NCBI Conserved Domain Search

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: 502.55 E-value: 2.33e-177

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 107 YPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKC 186
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 187 YQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLN 266
Cdd:cd14620   81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVN 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940373627 267 PSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14620  161 PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

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: 482.99 E-value: 1.43e-168

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  52 KKFFPIPVEHLEEEIRVRSADDCKRFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDY 131
Cdd:cd14621    3 RKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 132 INASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVL 211
Cdd:cd14621   83 INASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 212 VDYTIRKFCIHPQLPDSCKAP-RLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVI 290
Cdd:cd14621  163 VDYTVRKFCIQQVGDVTNKKPqRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVI 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940373627 291 DAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYYLYGDTEL 344
Cdd:cd14621  243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296

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: 442.91 E-value: 2.43e-154

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 422 DYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDT 501
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 502 LSEAISVRDFLVTFKQplarqEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGT 581
Cdd:cd14622   81 LLETISIRDFLVTYNQ-----EKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGT 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 940373627 582 FIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDF 631
Cdd:cd14622  156 FIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205

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: 432.46 E-value: 2.65e-150

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTL 502
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 503 SEAISVRDFLVTFKQPlarqeEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGTF 582
Cdd:cd14552   81 YEDYTLRDFLVTKGKG-----GSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTF 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 940373627 583 IALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQ 629
Cdd:cd14552  156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202

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: 407.76 E-value: 1.15e-140

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 210
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCIHPQLPDS-CKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIV 289
Cdd:cd14551   81 LVDYTTRKFCIQKVNRGIgEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 940373627 290 IDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14551  161 IDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

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: 403.27 E-value: 1.74e-138

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 398 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 477
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 478 CYQYWPTEGSVTHGDITIEIKSDTLSEAISVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQ 557
Cdd:cd14623   81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVT-----NTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQ 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940373627 558 KQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQD 630
Cdd:cd14623  156 KQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 363.13 E-value: 2.36e-122

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627    77 FREEFNSLPSGHIQ-GTFELANKEENREKNRYPNILPNDHCRVILSQVDGiPCSDYINASYIDGYKEKNKFIAAQGPKQE 155
Cdd:smart00194   2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627   156 TVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG--CWTYGNIRVCVEDCVVLVDYTIRKFCIHPqlpDSCKAPR 233
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTN---TGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627   234 LVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIR 313
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|..
gi 940373627   314 NQRPQMVQTDVQYTFIYQALLE 335
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAILE 259

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: 345.15 E-value: 1.18e-115

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  99 EENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNL 178
Cdd:cd14553    1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 179 KERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKF 258
Cdd:cd14553   81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN---GSSEKREVRQFQFTAWPDHGVPEHPTPFLAF 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 259 LKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14553  158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 327.28 E-value: 9.09e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  101 NREKNRYPNILPNDHCRVILSqvDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKE 180
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  181 RKEEKCYQYWPD--QGCWTYGNIRV-CVEDCVVLVDYTIRKFcihpQLPDSC-KAPRLVSQLHFTSWPDFGVPFTPIGML 256
Cdd:pfam00102  79 KGREKCAQYWPEeeGESLEYGDFTVtLKKEKEDEKDYTVRTL----EVSNGGsEETRTVKHFHYTGWPDHGVPESPNSLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  257 KFLKKVKTL-NPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:pfam00102 155 DLLRKVRKSsLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 325.00 E-value: 2.07e-107

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627   367 GLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEfTDYINASFIDGYRQKDYFMATQGPLA 446
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627   447 HTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEG--SVTHGDITIEIKSDTLSEAISVRDFLVTFKqplarQEE 524
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNT-----GCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627   525 QVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAV 604
Cdd:smart00194 155 ETRTVTHYHYTNWPDHGVPESPESILDLIRAV-RKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                          250       260
                   ....*....|....*....|....*.
gi 940373627   605 KSLRLQRPHMVQTLEQYEFCYKVVQD 630
Cdd:smart00194 234 KELRSQRPGMVQTEEQYIFLYRAILE 259

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 318.03 E-value: 4.28e-105

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  393 NMKKARVIQIIPYDFNRVILSMKRGQEftDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQE 472
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPS--DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  473 REQDKCYQYWPT--EGSVTHGDITIEIK-SDTLSEAISVRDFLVTFKQplarqEEQVRMVRQFHFHGWPEVGIPAEGKGM 549
Cdd:pfam00102  79 KGREKCAQYWPEeeGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGG-----SEETRTVKHFHYTGWPDHGVPESPNSL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  550 IDLIAAVQKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQ 629
Cdd:pfam00102 154 LDLLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233


                  .
gi 940373627  630 D 630
Cdd:pfam00102 234 E 234

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: 317.75 E-value: 2.31e-104

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  62 LEEEIRVRSADDCKRFREEFNSLPSGHiQGTFELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYK 141
Cdd:cd14626    3 LADNIERLKANDGLKFSQEYESIDPGQ-QFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 142 EKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCI 221
Cdd:cd14626   82 KQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 222 HpqlPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ 301
Cdd:cd14626  162 Y---KNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEK 238

                        250       260       270
                 ....*....|....*....|....*....|....
gi 940373627 302 KVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14626  239 TVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272

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: 305.86 E-value: 1.08e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  56 PIPVEHLEEEIRVRSADDCKRFREEFNSLPSGHiQGTFELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINAS 135
Cdd:cd14625    3 PIPISELAEHTERLKANDNLKLSQEYESIDPGQ-QFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 136 YIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYT 215
Cdd:cd14625   82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 216 IRKFCIHpqlPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMD 295
Cdd:cd14625  162 VRTFSLH---KNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 940373627 296 MIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14625  239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278

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: 304.06 E-value: 1.13e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 389 NLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLT 468
Cdd:cd14554    2 NLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 469 EVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEGKG 548
Cdd:cd14554   82 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVT-----DARDGQSRTVRQFQFTDWPEQGVPKSGEG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940373627 549 MIDLIAAVQKQQQQTGNH-PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd14554  157 FIDFIGQVHKTKEQFGQEgPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235

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: 300.36 E-value: 8.75e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG--CWTYGNIRVCVEDC 208
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGgkPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 209 VVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFI 288
Cdd:cd00047   81 EELSDYTIRTLELSPK---GCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 940373627 289 VIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd00047  158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

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: 303.19 E-value: 1.40e-98

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  56 PIPVEHLEEEIRVRSADDCKRFREEFNSLPSGHiQGTFELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINAS 135
Cdd:cd14624    3 PIPILELADHIERLKANDNLKFSQEYESIDPGQ-QFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 136 YIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYT 215
Cdd:cd14624   82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 216 IRKFCIHpqlPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMD 295
Cdd:cd14624  162 VRTFALY---KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 940373627 296 MIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYYLYGD 341
Cdd:cd14624  239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGN 284

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: 299.27 E-value: 2.32e-98

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 210
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCI---HPQLPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTF 287
Cdd:cd14549   81 LATYTVRTFSLknlKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 940373627 288 IVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIY 330
Cdd:cd14549  161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

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: 278.01 E-value: 4.13e-90

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGS--VTHGDITIEIKSD 500
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkpLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 501 TLSEAISVRDFLVTFKqplarQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTgNHPITVHCSAGAGRTG 580
Cdd:cd00047   81 EELSDYTIRTLELSPK-----GCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKP-NGPIVVHCSAGVGRTG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 940373627 581 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd00047  155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

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: 278.85 E-value: 4.53e-90

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 106 RYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEK 185
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 186 CYQYWP-DQGCWTYGNIRVCVEDCVVLVDYTIRKFCIhpQLPDSCkapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKT 264
Cdd:cd14548   81 CDHYWPfDQDPVYYGDITVTMLSESVLPDWTIREFKL--ERGDEV---RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 265 LNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14548  156 YIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

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: 276.61 E-value: 2.88e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 341 DTELDVSSLERHLQTLHSTATHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEF 420
Cdd:cd14627    1 NTEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 421 TDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSD 500
Cdd:cd14627   81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 501 TLSEAISVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTG-NHPITVHCSAGAGRT 579
Cdd:cd14627  161 YNMPQYILREFKVT-----DARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVGRT 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 940373627 580 GTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 632
Cdd:cd14627  236 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288

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: 274.30 E-value: 2.26e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 342 TELDVSSLERHLQTLHSTATHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFT 421
Cdd:cd14628    1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 422 DYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDT 501
Cdd:cd14628   81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 502 LSEAISVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTG-NHPITVHCSAGAGRTG 580
Cdd:cd14628  161 NMPQYILREFKVT-----DARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVGRTG 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 940373627 581 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFIDIF 635
Cdd:cd14628  236 VFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSF 290

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: 271.98 E-value: 1.67e-86

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 342 TELDVSSLERHLQTLHSTATHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFT 421
Cdd:cd14629    2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 422 DYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDT 501
Cdd:cd14629   82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 502 LSEAISVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTG-NHPITVHCSAGAGRTG 580
Cdd:cd14629  162 NMPQYILREFKVT-----DARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVGRTG 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 940373627 581 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFIDIF 635
Cdd:cd14629  237 VFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSF 291

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: 264.97 E-value: 1.80e-84

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  99 EENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNL 178
Cdd:cd14630    1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 179 KERKEEKCYQYWPDQgCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKF 258
Cdd:cd14630   81 VEVGRVKCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKK---GYHEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 259 LKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14630  157 VRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233

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: 264.23 E-value: 8.73e-84

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  91 GTFELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSA 170
Cdd:cd14543   19 GTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 171 TIVMLTNLKERKEEKCYQYWPDQG--CWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSckaPRLVSQLHFTSWPDFGV 248
Cdd:cd14543   99 VIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE---SRQVTHFQFTSWPDFGV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 249 PFTPIGMLKFLKKVK--------TLNPSHAG-----PIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQ 315
Cdd:cd14543  176 PSSAAALLDFLGEVRqqqalavkAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQ 255

                        250
                 ....*....|....*
gi 940373627 316 RPQMVQTDVQYTFIY 330
Cdd:cd14543  256 RAFSIQTPDQYYFCY 270

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

Pssm-ID: 350505 [Multi-domain] Cd Length: 274 Bit Score: 254.58 E-value: 5.45e-80

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  77 FREEFNSLP--SGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQVDGIPC--SDYINASYIDGYKEKNKFIAAQGP 152
Cdd:cd17667    1 FSEDFEEVQrcTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 153 KQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQL------- 225
Cdd:cd17667   81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkgqkg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 226 -PDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVD 304
Cdd:cd17667  161 nPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 940373627 305 VFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYYL 338
Cdd:cd17667  241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274

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: 253.81 E-value: 1.13e-79

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  77 FREEFNSLPSGHiQGTFELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQET 156
Cdd:cd14633   17 FKEEYESFFEGQ-SAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQET 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 157 VNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQgCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVS 236
Cdd:cd14633   96 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAVEKR---GVHEIREIR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 237 QLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQR 316
Cdd:cd14633  172 QFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRR 251

                        250
                 ....*....|....*....
gi 940373627 317 PQMVQTDVQYTFIYQALLE 335
Cdd:cd14633  252 VNMVQTEEQYVFIHDAILE 270

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: 248.81 E-value: 1.44e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 398 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 477
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 478 CYQYWP-TEGSVTHGDITIEIKSDTLSEAISVRDFLVTfkqplarQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAV 556
Cdd:cd14548   81 CDHYWPfDQDPVYYGDITVTMLSESVLPDWTIREFKLE-------RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 557 QKQQQQtGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 623
Cdd:cd14548  154 RDYIKQ-EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219

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: 249.30 E-value: 2.83e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 101 NREKNRYPNILPNDHCRVILSQVD-GIPCSDYINASYI------DGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATI 172
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDpNVPGSDYINANYIrnenegPTTDENAKtYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 173 VMLTNLKERKEEKCYQYWPDQG-CWTYGNIRV-CVEDCVVlVDYTIRKFCIHPQlpDSCKAPRLVSQLHFTSWPDFGVPF 250
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGmQKQYGPYRVqNVSEHDT-TDYTLRELQVSKL--DQGDPIREIWHYQYLSWPDHGVPS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 251 TPIGMLKFLKKVKTLNPS--HAGPIVVHCSAGVGRTGTFIVIDAMMDMIhSEQ----KVDVFEFVSRIRNQRPQMVQTDV 324
Cdd:cd14544  158 DPGGVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQI-KRKgldcDIDIQKTIQMVRSQRSGMVQTEA 236

                        250
                 ....*....|..
gi 940373627 325 QYTFIYQALLEY 336
Cdd:cd14544  237 QYKFIYVAVAQY 248

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: 242.90 E-value: 1.70e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQgCWTYGNIRVCVEDCVV 210
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVI 290
Cdd:cd14555   80 LAEYVVRTFALERR---GYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 940373627 291 DAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14555  157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201

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: 241.88 E-value: 3.72e-75

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 390 LPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTE 469
Cdd:cd14543   26 APANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 470 VQEREQDKCYQYWPTEG--SVTHGDITIEIKSDTLSEaisvrDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPAEGK 547
Cdd:cd14543  106 VVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKE-----HYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAA 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 548 GMIDLIAAVQKQQQQ---------TGNH---PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMV 615
Cdd:cd14543  181 ALLDFLGEVRQQQALavkamgdrwKGHPpgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSI 260

                        250
                 ....*....|.
gi 940373627 616 QTLEQYEFCYK 626
Cdd:cd14543  261 QTPDQYYFCYK 271

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: 239.79 E-value: 5.50e-75

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 105 NRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE 184
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 185 KCYQYWP-DQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCKAPRlvsQLHFTSWPDFGVPFTPIGMLKFLKKVK 263
Cdd:cd14619   81 KCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVR---HFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940373627 264 TLNPSH--AGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:cd14619  158 QWLDQTmsGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232

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: 238.95 E-value: 9.90e-75

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 105 NRYPNILPNDHCRVILSqVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE 184
Cdd:cd14615    1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 185 KCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCI-HPQLPDSckapRLVSQLHFTSWPDFGVPFTP---IGMLKFLK 260
Cdd:cd14615   80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVkNAQTNES----RTVRHFHFTSWPDHGVPETTdllINFRHLVR 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940373627 261 KVKTLNPSHaGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14615  156 EYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

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: 239.35 E-value: 1.12e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  96 ANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVML 175
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 176 TNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCkapRLVSQLHFTSWPDFGVPFTPIGM 255
Cdd:cd14554   81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS---RTVRQFQFTDWPEQGVPKSGEGF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 256 LKFLKKV-KTLNP-SHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQAL 333
Cdd:cd14554  158 IDFIGQVhKTKEQfGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAA 237


                 .
gi 940373627 334 L 334
Cdd:cd14554  238 L 238

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: 238.45 E-value: 1.97e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 391 PANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEV 470
Cdd:cd14553    1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 471 QEREQDKCYQYWPTEGSVTHGDITIeiksdTLSEAISVRDFLV-TFKqpLARQ-EEQVRMVRQFHFHGWPEVGIPAEGKG 548
Cdd:cd14553   81 EERSRVKCDQYWPTRGTETYGLIQV-----TLLDTVELATYTVrTFA--LHKNgSSEKREVRQFQFTAWPDHGVPEHPTP 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 549 MIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 625
Cdd:cd14553  154 FLAFLRRV-KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIH 229

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: 236.52 E-value: 7.64e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 105 NRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKE 183
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 184 eKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIhpqlpDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVK 263
Cdd:cd14547   81 -KCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTL-----KYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 264 TL--NPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14547  155 EArqTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

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: 236.07 E-value: 8.64e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 117 RVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQgCW 196
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 197 TYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVH 276
Cdd:cd14631   80 VYGDFKVTCVEMEPLAEYVVRTFTLERR---GYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 940373627 277 CSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14631  157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215

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: 233.84 E-value: 3.57e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDkCYQYWPTEGSVTHGDITIEIKSDTL 502
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDEGSGTYGPIQVEFVSTTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 503 SEAISVRDFLVtfkQPLARQEEQVRMVRQFHFHGWPEVG-IPAEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGT 581
Cdd:cd14556   80 DEDVISRIFRL---QNTTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 940373627 582 FIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 625
Cdd:cd14556  157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200

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: 234.18 E-value: 3.99e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCwTYGNIRVCVEDCVV 210
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD-TYGDIKITLLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVI 290
Cdd:cd14632   80 LAEYSVRTFALERR---GYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 940373627 291 DAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14632  157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201

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: 233.18 E-value: 7.71e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWP--DQGCWTYGNIRVCVEDC 208
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 209 VVLVDYTIRKFCIHPQlpDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFI 288
Cdd:cd14557   81 KICPDYIIRKLNINNK--KEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 940373627 289 VIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14557  159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

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: 233.27 E-value: 1.91e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 105 NRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE 184
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 185 KCYQYWP-DQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVK 263
Cdd:cd14617   81 KCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSE--EQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 264 T-LNPS-HAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14617  159 DyINRTpGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

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: 230.74 E-value: 5.79e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSvTHGDITIEIKSDTL 502
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK-TYGDIEVELKDTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 503 SEAISVRDFLVTFKQplaRQEEQVrmVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQ----QQTGNH-PITVHCSAGAG 577
Cdd:cd14558   80 SPTYTVRVFEITHLK---RKDSRT--VYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLpyknSKHGRSvPIVVHCSDGSS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940373627 578 RTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 625
Cdd:cd14558  155 RTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

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: 227.15 E-value: 1.58e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 210
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCIHPQLPDSCkapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV-KTLNPSHAGPIVVHCSAGVGRTGTFIV 289
Cdd:cd14552   81 YEDYTLRDFLVTKGKGGST---RTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 940373627 290 IDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQAL 333
Cdd:cd14552  158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

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: 228.36 E-value: 3.16e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 100 ENREKNRYPNILPNDHCRVILSQVD-GIPCSDYINASYI--------DGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSA 170
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 171 TIVMLTNLKERKEEKCYQYWPDQGCWT-YGNIRVCVEDCVVLVDYTIRKFCIHPQlpDSCKAPRLVSQLHFTSWPDFGVP 249
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWPDEYALKeYGVMRVRNVKESAAHDYILRELKLSKV--GQGNTERTVWQYHFRTWPDHGVP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 250 FTPIGMLKFLKKV--KTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ---KVDVFEFVSRIRNQRPQMVQTDV 324
Cdd:cd14605  159 SDPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEA 238

                        250
                 ....*....|..
gi 940373627 325 QYTFIYQALLEY 336
Cdd:cd14605  239 QYRFIYMAVQHY 250

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: 227.13 E-value: 3.20e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 402 IIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQY 481
Cdd:cd14620    4 ILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 482 WPTEGSVTHGDITIEIKSDTLSEAISVRDFLVTFKQPLARQEEqvRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVqKQQQ 561
Cdd:cd14620   84 WPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAP--RLVTQLHFTSWPDFGVPFTPIGMLKFLKKV-KSVN 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 562 QTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14620  161 PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227

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: 225.59 E-value: 7.75e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYID-GYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWT-YGNIRV-CVED 207
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGeYGDLTVeLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 208 CVV-LVDYTIRKFCI-HPQLPdsckaPRLVSQLHFTSWPDFGVPFTPIGMLK--FLKKVKTLNPSHAGPIVVHCSAGVGR 283
Cdd:cd18533   81 EENdDGGFIVREFELsKEDGK-----VKKVYHIQYKSWPDFGVPDSPEDLLTliKLKRELNDSASLDPPIIVHCSAGVGR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 284 TGTFIVIDAMMDMIHS--------EQKVD-VFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd18533  156 TGTFIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

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: 225.85 E-value: 1.20e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 398 RVIQIIPYDFNRVILSMKrGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 477
Cdd:cd14615    2 RYNNVLPYDISRVKLSVQ-SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 478 CYQYWPTEGSVTHGDITIEIKSDTLSEAISVRDFLVTFKqplarQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAV- 556
Cdd:cd14615   81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNA-----QTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVr 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940373627 557 QKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQD 630
Cdd:cd14615  156 EYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

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: 223.60 E-value: 2.99e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  98 KEENREKNRYPNILPNDHCRVILSQVD-GIPCSDYINASYID----GYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSAT 171
Cdd:cd14606   15 RPENKSKNRYKNILPFDHSRVILQGRDsNIPGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAWQENSRV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 172 IVMLTNLKERKEEKCYQYWPDQGCWT-YGniRVCVEDCVVL--VDYTIRKFCIHPqlPDSCKAPRLVSQLHFTSWPDFGV 248
Cdd:cd14606   95 IVMTTREVEKGRNKCVPYWPEVGMQRaYG--PYSVTNCGEHdtTEYKLRTLQVSP--LDNGELIREIWHYQYLSWPDHGV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 249 PFTPIGMLKFLKKVKTLNPS--HAGPIVVHCSAGVGRTGTFIVIDAMMDMIHS---EQKVDVFEFVSRIRNQRPQMVQTD 323
Cdd:cd14606  171 PSEPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRSGMVQTE 250

                        250
                 ....*....|...
gi 940373627 324 VQYTFIYQALLEY 336
Cdd:cd14606  251 AQYKFIYVAIAQF 263

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: 220.30 E-value: 5.64e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTL 502
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 503 SEAISVRDFLVT-FKQPLARQEEQVRMVRQFHFHGWPEVGIPAEgkgMIDLIAAVQKQQ--QQTGNHPITVHCSAGAGRT 579
Cdd:cd14549   81 LATYTVRTFSLKnLKLKKVKGRSSERVVYQYHYTQWPDHGVPDY---TLPVLSFVRKSSaaNPPGAGPIVVHCSAGVGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 940373627 580 GTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 625
Cdd:cd14549  158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

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: 220.24 E-value: 8.63e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 210
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCI-HPQLPDSCK----APRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTG 285
Cdd:cd17668   81 LAYYTVRNFTLrNTKIKKGSQkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 940373627 286 TFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALL 334
Cdd:cd17668  161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

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: 218.27 E-value: 7.52e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 105 NRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE 184
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 185 KCYQYWPDQGC-WTYGNIRVCVEDCVVLVDYTIRKFCI-HPQLpdscKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV 262
Cdd:cd14618   81 LCDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKLwHEDL----RKERRVKHLHYTAWPDHGIPESTSSLMAFRELV 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940373627 263 K--TLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALL 334
Cdd:cd14618  157 RehVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

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: 216.41 E-value: 1.75e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 130 DYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCV 209
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 210 VLVDYTIRKFCIHpqlPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV-KTLNPSHAGPIVVHCSAGVGRTGTFI 288
Cdd:cd14622   81 LLETISIRDFLVT---YNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940373627 289 VIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:cd14622  158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205

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: 216.29 E-value: 6.01e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 398 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 477
Cdd:cd14619    2 RFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 478 CYQYWPTEGS-VTHGDITIEIKSDTLSEAISVRDFLVtfkqpLARQEEQVRMVRQFHFHGWPEVGIPAEGKGMI---DLI 553
Cdd:cd14619   82 CEHYWPLDYTpCTYGHLRVTVVSEEVMENWTVREFLL-----KQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLafrRLL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940373627 554 AAVQKQQQQTGnhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 632
Cdd:cd14619  157 RQWLDQTMSGG--PTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

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: 213.44 E-value: 4.53e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  61 HLEEEIRVRSADDCKRFREEFNSLPSGHIQGT-FELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDG 139
Cdd:cd14628   11 YIQKLTQIETGENVTGMELEFKRLASSKAHTSrFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 140 YKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKF 219
Cdd:cd14628   91 YRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 220 cihpQLPDSCKA-PRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDM 296
Cdd:cd14628  171 ----KVTDARDGqSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLER 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 940373627 297 IHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:cd14628  247 MRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286

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: 210.18 E-value: 9.39e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 398 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 477
Cdd:cd14618    2 RYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 478 CYQYWPTEGS-VTHGDITIEIKSDTLSEAISVRDFLVtfkQPLARQEEqvRMVRQFHFHGWPEVGIPAEGKGMIDLIAAV 556
Cdd:cd14618   82 CDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKL---WHEDLRKE--RRVKHLHYTAWPDHGIPESTSSLMAFRELV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940373627 557 QKQQQQT-GNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 623
Cdd:cd14618  157 REHVQATkGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIF 224

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: 211.90 E-value: 1.57e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  80 EFNSLPSGHIQGT-FELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVN 158
Cdd:cd14627   31 EFKRLANSKAHTSrFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 159 DFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFcihpQLPDSCKA-PRLVSQ 237
Cdd:cd14627  111 DFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF----KVTDARDGqSRTVRQ 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 238 LHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQ 315
Cdd:cd14627  187 FQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 266

                        250       260
                 ....*....|....*....|.
gi 940373627 316 RPQMVQTDVQYTFIYQALLEY 336
Cdd:cd14627  267 RPAMVQTEDEYQFCYQAALEY 287

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: 208.77 E-value: 1.61e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYI--DGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPD---QGCWTYGNIRVCV 205
Cdd:cd14538    1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 206 EDCVVLVDYTIRKFCI-HPQLPDSckapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNpsHAGPIVVHCSAGVGRT 284
Cdd:cd14538   81 EKYQSLQDFVIRRISLrDKETGEV----HHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940373627 285 GTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14538  155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205

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: 207.25 E-value: 1.21e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 402 IIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKD-YFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQdKCYQ 480
Cdd:cd14547    6 ILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEkAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE-KCAQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 481 YWPTEGSVTHGDITIEIKSDTLSEAISVRDFLVtfkqplaRQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQ--- 557
Cdd:cd14547   85 YWPEEENETYGDFEVTVQSVKETDGYTVRKLTL-------KYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEear 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940373627 558 KQQQQTGnhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 623
Cdd:cd14547  158 QTEPHRG--PIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221

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: 207.43 E-value: 1.70e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  96 ANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVML 175
Cdd:cd14614    7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 176 TNLKERKEEKCYQYWP-DQGCWTYGNIRVCVEDCVVLVDYTIRKFCIhpqlpDSCKAPRLVSQLHFTSWPDFGVPFTPIG 254
Cdd:cd14614   87 TQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRV-----SYADEVQDVMHFNYTAWPDHGVPTANAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 255 --MLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQA 332
Cdd:cd14614  162 esILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQC 241


                 ..
gi 940373627 333 LL 334
Cdd:cd14614  242 VQ 243

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: 209.20 E-value: 1.80e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  61 HLEEEIRVRSADDCKRFREEFNSLPSGHIQGT-FELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDG 139
Cdd:cd14629   12 HIQKLTQVPPGESVTAMELEFKLLANSKAHTSrFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 140 YKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKF 219
Cdd:cd14629   92 YRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 220 cihpQLPDSCKA-PRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDM 296
Cdd:cd14629  172 ----KVTDARDGqSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGqdGPITVHCSAGVGRTGVFITLSIVLER 247

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 940373627 297 IHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:cd14629  248 MRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287

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: 207.58 E-value: 3.54e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 389 NLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLT 468
Cdd:cd14626   37 NLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMT 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 469 EVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISVRDFLVtFKQPLARQEEqvrmVRQFHFHGWPEVGIPAEGKG 548
Cdd:cd14626  117 RLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFAL-YKNGSSEKRE----VRQFQFMAWPDHGVPEYPTP 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 549 MIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14626  192 ILAFLRRV-KACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270

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: 206.05 E-value: 3.68e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 106 RYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEK 185
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 186 CYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCKAPRlvsQLHFTSWPDFGVPFTPIGMLKFLKKV-KT 264
Cdd:cd14623   81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIR---QFHFHGWPEVGIPSDGKGMINIIAAVqKQ 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940373627 265 LNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14623  158 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

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: 204.38 E-value: 6.86e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTL 502
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 503 SEAISVRDFLVTfKQPLARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTGNhPITVHCSAGAGRTGTF 582
Cdd:cd14551   81 LVDYTTRKFCIQ-KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAG-PIVVHCSAGVGRTGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 940373627 583 IALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd14551  159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

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: 203.25 E-value: 2.36e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFID-GYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEG-SVTHGDITIE-IKS 499
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEyEGEYGDLTVElVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 500 DTLSE-AISVRDFLVTfkqplaRQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQ-KQQQQTGNHPITVHCSAGAG 577
Cdd:cd18533   81 EENDDgGFIVREFELS------KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKReLNDSASLDPPIIVHCSAGVG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 578 RTGTFIAL--------SNILERVKAEGLLD-VFQAVKSLRLQRPHMVQTLEQYEFCY 625
Cdd:cd18533  155 RTGTFIALdslldelkRGLSDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLY 211

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: 202.94 E-value: 2.70e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 130 DYINASYID----GYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG-CWTYGNIRVC 204
Cdd:cd14541    1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 205 VEDCVVLVDYTIRKFCI-HPQLPDSckapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGR 283
Cdd:cd14541   81 CVSEEVTPSFAFREFILtNTNTGEE----RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGR 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940373627 284 TGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYY 337
Cdd:cd14541  157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRVY 210

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: 205.64 E-value: 3.59e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 368 LEEEFRKLTNVRImKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAH 447
Cdd:cd14621   28 FREEFNALPACPI-QATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 448 TVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISVRDFLVTFKQPLARQEEQvR 527
Cdd:cd14621  107 TVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVTNKKPQ-R 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 528 MVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTGNhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSL 607
Cdd:cd14621  186 LITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAG-AIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRI 264

                        250       260
                 ....*....|....*....|.
gi 940373627 608 RLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14621  265 RAQRCQMVQTDMQYVFIYQAL 285

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: 203.21 E-value: 4.03e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 105 NRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE 184
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 185 KCYQYWPDQG--CWTYGNIRVC--VEDcvVLVDYTIRKFCIHPQlpDSCKaprLVSQLHFTSWPDFGVPFTPIGMLKFLK 260
Cdd:cd14616   81 RCHQYWPEDNkpVTVFGDIVITklMED--VQIDWTIRDLKIERH--GDYM---MVRQCNFTSWPEHGVPESSAPLIHFVK 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940373627 261 KVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14616  154 LVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

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: 203.58 E-value: 4.34e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 387 TGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVM 466
Cdd:cd14614    6 AADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 467 LTEVQEREQDKCYQYWP-TEGSVTHGDITIEIKSDTLSEAISVRDFLVTFKqplarqeEQVRMVRQFHFHGWPEVGIPAE 545
Cdd:cd14614   86 LTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA-------DEVQDVMHFNYTAWPDHGVPTA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 546 GKGMiDLIAAVQKQQQQTGNH--PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 623
Cdd:cd14614  159 NAAE-SILQFVQMVRQQAVKSkgPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                 ....*.
gi 940373627 624 CYKVVQ 629
Cdd:cd14614  238 IHQCVQ 243

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: 202.96 E-value: 2.35e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 369 EEEFRKLTNVRIMKENmrtGNLPANMKKARVIQIIPYDFNRVILSMKRGQE--FTDYINASFIDGYRQKDYFMATQGPLA 446
Cdd:cd17667    6 EEVQRCTADMNITAEH---SNHPDNKHKNRYINILAYDHSRVKLRPLPGKDskHSDYINANYVDGYNKAKAYIATQGPLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 447 HTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISVRDFLV--------TFKQP 518
Cdd:cd17667   83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIrntkvkkgQKGNP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 519 LARQEEqvRMVRQFHFHGWPEVGIPAEGKGMIDLI-AAVQKQQQQTGnhPITVHCSAGAGRTGTFIALSNILERVKAEGL 597
Cdd:cd17667  163 KGRQNE--RTVIQYHYTQWPDMGVPEYALPVLTFVrRSSAARTPEMG--PVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 940373627 598 LDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 632
Cdd:cd17667  239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273

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: 202.39 E-value: 3.81e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  96 ANKEENREKNRYPNILPNDHCRVILSQVDgipcsDYINASYID----GYKEKNKFIAAQGPKQETVNDFWRMVWEQRSAT 171
Cdd:cd14600   35 AKLPQNMDKNRYKDVLPYDATRVVLQGNE-----DYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 172 IVMLTNLKERKEEKCYQYWPD-QGCWTYGNIRVCV--EDCVVLvdYTIRKFCI-HPQLPDSckapRLVSQLHFTSWPDFG 247
Cdd:cd14600  110 IVMLTTLTERGRTKCHQYWPDpPDVMEYGGFRVQChsEDCTIA--YVFREMLLtNTQTGEE----RTVTHLQYVAWPDHG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 248 VPFTPIGMLKFLKKVKTLNPSHAgPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYT 327
Cdd:cd14600  184 VPDDSSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYK 262

                        250
                 ....*....|
gi 940373627 328 FIYQALLEYY 337
Cdd:cd14600  263 FVCEAILRVY 272

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: 200.64 E-value: 5.84e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 393 NMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQE 472
Cdd:cd14630    3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 473 REQDKCYQYWPTEGSVtHGDITIE-IKSDTLSEAIsVRDFLVTFKqplarQEEQVRMVRQFHFHGWPEVGIPAEGKGMID 551
Cdd:cd14630   83 VGRVKCVRYWPDDTEV-YGDIKVTlIETEPLAEYV-IRTFTVQKK-----GYHEIREIRQFHFTSWPDHGVPCYATGLLG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 552 LIAAVQKQQQQTGNhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14630  156 FVRQVKFLNPPDAG-PIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231

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: 199.76 E-value: 8.17e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 398 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 477
Cdd:cd14617    2 RYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 478 CYQYWPTE-GSVTHGDITIEIKSDTLSEAISVRDFLVTfkqplarQEEQV---RMVRQFHFHGWPEVGIPAEGKGMIDLI 553
Cdd:cd14617   82 CDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREFKIC-------SEEQLdapRLVRHFHYTVWPDHGVPETTQSLIQFV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940373627 554 AAVQKQQQQT-GNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd14617  155 RTVRDYINRTpGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

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: 199.55 E-value: 5.29e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 346 VSSLERHLQTLHSTathfDKIGLEEEFRKLTNVRimKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYIN 425
Cdd:cd14625    6 ISELAEHTERLKAN----DNLKLSQEYESIDPGQ--QFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYIN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 426 ASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIeiksdTLSEA 505
Cdd:cd14625   80 ANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQV-----TLLDT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 506 ISVRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGTFIAL 585
Cdd:cd14625  155 IELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRV-KTCNPPDAGPIVVHCSAGVGRTGCFIVI 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 940373627 586 SNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14625  234 DAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276

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: 197.26 E-value: 3.43e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 389 NLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLT 468
Cdd:cd14624   43 NLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 469 EVQEREQDKCYQYWPTEGSVTHGDITIeiksdTLSEAISVRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPAEGKG 548
Cdd:cd14624  123 KLEERSRVKCDQYWPSRGTETYGLIQV-----TLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTP 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 549 MIDLIAAVQKQQQQTGNhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 625
Cdd:cd14624  198 FLAFLRRVKTCNPPDAG-PMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIH 273

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: 196.20 E-value: 5.54e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 388 GNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVML 467
Cdd:cd14603   25 GGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 468 TEVQEREQDKCYQYWP-TEGSVTHGDITI-EIKSDTLSEAISVRDFLVTFKQplarqeeQVRMVRQFHFHGWPEVGIPAE 545
Cdd:cd14603  105 CREIEMGKKKCERYWAqEQEPLQTGPFTItLVKEKRLNEEVILRTLKVTFQK-------ESRSVSHFQYMAWPDHGIPDS 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 546 GKGMIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGTFIALSNI-----LERVKAEglLDVFQAVKSLRLQRPHMVQTLEQ 620
Cdd:cd14603  178 PDCMLAMIELA-RRLQGSGPEPLCVHCSAGCGRTGVICTVDYVrqlllTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQ 254


                 ....*...
gi 940373627 621 YEFCYKVV 628
Cdd:cd14603  255 YEFLYHTV 262

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: 195.44 E-value: 7.11e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 104 KNRYPNILPNDHCRVIL----SQVDGipcSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATIVMLTNL 178
Cdd:cd14612   18 KDRYKTILPNPQSRVCLrragSQEEE---GSYINANYIRGYDGKEKaYIATQGPMLNTVSDFWEMVWQEECPIIVMITKL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 179 KERKEeKCYQYWPD-QGcwTYGNIRVCVEDCVVLVDYTIRKFCIhpQLPDSCkapRLVSQLHFTSWPDFGVPFTPIGMLK 257
Cdd:cd14612   95 KEKKE-KCVHYWPEkEG--TYGRFEIRVQDMKECDGYTIRDLTI--QLEEES---RSVKHYWFSSWPDHQTPESAGPLLR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 258 FLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14612  167 LVAEVEESRQTAAspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLAL 246


                 .
gi 940373627 336 Y 336
Cdd:cd14612  247 Y 247

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: 195.47 E-value: 8.08e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 104 KNRYPNILPNDHCRVILSQVD-GIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKEr 181
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 182 KEEKCYQYWPDQGCwTYGNIRVCVEDCVVLVDYTIRKFCIHpqlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKK 261
Cdd:cd14613  107 MNEKCTEYWPEEQV-TYEGIEITVKQVIHADDYRLRLITLK-----SGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940373627 262 VKTLN---PSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:cd14613  181 VEEARqqaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLSLY 258

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: 194.15 E-value: 1.30e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 104 KNRYPNILPNDHCRVILSQVDGipCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKE 183
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 184 EKCYQYWP----DQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFL 259
Cdd:cd14545   79 IKCAQYWPqgegNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENL---KTQETREVLHFHYTTWPDFGVPESPAAFLNFL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 260 KKVK---TLNPSHaGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ--KVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14545  156 QKVResgSLSSDV-GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231

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: 195.66 E-value: 1.31e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  95 LANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKN-KFIAAQGPKQETVNDFWRMVWEQRSATIV 173
Cdd:cd14610   38 VAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCVVIV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 174 MLTNLKERKEEKCYQYWPDQGCWTYGNIRV-CVEDCVVLVDYTIRKFCIHPQLPDSCkapRLVSQLHFTSWPDFGVPFTP 252
Cdd:cd14610  118 MLTPLAENGVKQCYHYWPDEGSNLYHIYEVnLVSEHIWCEDFLVRSFYLKNLQTNET---RTVTQFHFLSWNDQGVPAST 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 253 IGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMD-MIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14610  195 RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                 ....
gi 940373627 332 ALLE 335
Cdd:cd14610  275 AVAE 278

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: 192.22 E-value: 2.57e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCwTYGNIRVCVEDCVV 210
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK-TYGDIEVELKDTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCI-HPQLPDSckapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVK---TLNPSHAG---PIVVHCSAGVGR 283
Cdd:cd14558   80 SPTYTVRVFEItHLKRKDS----RTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklPYKNSKHGrsvPIVVHCSDGSSR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 940373627 284 TGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIY 330
Cdd:cd14558  156 TGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

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: 191.28 E-value: 6.52e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPtEGSVTHGDITIE-IKSDT 501
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTlVETEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 502 LSEAIsVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTGNhPITVHCSAGAGRTGT 581
Cdd:cd14555   80 LAEYV-VRTFALE-----RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAG-PIVVHCSAGAGRTGC 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 940373627 582 FIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14555  153 YIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199

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: 193.70 E-value: 6.83e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  94 ELANKEENREKNRYPNILPNDHCRVILSQvdgiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIV 173
Cdd:cd14608   18 RVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 174 MLTNLKERKEEKCYQYWP----DQGCWTYGNIRVCVEDCVVLVDYTIRKFcihpQLPD-SCKAPRLVSQLHFTSWPDFGV 248
Cdd:cd14608   94 MLNRVMEKGSLKCAQYWPqkeeKEMIFEDTNLKLTLISEDIKSYYTVRQL----ELENlTTQETREILHFHYTTWPDFGV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 249 PFTPIGMLKFLKKVK---TLNPSHaGPIVVHCSAGVGRTGTFIVIDA---MMDMIHSEQKVDVFEFVSRIRNQRPQMVQT 322
Cdd:cd14608  170 PESPASFLNFLFKVResgSLSPEH-GPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQT 248

                        250       260
                 ....*....|....*....|....
gi 940373627 323 DVQYTFIYQALLE--YYLYGDTEL 344
Cdd:cd14608  249 ADQLRFSYLAVIEgaKFIMGDSSV 272

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: 192.73 E-value: 1.22e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  92 TFELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSAT 171
Cdd:cd14603   21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 172 IVMLTNLKERKEEKCYQYWP-DQGCWTYGNIRVC-VEDCVVLVDYTIRKFCIhpqlpDSCKAPRLVSQLHFTSWPDFGVP 249
Cdd:cd14603  101 ILMACREIEMGKKKCERYWAqEQEPLQTGPFTITlVKEKRLNEEVILRTLKV-----TFQKESRSVSHFQYMAWPDHGIP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 250 FTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ---KVDVFEFVSRIRNQRPQMVQTDVQY 326
Cdd:cd14603  176 DSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRippDFSIFDVVLEMRKQRPAAVQTEEQY 255

                        250
                 ....*....|.
gi 940373627 327 TFIYQALLEYY 337
Cdd:cd14603  256 EFLYHTVAQMF 266

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: 188.77 E-value: 4.08e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKErKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 210
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDP-KDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCIHPQLPDSCKApRLVSQLHFTSWPDFG-VPFTPIGMLKFLKKV-KTLNPSHAGPIVVHCSAGVGRTGTFI 288
Cdd:cd14556   80 DEDVISRIFRLQNTTRPQEGY-RMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 940373627 289 VIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14556  159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

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: 188.89 E-value: 1.20e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  99 EENREKNRYPNILPNDHCRVILSQVDGipcsdYINASYID---GyKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVML 175
Cdd:cd14597    1 KENRKKNRYKNILPYDTTRVPLGDEGG-----YINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 176 TNLKERKEEKCYQYWPDQGCWTY---GNIRVCVEDCVVLVDYTIRkfciHPQLPD-SCKAPRLVSQLHFTSWPDFGVPFT 251
Cdd:cd14597   75 TQEVEGGKIKCQRYWPEILGKTTmvdNRLQLTLVRMQQLKNFVIR----VLELEDiQTREVRHITHLNFTAWPDHDTPSQ 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 252 PIGMLKFLKKVKTLNPShaGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14597  151 PEQLLTFISYMRHIHKS--GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                 ...
gi 940373627 332 ALL 334
Cdd:cd14597  229 VIL 231

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: 187.95 E-value: 1.30e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEgSVTHGDITIE-IKSDT 501
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITlLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 502 LSEaISVRDFLVTFKQPLARQEeqvrmVRQFHFHGWPEVGIPAEGKGMIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGT 581
Cdd:cd14632   80 LAE-YSVRTFALERRGYSARHE-----VKQFHFTSWPEHGVPYHATGLLAFIRRV-KASTPPDAGPVVVHCSAGAGRTGC 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 940373627 582 FIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14632  153 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199

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: 189.88 E-value: 2.28e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 346 VSSLERHLQtlhstathfDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYIN 425
Cdd:cd14610    6 LSYMEDHLK---------NKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYIN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 426 ASFI-DGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSvthgDITIEIKSDTLSE 504
Cdd:cd14610   77 ASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGS----NLYHIYEVNLVSE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 505 AISVRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTgNHPITVHCSAGAGRTGTFIA 584
Cdd:cd14610  153 HIWCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRSGTYIL 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 940373627 585 LSNILERV-KAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFID 633
Cdd:cd14610  232 IDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVN 281

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: 189.09 E-value: 4.22e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  61 HLEEEIRVRSaddckRFREEFNSLPSGHIQ-GTFELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINAS-YID 138
Cdd:cd14609    6 YMEDHLRNRD-----RLAKEWQALCAYQAEpNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 139 GYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRV-CVEDCVVLVDYTIR 217
Cdd:cd14609   81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVnLVSEHIWCEDFLVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 218 KFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMD-M 296
Cdd:cd14609  161 SFYLKNV---QTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrM 237

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 940373627 297 IHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14609  238 AKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276

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: 187.67 E-value: 5.05e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 393 NMKKARVIQIIPYDFNRVILSMKRGQE-FTDYINASFI----DGYRQKDY---FMATQGPLAHTVEDFWRMVWEWKSHTI 464
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVpGSDYINANYIrnenEGPTTDENaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 465 VMLTEVQEREQDKCYQYWPTEGSV-THGDITIEIKSDTLSEAISVRDFLVTfkqPLARQEEQvRMVRQFHFHGWPEVGIP 543
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQkQYGPYRVQNVSEHDTTDYTLRELQVS---KLDQGDPI-REIWHYQYLSWPDHGVP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 544 AEGKGMIDLIAAV-QKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLL---DVFQAVKSLRLQRPHMVQTLE 619
Cdd:cd14544  157 SDPGGVLNFLEDVnQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcdiDIQKTIQMVRSQRSGMVQTEA 236

                        250
                 ....*....|....
gi 940373627 620 QYEFCYKVVQDFID 633
Cdd:cd14544  237 QYKFIYVAVAQYIE 250

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: 185.88 E-value: 1.16e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 398 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 477
Cdd:cd14616    2 RFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 478 CYQYWPTEGS--VTHGDITIEIKSDTLSEAISVRDFLVtfkqplaRQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAA 555
Cdd:cd14616   82 CHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKI-------ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940373627 556 VQKQQQQTgNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd14616  155 VRASRAHD-NTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

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: 185.22 E-value: 1.48e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 409 RVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSV 488
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 489 tHGDITIE-IKSDTLSEAIsVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVqKQQQQTGNHP 567
Cdd:cd14631   81 -YGDFKVTcVEMEPLAEYV-VRTFTLE-----RRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV-KLSNPPSAGP 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940373627 568 ITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14631  153 IVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213

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: 185.63 E-value: 7.98e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 368 LEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINAS-FIDGYRQKDYFMATQGPLA 446
Cdd:cd14609   17 LAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPAYIATQGPLS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 447 HTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIksdtLSEAISVRDFLVTFKQPLARQEEQV 526
Cdd:cd14609   97 HTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNL----VSEHIWCEDFLVRSFYLKNVQTQET 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 527 RMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTgNHPITVHCSAGAGRTGTFIALSNILERVkAEGL--LDVFQAV 604
Cdd:cd14609  173 RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAATL 250

                        250       260
                 ....*....|....*....|....*....
gi 940373627 605 KSLRLQRPHMVQTLEQYEFCYKVVQDFID 633
Cdd:cd14609  251 EHVRDQRPGMVRTKDQFEFALTAVAEEVN 279

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: 185.25 E-value: 1.02e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 393 NMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQE 472
Cdd:cd14633   40 NRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 473 REQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAIsVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDL 552
Cdd:cd14633  120 VGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYV-IRTFAVE-----KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF 193

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940373627 553 IAAVQKQQQQTGNhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14633  194 VRQVKSKSPPNAG-PLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268

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: 184.27 E-value: 1.05e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 389 NLPANMKKARVIQIIPYDFNRVILSMKRGQ-EFTDYINASFIDGY--RQKDYfMATQGPLAHTVEDFWRMVWEWKSHTIV 465
Cdd:cd14612   11 DIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYdgKEKAY-IATQGPMLNTVSDFWEMVWQEECPIIV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 466 MLTEVQEReQDKCYQYWPTEGSvTHGDITIEIKSDTLSEAISVRDFLVtfkqplaRQEEQVRMVRQFHFHGWPEVGIPAE 545
Cdd:cd14612   90 MITKLKEK-KEKCVHYWPEKEG-TYGRFEIRVQDMKECDGYTIRDLTI-------QLEEESRSVKHYWFSSWPDHQTPES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 546 GKGMIDLIAAVQKQQQQTGNH-PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFC 624
Cdd:cd14612  161 AGPLLRLVAEVEESRQTAASPgPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                 .
gi 940373627 625 Y 625
Cdd:cd14612  241 H 241

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: 185.14 E-value: 2.11e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 387 TGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVM 466
Cdd:cd14604   51 TGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVM 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 467 LTEVQEREQDKCYQYWPT--EGSVTHGDITIEIKSDTLSEAISVRDFLVTFKQplarqeeQVRMVRQFHFHGWPEVGIPA 544
Cdd:cd14604  131 ACREFEMGRKKCERYWPLygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQN-------ETRRLYQFHYVNWPDHDVPS 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 545 EGKGMIDLIAAVQKQQQQTgNHPITVHCSAGAGRTGTFIALS---NILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQY 621
Cdd:cd14604  204 SFDSILDMISLMRKYQEHE-DVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 282


                 ....*..
gi 940373627 622 EFCYKVV 628
Cdd:cd14604  283 ELVHRAI 289

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: 181.72 E-value: 2.44e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTL 502
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 503 SEAISVRDFLV---TFKQPLARQEEQVRMVRQFHFHGWPEVGIPaegKGMIDLIAAVQK--QQQQTGNHPITVHCSAGAG 577
Cdd:cd17668   81 LAYYTVRNFTLrntKIKKGSQKGRPSGRVVTQYHYTQWPDMGVP---EYTLPVLTFVRKasYAKRHAVGPVVVHCSAGVG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 940373627 578 RTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 623
Cdd:cd17668  158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVF 203

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: 180.98 E-value: 1.87e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 393 NMKKARVIQIIPYDFNRVILSMKRGQE-FTDYINASFI--------DGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHT 463
Cdd:cd14605    2 NKNKNRYKNILPFDHTRVVLHDGDPNEpVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 464 IVMLTEVQEREQDKCYQYWPTEGSVT-HGDITIEIKSDTLSEAISVRDflvtFKQPLARQEEQVRMVRQFHFHGWPEVGI 542
Cdd:cd14605   82 IVMTTKEVERGKSKCVKYWPDEYALKeYGVMRVRNVKESAAHDYILRE----LKLSKVGQGNTERTVWQYHFRTWPDHGV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 543 PAEGKGMIDLIAAVQ-KQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGL---LDVFQAVKSLRLQRPHMVQTL 618
Cdd:cd14605  158 PSDPGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTE 237

                        250
                 ....*....|....*
gi 940373627 619 EQYEFCYKVVQDFID 633
Cdd:cd14605  238 AQYRFIYMAVQHYIE 252

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: 179.57 E-value: 2.35e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYID---GYKEKnKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG----CWTYGNIRV 203
Cdd:cd14540    1 YINASHITatvGGKQR-FYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgehdALTFGEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 204 CVEDCVVLVDYTIRKFCIHPQLPDSckaPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV-------------KTLNPsha 270
Cdd:cd14540   80 STKFSVSSGCYTTTGLRVKHTLSGQ---SRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrhtnqdvagHNRNP--- 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940373627 271 gPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:cd14540  154 -PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218

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: 179.34 E-value: 3.31e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 104 KNRYPNILPNDHCRVILSQVDGI-PCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKEr 181
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNdSLSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 182 KEEKCYQYWPDQGCwTYGNIRV---CVEDCVvlvDYTIRKFCIHpqlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKF 258
Cdd:cd14611   81 KNEKCVLYWPEKRG-IYGKVEVlvnSVKECD---NYTIRNLTLK-----QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940373627 259 LKKVKT--LNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14611  152 MLDVEEdrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 182.05 E-value: 5.05e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  73 DCKRF-REEFNSLPSGHIQGTFELANKeeNREKNRYPNILPNDHCRVILSQVDGIpcSDYINASYIDGYKEKNKFIAAQG 151
Cdd:PHA02738  22 DCEEViTREHQKVISEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 152 PKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPD--QGCWTYGNIRVC---VEDCVVLVDYTIrkfcihpQLP 226
Cdd:PHA02738  98 PTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITttqVETHPHYVKSTL-------LLT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 227 DSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTL-------------NPSHAGPIVVHCSAGVGRTGTFIVIDAM 293
Cdd:PHA02738 171 DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDIS 250

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 940373627 294 MDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:PHA02738 251 ISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRY 293

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: 177.64 E-value: 8.27e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFI--DGYRQKDYfMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIksd 500
Cdd:cd14546    1 YINASTIydHDPRNPAY-IATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHL--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 501 tLSEAISVRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTGNhPITVHCSAGAGRTG 580
Cdd:cd14546   77 -VSEHIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSC-PIVVHCSDGAGRTG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 940373627 581 TFIALSNILERV-KAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14546  155 TYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

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: 177.64 E-value: 9.46e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRV-CVEDC 208
Cdd:cd14546    1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVhLVSEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 209 VVLVDYTIRKFCIHpQLPDSckAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFI 288
Cdd:cd14546   81 IWCDDYLVRSFYLK-NLQTS--ETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940373627 289 VIDAMMD-MIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14546  158 LIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205

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: 179.01 E-value: 1.04e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  93 FELANKEENREKNRYPNILPNDHCRVILSQVDgipcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATI 172
Cdd:cd14607   16 HRVAKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 173 VMLTNLKERKEEKCYQYWP--DQGCWTYGNIRVCV----EDcvVLVDYTIRKFcihpQLPD-SCKAPRLVSQLHFTSWPD 245
Cdd:cd14607   92 VMLNRIVEKDSVKCAQYWPtdEEEVLSFKETGFSVkllsED--VKSYYTVHLL----QLENiNSGETRTISHFHYTTWPD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 246 FGVPFTPIGMLKFLKKVK---TLNPSHaGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ--KVDVFEFVSRIRNQRPQMV 320
Cdd:cd14607  166 FGVPESPASFLNFLFKVResgSLSPEH-GPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244

                        250
                 ....*....|...
gi 940373627 321 QTDVQYTFIYQAL 333
Cdd:cd14607  245 QTPDQLRFSYMAV 257

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 179.84 E-value: 3.12e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  74 CKRFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQVDGIPCSD-------------------YINA 134
Cdd:PHA02746  24 CEFVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAHESLKMFDvgdsdgkkievtsednaenYIHA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 135 SYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLkERKEEKCYQYW--PDQGCWTYGNIRVCVEDCVVLV 212
Cdd:PHA02746 104 NFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWtkEEDSELAFGRFVAKILDIIEEL 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 213 DYTIRKFCIHPQLPDSckaPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV--------KTL--NPSHAGPIVVHCSAGVG 282
Cdd:PHA02746 183 SFTKTRLMITDKISDT---SREIHHFWFPDWPDNGIPTGMAEFLELINKVneeqaeliKQAdnDPQTLGPIVVHCSAGIG 259

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940373627 283 RTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQAL 333
Cdd:PHA02746 260 RAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310

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: 174.92 E-value: 7.61e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTH--GDITIE-IKS 499
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLqfGPFKISlEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 500 DTLSEAISVRDFLVTFKqplarQEEqvRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKqQQQTGNHPITVHCSAGAGRT 579
Cdd:cd14542   81 KRVGPDFLIRTLKVTFQ-----KES--RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRD-YQGSEDVPICVHCSAGCGRT 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 940373627 580 GTFIALS---NILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd14542  153 GTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

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: 173.67 E-value: 3.12e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 422 DYINASFID----GYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWP-TEGSVTHGDITIE 496
Cdd:cd14541    1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 497 IKSDTLSEAISVRDFLVTFKQPLarqEEqvRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVqKQQQQTGNHPITVHCSAGA 576
Cdd:cd14541   81 CVSEEVTPSFAFREFILTNTNTG---EE--RHITQMQYLAWPDHGVPDDSSDFLDFVKRV-RQNRVGMVEPTVVHCSAGI 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 940373627 577 GRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 623
Cdd:cd14541  155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201

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: 172.32 E-value: 6.29e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPT--EGSVTHGDITIEIKSD 500
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 501 TLSEAISVRDFLVTFKqplaRQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQkQQQQTGNHPITVHCSAGAGRTG 580
Cdd:cd14557   81 KICPDYIIRKLNINNK----KEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN-AFNNFFSGPIVVHCSAGVGRTG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 940373627 581 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd14557  156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

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: 174.28 E-value: 6.58e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 389 NLPANMKKARVIQIIPYDFNRVIL-SMKRGQEFTDYINASFIDGYRQKD-YFMATQGPLAHTVEDFWRMVWEWKSHTIVM 466
Cdd:cd14613   21 DIPGLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 467 LTEVQEREQdKCYQYWPTEgSVTHGDITIEIKSDTLSEAISVRdfLVTFKQplarqEEQVRMVRQFHFHGWPEVGIPAEG 546
Cdd:cd14613  101 ITNIEEMNE-KCTEYWPEE-QVTYEGIEITVKQVIHADDYRLR--LITLKS-----GGEERGLKHYWYTSWPDQKTPDNA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 547 KGMIDLIAAVQKQQQQTGNH--PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFC 624
Cdd:cd14613  172 PPLLQLVQEVEEARQQAEPNcgPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFV 251


                 ....
gi 940373627 625 YKVV 628
Cdd:cd14613  252 HHVL 255

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 175.96 E-value: 6.62e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  78 REEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQVDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETV 157
Cdd:PHA02747  28 RDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIDGFEDDKKFIATQGPFAETC 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 158 NDFWRMVWEQRSATIVMLTNLKERK-EEKCYQYW-PDQgcwtygNIRVCVEDCVV-LVDYTIRKFCIHPQLP---DSCKA 231
Cdd:PHA02747 107 ADFWKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWcLNE------DGNIDMEDFRIeTLKTSVRAKYILTLIEitdKILKD 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 232 PRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV--------KTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ 301
Cdd:PHA02747 181 SRKISHFQCSEWFEDETPSDHPDFIKFIKIIdinrkksgKLFNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRK 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 940373627 302 KVDVFEFVSRIRNQRPQMVQTDVQYTFIYQA--LLEYYLY 339
Cdd:PHA02747 261 AICLAKTAEKIREQRHAGIMNFDDYLFIQPGyeVLHYFLS 300

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: 172.24 E-value: 7.36e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGY--KEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPD--QGCWTYGNIRVCVE 206
Cdd:cd14596    1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 207 DCVVLVDYTIRKFCIhpqLPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPShaGPIVVHCSAGVGRTGT 286
Cdd:cd14596   81 NYQALQYFIIRIIKL---VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT--GPIVVHCSAGIGRAGV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 940373627 287 FIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14596  156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204

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: 172.22 E-value: 7.61e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG--CWTYGNIRV-CVED 207
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeeQLQFGPFKIsLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 208 CVVLVDYTIRKFCIHPQlpdscKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTF 287
Cdd:cd14542   81 KRVGPDFLIRTLKVTFQ-----KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTI 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 940373627 288 IVIDAMMDMIHSE---QKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14542  156 CAIDYVWNLLKTGkipEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

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: 170.51 E-value: 4.55e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 130 DYINASYID----GYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPD-QGCWTYGNIRVC 204
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 205 VEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRT 284
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNL---EKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRT 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 940373627 285 GTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYY 337
Cdd:cd14601  158 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210

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: 172.42 E-value: 8.07e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  98 KEENREKNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTN 177
Cdd:cd14604   54 KEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACR 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 178 LKERKEEKCYQYWPDQG--CWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdscKAPRLVSQLHFTSWPDFGVPFTPIGM 255
Cdd:cd14604  134 EFEMGRKKCERYWPLYGeePMTFGPFRISCEAEQARTDYFIRTLLLEFQ-----NETRRLYQFHYVNWPDHDVPSSFDSI 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 256 LKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHS---EQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQA 332
Cdd:cd14604  209 LDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRA 288


                 ....*
gi 940373627 333 LLEYY 337
Cdd:cd14604  289 IAQLF 293

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: 169.32 E-value: 1.01e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEV-QEREQDKCYQYWPTEGSVTHGDITIEIKSDT 501
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLnQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 502 LSEAISVRDFLVtfkQPLARQEEQVRMVRQFHFHGW-PEVGIPAEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTG 580
Cdd:cd14637   81 ADEDIVTRLFRV---QNITRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940373627 581 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14637  158 TYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205

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: 167.89 E-value: 3.00e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQdkCYQYWPTEGSVTHGDITIEIKSDTL 502
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL--CMQYWPEKTSCCYGPIQVEFVSADI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 503 SEAISVRDFLVTfkqPLARQEEQVRMVRQFHFHGWPEV-GIPAEGKGMIDLIAAVQKQQQQ--TGNHPITVHCSAGAGRT 579
Cdd:cd14634   79 DEDIISRIFRIC---NMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940373627 580 GTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQD 630
Cdd:cd14634  156 GTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

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: 167.89 E-value: 3.08e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREqdKCYQYWPTEGSVTHGDITIEIKSDTL 502
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWPEEGMLRYGPIQVECMSCSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 503 SEAISVRDFLVTfkqPLARQEEQVRMVRQFHFHGWP-EVGIPAEGKGMIDLIAAVQKQQQQT--GNHPITVHCSAGAGRT 579
Cdd:cd14636   79 DCDVISRIFRIC---NLTRPQEGYLMVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEECdeGEGRTIIHCLNGGGRS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940373627 580 GTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKV 627
Cdd:cd14636  156 GMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203

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: 168.47 E-value: 3.90e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 393 NMKKARVIQIIPYDFNRVILsmkrGQEfTDYINASFIDGYRQKDYFM--ATQGPLAHTVEDFWRMVWEWKSHTIVMLTEV 470
Cdd:cd14597    3 NRKKNRYKNILPYDTTRVPL----GDE-GGYINASFIKMPVGDEEFVyiACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 471 QEREQDKCYQYWPTE-GSVTHGDITIEIksdTLSEAISVRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPAEGKGM 549
Cdd:cd14597   78 VEGGKIKCQRYWPEIlGKTTMVDNRLQL---TLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940373627 550 IDLIAAVqKQQQQTGnhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14597  155 LTFISYM-RHIHKSG--PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230

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: 167.95 E-value: 6.00e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 404 PYDFNRVILSMKRGQefTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWP 483
Cdd:cd14545    9 PYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKCAQYWP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 484 TEGS----VTHGDITIEIKSDTLSEAISVRDFLVTfkqPLARQEEqvRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQ 559
Cdd:cd14545   87 QGEGnamiFEDTGLKVTLLSEEDKSYYTVRTLELE---NLKTQET--REVLHFHYTTWPDFGVPESPAAFLNFLQKVRES 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 560 QQQTGNH-PITVHCSAGAGRTGTFIALSNILERVKAEGL--LDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd14545  162 GSLSSDVgPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231

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: 168.49 E-value: 1.47e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 390 LPANMKKARVIQIIPYDFNRVILsmkrgQEFTDYINASFID----GYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIV 465
Cdd:cd14600   37 LPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 466 MLTEVQEREQDKCYQYWPTEGSV-THGDITIEIKSDTLSEAISVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPA 544
Cdd:cd14600  112 MLTTLTERGRTKCHQYWPDPPDVmEYGGFRVQCHSEDCTIAYVFREMLLT-----NTQTGEERTVTHLQYVAWPDHGVPD 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 545 EGKGMIDLIAAVQKQQQQtgNHPITVHCSAGAGRTGTFIALSN---ILERVKAEGLLDVfqaVKSLRLQRPHMVQTLEQY 621
Cdd:cd14600  187 DSSDFLEFVNYVRSKRVE--NEPVLVHCSAGIGRTGVLVTMETamcLTERNQPVYPLDI---VRKMRDQRAMMVQTSSQY 261


                 ..
gi 940373627 622 EF 623
Cdd:cd14600  262 KF 263

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: 167.36 E-value: 3.05e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 374 KLTNVRimKENMRtgnlPANMKKARVIQIIPYDFNRVILSMKRGQ-EFTDYINASFI------DGYRQKDYfMATQGPLA 446
Cdd:cd14606    5 KNLHQR--LEGQR----PENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVknqllgPDENAKTY-IASQGCLE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 447 HTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVT-HGDITIEIKSDTLSEAISVRDFLVTfkqPLARQeEQ 525
Cdd:cd14606   78 ATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRaYGPYSVTNCGEHDTTEYKLRTLQVS---PLDNG-EL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 526 VRMVRQFHFHGWPEVGIPAEGKGMIDLIAAV-QKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGL---LDVF 601
Cdd:cd14606  154 IREIWHYQYLSWPDHGVPSEPGGVLSFLDQInQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQ 233

                        250       260       270
                 ....*....|....*....|....*....|..
gi 940373627 602 QAVKSLRLQRPHMVQTLEQYEFCYKVVQDFID 633
Cdd:cd14606  234 KTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIE 265

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: 165.25 E-value: 3.07e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQ-KDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTE--GSVTHGDITIEIKS 499
Cdd:cd14539    1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 500 DTLSEAISVRDFLVTFKqplarQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQK--QQQQTGNHPITVHCSAGAG 577
Cdd:cd14539   81 VRTTPTHVERIISIQHK-----DTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShyLQQRSLQTPIVVHCSSGVG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 940373627 578 RTGTFIALSNILERVKAE-GLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd14539  156 RTGAFCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

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: 165.24 E-value: 3.56e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYF--MATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWP---TEGSVTHGDITIEI 497
Cdd:cd14538    1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 498 KSDTLSEAISVRDFLVTFKQplarqEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQqTGnhPITVHCSAGAG 577
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKE-----TGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN-SG--PIVVHCSAGIG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940373627 578 RTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14538  153 RTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203

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: 165.78 E-value: 5.12e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 104 KNRYPNILPNDHCRVILSQVDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKE 183
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 184 EKCYQYWPDQG--CWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdscKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKK 261
Cdd:cd14602   81 KKCERYWAEPGemQLEFGPFSVTCEAEKRKSDYIIRTLKVKFN-----SETRTIYQFHYKNWPDHDVPSSIDPILELIWD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 262 VKTLNPSHAGPIVVHCSAGVGRTGTFIVID----AMMDMIHSEQkVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYY 337
Cdd:cd14602  156 VRCYQEDDSVPICIHCSAGCGRTGVICAIDytwmLLKDGIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 166.33 E-value: 2.21e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 393 NMKKARVIQIIPYDFNRVILSMKRGqeFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQE 472
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 473 REQDKCYQYWPTE--GSVTHGDITIEIKsdtlsEAISVRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPAEGKGMI 550
Cdd:PHA02742 130 DGKEACYPYWMPHerGKATHGEFKIKTK-----KIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 551 DLIAAVQKQQQQT----------GNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQ 620
Cdd:PHA02742 205 DFVLAVREADLKAdvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQ 284

                        250
                 ....*....|....*..
gi 940373627 621 YEFCYKVVQDFIDIFSD 637
Cdd:PHA02742 285 YIFCYFIVLIFAKLMAD 301

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

Pssm-ID: 350459 [Multi-domain] Cd Length: 226 Bit Score: 163.17 E-value: 2.77e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 396 KARVIQIIPYDFNRVILSMKRGQEF-TDYINASFIDGYRQKD-YFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQER 473
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEkAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 474 EQdKCYQYWPTEGSVtHGDITIEIKSDTLSEAISVRDFLVtfkqplaRQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLI 553
Cdd:cd14611   82 NE-KCVLYWPEKRGI-YGKVEVLVNSVKECDNYTIRNLTL-------KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940373627 554 AAVQKQQQQ-TGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 625
Cdd:cd14611  153 LDVEEDRLAsPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225

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

Pssm-ID: 350388 [Multi-domain] Cd Length: 219 Bit Score: 161.86 E-value: 6.60e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFID---GYRQKDYfMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGS----VTHGDITI 495
Cdd:cd14540    1 YINASHITatvGGKQRFY-IAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGehdaLTFGEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 496 EIKSDTLSEAISVRDFLVtfKQPLARQEeqvRMVRQFHFHGWPEVGIPAEGKGMIDLI--------AAVQKQQQQTGNHP 567
Cdd:cd14540   80 STKFSVSSGCYTTTGLRV--KHTLSGQS---RTVWHLQYTDWPDHGCPEDVSGFLDFLeeinsvrrHTNQDVAGHNRNPP 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940373627 568 ITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 632
Cdd:cd14540  155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219

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: 162.32 E-value: 8.17e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 396 KARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQ 475
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 476 DKCYQYW--PTEGSVTHGDITIEIKSDTLSEAISVRDFLVTFkqplarqEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLI 553
Cdd:cd14602   81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKF-------NSETRTIYQFHYKNWPDHDVPSSIDPILELI 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940373627 554 AAVqKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKaEGLL----DVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14602  154 WDV-RCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230

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: 160.62 E-value: 1.40e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQdkCYQYWPTEGSVTHGDITIEIKSDTL 502
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWPENGVHRHGPIQVEFVSADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 503 SEAISVRDFLVtfkQPLARQEEQVRMVRQFHFHGWPEV-GIPAEGKGMIDLIAAVQKQQQQ--TGNHPITVHCSAGAGRT 579
Cdd:cd14635   79 EEDIISRIFRI---YNAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940373627 580 GTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKV 627
Cdd:cd14635  156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203

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: 162.09 E-value: 4.44e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  80 EFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILsqvdgIPCSD----YINASYIDGY--KEKNKFIAAQGPK 153
Cdd:cd14599   17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVEL-----VPTKEnntgYINASHIKVTvgGEEWHYIATQGPL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 154 QETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG----CWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSc 229
Cdd:cd14599   92 PHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ- 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 230 kaPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTL----NPSHAG------PIVVHCSAGVGRTGTFIVIDAMMDMIHS 299
Cdd:cd14599  171 --ERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVrrhtNSMLDStkncnpPIVVHCSAGVGRTGVVILTELMIGCLEH 248

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 940373627 300 EQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:cd14599  249 NEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285

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: 159.02 E-value: 5.40e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREqdKCYQYWPTEG--------SVTHGDit 494
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEkplecetfKVTLSG-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 495 IEIKSDTLSEAISVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAegKGMIDLIAAVQKQQQQTgNHPITVHCSA 574
Cdd:cd14550   77 EDHSCLSNEIRLIVRDFILE-----STQDDYVLEVRQFQCPSWPNPCSPI--HTVFELINTVQEWAQQR-DGPIVVHDRY 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940373627 575 GAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd14550  149 GGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 162.09 E-value: 6.54e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  60 EHLEEEIRVRSAddckrFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQVDGIpcSDYINASYIDG 139
Cdd:PHA02742  16 EQLIEESNLAEI-----LKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDGG--DDFINASYVDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 140 YKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYW--PDQGCWTYGNIRVCVEDCVVLVDYTIR 217
Cdd:PHA02742  89 HNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmpHERGKATHGEFKIKTKKIKSFRNYAVT 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 218 KFCihpqLPDSCKAPRL-VSQLHFTSWPDFGVPFTPIGMLKFLKKV-----------KTLNPSHAGPIVVHCSAGVGRTG 285
Cdd:PHA02742 169 NLC----LTDTNTGASLdIKHFAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVKEPPILVHCSAGLDRAG 244

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940373627 286 TFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:PHA02742 245 AFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 295

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: 157.85 E-value: 1.53e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 387 TGNLPANMKKARVIQIIPYDFNRVILSMKRgQEFTDYINASFID-GYRQKDY-FMATQGPLAHTVEDFWRMVWEWKSHTI 464
Cdd:cd14599   32 TATLPENAERNRIREVVPYEENRVELVPTK-ENNTGYINASHIKvTVGGEEWhYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 465 VMLTEVQEREQDKCYQYWPTEG----SVTHGDITIEIKSDTLSEAISVRDFLVtfKQPLARQEeqvRMVRQFHFHGWPEV 540
Cdd:cd14599  111 AMVTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKV--KHLLSGQE---RTVWHLQYTDWPDH 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 541 GIPAEGKGMIDLIAAVQKQQQQTG---------NHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQR 611
Cdd:cd14599  186 GCPEEVQGFLSYLEEIQSVRRHTNsmldstkncNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQR 265

                        250       260
                 ....*....|....*....|.
gi 940373627 612 PHMVQTLEQYEFCYKVVQDFI 632
Cdd:cd14599  266 MFMIQTIAQYKFVYQVLIQFL 286

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: 154.85 E-value: 1.97e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKN-KFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWP-DQG-CWTYGNIRVCVED 207
Cdd:cd14539    1 YINASLIEDLTPYCpRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPtERGqALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 208 CVVLVDYTIRKFCI--HPQlpdscKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV----KTLNPSHAgPIVVHCSAGV 281
Cdd:cd14539   81 VRTTPTHVERIISIqhKDT-----RLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhshyLQQRSLQT-PIVVHCSSGV 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940373627 282 GRTGTF-IVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14539  155 GRTGAFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 156.40 E-value: 4.69e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 100 ENREKNRYPNILPNDHCRVilsQVDGipcsDYINASYIDGyKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLK 179
Cdd:COG5599   41 NGSPLNRFRDIQPYKETAL---RANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 180 ERKE--EKCYQYWPDQGcwTYG--NIRVCVEDCVVLVD-YTIRKFCIhpQLPDSCKAPRLVSQLHFTSWPDFGVPFTPI- 253
Cdd:COG5599  113 EISKpkVKMPVYFRQDG--EYGkyEVSSELTESIQLRDgIEARTYVL--TIKGTGQKKIEIPVLHVKNWPDHGAISAEAl 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 254 -GMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMI--HSEQKVDVFEFVSRIRNQR-PQMVQTDVQYTFI 329
Cdd:COG5599  189 kNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268

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: 153.39 E-value: 6.72e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYI--DGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKE-RKEEKCYQYWP--DQGCWTYGNIRV-- 203
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPaeENESREFGRISVtn 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 204 ----CVEDCVVLvdytiRKFCIHPQlpDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPShAGPIVVHCSA 279
Cdd:cd17658   81 kklkHSQHSITL-----RVLEVQYI--ESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPS-AGPIVVHCSA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 940373627 280 GVGRTGTFIVIDAMMDMI--HSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIY 330
Cdd:cd17658  153 GIGRTGAYCTIHNTIRRIleGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205

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: 151.46 E-value: 3.38e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDY--FMATQGPLAHTVEDFWRMVWEWKSHTIVMLTE-VQEREQDKCYQYWPTE--GSVTHGDITIEI 497
Cdd:cd17658    1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRlVDNYSTAKCADYFPAEenESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 498 KSDTLSE-AISVRDFLVTFKQplarQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVqkQQQQTGNHPITVHCSAGA 576
Cdd:cd17658   81 KKLKHSQhSITLRVLEVQYIE----SEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRL--YGIPPSAGPIVVHCSAGI 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940373627 577 GRTGTFIALSNILERVKAEGL--LDVFQAVKSLRLQRPHMVQTLEQYEFCY 625
Cdd:cd17658  155 GRTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205

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: 149.90 E-value: 1.33e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGY--RQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVThgdITIEIKSD 500
Cdd:cd14596    1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEP---MELENYQL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 501 TLSEAISVRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQqTGnhPITVHCSAGAGRTG 580
Cdd:cd14596   78 RLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN-TG--PIVVHCSAGIGRAG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940373627 581 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd14596  155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 152.49 E-value: 3.42e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 391 PANMKKARVIQIIPYDFNRVILSMK-------------RGQEFT------DYINASFIDGYRQKDYFMATQGPLAHTVED 451
Cdd:PHA02746  49 KENLKKNRFHDIPCWDHSRVVINAHeslkmfdvgdsdgKKIEVTsednaeNYIHANFVDGFKEANKFICAQGPKEDTSED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 452 FWRMVWEWKSHTIVMLTEVqEREQDKCYQYWPTE--GSVTHGDITIEIKsdtlsEAISVRDFLVTFKQPLARQEEQVRMV 529
Cdd:PHA02746 129 FFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEedSELAFGRFVAKIL-----DIIEELSFTKTRLMITDKISDTSREI 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 530 RQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQ---------QQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDV 600
Cdd:PHA02746 203 HHFWFPDWPDNGIPTGMAEFLELINKVNEEQaelikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCL 282

                        250       260
                 ....*....|....*....|....*....
gi 940373627 601 FQAVKSLRLQRPHMVQTLEQYEFCYKVVQ 629
Cdd:PHA02746 283 GEIVLKIRKQRHSSVFLPEQYAFCYKALK 311

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: 147.43 E-value: 1.36e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYID---GYKEKNkFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCW----TYGNIRV 203
Cdd:cd14598    1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 204 CVE-----DCVVLVDYTIRKFCIHPQlpdsckapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVK--------TLNPSHA 270
Cdd:cd14598   80 TTRfrtdsGCYATTGLKIKHLLTGQE--------RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnsTIDPKSP 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 271 G-PIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:cd14598  152 NpPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218

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: 142.88 E-value: 2.34e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627   235 VSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ-KVDVFEFVSR 311
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVKE 81

                           90       100
                   ....*....|....*....|....
gi 940373627   312 IRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:smart00012  82 LRSQRPGMVQTEEQYLFLYRALLE 105

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 142.88 E-value: 2.34e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627   235 VSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ-KVDVFEFVSR 311
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVKE 81

                           90       100
                   ....*....|....*....|....
gi 940373627   312 IRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:smart00404  82 LRSQRPGMVQTEEQYLFLYRALLE 105

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: 146.66 E-value: 2.49e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFID---GYRQKDYfMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGS----VTHG--DI 493
Cdd:cd14598    1 YINASHIKvtvGGKEWDY-IATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSrhntVTYGrfKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 494 TIEIKSDTLSEAISVrdflVTFKQPLARQEeqvRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVQKQQQQTG--------N 565
Cdd:cd14598   80 TTRFRTDSGCYATTG----LKIKHLLTGQE---RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNstidpkspN 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 566 HPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 632
Cdd:cd14598  153 PPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219

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: 147.09 E-value: 9.61e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 386 RTGNLPANMKKARVIQIIPYDFNRVILSmkrgQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIV 465
Cdd:cd14608   18 RVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 466 MLTEVQEREQDKCYQYWP----TEGSVTHGDITIEIKSDTLSEAISVRDFLVtfkQPLARQEeqVRMVRQFHFHGWPEVG 541
Cdd:cd14608   94 MLNRVMEKGSLKCAQYWPqkeeKEMIFEDTNLKLTLISEDIKSYYTVRQLEL---ENLTTQE--TREILHFHYTTWPDFG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 542 IPAEGKGMIDLIAAVQKQQQQTGNH-PITVHCSAGAGRTGTFIALSN---ILERVKAEGLLDVFQAVKSLRLQRPHMVQT 617
Cdd:cd14608  169 VPESPASFLNFLFKVRESGSLSPEHgPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQT 248

                        250
                 ....*....|.
gi 940373627 618 LEQYEFCYKVV 628
Cdd:cd14608  249 ADQLRFSYLAV 259

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: 141.24 E-value: 2.35e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 422 DYINASFID----GYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWP-TEGSVTHGDITIE 496
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 497 IKSDTLSEAISVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEGKGMIDLIAAVqKQQQQTGNHPITVHCSAGA 576
Cdd:cd14601   81 CHSEEGNPAYVFREMTLT-----NLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLV-RNKRAGKDEPVVVHCSAGI 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 940373627 577 GRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 623
Cdd:cd14601  155 GRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRF 201

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: 138.20 E-value: 2.15e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYqYWPTEGSVTHGD------ITIE 496
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCEtfkvtlIAEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 497 IKSDTLSEAISVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEgkGMIDLIAAVqKQQQQTGNHPITVHCSAGA 576
Cdd:cd17669   80 HKCLSNEEKLIIQDFILE-----ATQDDYVLEVRHFQCPKWPNPDSPIS--KTFELISII-KEEAANRDGPMIVHDEHGG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940373627 577 GRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd17669  152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 133.64 E-value: 4.54e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627   528 MVRQFHFHGWPEVGIPAEGKGMIDLIAAVQK-QQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGL-LDVFQAVK 605
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKnLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 940373627   606 SLRLQRPHMVQTLEQYEFCYKVVQD 630
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105

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: 133.64 E-value: 4.54e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627   528 MVRQFHFHGWPEVGIPAEGKGMIDLIAAVQK-QQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGL-LDVFQAVK 605
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKnLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 940373627   606 SLRLQRPHMVQTLEQYEFCYKVVQD 630
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 138.69 E-value: 8.99e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 389 NLPANMKKARVIQIIPYDFNRVilsmkrgQEFTDYINASFIDGYRQKDYfMATQGPLAHTVEDFWRMVWEWKSHTIVMLT 468
Cdd:COG5599   38 QNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNHRY-IATQYPLEEQLEDFFQMLFDNNTPVLVVLA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 469 EVQE--REQDKCYQYWPTEGSVTHGDITIE-IKSDTLSEAISVRDFLVTFKQplarQEEQVRMVRQFHFHGWPE-VGIPA 544
Cdd:COG5599  110 SDDEisKPKVKMPVYFRQDGEYGKYEVSSElTESIQLRDGIEARTYVLTIKG----TGQKKIEIPVLHVKNWPDhGAISA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 545 EG-KGMIDLIAAVQKQQQQTGNHPItVHCSAGAGRTGTFIALSNILERVKAEGL--LDVFQAVKSLRLQR-PHMVQTLEQ 620
Cdd:COG5599  186 EAlKNLADLIDKKEKIKDPDKLLPV-VHCRAGVGRTGTLIACLALSKSINALVQitLSVEEIVIDMRTSRnGGMVQTSEQ 264

                        250
                 ....*....|....
gi 940373627 621 YEFCYKVVQDFIDI 634
Cdd:COG5599  265 LDVLVKLAEQQIRP 278

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 139.29 E-value: 1.44e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 392 ANMKKARVIQIIPYDFNRVILSMKRGQefTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQ 471
Cdd:PHA02738  48 KNRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKK 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 472 EREQDKCYQYWPT--EGSVTHGDITIeiksdtlsEAISVRDFLVTFKQPLARQE--EQVRMVRQFHFHGWPEVGIPAEGK 547
Cdd:PHA02738 126 ENGREKCFPYWSDveQGSIRFGKFKI--------TTTQVETHPHYVKSTLLLTDgtSATQTVTHFNFTAWPDHDVPKNTS 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 548 GMIDLIAAVQKQQQ-------QTGNH-----PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMV 615
Cdd:PHA02738 198 EFLNFVLEVRQCQKelaqeslQIGHNrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSL 277

                        250
                 ....*....|....*....
gi 940373627 616 QTLEQYEFCYKVVQDFIDI 634
Cdd:PHA02738 278 FIPFQYFFCYRAVKRYVNL 296

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.

Pssm-ID: 350455 [Multi-domain] Cd Length: 257 Bit Score: 136.63 E-value: 2.86e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 386 RTGNLPANMKKARVIQIIPYDFNRVILSMKRgqefTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIV 465
Cdd:cd14607   17 RVAKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 466 MLTEVQEREQDKCYQYWPTEGS--VTHGDITIEIKsdTLSEAISVRdFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIP 543
Cdd:cd14607   93 MLNRIVEKDSVKCAQYWPTDEEevLSFKETGFSVK--LLSEDVKSY-YTVHLLQLENINSGETRTISHFHYTTWPDFGVP 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 544 AEGKGMIDLIAAVQKQQQQTGNH-PITVHCSAGAGRTGTFIALSN--ILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQ 620
Cdd:cd14607  170 ESPASFLNFLFKVRESGSLSPEHgPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQ 249


                 ....*...
gi 940373627 621 YEFCYKVV 628
Cdd:cd14607  250 LRFSYMAV 257

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 137.44 E-value: 5.44e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 391 PANMKKARVIQIIPYDFNRVILSMKRGQEfTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEV 470
Cdd:PHA02747  49 PENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 471 QERE-QDKCYQYW-PTE-GSVTHGDITIEiksdTLSeaISVR-DFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPAEG 546
Cdd:PHA02747 128 KGTNgEEKCYQYWcLNEdGNIDMEDFRIE----TLK--TSVRaKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDH 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 547 KGMIDLIAAVQKQQQQTGNH---------PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQT 617
Cdd:PHA02747 202 PDFIKFIKIIDINRKKSGKLfnpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMN 281


                 ....*.
gi 940373627 618 LEQYEF 623
Cdd:PHA02747 282 FDDYLF 287

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: 133.99 E-value: 5.62e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCyqYWPDQG----CWTYgNIRVCVE 206
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEkpleCETF-KVTLSGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 207 DCVVL---VDYTIRKFCIHPQLPDSCKAprlVSQLHFTSWPDfgvPFTPI-GMLKFLKKVKTLNPSHAGPIVVHCSAGVG 282
Cdd:cd14550   78 DHSCLsneIRLIVRDFILESTQDDYVLE---VRQFQCPSWPN---PCSPIhTVFELINTVQEWAQQRDGPIVVHDRYGGV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 940373627 283 RTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14550  152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

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: 132.84 E-value: 1.73e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKerKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 210
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD--AAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCI----HPQlpdscKAPRLVSQLHFTSWPDFGVpfTPIGMLKFLKKVKTLNP------SHAGPIVVHCSAG 280
Cdd:cd14634   79 DEDIISRIFRIcnmaRPQ-----DGYRIVQHLQYIGWPAYRD--TPPSKRSILKVVRRLEKwqeqydGREGRTVVHCLNG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 940373627 281 VGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14634  152 GGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

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: 132.11 E-value: 3.68e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 423 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKcYQYWPT-EGSVTHGDITIE-IKSD 500
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWPSrEESMNCEAFTVTlISKD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 501 TL----SEAISVRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPAEgkGMIDLIAAVqKQQQQTGNHPITVHCSAGA 576
Cdd:cd17670   80 RLclsnEEQIIIHDFILE-----ATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVI-KEEALTRDGPTIVHDEFGA 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940373627 577 GRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 628
Cdd:cd17670  152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203

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: 126.34 E-value: 4.32e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKerKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 210
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVD--PAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCIH----PQlpdscKAPRLVSQLHFTSWPDF-GVPFTPIGMLKFLKKVKTLNPSH---AGPIVVHCSAGVG 282
Cdd:cd14635   79 EEDIISRIFRIYnaarPQ-----DGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYnggEGRTVVHCLNGGG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 940373627 283 RTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14635  154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206

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: 122.83 E-value: 5.74e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKerKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 210
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVD--LAQGCPQYWPEEGMLRYGPIQVECMSCSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 211 LVDYTIRKFCI----HPQlpdscKAPRLVSQLHFTSWPDF-GVPFTPIGMLKFLKKVKTLNPS---HAGPIVVHCSAGVG 282
Cdd:cd14636   79 DCDVISRIFRIcnltRPQ-----EGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdeGEGRTIIHCLNGGG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 940373627 283 RTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14636  154 RSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206

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: 118.17 E-value: 3.01e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYqYWPDQ----GCWTYgNIRVCVE 206
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKdepiNCETF-KVTLIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 207 DCVVLVDYtiRKFCIHPQLPDSCKAPRLVSQLHFT--SWPDfgvPFTPIG-MLKFLKKVKTLNPSHAGPIVVHCSAGVGR 283
Cdd:cd17669   79 EHKCLSNE--EKLIIQDFILEATQDDYVLEVRHFQcpKWPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEHGGVT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940373627 284 TGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQmVQTDV-QYTFIYQALL 334
Cdd:cd17669  154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPG-VFTDIeQYQFLYKAIL 204

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: 117.32 E-value: 5.74e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE-KCYQYWPDQGCWTYGNIRVCVEDCV 209
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 210 VLVDYTIRKFCIHpQLPDSCKAPRLVSQLHFTSWPDF-GVPFTPIGMLKFLKKV-KTLNPSHAGPIVVHCSAGVGRTGTF 287
Cdd:cd14637   81 ADEDIVTRLFRVQ-NITRLQEGHLMVRHFQFLRWSAYrDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGGRSGTY 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940373627 288 IVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 335
Cdd:cd14637  160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207

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: 106.30 E-value: 3.62e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 131 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKcYQYWPDQ----GCWTYgNIRVCVE 206
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWPSReesmNCEAF-TVTLISK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 207 DCVVLVDYtiRKFCIHPQLPDSCKAPRLVSQLHFT--SWPDfgvPFTPI-GMLKFLKKVKTLNPSHAGPIVVHCSAGVGR 283
Cdd:cd17670   79 DRLCLSNE--EQIIIHDFILEATQDDYVLEVRHFQcpKWPN---PDAPIsSTFELINVIKEEALTRDGPTIVHDEFGAVS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940373627 284 TGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQmVQTDV-QYTFIYQALL 334
Cdd:cd17670  154 AGTLCALTTLSQQLENENAVDVYQVAKMINLMRPG-VFTDIeQYQFLYKAML 204

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: 84.76 E-value: 1.85e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 109 NILPNDHCRVilSQVDGIPcsdyINASYIDgYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQ 188
Cdd:cd14559    1 NRFTNIQTRV--STPVGKN----LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 189 YWPDQGcwTYGNIRVCVEDcvVLVDYTIRKFCIHP---QLPDSCKaPRLVSQLHFTSWPDFGVpfTPIGMLKFL------ 259
Cdd:cd14559   74 YFRQSG--TYGSVTVKSKK--TGKDELVDGLKADMynlKITDGNK-TITIPVVHVTNWPDHTA--ISSEGLKELadlvnk 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940373627 260 ---KKVKTLNPSHAGPI--------VVHCSAGVGRTGTFIvidAMMDMIHSEQKVDVFEFVSRIRNQR-PQMVQTDVQY 326
Cdd:cd14559  147 saeEKRNFYKSKGSSAIndknkllpVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRnGKMVQKDEQL 222

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 83.86 E-value: 1.18e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 424 INASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEReqdKCY-QYWPT-EGSVTHGDitiEIKSDT 501
Cdd:PHA02740  79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCFnQFWSLkEGCVITSD---KFQIET 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 502 LsEAISVRDFLVTFKQpLARQEEQVRMVRQFHFHGWPEVGIPAEGKGMID-------LIAAVQKQQQQTGNHPITVHCSA 574
Cdd:PHA02740 153 L-EIIIKPHFNLTLLS-LTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDffcniddLCADLEKHKADGKIAPIIIDCID 230

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 940373627 575 GAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 632
Cdd:PHA02740 231 GISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYL 288

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 81.94 E-value: 6.45e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  68 VRSADDCKRFREEFNSLPSGHIQGTFELANKEENREKNRyPNILPndHCRVILSQVDGIPCSDYINASYIDGYKEKNKFI 147
Cdd:PHA02740  18 INKPDLLSCIIKEYRAIVPEHEDEANKACAQAENKAKDE-NLALH--ITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 148 AAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERkeeKCY-QYWP-DQGC-WTYGNIRVCVEDCVVLVDYTIRKFCihpq 224
Cdd:PHA02740  95 CIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCFnQFWSlKEGCvITSDKFQIETLEIIIKPHFNLTLLS---- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 225 LPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTL--------NPSHAGPIVVHCSAGVGRTGTFIVIDAMMDM 296
Cdd:PHA02740 168 LTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadlekhkADGKIAPIIIDCIDGISSSAVFCVFDICATE 247

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 940373627 297 IHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 336
Cdd:PHA02740 248 FDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAY 287

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: 65.06 E-value: 7.95e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 511 FLVTFKQPLARQEEQVRMVRQFhfhgwpEVG-----IPAEGKGMIDLIaavqkQQQQTGNHPITVHCSAGAGRTGTFIAL 585
Cdd:cd14494    8 RLIAGALPLSPLEADSRFLKQL------GVTtivdlTLAMVDRFLEVL-----DQAEKPGEPVLVHCKAGVGRTGTLVAC 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 940373627 586 snileRVKAEGLLDVFQAVKSLRLQRPH-MVQTLEQYEFCYK 626
Cdd:cd14494   77 -----YLVLLGGMSAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113

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: 65.50 E-value: 7.26e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 438 FMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWptEGSVTHGDITI---EIKSDTLSEAISVRDFLVT 514
Cdd:cd14559   31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF--RQSGTYGSVTVkskKTGKDELVDGLKADMYNLK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 515 FkqplaRQEEQVRMVRQFHFHGWPEVG-IPAEG-KGMIDLIAAVQKQQ----QQTGNHPIT--------VHCSAGAGRTG 580
Cdd:cd14559  109 I-----TDGNKTITIPVVHVTNWPDHTaISSEGlKELADLVNKSAEEKrnfyKSKGSSAINdknkllpvIHCRAGVGRTG 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 940373627 581 TFIAlsnILERVKAEGLLDVFQAVKSLRLQR-PHMVQTLEQYE 622
Cdd:cd14559  184 QLAA---AMELNKSPNNLSVEDIVSDMRTSRnGKMVQKDEQLD 223

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 62.30 E-value: 1.62e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 222 HPQLPDSCKAPRLVSqLHFTsWPDFGVPfTPIGMLKFLKKVKTLNPSHaGPIVVHCSAGVGRTGTFIvidAMMDMihsEQ 301
Cdd:COG2453   36 EELLLGLLEEAGLEY-LHLP-IPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVA---AAYLV---LL 105

                         90       100       110
                 ....*....|....*....|....*....|
gi 940373627 302 KVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:COG2453  106 GLSAEEALARVRAARPGAVETPAQRAFLER 135

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: 57.74 E-value: 3.45e-10

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940373627 255 MLKFLKKVKTLnPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSeqkvdVFEFVSRIRNQRPQ-MVQTDVQYTFIYQ 331
Cdd:cd14494   42 VDRFLEVLDQA-EKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRPGgIPQTIEQLDFLIK 113

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: 55.05 E-value: 1.94e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 242 SWPDFGVPfTPIGMLKFLKkVKTLNPSHAGPIVVHCSAGVGRTGtfIVIDAMMDMIHSEQKVDVFEFVsriRNQRPQMVQ 321
Cdd:cd14506   83 GWKDYGVP-SLTTILDIVK-VMAFALQEGGKVAVHCHAGLGRTG--VLIACYLVYALRMSADQAIRLV---RSKRPNSIQ 155


                 ....*...
gi 940373627 322 TDVQYTFI 329
Cdd:cd14506  156 TRGQVLCV 163

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.

Pssm-ID: 350356 [Multi-domain] Cd Length: 206 Bit Score: 53.12 E-value: 7.94e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 518 PLARQEEQVRmvrqFHFHGWPEVGIPAEGKgMIDLIAAVQKQQQQTGNhpITVHCSAGAGRTGTFIALSNI-LERVKAEg 596
Cdd:cd14506   69 PEAFMRAGIY----FYNFGWKDYGVPSLTT-ILDIVKVMAFALQEGGK--VAVHCHAGLGRTGVLIACYLVyALRMSAD- 140

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 940373627 597 lldvfQAVKSLRLQRPHMVQTLEQYEFcykvVQDF 631
Cdd:cd14506  141 -----QAIRLVRSKRPNSIQTRGQVLC----VREF 166

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 50.74 E-value: 1.63e-07

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940373627 549 MIDLIAAVQKQQQQtgNHPITVHCSAGAGRTGTFIALSNILERVKAEglldvfQAVKSLRLQRPHMVQTLEQYEF 623
Cdd:COG2453   66 LQEAVDFIDEALRE--GKKVLVHCRGGIGRTGTVAAAYLVLLGLSAE------EALARVRAARPGAVETPAQRAF 132

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.

Pssm-ID: 350354 [Multi-domain] Cd Length: 142 Bit Score: 48.43 E-value: 9.70e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 940373627 565 NHPITVHCSAGAGRTGTFIALSNILERvKAEGLldvfQAVKSLRLQRPHMVQTLEQYEF 623
Cdd:cd14504   82 NEAVLVHCLAGKGRTGTMLACYLVKTG-KISAV----DAINEIRRIRPGSIETSEQEKF 135

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.

Pssm-ID: 350354 [Multi-domain] Cd Length: 142 Bit Score: 46.89 E-value: 3.72e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 237 QLHFTSWPDFGVP-FTPIG-MLKFLKKVKTLNpshaGPIVVHCSAGVGRTGTFIVIDAMMdmihsEQKVDVFEFVSRIRN 314
Cdd:cd14504   51 RYHHIPIEDYTPPtLEQIDeFLDIVEEANAKN----EAVLVHCLAGKGRTGTMLACYLVK-----TGKISAVDAINEIRR 121

                         90
                 ....*....|....*..
gi 940373627 315 QRPQMVQTDVQYTFIYQ 331
Cdd:cd14504  122 IRPGSIETSEQEKFVIQ 138

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: 46.87 E-value: 5.61e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 205 VEDCVVLV-DYTIRKFCIhPQLPDSCKAPRLvSQLHFtSWPDFGVPfTPIG----MLKFLKKVKtlnpSHAGPIVVHCSA 279
Cdd:cd14505   44 VDDVVTLCtDGELEELGV-PDLLEQYQQAGI-TWHHL-PIPDGGVP-SDIAqwqeLLEELLSAL----ENGKKVLIHCKG 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 940373627 280 GVGRTGTfiVIDAMMDMIHseQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 331
Cdd:cd14505  116 GLGRTGL--IAACLLLELG--DTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163

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: 46.10 E-value: 1.14e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627 570 VHCSAGAGRTGTfIALSNILERvkaEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 626
Cdd:cd14505  111 IHCKGGLGRTGL-IAACLLLEL---GDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.

Pssm-ID: 350349 [Multi-domain] Cd Length: 174 Bit Score: 43.21 E-value: 1.14e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940373627 238 LHFtswPDFGVPFTPIgMLKFLKKVKtlnpSHAGPIVVHCSAGVGRTGTFI 288
Cdd:cd14499   85 LYF---PDGSTPSDDI-VKKFLDICE----NEKGAIAVHCKAGLGRTGTLI 127

type III secretion system effector GTPase-activating protein SptP;

Pssm-ID: 185273 [Multi-domain] Cd Length: 535 Bit Score: 44.02 E-value: 2.49e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 113 NDHCRVILSqvDGIPCSdyINASYIDGykeKNKFIAAQGPKQ--ETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYW 190
Cdd:PRK15375 310 NQQTQVKLS--DGMPVP--VNTLTFDG---KPVALAGSYPKNtpDALEAHMKMLLEKECSCLVVLTSEDQMQAKQLPPYF 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 191 pdQGCWTYGNIRVCVEDCVVLVDY-TIRKFCIHPqlpdSCKAPRL-VSQLHFTSWPDFGvPFTPIGMLKFL-KKVKTLNP 267
Cdd:PRK15375 383 --RGSYTFGEVHTNSQKVSSASQGeAIDQYNMQL----SCGEKRYtIPVLHVKNWPDHQ-PLPSTDQLEYLaDRVKNSNQ 455

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 940373627 268 SHAG---------PIVvHCSAGVGRTGTFIVIDAMMDMIHS 299
Cdd:PRK15375 456 NGAPgrsssdkhlPMI-HCLGGVGRTGTMAAALVLKDNPHS 495

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

Pssm-ID: 395632 [Multi-domain] Cd Length: 127 Bit Score: 41.09 E-value: 3.08e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627  257 KFLKKVKTLNpshaGPIVVHCSAGVGRTGTfIVIDAMMDmihsEQKVDVFEFVSRIRNQRPQMVQTDvqyTFIYQaLLEY 336
Cdd:pfam00782  60 EFIDDARQKG----GKVLVHCQAGISRSAT-LIIAYLMK----TRNLSLNEAYSFVKERRPGISPNF---GFKRQ-LLEY 126


                  .
gi 940373627  337 Y 337
Cdd:pfam00782 127 E 127

Dual specificity phosphatase, catalytic domain;

Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 37.65 E-value: 4.70e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940373627   271 GPIVVHCSAGVGRTGTFIVidAMMDMIHSEQKVDVFEFVsriRNQRPQMVQTDvqyTFIYQaLLEYY 337
Cdd:smart00195  79 GKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFV---KDRRPIISPNF---GFLRQ-LIEYE 136

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.

Pssm-ID: 350349 [Multi-domain] Cd Length: 174 Bit Score: 37.82 E-value: 6.92e-03

                         10        20
                 ....*....|....*....|.
gi 940373627 565 NHPITVHCSAGAGRTGTFIAL 585
Cdd:cd14499  109 KGAIAVHCKAGLGRTGTLIAC 129

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.

Pssm-ID: 464208 [Multi-domain] Cd Length: 157 Bit Score: 37.68 E-value: 6.92e-03

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 940373627  258 FLKKVKTlNPSHAgPIVVHCSAGVGRTGTFIVIDAMM 294
Cdd:pfam14566 122 LISIVKD-APEDT-ALVFNCQMGRGRTTTAMVIADLV 156

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.

Pssm-ID: 350345 Cd Length: 278 Bit Score: 38.89 E-value: 7.22e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940373627 257 KFLKKVKTLnPSHAGpIVVHCSAGVGRTGTFIVIDAMM--------DMIHSEQK----VDVFEFVSRIRN-------QRP 317
Cdd:cd14495  175 AFVAFYRSL-PADAW-LHFHCRAGKGRTTTFMVMYDMLknpkdvsfDDIIARQYliggNYLAYEVDKDKNwkrpyyeERA 252


                 ....*....
gi 940373627 318 QMVQTDVQY 326
Cdd:cd14495  253 QFLQKFYQY 261

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: 37.56 E-value: 7.88e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 940373627 243 WPDFGVPftPIGML-KFLKKVKT---LNPSHAgpIVVHCSAGVGRTGTFIV 289
Cdd:cd14497   68 FPDHHPP--PLGLLlEIVDDIDSwlsEDPNNV--AVVHCKAGKGRTGTVIC 114