: 9.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1212 ALLPRNRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML 1290
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEgSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1291 NQLNQSNSAwPCLQYWP---EPgrQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSAYR-DTPD 1366
Cdd:cd14614    87 TQCNEKRRV-KCDHYWPfteEP--VAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHGvPTAN 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1367 SRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1445
Cdd:cd14614   160 AAESILQFVQMV-RQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 902-1157 2.75e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 137.06  E-value: 2.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  902 FKQEYESFFEG------WDATKKKDkLKGGRQEPVSAYDRHHVKLHpmLADPDADYISANYIDirinrqGYHRSNHFIAT 975
Cdd:PHA02742   28 LKEEHEHIMQEivafscNESLELKN-MKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVD------GHNAKGRFICT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  976 QGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYW---PEDSDMYGDIKITLVKTETLAEYVVRTFALERRGYS 1052
Cdd:PHA02742   99 QAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmphERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1053 ARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV-----------KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAEC 1121
Cdd:PHA02742  179 ASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNE 258

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568930827 1122 EGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:PHA02742  259 RAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1246-1447 3.78e-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: 3.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPClqYWPEPGRQQYG------LMEV 1319
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTD-NELNEDEPI--YWPTKEKPLECetfkvtLSGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1320 EFVSGTANEDLVSRVFRVQNSsrlQEGHLL-VRHFQFLRWSAyRDTPDSrkAFLHLLAEVDKWqAESGDGRTVVHCLNGG 1398
Cdd:cd14550    78 DHSCLSNEIRLIVRDFILEST---QDDYVLeVRQFQCPSWPN-PCSPIH--TVFELINTVQEW-AQQRDGPIVVHDRYGG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568930827 1399 GRSGTFCACATVL-EMIRCHSlVDVFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd14550   151 VQAATFCALTTLHqQLEHESS-VDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1246-1448 4.49e-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: 4.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRR-KCDQYWPKEGTETYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQN----SSRLQEGHLLVRHFQFLRWSAYrDTPDSRkafLHLLAEVDKWQAES--GDGRTVVHCLNGGG 1399
Cdd:cd14549    80 VLATYTVRTFSLKNlklkKVKGRSSERVVYQYHYTQWPDH-GVPDYT---LPVLSFVRKSSAANppGAGPIVVHCSAGVG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1400 RSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1448
Cdd:cd14549   156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1056-1157 5.64e-35

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 129.02  E-value: 5.64e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1056 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP--PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECE-GVVDIYNCVK 1132
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 568930827   1133 TLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1056-1157 5.64e-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: 129.02  E-value: 5.64e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1056 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP--PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECE-GVVDIYNCVK 1132
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 568930827   1133 TLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 951-1157 2.90e-34

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


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 131.64  E-value: 2.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDIRINRQGYHrsnhFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWP-----EDSDMYGD 1025
Cdd:cd14598     1 YINASHIKVTVGGKEWD----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1026 IKITL-VKTETLAeYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFI-------RRVKASTPPDAG--PI 1095
Cdd:cd14598    77 FKITTrFRTDSGC-YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLeeiqsvrRHTNSTIDPKSPnpPV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1096 VIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14598   156 LVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1246-1447 3.41e-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: 3.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAA-LTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSG 1324
Cdd:cd14546     1 YINAStIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRL-QENGVKQCARYWPEEGSEVYHIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1325 TA-NEDLVSRVFRVQNssrLQEGHL-LVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKwqaeSGDGRT---VVHCLNGGG 1399
Cdd:cd14546    80 HIwCDDYLVRSFYLKN---LQTSETrTVTQFHFLSWPD-EGIPASAKPLLEFRRKVNK----SYRGRScpiVVHCSDGAG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1400 RSGTFCACATVLE-MIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd14546   152 RTGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
947-1151 3.98e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 133.29  E-value: 3.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  947 PDADYISANYIDIRINRQgyhrsnhFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVG--RVKCSRYWPEDSDmYG 1024
Cdd:COG5599    61 ANLGYLNANYIQVIGNHR-------YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGE-YG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1025 --DIKITLVKTETLAEYV-VRTFALERRGYSAR-HEVRQFHFTAWPEHGVPyHATGLLAFIRRVKAS---TPPDAGPIVI 1097
Cdd:COG5599   133 kyEVSSELTESIQLRDGIeARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKekiKDPDKLLPVV 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827 1098 HCSAGTGRTGCYIVLDVMLDM--AECEGVVDIYNCVKTL-CSRRVNMIQTEEQYIFI 1151
Cdd:COG5599   212 HCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMrTSRNGGMVQTSEQLDVL 268
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1221-1451 4.35e-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: 4.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1221 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqLNQSNSA 1299
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLT-VGMENGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1300 WPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYR--DTPDSRKAFLHLLA 1376
Cdd:cd14618    80 VLCDHYWPsESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERR--VKHLHYTAWPDHGipESTSSLMAFRELVR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1377 EvdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1451
Cdd:cd14618   158 E--HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1182-1457 5.43e-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: 5.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1182 DPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRClPFLISSDGDPN--NYINAA-LTDSYTRS 1258
Cdd:cd14609     9 DHLRNRDRLAKEWQALCAYQA--EPNTCSTAQGEANVKKNRNPDFVPYDHA-RIKLKAESNPSrsDYINASpIIEHDPRM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1259 AAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFVSGTA-NEDLVSRVFRV 1337
Cdd:cd14609    86 PAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVE-DGVKQCDRYWPDEGSSLYHIYEVNLVSEHIwCEDFLVRSFYL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1338 QNsSRLQEGHLLVRhFQFLRWSAyRDTPDSRKAFLHLLAEVDKwqaeSGDGRT---VVHCLNGGGRSGTFCACATVL-EM 1413
Cdd:cd14609   165 KN-VQTQETRTLTQ-FHFLSWPA-EGIPSSTRPLLDFRRKVNK----CYRGRScpiIVHCSDGAGRTGTYILIDMVLnRM 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568930827 1414 IRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEAL 1457
Cdd:cd14609   238 AKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1217-1452 6.38e-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: 6.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1217 NRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQ 1295
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSVDGVPgSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRL-E 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1296 SNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRV--QNSSRLQEghllVRHFQFLRWSAY--RDTPDSRKAF 1371
Cdd:cd14626   120 EKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALykNGSSEKRE----VRQFQFMAWPDHgvPEYPTPILAF 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1372 LHLLAEVDKWQAesgdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1451
Cdd:cd14626   196 LRRVKACNPPDA----GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271


                  .
gi 568930827 1452 E 1452
Cdd:cd14626   272 E 272
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1221-1452 8.22e-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: 130.32  E-value: 8.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1221 NRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAw 1300
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1301 PCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYR--DTPDSRKAFLHLLAEV 1378
Cdd:cd14615    80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRT--VRHFHFTSWPDHGvpETTDLLINFRHLVREY 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568930827 1379 DKwqAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14615   158 MK--QNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 951-1151 1.16e-33

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 128.98  E-value: 1.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCsrYWPEDSDM--YGDIKI 1028
Cdd:cd14550     1 YINASYL------QGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPleCETFKV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1029 TLVKTETL-----AEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPIVIH----- 1098
Cdd:cd14550    73 TLSGEDHSclsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHdrygg 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1099 CSAGTgrtgcYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFI 1151
Cdd:cd14550   151 VQAAT-----FCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1217-1452 6.28e-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: 6.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1217 NRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQ 1295
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1296 SNSAwPCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQN--SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLH 1373
Cdd:cd14630    83 VGRV-KCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKkgYHEIRE----IRQFHFTSWPDH-GVPCYATGLLG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1374 LLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14630   156 FVRQV-KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1218-1447 2.50e-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: 2.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1218 RDKNRSMDVLPPDRCLPFLISSDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSN 1297
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD---NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1298 SAwPCLQYWPEPGRQQYGL----MEVEFVSGTANEDLVSRVFRVQNSSRLQEghLLVRHFQFLRWSAYrDTPDSRKAFLH 1373
Cdd:cd14545    78 QI-KCAQYWPQGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDF-GVPESPAAFLN 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827 1374 LLAEV-DKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL--VDVFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd14545   154 FLQKVrESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 913-1152 6.70e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 127.43  E-value: 6.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  913 WDATKKKDKLKGGRQEPVSAYDRHHVKLHPMlADPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQ 992
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWID------GFEDDKKFIATQGPFAETCADFWKAVWQ 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  993 EQCASIVMITKLVEV-GRVKCSRYW--PEDSDM-YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEH 1068
Cdd:PHA02747  116 EHCSIIVMLTPTKGTnGEEKCYQYWclNEDGNIdMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFED 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1069 GVPYHATGLLAFI------RRVKAS--TPPDA--GPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRR 1138
Cdd:PHA02747  196 ETPSDHPDFIKFIkiidinRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQR 275

                         250
                  ....*....|....
gi 568930827 1139 VNMIQTEEQYIFIH 1152
Cdd:PHA02747  276 HAGIMNFDDYLFIQ 289
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1166-1452 8.94e-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: 8.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1166 IPVNEFkATYREMIRIDpqsNSSQLREEFQTLNsvtpPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISSDG-DPN 1244
Cdd:cd14625     4 IPISEL-AEHTERLKAN---DNLKLSQEYESID----PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1245 NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSG 1324
Cdd:cd14625    76 DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKL-EEKSRIKCDQYWPSRGTETYGMIQVTLLDT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1325 TANEDLVSRVFRVQN--SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGdGRTVVHCLNGGGRSG 1402
Cdd:cd14625   155 IELATFCVRTFSLHKngSSEKRE----VRQFQFTAWPDH-GVPEYPTPFLAFLRRVKTCNPPDA-GPIVVHCSAGVGRTG 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 568930827 1403 TFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14625   229 CFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1225-1452 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 568930827 1225 DVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCL 1303
Cdd:cd14620     3 NILPYDHSRVILSQLDGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE-KCY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1304 QYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQnsSRLQEGH---LLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdK 1380
Cdd:cd14620    82 QYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ--PQLPDGCkapRLVTQLHFTSWPDF-GVPFTPIGMLKFLKKV-K 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1381 WQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14620   158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1209-1452 2.79e-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: 2.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1209 CSIALLPRNRDKNRSMDVLPPDRCLPFLISSDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1288
Cdd:cd14608    17 CRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED---NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1289 MLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVS----RVFRVQNSSRLQEGHLLvrHFQFLRWSAYrDT 1364
Cdd:cd14608    94 MLNRVMEKGSL-KCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSyytvRQLELENLTTQETREIL--HFHYTTWPDF-GV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1365 PDSRKAFLHLLAEVdkwqAESGD-----GRTVVHCLNGGGRSGTFC---ACATVLEMIRCHSLVDVFFAAKTLRNYKPNM 1436
Cdd:cd14608   170 PESPASFLNFLFKV----RESGSlspehGPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGL 245

                         250
                  ....*....|....*.
gi 568930827 1437 VETMDQYHFCYDVALE 1452
Cdd:cd14608   246 IQTADQLRFSYLAVIE 261
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1190-1453 3.88e-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: 3.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1190 LREEFQTLNSVtpPLDVEeCSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPN-NYINAALTDSYTRSAAFIVTLHPL 1268
Cdd:cd14621    28 FREEFNALPAC--PIQAT-CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDsDYINASFINGYQEKNKFIAAQGPK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1269 QSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRL--QEG 1346
Cdd:cd14621   105 EETVNDFWRMIWEQNTATIVMVTNLKERKEC-KCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVtnKKP 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1347 HLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAA 1426
Cdd:cd14621   184 QRLITQFHFTSWPDF-GVPFTPIGMLKFLKKVKNCNPQYA-GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFV 261

                         250       260
                  ....*....|....*....|....*..
gi 568930827 1427 KTLRNYKPNMVETMDQYHFCYDVALEY 1453
Cdd:cd14621   262 SRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1246-1452 8.58e-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: 8.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGrQQYGLMEVEFVSGT 1325
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRV-KCSKYWPDDS-DTYGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNssRLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGTFC 1405
Cdd:cd14632    79 TLAEYSVRTFALER--RGYSARHEVKQFHFTSWPEH-GVPYHATGLLAFIRRV-KASTPPDAGPVVVHCSAGAGRTGCYI 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568930827 1406 ACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14632   155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1246-1447 9.21e-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: 9.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKE-RKEKKCSQYWPDQGCWTYGNLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNSSRL--QEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGT 1403
Cdd:cd14551    80 VLVDYTTRKFCIQKVNRGigEKRVRLVTQFHFTSWPDF-GVPFTPIGMLKFLKKV-KSANPPRAGPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568930827 1404 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1246-1448 1.76e-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: 1.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAA-LTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQ-YGLMEVEFVS 1323
Cdd:cd18533     1 YINASyITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVE-NGREKCDQYWPSGEYEGeYGDLTVELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1324 GTANED--LVSRVFRVQNSsrlQEGHLLVRHFQFLRWSAYRdTPDSRKAFLHLLAEVDKW-QAESGDGRTVVHCLNGGGR 1400
Cdd:cd18533    80 EEENDDggFIVREFELSKE---DGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLIKLKRELnDSASLDPPIIVHCSAGVGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827 1401 SGTFCACATVLEMIRCHSLVD---------VFFAAKTLRNYKPNMVETMDQYHFCYD 1448
Cdd:cd18533   156 TGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1246-1452 2.16e-30

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


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 119.64  E-value: 2.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEpGRQQYGLMEVEFVSGT 1325
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRV-KCSRYWPD-DTEVYGDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQNS--SRLQEghllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLNGGGRSGT 1403
Cdd:cd14555    79 PLAEYVVRTFALERRgyHEIRE----VRQFHFTGWPDH-GVPYHATGLLGFIRRV-KASNPPSAGPIVVHCSAGAGRTGC 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1404 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14555   153 YIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1214-1452 3.49e-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: 3.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1214 LPRNRDKNRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQ 1292
Cdd:cd14624    44 LEVNKPKNRYANVIAYDHSRVLLSAIEGIPgSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1293 LnQSNSAWPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRV--QNSSRLQEghllVRHFQFLRWSAYrDTPDSRKA 1370
Cdd:cd14624   124 L-EERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALykNGSSEKRE----VRQFQFTAWPDH-GVPEHPTP 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1371 FLHLLAEVDKWQAESGdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVA 1450
Cdd:cd14624   198 FLAFLRRVKTCNPPDA-GPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276


                  ..
gi 568930827 1451 LE 1452
Cdd:cd14624   277 LE 278
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 951-1157 6.06e-30

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: 118.59  E-value: 6.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLvEVGRVkCSRYWPEDSD-MYGDIKIT 1029
Cdd:cd14634     1 YINAALMD------SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQL-CMQYWPEKTScCYGPIQVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1030 LVKTETLAEYVVRTF-----ALERRGYSArheVRQFHFTAWPEH-GVPYHATGLLAFIRRV-KASTPPDA--GPIVIHCS 1100
Cdd:cd14634    73 FVSADIDEDIISRIFricnmARPQDGYRI---VQHLQYIGWPAYrDTPPSKRSILKVVRRLeKWQEQYDGreGRTVVHCL 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827 1101 AGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14634   150 NGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1246-1448 6.18e-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: 6.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAA-FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLnQLNQSNSAWPCLQYWPEPGRQQ--YGLMEVEFV 1322
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVML-VSEQENEKQKVHRYWPTERGQAlvYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1323 SGTANEDLVSRVFRVQNssRLQEGHLLVRHFQFLRWSAYRdTPDSRKAFLHLLAEVDKW--QAESGDGRTVVHCLNGGGR 1400
Cdd:cd14539    80 SVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHylQQRSLQTPIVVHCSSGVGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1401 SGTFCAC-ATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1448
Cdd:cd14539   157 TGAFCLLyAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 951-1157 2.64e-29

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 116.66  E-value: 2.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGrvKCSRYWPEDSDM-YGDIKIT 1029
Cdd:cd14636     1 YINAALMD------SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWPEEGMLrYGPIQVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1030 LVKTETLAEYVVRTFAL-----ERRGYSArheVRQFHFTAWPEH-GVPYHATGLLAFIRRV---KASTPPDAGPIVIHCS 1100
Cdd:cd14636    73 CMSCSMDCDVISRIFRIcnltrPQEGYLM---VQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECDEGEGRTIIHCL 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568930827 1101 AGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14636   150 NGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1246-1447 3.24e-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: 3.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAAL--TDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQ--YGLMEVEF 1321
Cdd:cd17658     1 YINASLveTPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAKCADYFPAEENESreFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1322 VS-GTANEDLVSRVFRVQNsSRLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdkWQAESGDGRTVVHCLNGGGR 1400
Cdd:cd17658    81 KKlKHSQHSITLRVLEVQY-IESEEPPLSVLHIQYPEWPDH-GVPKDTRSVRELLKRL--YGIPPSAGPIVVHCSAGIGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568930827 1401 SGTFCACATVLEMIRCHSL--VDVFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd17658   157 TGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1211-1447 3.44e-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: 3.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1211 IALLPRNRDKNRSMDVLPPDRCLPFLISSDgdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML 1290
Cdd:cd14607    18 VAKYPENRNRNRYRDVSPYDHSRVKLQNTE---NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1291 NQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVS----RVFRVQNssrLQEGHL-LVRHFQFLRWSAYrDTP 1365
Cdd:cd14607    95 NRIVEKDSV-KCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSyytvHLLQLEN---INSGETrTISHFHYTTWPDF-GVP 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1366 DSRKAFLHLLAEVdkwqAESG-----DGRTVVHCLNGGGRSGTFCACATVLEMIRCHS--LVDVFFAAKTLRNYKPNMVE 1438
Cdd:cd14607   170 ESPASFLNFLFKV----RESGslspeHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQ 245


                  ....*....
gi 568930827 1439 TMDQYHFCY 1447
Cdd:cd14607   246 TPDQLRFSY 254
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 951-1157 1.20e-28

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 115.01  E-value: 1.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRV-KCSRYWPEDS-DMYGDIKI 1028
Cdd:cd14637     1 YINAALTD------SYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGlQQYGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1029 TLVKTETLAEYVVRTFALER--RGYSARHEVRQFHFTAW-PEHGVPYHATGLLAFIRRV-KASTPPDAGPIVIHCSAGTG 1104
Cdd:cd14637    75 EFVSGSADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1105 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14637   155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1215-1447 1.32e-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: 116.46  E-value: 1.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1215 PRNRDKNRSMDVLPPDR---CLPFLISSDGdpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1291
Cdd:cd14603    28 KENVKKNRYKDILPYDQtrvILSLLQEEGH--SDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMAC 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1292 QlNQSNSAWPCLQYWP-EPGRQQYGLMEVEFVSGT-ANEDLVSRVFRV--QNSSRlqeghlLVRHFQFLRWSAyRDTPDS 1367
Cdd:cd14603   106 R-EIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKVtfQKESR------SVSHFQYMAWPD-HGIPDS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1368 RKAFLHLLAEVDKWQAESGDgRTVVHCLNGGGRSGTFCACATV-----LEMIRCH-SLVDVFFaakTLRNYKPNMVETMD 1441
Cdd:cd14603   178 PDCMLAMIELARRLQGSGPE-PLCVHCSAGCGRTGVICTVDYVrqlllTQRIPPDfSIFDVVL---EMRKQRPAAVQTEE 253


                  ....*.
gi 568930827 1442 QYHFCY 1447
Cdd:cd14603   254 QYEFLY 259
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1217-1455 2.63e-28

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


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 115.25  E-value: 2.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1217 NRDKNRSMDVLPPDRCLpfLISSDGDPN----NYINAaltdSYTRSAA-----------FIVTLHPLQSTTPDFWRLVYD 1281
Cdd:cd14544     1 NKGKNRYKNILPFDHTR--VILKDRDPNvpgsDYINA----NYIRNENegpttdenaktYIATQGCLENTVSDFWSMVWQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1282 YGCTSIVML-NQLNQSNSAwpCLQYWPEPGRQ-QYGLMEVEFVSGTANEDLVSRVFRVqnsSRLQEGHLL--VRHFQFLR 1357
Cdd:cd14544    75 ENSRVIVMTtKEVERGKNK--CVRYWPDEGMQkQYGPYRVQNVSEHDTTDYTLRELQV---SKLDQGDPIreIWHYQYLS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1358 WSAYrDTPDSRKAFLHLLAEVDKWQAESGD-GRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYK 1433
Cdd:cd14544   150 WPDH-GVPSDPGGVLNFLEDVNQRQESLPHaGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQR 228

                         250       260
                  ....*....|....*....|..
gi 568930827 1434 PNMVETMDQYHFCYDVALEYLE 1455
Cdd:cd14544   229 SGMVQTEAQYKFIYVAVAQYIE 250
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1204-1449 3.25e-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: 3.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1204 LDVEECSIALLPRnrdKNRSMDVLPPDRCLPFLISSD-GDP-NNYINAALTDSY-TRSAAFIVTLHPLQSTTPDFWRLVY 1280
Cdd:cd14613    15 VDPKEYDIPGLVR---KNRYKTILPNPHSRVCLTSPDqDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVW 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1281 DYGCTSIVMLNQLNQSNSAwpCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSA 1360
Cdd:cd14613    92 QERSPIIVMITNIEEMNEK--CTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITLKSGGEERG----LKHYWYTSWPD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1361 YRdTPDSRKAFLHLLAEVD--KWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVE 1438
Cdd:cd14613   165 QK-TPDNAPPLLQLVQEVEeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQ 243

                         250
                  ....*....|.
gi 568930827 1439 TMDQYHFCYDV 1449
Cdd:cd14613   244 TCEQYQFVHHV 254
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1221-1447 4.79e-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: 4.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1221 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSA 1299
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1300 wPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLqEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEV 1378
Cdd:cd14617    81 -KCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQL-DAPRLVRHFHYTVWPDH-GVPETTQSLIQFVRTV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1379 -DKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd14617   158 rDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1217-1455 5.14e-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: 5.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1217 NRDKNRSMDVLPPDRCLpfLISSDGDPN----NYINA--ALTDSYTRS------AAFIVTLHPLQSTTPDFWRLVYDYGC 1284
Cdd:cd14605     2 NKNKNRYKNILPFDHTR--VVLHDGDPNepvsDYINAniIMPEFETKCnnskpkKSYIATQGCLQNTVNDFWRMVFQENS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1285 TSIVMLNQLNQSNSAwPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVqnsSRLQEGHL--LVRHFQFLRWSAY 1361
Cdd:cd14605    80 RVIVMTTKEVERGKS-KCVKYWPdEYALKEYGVMRVRNVKESAAHDYILRELKL---SKVGQGNTerTVWQYHFRTWPDH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1362 rDTPDSRKAFLHLLAEVD-KWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYKPNMV 1437
Cdd:cd14605   156 -GVPSDPGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMV 234

                         250
                  ....*....|....*...
gi 568930827 1438 ETMDQYHFCYDVALEYLE 1455
Cdd:cd14605   235 QTEAQYRFIYMAVQHYIE 252
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1221-1445 6.01e-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: 6.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1221 NRSMDVLPPDR---CLPfliSSDGDP-NNYINAaltdSYTR-----SAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1291
Cdd:cd14547     1 NRYKTILPNEHsrvCLP---SVDDDPlSSYINA----NYIRgydgeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMIT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1292 QLNQSNSAwpCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSAYRdTPDSRKAF 1371
Cdd:cd14547    74 NLTEAKEK--CAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRY----LKHYWYTSWPDHK-TPEAAQPL 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1372 LHLLAEVDKW-QAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1445
Cdd:cd14547   147 LSLVQEVEEArQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1214-1447 6.97e-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: 6.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1214 LPRNRDKNRSMDVLP-PDR--CLPFLISSDgDPNNYINAALTDSYT-RSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVM 1289
Cdd:cd14612    12 IPGHASKDRYKTILPnPQSrvCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1290 LNQLNQSNSAwpCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQnssrLQEGHLLVRHFQFLRWSAYRdTPDSRK 1369
Cdd:cd14612    91 ITKLKEKKEK--CVHYWPEK-EGTYGRFEIRVQDMKECDGYTIRDLTIQ----LEEESRSVKHYWFSSWPDHQ-TPESAG 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1370 AFLHLLAEVDKW-QAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd14612   163 PLLRLVAEVEESrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1246-1451 1.85e-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: 1.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqlNQSNSAWPCLQYWP---EPGRQQ---YGLMEV 1319
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLP--DGQNMAEDEFVYWPnkdEPINCEtfkVTLIAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1320 EFVSGTANEDLVSRVFRVQNSsrlQEGHLL-VRHFQFLRWSayrdTPDSRKAFLHLLAEVDKWQAESGDGRTVVHCLNGG 1398
Cdd:cd17669    79 EHKCLSNEEKLIIQDFILEAT---QDDYVLeVRHFQCPKWP----NPDSPISKTFELISIIKEEAANRDGPMIVHDEHGG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1399 GRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1451
Cdd:cd17669   152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1246-1451 1.94e-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: 1.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML--NQ-LNQSNSAwpclqYWPEpgRQQ--------Y 1314
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQgLAEDEFV-----YWPS--REEsmnceaftV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1315 GLMEVEFVSGTANEDLVSRVFRVQNSsrlQEGHLL-VRHFQFLRWSayrdTPDSRKAFLHLLAEVDKWQAESGDGRTVVH 1393
Cdd:cd17670    74 TLISKDRLCLSNEEQIIIHDFILEAT---QDDYVLeVRHFQCPKWP----NPDAPISSTFELINVIKEEALTRDGPTIVH 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568930827 1394 CLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1451
Cdd:cd17670   147 DEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1215-1452 2.97e-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: 2.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1215 PRNRDKNRSMDVLPPDRC---LPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1291
Cdd:cd17667    25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1292 QLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNS--SRLQEGHLLVRH-------FQFLRWsayr 1362
Cdd:cd17667   105 NLVEKGRR-KCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTkvKKGQKGNPKGRQnertviqYHYTQW---- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1363 dtPDS--RKAFLHLLAEVDKWQAE--SGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVE 1438
Cdd:cd17667   180 --PDMgvPEYALPVLTFVRRSSAArtPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQ 257

                         250
                  ....*....|....
gi 568930827 1439 TMDQYHFCYDVALE 1452
Cdd:cd17667   258 TEEQYIFIHDALLE 271
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1220-1447 3.76e-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: 3.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1220 KNRSMDVLPPDRCLPFL--ISSDGDPNNYINAALTDSYT-RSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1296
Cdd:cd14611     2 KNRYKTILPNPHSRVCLkpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1297 NSAwpCLQYWPEPgRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEghllVRHFQFLRWSAYRdTPDSRKAFLHLLA 1376
Cdd:cd14611    82 NEK--CVLYWPEK-RGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRS----VKHYWYTSWPDHK-TPDSAQPLLQLML 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1377 EVDKWQAES-GDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd14611   154 DVEEDRLASpGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1221-1454 4.54e-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: 4.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1221 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSA 1299
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPgSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME-AGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1300 WPCLQYWP-EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNssRLQEGHLLVRHFQFLRWSAY--RDTPDSRKAFLHLLA 1376
Cdd:cd14619    80 VKCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQ--VEEQKTLSVRHFHFTAWPDHgvPSSTDTLLAFRRLLR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930827 1377 EVDKWQAESGDgrTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1454
Cdd:cd14619   158 QWLDQTMSGGP--TVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1246-1445 4.89e-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: 4.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAA----FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPG-RQQYGLMEVE 1320
Cdd:cd14541     2 YINANYVNMEIPGSGivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRV-KCHQYWPDLGeTMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1321 FVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDgRTVVHCLNGGGR 1400
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERH--ITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRVGMVE-PTVVHCSAGIGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568930827 1401 SGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1445
Cdd:cd14541   157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 951-1157 1.30e-26

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 109.01  E-value: 1.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKlVEVGRVkCSRYWPEDS-DMYGDIKIT 1029
Cdd:cd14635     1 YINAALMD------SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWPENGvHRHGPIQVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1030 LVKTETLAEYVVRTFAL--ERRGYSARHEVRQFHFTAWPEH-GVPYHATGLLAFIRRV-KASTPPDAGP--IVIHCSAGT 1103
Cdd:cd14635    73 FVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdKWQEEYNGGEgrTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568930827 1104 GRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1157
Cdd:cd14635   153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1246-1454 2.23e-26

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 108.23  E-value: 2.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAaltdSYTR------SAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWPEPGRQQ---YGL 1316
Cdd:cd14538     1 YINA----SHIRipvggdTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQ-DVEGGKVKCHRYWPDSLNKPlicGGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1317 MEVEFVSGTANEDLVSRVFRVQNSSRLQEGHllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAesgDGRTVVHCLN 1396
Cdd:cd14538    76 LEVSLEKYQSLQDFVIRRISLRDKETGEVHH--ITHLNFTTWPDH-GTPQSADPLLRFIRYMRRIHN---SGPIVVHCSA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568930827 1397 GGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1454
Cdd:cd14538   150 GIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1217-1452 2.37e-26

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 110.13  E-value: 2.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1217 NRDKNRSMDVLPPDRCLPFLISSDGDPN-NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQ 1295
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETSsDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1296 SNSAwPCLQYWPEpGRQQYGLMEVEFVSGTANEDLVSRVFRVQN--SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFLH 1373
Cdd:cd14633   120 VGRV-KCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFAVEKrgVHEIRE----IRQFHFTGWPDH-GVPYHATGLLG 192

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1374 LLAEVdKWQAESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14633   193 FVRQV-KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 946-1155 3.37e-26

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 111.27  E-value: 3.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  946 DPDADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKlVEVGRVKCSRYW--PEDSDM- 1022
Cdd:PHA02746   95 DNAENYIHANFVD------GFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELa 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1023 YGDIKITLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA----------STPPDA 1092
Cdd:PHA02746  168 FGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTL 247

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1093 GPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1155
Cdd:PHA02746  248 GPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1240-1452 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 568930827 1240 DGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGrQQYGLME 1318
Cdd:cd14631     8 EDDPsSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRV-KCYKYWPDDT-EVYGDFK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1319 VEFVSGTANEDLVSRVFRVQNS--SRLQEghllVRHFQFLRWSAYrDTPDSRKAFLHLLAEVdKWQAESGDGRTVVHCLN 1396
Cdd:cd14631    86 VTCVEMEPLAEYVVRTFTLERRgyNEIRE----VKQFHFTGWPDH-GVPYHATGLLSFIRRV-KLSNPPSAGPIVVHCSA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930827 1397 GGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:cd14631   160 GAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1221-1445 3.14e-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: 3.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1221 NRSMDVLPPDRCLPFLISSDGDP-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSA 1299
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1300 wPCLQYWPEPGR--QQYGLMEVEFVSGTANEDLVSRVFRVQnssrlQEGH-LLVRHFQFLRWSAYrDTPDSRKAFLHLLA 1376
Cdd:cd14616    81 -RCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKIE-----RHGDyMMVRQCNFTSWPEH-GVPESSAPLIHFVK 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930827 1377 EVDKWQAESgDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1445
Cdd:cd14616   154 LVRASRAHD-NTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 951-1156 4.76e-25

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 104.31  E-value: 4.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSrYWP-EDSDMYGD-IKI 1028
Cdd:cd17669     1 YINASYI------MGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPnKDEPINCEtFKV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1029 TLVKTETLA-----EYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPIVIHCSAGT 1103
Cdd:cd17669    74 TLIAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1104 GRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1156
Cdd:cd17669   152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1215-1454 6.38e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.01  E-value: 6.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1215 PRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1294
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1295 QSNSAWPCLQYW--PEPGRQQYGLMEVEFVSGTANEDLVSRVFRVQNSSRLQEGHLlvRHFQFLRWSAYrDTPDSRKAFL 1372
Cdd:PHA02747  129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI--SHFQCSEWFED-ETPSDHPDFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1373 HLLAEVDKWQAESGDGRT---------VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQY 1443
Cdd:PHA02747  206 KFIKIIDINRKKSGKLFNpkdallcpiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                         250
                  ....*....|....
gi 568930827 1444 HF---CYDVALEYL 1454
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1246-1448 7.17e-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: 7.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFVSGT 1325
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPADGSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1326 ANEDLVSRVFRVQN------SSRLQEGHLLVRHFQFLRWsayrdtPDS--RKAFLHLLAEVDKWQA--ESGDGRTVVHCL 1395
Cdd:cd17668    80 VLAYYTVRNFTLRNtkikkgSQKGRPSGRVVTQYHYTQW------PDMgvPEYTLPVLTFVRKASYakRHAVGPVVVHCS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1396 NGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1448
Cdd:cd17668   154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1245-1454 2.52e-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: 2.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1245 NYINAALTDSYTRsaaFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWP----EPGRQQYGLMEVE 1320
Cdd:cd14540     5 SHITATVGGKQRF---YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTA-EEEGGREKCFRYWPtlggEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1321 FVSGTANEDLVSRVFRVQNSSRLQegHLLVRHFQFLRWsAYRDTPDSRKAFLHLLAEVDK-----WQAESGDGR---TVV 1392
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQ--SRTVWHLQYTDW-PDHGCPEDVSGFLDFLEEINSvrrhtNQDVAGHNRnppTLV 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1393 HCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1454
Cdd:cd14540   158 HCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 951-1156 4.33e-24

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: 101.68  E-value: 4.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  951 YISANYIdirinrQGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITK---LVEVGRVkcsrYWP--EDSDMYGD 1025
Cdd:cd17670     1 YINASYI------MGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAEDEFV----YWPsrEESMNCEA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1026 IKITLVKTETLA-----EYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPIVIHCS 1100
Cdd:cd17670    71 FTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930827 1101 AGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1156
Cdd:cd17670   149 FGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1246-1447 9.25e-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: 9.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWPEPGRQ--QYGLMEVEFVS 1323
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACR-EFEMGKKKCERYWPEEGEEqlQFGPFKISLEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1324 GTA-NEDLVSRVFRV--QNSSRlqeghlLVRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGR 1400
Cdd:cd14542    80 EKRvGPDFLIRTLKVtfQKESR------TVYQFHYTAWPD-HGVPSSVDPILDLVRLVRDYQ-GSEDVPICVHCSAGCGR 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568930827 1401 SGTFCACATVLEMIRCHSLVD---VFFAAKTLRNYKPNMVETMDQYHFCY 1447
Cdd:cd14542   152 TGTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1246-1455 9.53e-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: 100.59  E-value: 9.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAaltdSYTRSAA------FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGL--M 1317
Cdd:cd14596     1 YINA----SYITMPVgeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKV-KCHRYWPETLQEPMELenY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1318 EVEFVSGTANEDLVSRVFR-VQNSSrlQEGHLlVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAEsgdGRTVVHCLN 1396
Cdd:cd14596    76 QLRLENYQALQYFIIRIIKlVEKET--GENRL-IKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT---GPIVVHCSA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1397 GGGRSGTFCACATVLEMIR---CHSLVDVffaAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1455
Cdd:cd14596   149 GIGRAGVLICVDVLLSLIEkdlSFNIKDI---VREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1217-1454 1.67e-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: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1217 NRDKNRSMDVLPPDRCLPFLissdGDPNNYINAALTDSYTRSAAF--IVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1294
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1295 QSNSAwPCLQYWPEPGRQQYGL---MEVEFVSGTANEDLVSRVFRVQNssrLQEGHllVRHFQFLRWSAYRD--TPDSRK 1369
Cdd:cd14597    79 EGGKI-KCQRYWPEILGKTTMVdnrLQLTLVRMQQLKNFVIRVLELED---IQTRE--VRHITHLNFTAWPDhdTPSQPE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1370 AFLHLLAEVDKWQAEsgdGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDV 1449
Cdd:cd14597   153 QLLTFISYMRHIHKS---GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                  ....*
gi 568930827 1450 ALEYL 1454
Cdd:cd14597   230 ILYVL 234
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1246-1443 2.94e-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: 2.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEP--GRQQYGLMEVEFVS 1323
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRN-KCAQYWPSMeeGSRAFGDVVVKINE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1324 GTANEDLVSRVFRVQNSSRLQEGHlLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGT 1403
Cdd:cd14557    80 EKICPDYIIRKLNINNKKEKGSGR-EVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN-NFFSGPIVVHCSAGVGRTGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568930827 1404 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQY 1443
Cdd:cd14557   157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1178-1445 4.55e-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: 4.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1178 MIRIDPQSNSSQLREEFQTLNSVTPPLDVeecSIALLPRNRDKNRSMDVLPPDRCLPFLISSDgdpnNYINAALTDSYTR 1257
Cdd:cd14600     4 MAQLKKGLESGTVLIQFEQLYRKKPGLAI---TCAKLPQNMDKNRYKDVLPYDATRVVLQGNE----DYINASYVNMEIP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1258 SAA----FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGR-QQYGLMEVEFVSGTANEDLVS 1332
Cdd:cd14600    77 SANivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRT-KCHQYWPDPPDvMEYGGFRVQCHSEDCTIAYVF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1333 RVFRVQNSSRLQEghLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAESGDgrTVVHCLNGGGRSGTFCACATVLE 1412
Cdd:cd14600   156 REMLLTNTQTGEE--RTVTHLQYVAWPDH-GVPDDSSDFLEFVNYVRSKRVENEP--VLVHCSAGIGRTGVLVTMETAMC 230

                         250       260       270
                  ....*....|....*....|....*....|...
gi 568930827 1413 MIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHF 1445
Cdd:cd14600   231 LTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKF 263
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1350-1452 1.31e-22

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 93.96  E-value: 1.31e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1350 VRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQ-AESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL-VDVFFAAK 1427
Cdd:smart00404    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 568930827   1428 TLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1350-1452 1.31e-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: 1.31e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   1350 VRHFQFLRWSAyRDTPDSRKAFLHLLAEVDKWQ-AESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL-VDVFFAAK 1427
Cdd:smart00012    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 568930827   1428 TLRNYKPNMVETMDQYHFCYDVALE 1452
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1220-1452 1.97e-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: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1220 KNRSMDVLPPDRCLP--FLISSDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSN 1297
Cdd:cd14602     1 KNRYKDILPYDHSRVelSLITSDED-SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1298 SAwPCLQYWPEPGRQ--QYGLMEVEFVSGTANEDLVSRVFRVQnssrLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLL 1375
Cdd:cd14602    80 KK-KCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIRTLKVK----FNSETRTIYQFHYKNWPDH-DVPSSIDPILELI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1376 AEVDKWQAESgDGRTVVHCLNGGGRSGTFCACATVLEMIR------CHSlvdVFFAAKTLRNYKPNMVETMDQYHFCYDV 1449
Cdd:cd14602   154 WDVRCYQEDD-SVPICIHCSAGCGRTGVICAIDYTWMLLKdgiipeNFS---VFSLIQEMRTQRPSLVQTKEQYELVYNA 229


                  ...
gi 568930827 1450 ALE 1452
Cdd:cd14602   230 VIE 232
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1215-1456 3.88e-22

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 97.64  E-value: 3.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1215 PRNRDKNRSMDVLPPDRCLpfLISSDGDPN---------NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCT 1285
Cdd:cd14606    16 PENKSKNRYKNILPFDHSR--VILQGRDSNipgsdyinaNYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1286 SIVMLNQLNQSNSAwPCLQYWPEPGRQ-QYGLMEVEFVSGTANEDLVSRVFRV---QNSSRLQEGHllvrHFQFLRWSAY 1361
Cdd:cd14606    94 VIVMTTREVEKGRN-KCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVsplDNGELIREIW----HYQYLSWPDH 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1362 rDTPDSRKAFLHLLAEVDKWQAE-SGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYKPNMV 1437
Cdd:cd14606   169 -GVPSEPGGVLSFLDQINQRQESlPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMV 247

                         250
                  ....*....|....*....
gi 568930827 1438 ETMDQYHFCYDVALEYLEA 1456
Cdd:cd14606   248 QTEAQYKFIYVAIAQFIET 266
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1237-1453 2.90e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 96.64  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1237 ISSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwpCLQYWPEPgrQQYGL 1316
Cdd:PHA02746   91 VTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEK--CFELWTKE--EDSEL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1317 MEVEFVSGTAN--EDLVSRVFRVQNSSRLQEGHLLVRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAE---------S 1385
Cdd:PHA02746  167 AFGRFVAKILDiiEELSFTKTRLMITDKISDTSREIHHFWFPDWPDN-GIPTGMAEFLELINKVNEEQAElikqadndpQ 245

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930827 1386 GDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYdVALEY 1453
Cdd:PHA02746  246 TLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCY-KALKY 312
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1245-1455 2.91e-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: 2.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1245 NYINAALTDSyTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEP-GRQQYGLMEVEFVS 1323
Cdd:cd14601     6 NYINMEIPSS-SIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRV-KCHQYWPEPsGSSSYGGFQVTCHS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1324 GTANEDLVSRVFRVQNSSRLQEGHLLvrHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQAeSGDGRTVVHCLNGGGRSGT 1403
Cdd:cd14601    84 EEGNPAYVFREMTLTNLEKNESRPLT--QIQYIAWPDH-GVPDDSSDFLDFVCLVRNKRA-GKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568930827 1404 FCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1455
Cdd:cd14601   160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1210-1455 1.01e-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: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1210 SIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDPNNYINAALTDSYTRSAA--FIVTLHPLQSTTPDFWRLVYDYGCTSI 1287
Cdd:cd14599    31 TTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1288 VMLNQLNQSNSAwPCLQYWPEPGRQQYglmevefvSGTANEDLVSRVFRVQN----SSRLQEGHLL------VRHFQFLR 1357
Cdd:cd14599   111 AMVTAEEEGGRS-KSHRYWPKLGSKHS--------SATYGKFKVTTKFRTDSgcyaTTGLKVKHLLsgqertVWHLQYTD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1358 WSAYrDTPDSRKAFLHLLAEVDKWQ---------AESGDGRTVVHCLNGGGRSGTFCACATvleMIRC---HSLVDVFFA 1425
Cdd:cd14599   182 WPDH-GCPEEVQGFLSYLEEIQSVRrhtnsmldsTKNCNPPIVVHCSAGVGRTGVVILTEL---MIGClehNEKVEVPVM 257

                         250       260       270
                  ....*....|....*....|....*....|
gi 568930827 1426 AKTLRNYKPNMVETMDQYHFCYDVALEYLE 1455
Cdd:cd14599   258 LRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PHA02738 PHA02738
hypothetical protein; Provisional
 1216-1455 8.28e-20

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 92.30  E-value: 8.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1216 RNRDKNRSMDVLPPDRCLPFLiSSDGDPNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQ 1295
Cdd:PHA02738   48 KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK-KK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1296 SNSAWPCLQYWP--EPGRQQYGLMEVEFVSGTANEDLVSRVFRVQN-SSRLQEghllVRHFQFLRWSAYrDTPDSRKAFL 1372
Cdd:PHA02738  126 ENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDgTSATQT----VTHFNFTAWPDH-DVPKNTSEFL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1373 HLLAEVDKWQAE-------SGDGRT-----VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETM 1440
Cdd:PHA02738  201 NFVLEVRQCQKElaqeslqIGHNRLqpppiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIP 280

                         250
                  ....*....|....*
gi 568930827 1441 DQYHFCYDVALEYLE 1455
Cdd:PHA02738  281 FQYFFCYRAVKRYVN 295
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1209-1453 4.31e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 86.59  E-value: 4.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1209 CSIALLPRNRDKNRSMDVLPPDRCLPFLISSDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1288
Cdd:PHA02742   44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDGG-DDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1289 MLNQLNQSNSAwPCLQYW--PEPGRQQYGLMEVefvsgtanEDLVSRVFRVQNSSRLQ-----EGHLL-VRHFQFLRWSa 1360
Cdd:PHA02742  123 MITKIMEDGKE-ACYPYWmpHERGKATHGEFKI--------KTKKIKSFRNYAVTNLCltdtnTGASLdIKHFAYEDWP- 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1361 YRDTPDSRKAFLHLLAEVDKWQAE-----SGDGRT-----VVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLR 1430
Cdd:PHA02742  193 HGGLPRDPNKFLDFVLAVREADLKadvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLR 272

                         250       260
                  ....*....|....*....|...
gi 568930827 1431 NYKPNMVETMDQYHFCYDVALEY 1453
Cdd:PHA02742  273 KQRHNCLSLPQQYIFCYFIVLIF 295
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1217-1443 2.63e-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: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1217 NRDKNRSMDVLPPD--RCLPFLISSDGDpNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1294
Cdd:cd14604    57 NVKKNRYKDILPFDhsRVKLTLKTSSQD-SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1295 QSNSAwPCLQYWPEPGRQ--QYGLMEVEFVSGTANEDLVSRVFRV--QNSSRlqeghlLVRHFQFLRWSAYrDTPDSRKA 1370
Cdd:cd14604   136 EMGRK-KCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLLefQNETR------RLYQFHYVNWPDH-DVPSSFDS 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568930827 1371 FLHLLAEVDKWQaESGDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSL---VDVFFAAKTLRNYKPNMVETMDQY 1443
Cdd:cd14604   208 ILDMISLMRKYQ-EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 282
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1246-1455 4.59e-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: 4.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1246 YINAALTDSYTRSAA--FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqLNQSNSAWPCLQYWPEPGRQQYGLMEVEFvs 1323
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVT-AEEEGGREKSFRYWPRLGSRHNTVTYGRF-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1324 gtaneDLVSRvFRVQN----SSRLQEGHLL------VRHFQFLRWSAYrDTPDSRKAFLHLLAEVDKWQ--------AES 1385
Cdd:cd14598    78 -----KITTR-FRTDSgcyaTTGLKIKHLLtgqertVWHLQYTDWPEH-GCPEDLKGFLSYLEEIQSVRrhtnstidPKS 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1386 GDGRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1455
Cdd:cd14598   151 PNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 947-1148 2.31e-14

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 73.97  E-value: 2.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  947 PDADYISANYIDIRINrqgyhrsNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVGRVKCSRYWPEDSDmYGdi 1026
Cdd:cd14559    13 PVGKNLNANRVQIGNK-------NVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGT-YG-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1027 KITLVKTETLAEYVVRTFA-----LERRGYSARHEVRQFHFTAWPEHG-VPYHATGLLAfiRRVKAST------------ 1088
Cdd:cd14559    83 SVTVKSKKTGKDELVDGLKadmynLKITDGNKTITIPVVHVTNWPDHTaISSEGLKELA--DLVNKSAeekrnfykskgs 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568930827 1089 ----PPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTlcSRRVNMIQTEEQY 1148
Cdd:cd14559   161 sainDKNKLLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVSDMRT--SRNGKMVQKDEQL 222
fn3 pfam00041
Fibronectin type III domain;
502-585 1.42e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.44  E-value: 1.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   502 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTS 580
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*
gi 568930827   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 2.34e-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: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  492 DVPGGIAAESLTftplEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPA-VNVPGPrrtisklrNETYHVFSNLHPGTT 570
Cdd:cd00063     2 SPPTNLRVTDVT----STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeVEVTPG--------SETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....
gi 568930827  571 YLFSVRARTSKGFGQAA-LTEITT 593
Cdd:cd00063    70 YEFRVRAVNGGGESPPSeSVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
355-632 1.13e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.26  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  355 LDPDTEYEISVLLTrpGDGGTGRPGPPlISRTKCAEPTRAPKGLAFAEIQARQLTLQWEP------LGYNVtrchtyavs 428
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRV--------- 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  429 lcYRYTLGGSHNQTIREcVKmergASRYTIKNLLPFRNIHVRLILTNPEGRKEGK--EVTFQTDEDVPGgiAAESLTFTP 506
Cdd:COG3401   267 --YRSNSGDGPFTKVAT-VT----TTSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  507 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTSKGfgq 585
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568930827  586 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 632
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 948-1155 1.96e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 63.83  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  948 DADYISANYIDirinrqGYHRSNHFIATQGPKPEMIYDFWRMVWQEQCASIVMITKLVEVgrvKC-SRYWPEDSD---MY 1023
Cdd:PHA02740   75 DEKVLDARFVD------GYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGcviTS 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1024 GDIKITLVKTETLAEYVVRTFALERRGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA--------STPPDAGPI 1095
Cdd:PHA02740  146 DKFQIETLEIIIKPHFNLTLLSLTDKFGQAQ-KISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadlekhKADGKIAPI 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1096 VIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1155
Cdd:PHA02740  225 IIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 494-584 3.07e-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: 3.07e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    494 PGGIAAESLTftplEDMIFLKWEEPQEPNGL--ITQYEISYQSIESSDPAVNVPGprrtisklrNETYHVFSNLHPGTTY 571
Cdd:smart00060    4 PSNLRVTDVT----STSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTP---------SSTSYTLTGLKPGTEY 70

                            90
                    ....*....|...
gi 568930827    572 LFSVRARTSKGFG 584
Cdd:smart00060   71 EFRVRAVNGAGEG 83
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1352-1448 3.95e-08

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 52.74  E-value: 3.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1352 HFQFLRWSAYRDTPDSRKAFLHLLAEVDKwQAESGDGRTVVHCLNGGGRSGTFCACATVlemirCHSLVDVFFAAKTLR- 1430
Cdd:cd14494    22 DSRFLKQLGVTTIVDLTLAMVDRFLEVLD-QAEKPGEPVLVHCKAGVGRTGTLVACYLV-----LLGGMSAEEAVRIVRl 95

                          90
                  ....*....|....*...
gi 568930827 1431 NYKPNMVETMDQYHFCYD 1448
Cdd:cd14494    96 IRPGGIPQTIEQLDFLIK 113
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1247-1455 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 568930827 1247 INAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWpclQYWpepgrqqyglmevefvsgTA 1326
Cdd:PHA02740   79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFN---QFW------------------SL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1327 NEDLV--SRVFRVQNSSRLQEGH----LLV-----------RHFQFLRWSA--YRDTPDSRKAFL----HLLAEVDKWQA 1383
Cdd:PHA02740  138 KEGCVitSDKFQIETLEIIIKPHfnltLLSltdkfgqaqkiSHFQYTAWPAdgFSHDPDAFIDFFcnidDLCADLEKHKA 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930827 1384 ESGDGRTVVHCLNGGGRSGTFCA---CATVLEMIRCHSLVDVFfaaKTLRNYKPNMVETMDQYHFCYDVALEYLE 1455
Cdd:PHA02740  218 DGKIAPIIIDCIDGISSSAVFCVfdiCATEFDKTGMLSIANAL---KKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1053-1153 2.95e-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: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1053 ARHEVRQFHFtAWPEHGVPyhATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTG----CYIVLdvMLDMAECEgvvdiy 1128
Cdd:cd14506    73 MRAGIYFYNF-GWKDYGVP--SLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGvliaCYLVY--ALRMSADQ------ 141

                          90       100
                  ....*....|....*....|....*
gi 568930827 1129 nCVKTLCSRRVNMIQTEEQYIFIHD 1153
Cdd:cd14506   142 -AIRLVRSKRPNSIQTRGQVLCVRE 165
fn3 pfam00041
Fibronectin type III domain;
299-373 1.95e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827   299 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---NLQTYKLWHLDPDTEYEISVlLTRPGD 372
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 568930827   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 3.35e-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: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827  394 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYAVSLCyrytlgGSHNQTIRECVKMERGASRYTIKNLLPFRNIHVRLIL 473
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR------EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                          90
                  ....*....|....*..
gi 568930827  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 ...
 1356-1448 4.79e-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: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1356 LRWSAY--RD--TPDSRKAFLHLLAEVDkwQAESGDGRTVVHCLNGGGRSGTFCACAtvleMIRCHSLVDVFFAAKTLRN 1431
Cdd:cd14505    73 ITWHHLpiPDggVPSDIAQWQELLEELL--SALENGKKVLIHCKGGLGRTGLIAACL----LLELGDTLDPEQAIAAVRA 146

                          90
                  ....*....|....*..
gi 568930827 1432 YKPNMVETMDQYHFCYD 1448
Cdd:cd14505   147 LRPGAIQTPKQENFLHQ 163
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 294-365 1.37e-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: 1.37e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568930827    294 PTPIAPPQLLRAGPTYLIIQ-LNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVNLQT-YKLWHLDPDTEYEISV 365
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1363-1445 3.34e-04

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 42.27  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1363 DTPDSRKAFLHLLAEVDKWQAEsgDGRTVVHCLNGGGRSGTFCACatVLeMIRCHSLVDvffAAKTLRNYKPNMVETMDQ 1442
Cdd:COG2453    58 FGAPDDEQLQEAVDFIDEALRE--GKKVLVHCRGGIGRTGTVAAA--YL-VLLGLSAEE---ALARVRAARPGAVETPAQ 129


                  ...
gi 568930827 1443 YHF 1445
Cdd:COG2453   130 RAF 132
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1077-1153 3.54e-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: 3.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930827 1077 LLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAEC-EGVVDIYNcvktlCSRRVNMIQTEEQYIFIHD 1153
Cdd:cd14494    41 MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSaEEAVRIVR-----LIRPGGIPQTIEQLDFLIK 113
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 204-290 7.02e-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: 7.02e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827    204 GDVEVNAGQNASFQCMAAGraAEAEHFFLQRQSGVLVPAAGVRHISHRRFLATFPLASVGRSEQDLYRCVSQAPRGaGVS 283
Cdd:smart00410    2 PSVTVKEGESVTLSCEASG--SPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78


                    ....*..
gi 568930827    284 NFAELIV 290
Cdd:smart00410   79 SGTTLTV 85
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 1372-1407 1.38e-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: 1.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568930827 1372 LHLLAEVDKWQAESGDGRTVVHCLNGGGRSGTFCAC 1407
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 568930827    394 APKGLAFAEIQARQLTLQWEPLGYNVTRChtYAVSLCYRYTLGGSHNQTirecVKMERGASRYTIKNLLPFRNIHVRLIL 473
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIVGYRVEYREEGSEWKE----VNVTPSSTSYTLTGLKPGTEYEFRVRA 76


                    ....*.
gi 568930827    474 TNPEGR 479
Cdd:smart00060   77 VNGAGE 82
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1053-1153 2.76e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.57  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930827 1053 ARHEVRQFHFtAWPEHGVPyHATGLLAFIRRVKASTPPDaGPIVIHCSAGTGRTGCyiVLdVMLDMAECEGVVDIYNCVK 1132
Cdd:COG2453    44 EEAGLEYLHL-PIPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGT--VA-AAYLVLLGLSAEEALARVR 117

                          90       100
                  ....*....|....*....|.
gi 568930827 1133 tlcSRRVNMIQTEEQYIFIHD 1153
Cdd:COG2453   118 ---AARPGAVETPAQRAFLER 135
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1388-1443 3.30e-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: 3.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930827 1388 GRTVVHCLNGGGRSGTFCACATVLEMIRCHSLVDVFFAAKTLRNYKpnMVETMDQY 1443
Cdd:cd14559   169 LLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVSDMRTSRNGK--MVQKDEQL 222
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1095-1153 7.32e-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: 7.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568930827 1095 IVIHCSAGTGRTG----CyivldVMLDMAECEGVVDIYNCVKTLcsrRVNMIQTEEQYIFIHD 1153
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 9.37e-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: 9.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930827  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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH