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: 502.16 E-value: 2.08e-176

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 164 YPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKC 243
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 244 YQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLN 323
Cdd:cd14620   81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVN 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 198386315 324 PSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
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: 483.37 E-value: 5.68e-168

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 109 KKYFPIPVEHLEEEIRVRSADDCKRFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDY 188
Cdd:cd14621    3 RKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 189 INASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVL 268
Cdd:cd14621   83 INASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 269 VDYTIRKFCIHPQLPDSCKAP-RLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVI 347
Cdd:cd14621  163 VDYTVRKFCIQQVGDVTNKKPqRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVI 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 198386315 348 DAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYYLYGDTEL 401
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: 1.37e-153

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 479 DYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDT 558
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 559 LSEAISIRDFLVTFKQplarqEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGT 638
Cdd:cd14622   81 LLETISIRDFLVTYNQ-----EKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGT 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 198386315 639 FIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDF 688
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: 1.80e-149

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTL 559
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 560 SEAISIRDFLVTFKQPlarqeEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGTF 639
Cdd:cd14552   81 YEDYTLRDFLVTKGKG-----GSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTF 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 198386315 640 IALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQ 686
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: 408.53 E-value: 3.50e-140

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 267
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCIHPQLPDS-CKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIV 346
Cdd:cd14551   81 LVDYTTRKFCIQKVNRGIgEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 198386315 347 IDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
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: 9.52e-138

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 455 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 534
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 535 CYQYWPTEGSVTHGDITIEIKSDTLSEAISIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQ 614
Cdd:cd14623   81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVT-----NTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQ 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 198386315 615 KQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQD 687
Cdd:cd14623  156 KQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 365.83 E-value: 1.23e-122

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315   134 FREEFNSLPSGHIQ-GTFELANKEENREKNRYPNILPNDHCRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQE 212
Cdd:smart00194   2 LEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315   213 TVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG--CWTYGNIRVCVEDCVVLVDYTIRKFCIHPqlpDSCKAPR 290
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTN---TGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315   291 LVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIR 370
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|..
gi 198386315   371 NQRPQMVQTDVQYTFIYQALLE 392
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: 344.77 E-value: 1.01e-114

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 156 EENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNL 235
Cdd:cd14553    1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 236 KERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKF 315
Cdd:cd14553   81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN---GSSEKREVRQFQFTAWPDHGVPEHPTPFLAF 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 316 LKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14553  158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 329.20 E-value: 7.44e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315  158 NREKNRYPNILPNDHCRVILSQLDGipCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKE 237
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315  238 RKEEKCYQYWPD--QGCWTYGNIRV-CVEDCVVLVDYTIRKFcihpQLPDSC-KAPRLVSQLHFTSWPDFGVPFTPIGML 313
Cdd:pfam00102  79 KGREKCAQYWPEeeGESLEYGDFTVtLKKEKEDEKDYTVRTL----EVSNGGsEETRTVKHFHYTGWPDHGVPESPNSLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315  314 KFLKKVKTL-NPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:pfam00102 155 DLLRKVRKSsLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 326.92 E-value: 1.53e-107

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315   424 GLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEfTDYINASFIDGYRQKDYFMATQGPLA 503
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315   504 HTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEG--SVTHGDITIEIKSDTLSEAISIRDFLVTFKqplarQEE 581
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNT-----GCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315   582 QVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAV 661
Cdd:smart00194 155 ETRTVTHYHYTNWPDHGVPESPESILDLIRAV-RKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                          250       260
                   ....*....|....*....|....*.
gi 198386315   662 KSLRLQRPHMVQTLEQYEFCYKVVQD 687
Cdd:smart00194 234 KELRSQRPGMVQTEEQYIFLYRAILE 259

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 319.19 E-value: 6.99e-105

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315  450 NMKKARVIQIIPYDFNRVILSMKRGQEftDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQE 529
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPS--DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315  530 REQDKCYQYWPT--EGSVTHGDITIEIK-SDTLSEAISIRDFLVTFKQplarqEEQVRMVRQFHFHGWPEVGIPTEGKGM 606
Cdd:pfam00102  79 KGREKCAQYWPEeeGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGG-----SEETRTVKHFHYTGWPDHGVPESPNSL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315  607 IDLIAAVQKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQ 686
Cdd:pfam00102 154 LDLLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233


                  .
gi 198386315  687 D 687
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: 315.82 E-value: 5.78e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 119 LEEEIRVRSADDCKRFREEFNSLPSGHiQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYK 198
Cdd:cd14626    3 LADNIERLKANDGLKFSQEYESIDPGQ-QFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 199 EKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCI 278
Cdd:cd14626   82 KQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 279 HpqlPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ 358
Cdd:cd14626  162 Y---KNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEK 238

                        250       260       270
                 ....*....|....*....|....*....|....
gi 198386315 359 KVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14626  239 TVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272

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: 304.83 E-value: 2.45e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 446 NLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLT 525
Cdd:cd14554    2 NLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 526 EVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEGKG 605
Cdd:cd14554   82 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVT-----DARDGQSRTVRQFQFTDWPEQGVPKSGEG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 198386315 606 MIDLIAAVQKQQQQTGNH-PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
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: 302.28 E-value: 7.64e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG--CWTYGNIRVCVEDC 265
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGgkPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 266 VVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFI 345
Cdd:cd00047   81 EELSDYTIRTLELSPK---GCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 198386315 346 VIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd00047  158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

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: 304.32 E-value: 1.79e-98

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 113 PIPVEHLEEEIRVRSADDCKRFREEFNSLPSGHiQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINAS 192
Cdd:cd14625    3 PIPISELAEHTERLKANDNLKLSQEYESIDPGQ-QFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 193 YIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYT 272
Cdd:cd14625   82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 273 IRKFCIHpqlPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMD 352
Cdd:cd14625  162 VRTFSLH---KNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 198386315 353 MIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14625  239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278

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: 299.65 E-value: 8.28e-98

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 267
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCI---HPQLPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTF 344
Cdd:cd14549   81 LATYTVRTFSLknlKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 198386315 345 IVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIY 387
Cdd:cd14549  161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

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: 301.65 E-value: 2.15e-97

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 113 PIPVEHLEEEIRVRSADDCKRFREEFNSLPSGHiQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINAS 192
Cdd:cd14624    3 PIPILELADHIERLKANDNLKFSQEYESIDPGQ-QFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 193 YIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYT 272
Cdd:cd14624   82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 273 IRKFCIHpqlPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMD 352
Cdd:cd14624  162 VRTFALY---KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLE 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 198386315 353 MIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYYLYGD 398
Cdd:cd14624  239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGN 284

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: 279.94 E-value: 2.44e-90

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGS--VTHGDITIEIKSD 557
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkpLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 558 TLSEAISIRDFLVTFKqplarQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTgNHPITVHCSAGAGRTG 637
Cdd:cd00047   81 EELSDYTIRTLELSPK-----GCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKP-NGPIVVHCSAGVGRTG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 198386315 638 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
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: 1.52e-89

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 163 RYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEK 242
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 243 CYQYWP-DQGCWTYGNIRVCVEDCVVLVDYTIRKFCIhpQLPDSCkapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKT 321
Cdd:cd14548   81 CDHYWPfDQDPVYYGDITVTMLSESVLPDWTIREFKL--ERGDEV---RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 322 LNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
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: 276.23 E-value: 1.74e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 398 DTELDVSSLERHLQTLHGTATHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEF 477
Cdd:cd14627    1 NTEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 478 TDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSD 557
Cdd:cd14627   81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 558 TLSEAISIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTG-NHPITVHCSAGAGRT 636
Cdd:cd14627  161 YNMPQYILREFKVT-----DARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVGRT 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 198386315 637 GTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 689
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: 273.92 E-value: 1.20e-86

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 399 TELDVSSLERHLQTLHGTATHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFT 478
Cdd:cd14628    1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 479 DYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDT 558
Cdd:cd14628   81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 559 LSEAISIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTG-NHPITVHCSAGAGRTG 637
Cdd:cd14628  161 NMPQYILREFKVT-----DARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVGRTG 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 198386315 638 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFIDIF 692
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: 271.21 E-value: 1.34e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 399 TELDVSSLERHLQTLHGTATHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFT 478
Cdd:cd14629    2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 479 DYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDT 558
Cdd:cd14629   82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 559 LSEAISIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTG-NHPITVHCSAGAGRTG 637
Cdd:cd14629  162 NMPQYILREFKVT-----DARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVGRTG 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 198386315 638 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFIDIF 692
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: 265.74 E-value: 3.01e-84

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 156 EENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNL 235
Cdd:cd14630    1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 236 KERKEEKCYQYWPDQgCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKF 315
Cdd:cd14630   81 VEVGRVKCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKK---GYHEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 316 LKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
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: 263.84 E-value: 3.91e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 148 GTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSA 227
Cdd:cd14543   19 GTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 228 TIVMLTNLKERKEEKCYQYWPDQG--CWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSckaPRLVSQLHFTSWPDFGV 305
Cdd:cd14543   99 VIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE---SRQVTHFQFTSWPDFGV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 306 PFTPIGMLKFLKKVK--------TLNPSHAG-----PIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQ 372
Cdd:cd14543  176 PSSAAALLDFLGEVRqqqalavkAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQ 255

                        250
                 ....*....|....*
gi 198386315 373 RPQMVQTDVQYTFIY 387
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: 256.50 E-value: 3.36e-80

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 134 FREEFNSLP--SGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPC--SDYINASYIDGYKEKNKFIAAQGP 209
Cdd:cd17667    1 FSEDFEEVQrcTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 210 KQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQL------- 282
Cdd:cd17667   81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkgqkg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 283 -PDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVD 361
Cdd:cd17667  161 nPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 198386315 362 VFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYYL 395
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: 254.58 E-value: 1.74e-79

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 134 FREEFNSLPSGHiQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQET 213
Cdd:cd14633   17 FKEEYESFFEGQ-SAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQET 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 214 VNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQgCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVS 293
Cdd:cd14633   96 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAVEKR---GVHEIREIR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 294 QLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQR 373
Cdd:cd14633  172 QFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRR 251

                        250
                 ....*....|....*....
gi 198386315 374 PQMVQTDVQYTFIYQALLE 392
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: 250.35 E-value: 1.20e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 455 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 534
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 535 CYQYWP-TEGSVTHGDITIEIKSDTLSEAISIRDFLVTfkqplarQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAV 613
Cdd:cd14548   81 CDHYWPfDQDPVYYGDITVTMLSESVLPDWTIREFKLE-------RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 614 QKQQQQtGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 680
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: 247.38 E-value: 4.31e-77

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 158 NREKNRYPNILPNDHCRVILSQLD-GIPCSDYINASYI------DGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATI 229
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDpNVPGSDYINANYIrnenegPTTDENAKtYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 230 VMLTNLKERKEEKCYQYWPDQG-CWTYGNIRV-CVEDCVVlVDYTIRKFCIHPQlpDSCKAPRLVSQLHFTSWPDFGVPF 307
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGmQKQYGPYRVqNVSEHDT-TDYTLRELQVSKL--DQGDPIREIWHYQYLSWPDHGVPS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 308 TPIGMLKFLKKVKTLNPS--HAGPIVVHCSAGVGRTGTFIVIDAMMDMIhSEQ----KVDVFEFVSRIRNQRPQMVQTDV 381
Cdd:cd14544  158 DPGGVLNFLEDVNQRQESlpHAGPIVVHCSAGIGRTGTFIVIDMLLDQI-KRKgldcDIDIQKTIQMVRSQRSGMVQTEA 236

                        250
                 ....*....|..
gi 198386315 382 QYTFIYQALLEY 393
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: 243.29 E-value: 4.10e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQgCWTYGNIRVCVEDCVV 267
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVI 347
Cdd:cd14555   80 LAEYVVRTFALERR---GYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 198386315 348 DAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
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: 241.50 E-value: 1.24e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 447 LPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTE 526
Cdd:cd14543   26 APANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 527 VQEREQDKCYQYWPTEG--SVTHGDITIEIKSDTLSEaisirDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGK 604
Cdd:cd14543  106 VVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKE-----HYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAA 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 605 GMIDLIAAVQKQQQQ---------TGNH---PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMV 672
Cdd:cd14543  181 ALLDFLGEVRQQQALavkamgdrwKGHPpgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSI 260

                        250
                 ....*....|.
gi 198386315 673 QTLEQYEFCYK 683
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: 239.02 E-value: 3.38e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 162 NRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE 241
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 242 KCYQYWP-DQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCKAPRlvsQLHFTSWPDFGVPFTPIGMLKFLKKVK 320
Cdd:cd14619   81 KCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVR---HFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198386315 321 TLNPSH--AGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
Cdd:cd14619  158 QWLDQTmsGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232

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: 238.96 E-value: 4.19e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 153 ANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVML 232
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 233 TNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCkapRLVSQLHFTSWPDFGVPFTPIGM 312
Cdd:cd14554   81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS---RTVRQFQFTDWPEQGVPKSGEGF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 313 LKFLKKV-KTLNP-SHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQAL 390
Cdd:cd14554  158 IDFIGQVhKTKEQfGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAA 237


                 .
gi 198386315 391 L 391
Cdd:cd14554  238 L 238

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: 238.18 E-value: 7.55e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 162 NRYPNILPNDHCRVILSQLdGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE 241
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQ-SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 242 KCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCI-HPQLPDSckapRLVSQLHFTSWPDFGVPFTP---IGMLKFLK 317
Cdd:cd14615   80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVkNAQTNES----RTVRHFHFTSWPDHGVPETTdllINFRHLVR 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198386315 318 KVKTLNPSHaGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14615  156 EYMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

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: 237.68 E-value: 1.30e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 448 PANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEV 527
Cdd:cd14553    1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 528 QEREQDKCYQYWPTEGSVTHGDITIeiksdTLSEAISIRDFLV-TFKqpLARQ-EEQVRMVRQFHFHGWPEVGIPTEGKG 605
Cdd:cd14553   81 EERSRVKCDQYWPTRGTETYGLIQV-----TLLDTVELATYTVrTFA--LHKNgSSEKREVRQFQFTAWPDHGVPEHPTP 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 606 MIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 682
Cdd:cd14553  154 FLAFLRRV-KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIH 229

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: 3.59e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 174 RVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQgCW 253
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 254 TYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVH 333
Cdd:cd14631   80 VYGDFKVTCVEMEPLAEYVVRTFTLERR---GYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 198386315 334 CSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
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: 234.61 E-value: 5.64e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDkCYQYWPTEGSVTHGDITIEIKSDTL 559
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDEGSGTYGPIQVEFVSTTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 560 SEAISIRDFLVtfkQPLARQEEQVRMVRQFHFHGWPEVG-IPTEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGT 638
Cdd:cd14556   80 DEDVISRIFRL---QNTTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 198386315 639 FIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 682
Cdd:cd14556  157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200

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: 233.95 E-value: 1.14e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWP--DQGCWTYGNIRVCVEDC 265
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 266 VVLVDYTIRKFCIHPQlpDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFI 345
Cdd:cd14557   81 KICPDYIIRKLNINNK--KEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 198386315 346 VIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd14557  159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

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: 234.60 E-value: 1.14e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 162 NRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKE 240
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 241 eKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIhpqlpDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVK 320
Cdd:cd14547   81 -KCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTL-----KYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 321 TL--NPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd14547  155 EArqTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

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: 1.23e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCwTYGNIRVCVEDCVV 267
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD-TYGDIKITLLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVI 347
Cdd:cd14632   80 LAEYSVRTFALERR---GYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 198386315 348 DAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14632  157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 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: 232.50 E-value: 8.58e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 162 NRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE 241
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 242 KCYQYWP-DQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVK 320
Cdd:cd14617   81 KCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSE--EQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 321 T-LNPS-HAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
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: 231.13 E-value: 1.33e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSvTHGDITIEIKSDTL 559
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK-TYGDIEVELKDTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 560 SEAISIRDFLVTFKQplaRQEEQVrmVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQ----QQTGNH-PITVHCSAGAG 634
Cdd:cd14558   80 SPTYTVRVFEITHLK---RKDSRT--VYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLpyknSKHGRSvPIVVHCSDGSS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 198386315 635 RTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 682
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: 227.54 E-value: 3.11e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 267
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCIHPQLPDSCkapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV-KTLNPSHAGPIVVHCSAGVGRTGTFIV 346
Cdd:cd14552   81 YEDYTLRDFLVTKGKGGST---RTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 198386315 347 IDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQAL 390
Cdd:cd14552  158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

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: 227.90 E-value: 4.80e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 459 IIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQY 538
Cdd:cd14620    4 ILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 539 WPTEGSVTHGDITIEIKSDTLSEAISIRDFLVTFKQPLARQEEqvRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVqKQQQ 618
Cdd:cd14620   84 WPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAP--RLVTQLHFTSWPDFGVPFTPIGMLKFLKKV-KSVN 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 619 QTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
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: 226.75 E-value: 9.26e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYID-GYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWT-YGNIRV-CVED 264
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGeYGDLTVeLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 265 CVV-LVDYTIRKFCI-HPQLPdsckaPRLVSQLHFTSWPDFGVPFTPIGMLK--FLKKVKTLNPSHAGPIVVHCSAGVGR 340
Cdd:cd18533   81 EENdDGGFIVREFELsKEDGK-----VKKVYHIQYKSWPDFGVPDSPEDLLTliKLKRELNDSASLDPPIIVHCSAGVGR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 341 TGTFIVIDAMMDMIHS--------EQKVD-VFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd18533  156 TGTFIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

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: 227.98 E-value: 1.14e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 157 ENREKNRYPNILPNDHCRVILSQLD-GIPCSDYINASYI--------DGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSA 227
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 228 TIVMLTNLKERKEEKCYQYWPDQGCWT-YGNIRVCVEDCVVLVDYTIRKFCIHPQlpDSCKAPRLVSQLHFTSWPDFGVP 306
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWPDEYALKeYGVMRVRNVKESAAHDYILRELKLSKV--GQGNTERTVWQYHFRTWPDHGVP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 307 FTPIGMLKFLKKV--KTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ---KVDVFEFVSRIRNQRPQMVQTDV 381
Cdd:cd14605  159 SDPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEA 238

                        250
                 ....*....|..
gi 198386315 382 QYTFIYQALLEY 393
Cdd:cd14605  239 QYRFIYMAVQHY 250

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: 227.01 E-value: 1.34e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 455 RVIQIIPYDFNRVILSMKrGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 534
Cdd:cd14615    2 RYNNVLPYDISRVKLSVQ-SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 535 CYQYWPTEGSVTHGDITIEIKSDTLSEAISIRDFLVTFKqplarQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAV- 613
Cdd:cd14615   81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNA-----QTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVr 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 198386315 614 QKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQD 687
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: 223.22 E-value: 1.09e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 155 KEENREKNRYPNILPNDHCRVILSQLD-GIPCSDYINASYID----GYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSAT 228
Cdd:cd14606   15 RPENKSKNRYKNILPFDHSRVILQGRDsNIPGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAWQENSRV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 229 IVMLTNLKERKEEKCYQYWPDQGCWT-YGniRVCVEDCVVL--VDYTIRKFCIHPqlPDSCKAPRLVSQLHFTSWPDFGV 305
Cdd:cd14606   95 IVMTTREVEKGRNKCVPYWPEVGMQRaYG--PYSVTNCGEHdtTEYKLRTLQVSP--LDNGELIREIWHYQYLSWPDHGV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 306 PFTPIGMLKFLKKVKTLNPS--HAGPIVVHCSAGVGRTGTFIVIDAMMDMIHS---EQKVDVFEFVSRIRNQRPQMVQTD 380
Cdd:cd14606  171 PSEPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRSGMVQTE 250

                        250
                 ....*....|...
gi 198386315 381 VQYTFIYQALLEY 393
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: 220.69 E-value: 1.25e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTL 559
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 560 SEAISIRDFLVT-FKQPLARQEEQVRMVRQFHFHGWPEVGIPTEgkgMIDLIAAVQKQQ--QQTGNHPITVHCSAGAGRT 636
Cdd:cd14549   81 LATYTVRTFSLKnLKLKKVKGRSSERVVYQYHYTQWPDHGVPDY---TLPVLSFVRKSSaaNPPGAGPIVVHCSAGVGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 198386315 637 GTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 682
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: 220.62 E-value: 1.42e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 267
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCI-HPQLPDSCK----APRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTG 342
Cdd:cd17668   81 LAYYTVRNFTLrNTKIKKGSQkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 198386315 343 TFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALL 391
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: 219.81 E-value: 5.85e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 162 NRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE 241
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 242 KCYQYWPDQGC-WTYGNIRVCVEDCVVLVDYTIRKFCI-HPQLpdscKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV 319
Cdd:cd14618   81 LCDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKLwHEDL----RKERRVKHLHYTAWPDHGIPESTSSLMAFRELV 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 198386315 320 K--TLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALL 391
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: 217.18 E-value: 2.62e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 187 DYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCV 266
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 267 VLVDYTIRKFCIHpqlPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV-KTLNPSHAGPIVVHCSAGVGRTGTFI 345
Cdd:cd14622   81 LLETISIRDFLVT---YNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 198386315 346 VIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
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: 215.14 E-value: 4.34e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 455 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 534
Cdd:cd14619    2 RFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 535 CYQYWPTEGS-VTHGDITIEIKSDTLSEAISIRDFLVtfkqpLARQEEQVRMVRQFHFHGWPEVGIPTEGKGMI---DLI 610
Cdd:cd14619   82 CEHYWPLDYTpCTYGHLRVTVVSEEVMENWTVREFLL-----KQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLafrRLL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 198386315 611 AAVQKQQQQTGnhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 689
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: 213.05 E-value: 1.80e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 118 HLEEEIRVRSADDCKRFREEFNSLPSGHIQGT-FELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDG 196
Cdd:cd14628   11 YIQKLTQIETGENVTGMELEFKRLASSKAHTSrFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 197 YKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKF 276
Cdd:cd14628   91 YRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 277 cihpQLPDSCKA-PRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDM 353
Cdd:cd14628  171 ----KVTDARDGqSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLER 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 198386315 354 IHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
Cdd:cd14628  247 MRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286

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: 209.54 E-value: 2.08e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYI--DGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPD---QGCWTYGNIRVCV 262
Cdd:cd14538    1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 263 EDCVVLVDYTIRKFCI-HPQLPDSckapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNpsHAGPIVVHCSAGVGRT 341
Cdd:cd14538   81 EKYQSLQDFVIRRISLrDKETGEV----HHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198386315 342 GTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14538  155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205

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: 2.55e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 455 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 534
Cdd:cd14618    2 RYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 535 CYQYWPTEGS-VTHGDITIEIKSDTLSEAISIRDFLVtfkQPLARQEEqvRMVRQFHFHGWPEVGIPTEGKGMIDLIAAV 613
Cdd:cd14618   82 CDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKL---WHEDLRKE--RRVKHLHYTAWPDHGIPESTSSLMAFRELV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198386315 614 QKQQQQT-GNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 680
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: 211.52 E-value: 6.52e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 137 EFNSLPSGHIQGT-FELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVN 215
Cdd:cd14627   31 EFKRLANSKAHTSrFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 216 DFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFcihpQLPDSCKA-PRLVSQ 294
Cdd:cd14627  111 DFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF----KVTDARDGqSRTVRQ 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 295 LHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQ 372
Cdd:cd14627  187 FQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 266

                        250       260
                 ....*....|....*....|.
gi 198386315 373 RPQMVQTDVQYTFIYQALLEY 393
Cdd:cd14627  267 RPAMVQTEDEYQFCYQAALEY 287

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: 208.97 E-value: 1.26e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 153 ANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVML 232
Cdd:cd14614    7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 233 TNLKERKEEKCYQYWP-DQGCWTYGNIRVCVEDCVVLVDYTIRKFCIhpqlpDSCKAPRLVSQLHFTSWPDFGVPFTPIG 311
Cdd:cd14614   87 TQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRV-----SYADEVQDVMHFNYTAWPDHGVPTANAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 312 --MLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQA 389
Cdd:cd14614  162 esILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQC 241


                 ..
gi 198386315 390 LL 391
Cdd:cd14614  242 VQ 243

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: 4.96e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 444 TGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVM 523
Cdd:cd14614    6 AADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 524 LTEVQEREQDKCYQYWP-TEGSVTHGDITIEIKSDTLSEAISIRDFLVTFKqplarqeEQVRMVRQFHFHGWPEVGIPTE 602
Cdd:cd14614   86 LTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA-------DEVQDVMHFNYTAWPDHGVPTA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 603 GKGMiDLIAAVQKQQQQTGNH--PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 680
Cdd:cd14614  159 NAAE-SILQFVQMVRQQAVKSkgPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                 ....*.
gi 198386315 681 CYKVVQ 686
Cdd:cd14614  238 IHQCVQ 243

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: 206.43 E-value: 7.30e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 163 RYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEK 242
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 243 CYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCKAPRlvsQLHFTSWPDFGVPFTPIGMLKFLKKV-KT 321
Cdd:cd14623   81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIR---QFHFHGWPEVGIPSDGKGMINIIAAVqKQ 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 198386315 322 LNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14623  158 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

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: 208.04 E-value: 1.04e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 118 HLEEEIRVRSADDCKRFREEFNSLPSGHIQGT-FELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDG 196
Cdd:cd14629   12 HIQKLTQVPPGESVTAMELEFKLLANSKAHTSrFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 197 YKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKF 276
Cdd:cd14629   92 YRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 277 cihpQLPDSCKA-PRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDM 353
Cdd:cd14629  172 ----KVTDARDGqSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGqdGPITVHCSAGVGRTGVFITLSIVLER 247

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 198386315 354 IHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
Cdd:cd14629  248 MRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287

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: 204.76 E-value: 1.18e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTL 559
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 560 SEAISIRDFLVtfkQPLAR--QEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTGNhPITVHCSAGAGRTG 637
Cdd:cd14551   81 LVDYTTRKFCI---QKVNRgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAG-PIVVHCSAGVGRTG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 198386315 638 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
Cdd:cd14551  157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

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: 204.94 E-value: 1.75e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 459 IIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKD-YFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQdKCYQ 537
Cdd:cd14547    6 ILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEkAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE-KCAQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 538 YWPTEGSVTHGDITIEIKSDTLSEAISIRDFLVtfkqplaRQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQ--- 614
Cdd:cd14547   85 YWPEEENETYGDFEVTVQSVKETDGYTVRKLTL-------KYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEear 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198386315 615 KQQQQTGnhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 680
Cdd:cd14547  158 QTEPHRG--PIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221

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: 206.43 E-value: 2.55e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 446 NLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLT 525
Cdd:cd14626   37 NLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMT 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 526 EVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISIRDFLVtFKQPLARQEEqvrmVRQFHFHGWPEVGIPTEGKG 605
Cdd:cd14626  117 RLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFAL-YKNGSSEKRE----VRQFQFMAWPDHGVPEYPTP 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 606 MIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14626  192 ILAFLRRV-KACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270

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: 6.54e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 187 DYINASYID----GYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG-CWTYGNIRVC 261
Cdd:cd14541    1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 262 VEDCVVLVDYTIRKFCI-HPQLPDSckapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGR 340
Cdd:cd14541   81 CVSEEVTPSFAFREFILtNTNTGEE----RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGR 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 198386315 341 TGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYY 394
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: 9.33e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 425 LEEEFRKLTNVRImKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAH 504
Cdd:cd14621   28 FREEFNALPACPI-QATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 505 TVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISIRDFLVTFKQPLARQEEQvR 584
Cdd:cd14621  107 TVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVTNKKPQ-R 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 585 MVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTGNhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSL 664
Cdd:cd14621  186 LITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAG-AIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRI 264

                        250       260
                 ....*....|....*....|.
gi 198386315 665 RLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14621  265 RAQRCQMVQTDMQYVFIYQAL 285

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: 202.48 E-value: 1.06e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFID-GYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEG-SVTHGDITIE-IKS 556
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEyEGEYGDLTVElVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 557 DTLSE-AISIRDFLVTfkqplaRQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQ-KQQQQTGNHPITVHCSAGAG 634
Cdd:cd18533   81 EENDDgGFIVREFELS------KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKReLNDSASLDPPIIVHCSAGVG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 635 RTGTFIAL--------SNILERVKAEGLLD-VFQAVKSLRLQRPHMVQTLEQYEFCY 682
Cdd:cd18533  155 RTGTFIALdslldelkRGLSDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLY 211

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: 202.83 E-value: 1.18e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 162 NRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE 241
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 242 KCYQYWPDQG--CWTYGNIRVC--VEDcvVLVDYTIRKFCIHPQlpDSCKaprLVSQLHFTSWPDFGVPFTPIGMLKFLK 317
Cdd:cd14616   81 RCHQYWPEDNkpVTVFGDIVITklMED--VQIDWTIRDLKIERH--GDYM---MVRQCNFTSWPEHGVPESSAPLIHFVK 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 198386315 318 KVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd14616  154 LVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

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: 200.92 E-value: 7.37e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 455 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 534
Cdd:cd14617    2 RYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 535 CYQYWPTE-GSVTHGDITIEIKSDTLSEAISIRDFLVTfkqplarQEEQV---RMVRQFHFHGWPEVGIPTEGKGMIDLI 610
Cdd:cd14617   82 CDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREFKIC-------SEEQLdapRLVRHFHYTVWPDHGVPETTQSLIQFV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 198386315 611 AAVQKQQQQT-GNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
Cdd:cd14617  155 RTVRDYINRTpGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

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: 202.57 E-value: 7.58e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 426 EEEFRKLTNVRIMKENmrtGNLPANMKKARVIQIIPYDFNRVILSMKRGQE--FTDYINASFIDGYRQKDYFMATQGPLA 503
Cdd:cd17667    6 EEVQRCTADMNITAEH---SNHPDNKHKNRYINILAYDHSRVKLRPLPGKDskHSDYINANYVDGYNKAKAYIATQGPLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 504 HTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISIRDFLV--------TFKQP 575
Cdd:cd17667   83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIrntkvkkgQKGNP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 576 LARQEEqvRMVRQFHFHGWPEVGIPTEGKGMIDLI-AAVQKQQQQTGnhPITVHCSAGAGRTGTFIALSNILERVKAEGL 654
Cdd:cd17667  163 KGRQNE--RTVIQYHYTQWPDMGVPEYALPVLTFVrRSSAARTPEMG--PVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 198386315 655 LDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 689
Cdd:cd17667  239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273

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: 201.02 E-value: 8.26e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 450 NMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQE 529
Cdd:cd14630    3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 530 REQDKCYQYWPTEGSVtHGDITIE-IKSDTLSEAIsIRDFLVTFKqplarQEEQVRMVRQFHFHGWPEVGIPTEGKGMID 608
Cdd:cd14630   83 VGRVKCVRYWPDDTEV-YGDIKVTlIETEPLAEYV-IRTFTVQKK-----GYHEIREIRQFHFTSWPDHGVPCYATGLLG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 609 LIAAVQKQQQQTGNhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14630  156 FVRQVKFLNPPDAG-PIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 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: 202.00 E-value: 1.18e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 153 ANKEENREKNRYPNILPNDHCRVILSQLDgipcsDYINASYID----GYKEKNKFIAAQGPKQETVNDFWRMVWEQRSAT 228
Cdd:cd14600   35 AKLPQNMDKNRYKDVLPYDATRVVLQGNE-----DYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 229 IVMLTNLKERKEEKCYQYWPD-QGCWTYGNIRVCV--EDCVVLvdYTIRKFCI-HPQLPDSckapRLVSQLHFTSWPDFG 304
Cdd:cd14600  110 IVMLTTLTERGRTKCHQYWPDpPDVMEYGGFRVQChsEDCTIA--YVFREMLLtNTQTGEE----RTVTHLQYVAWPDHG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 305 VPFTPIGMLKFLKKVKTLNPSHAgPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYT 384
Cdd:cd14600  184 VPDDSSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYK 262

                        250
                 ....*....|
gi 198386315 385 FIYQALLEYY 394
Cdd:cd14600  263 FVCEAILRVY 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: 198.78 E-value: 2.67e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 403 VSSLERHLQTLHGTathfDKIGLEEEFRKLTNVRimKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYIN 482
Cdd:cd14625    6 ISELAEHTERLKAN----DNLKLSQEYESIDPGQ--QFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYIN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 483 ASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIeiksdTLSEA 562
Cdd:cd14625   80 ANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQV-----TLLDT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 563 ISIRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGTFIAL 642
Cdd:cd14625  155 IELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRV-KTCNPPDAGPIVVHCSAGVGRTGCFIVI 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 198386315 643 SNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14625  234 DAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276

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: 196.97 E-value: 6.79e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 445 GNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVML 524
Cdd:cd14603   25 GGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 525 TEVQEREQDKCYQYWP-TEGSVTHGDITI-EIKSDTLSEAISIRDFLVTFKQplarqeeQVRMVRQFHFHGWPEVGIPTE 602
Cdd:cd14603  105 CREIEMGKKKCERYWAqEQEPLQTGPFTItLVKEKRLNEEVILRTLKVTFQK-------ESRSVSHFQYMAWPDHGIPDS 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 603 GKGMIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGTFIALSNI-----LERVKAEglLDVFQAVKSLRLQRPHMVQTLEQ 677
Cdd:cd14603  178 PDCMLAMIELA-RRLQGSGPEPLCVHCSAGCGRTGVICTVDYVrqlllTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQ 254


                 ....*...
gi 198386315 678 YEFCYKVV 685
Cdd:cd14603  255 YEFLYHTV 262

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: 196.88 E-value: 1.20e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 446 NLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLT 525
Cdd:cd14624   43 NLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 526 EVQEREQDKCYQYWPTEGSVTHGDITIeiksdTLSEAISIRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGKG 605
Cdd:cd14624  123 KLEERSRVKCDQYWPSRGTETYGLIQV-----TLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTP 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 606 MIDLIAAVQKQQQQTGNhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 682
Cdd:cd14624  198 FLAFLRRVKTCNPPDAG-PMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIH 273

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

Pssm-ID: 350406 [Multi-domain] Cd Length: 203 Bit Score: 193.38 E-value: 2.33e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCwTYGNIRVCVEDCVV 267
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK-TYGDIEVELKDTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCI-HPQLPDSckapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVK---TLNPSHAG---PIVVHCSAGVGR 340
Cdd:cd14558   80 SPTYTVRVFEItHLKRKDS----RTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklPYKNSKHGrsvPIVVHCSDGSSR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 198386315 341 TGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIY 387
Cdd:cd14558  156 TGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

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: 194.67 E-value: 2.89e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 161 KNRYPNILPNDHCRVIL----SQLDGipcSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATIVMLTNL 235
Cdd:cd14612   18 KDRYKTILPNPQSRVCLrragSQEEE---GSYINANYIRGYDGKEKaYIATQGPMLNTVSDFWEMVWQEECPIIVMITKL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 236 KERKEeKCYQYWPD-QGcwTYGNIRVCVEDCVVLVDYTIRKFCIhpQLPDSCkapRLVSQLHFTSWPDFGVPFTPIGMLK 314
Cdd:cd14612   95 KEKKE-KCVHYWPEkEG--TYGRFEIRVQDMKECDGYTIRDLTI--QLEEES---RSVKHYWFSSWPDHQTPESAGPLLR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 315 FLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14612  167 LVAEVEESRQTAAspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLAL 246


                 .
gi 198386315 393 Y 393
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: 194.70 E-value: 3.39e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 161 KNRYPNILPNDHCRVILSQLD-GIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKEr 238
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 239 KEEKCYQYWPDQGCwTYGNIRVCVEDCVVLVDYTIRKFCIHpqlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKK 318
Cdd:cd14613  107 MNEKCTEYWPEEQV-TYEGIEITVKQVIHADDYRLRLITLK-----SGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198386315 319 VKTLN---PSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
Cdd:cd14613  181 VEEARqqaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLSLY 258

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: 3.65e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 152 LANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKN-KFIAAQGPKQETVNDFWRMVWEQRSATIV 230
Cdd:cd14610   38 VAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCVVIV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 231 MLTNLKERKEEKCYQYWPDQGCWTYGNIRV-CVEDCVVLVDYTIRKFCIHPQLPDSCkapRLVSQLHFTSWPDFGVPFTP 309
Cdd:cd14610  118 MLTPLAENGVKQCYHYWPDEGSNLYHIYEVnLVSEHIWCEDFLVRSFYLKNLQTNET---RTVTQFHFLSWNDQGVPAST 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 310 IGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMD-MIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd14610  195 RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                 ....
gi 198386315 389 ALLE 392
Cdd:cd14610  275 AVAE 278

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: 193.76 E-value: 3.83e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 159 REKNRYPNILPNDHCRVILSQLDgipcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKER 238
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD----NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 239 KEEKCYQYWP----DQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLK 314
Cdd:cd14545   77 GQIKCAQYWPqgegNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENL---KTQETREVLHFHYTTWPDFGVPESPAAFLN 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 198386315 315 FLKKVK---TLNPSHaGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ--KVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd14545  154 FLQKVResgSLSSDV-GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231

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: 194.66 E-value: 4.47e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 149 TFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSAT 228
Cdd:cd14603   21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 229 IVMLTNLKERKEEKCYQYWP-DQGCWTYGNIRVC-VEDCVVLVDYTIRKFCIhpqlpDSCKAPRLVSQLHFTSWPDFGVP 306
Cdd:cd14603  101 ILMACREIEMGKKKCERYWAqEQEPLQTGPFTITlVKEKRLNEEVILRTLKV-----TFQKESRSVSHFQYMAWPDHGIP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 307 FTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ---KVDVFEFVSRIRNQRPQMVQTDVQY 383
Cdd:cd14603  176 DSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRippDFSIFDVVLEMRKQRPAAVQTEEQY 255

                        250
                 ....*....|.
gi 198386315 384 TFIYQALLEYY 394
Cdd:cd14603  256 EFLYHTVAQMF 266

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: 191.67 E-value: 1.09e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPtEGSVTHGDITIE-IKSDT 558
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTlVETEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 559 LSEAIsIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTGNhPITVHCSAGAGRTGT 638
Cdd:cd14555   80 LAEYV-VRTFALE-----RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAG-PIVVHCSAGAGRTGC 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 198386315 639 FIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
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: 1.60e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 151 ELANKEENREKNRYPNILPNDHCRVILSQldgiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIV 230
Cdd:cd14608   18 RVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 231 MLTNLKERKEEKCYQYWP----DQGCWTYGNIRVCVEDCVVLVDYTIRKFcihpQLPD-SCKAPRLVSQLHFTSWPDFGV 305
Cdd:cd14608   94 MLNRVMEKGSLKCAQYWPqkeeKEMIFEDTNLKLTLISEDIKSYYTVRQL----ELENlTTQETREILHFHYTTWPDFGV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 306 PFTPIGMLKFLKKVK---TLNPSHaGPIVVHCSAGVGRTGTFIVIDA---MMDMIHSEQKVDVFEFVSRIRNQRPQMVQT 379
Cdd:cd14608  170 PESPASFLNFLFKVResgSLSPEH-GPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQT 248

                        250       260
                 ....*....|....*....|....
gi 198386315 380 DVQYTFIYQALLE--YYLYGDTEL 401
Cdd:cd14608  249 ADQLRFSYLAVIEgaKFIMGDSSV 272

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: 189.16 E-value: 6.83e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKErKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 267
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDP-KDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCIHPQLPDSCKApRLVSQLHFTSWPDFG-VPFTPIGMLKFLKKV-KTLNPSHAGPIVVHCSAGVGRTGTFI 345
Cdd:cd14556   80 DEDVISRIFRLQNTTRPQEGY-RMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 198386315 346 VIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
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: 2.35e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 156 EENREKNRYPNILPNDHCRVILSQLDGipcsdYINASYID---GyKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVML 232
Cdd:cd14597    1 KENRKKNRYKNILPYDTTRVPLGDEGG-----YINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 233 TNLKERKEEKCYQYWPDQGCWTY---GNIRVCVEDCVVLVDYTIRkfciHPQLPD-SCKAPRLVSQLHFTSWPDFGVPFT 308
Cdd:cd14597   75 TQEVEGGKIKCQRYWPEILGKTTmvdNRLQLTLVRMQQLKNFVIR----VLELEDiQTREVRHITHLNFTAWPDHDTPSQ 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 309 PIGMLKFLKKVKTLNPShaGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd14597  151 PEQLLTFISYMRHIHKS--GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                 ...
gi 198386315 389 ALL 391
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: 187.18 E-value: 5.15e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEgSVTHGDITIE-IKSDT 558
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITlLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 559 LSEaISIRDFLVTFKQPLARQEeqvrmVRQFHFHGWPEVGIPTEGKGMIDLIAAVqKQQQQTGNHPITVHCSAGAGRTGT 638
Cdd:cd14632   80 LAE-YSVRTFALERRGYSARHE-----VKQFHFTSWPEHGVPYHATGLLAFIRRV-KASTPPDAGPVVVHCSAGAGRTGC 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 198386315 639 FIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14632  153 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199

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: 188.71 E-value: 1.11e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 118 HLEEEIRVRSaddckRFREEFNSLPSGHIQ-GTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINAS-YID 195
Cdd:cd14609    6 YMEDHLRNRD-----RLAKEWQALCAYQAEpNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 196 GYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRV-CVEDCVVLVDYTIR 274
Cdd:cd14609   81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVnLVSEHIWCEDFLVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 275 KFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMD-M 353
Cdd:cd14609  161 SFYLKNV---QTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrM 237

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 198386315 354 IHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14609  238 AKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276

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: 188.73 E-value: 1.29e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 403 VSSLERHLQtlhgtathfDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYIN 482
Cdd:cd14610    6 LSYMEDHLK---------NKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYIN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 483 ASFI-DGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSvthgDITIEIKSDTLSE 561
Cdd:cd14610   77 ASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGS----NLYHIYEVNLVSE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 562 AISIRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTgNHPITVHCSAGAGRTGTFIA 641
Cdd:cd14610  153 HIWCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRSGTYIL 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 198386315 642 LSNILERV-KAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFID 690
Cdd:cd14610  232 IDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVN 281

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: 1.37e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 450 NMKKARVIQIIPYDFNRVILSMKRGQE-FTDYINASFI----DGYRQKDY---FMATQGPLAHTVEDFWRMVWEWKSHTI 521
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVpGSDYINANYIrnenEGPTTDENaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 522 VMLTEVQEREQDKCYQYWPTEGSV-THGDITIEIKSDTLSEAISIRDFLVTfkqPLARQEEQvRMVRQFHFHGWPEVGIP 600
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQkQYGPYRVQNVSEHDTTDYTLRELQVS---KLDQGDPI-REIWHYQYLSWPDHGVP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 601 TEGKGMIDLIAAV-QKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLL---DVFQAVKSLRLQRPHMVQTLE 676
Cdd:cd14544  157 SDPGGVLNFLEDVnQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcdiDIQKTIQMVRSQRSGMVQTEA 236

                        250
                 ....*....|....
gi 198386315 677 QYEFCYKVVQDFID 690
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: 186.27 E-value: 1.65e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 455 RVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDK 534
Cdd:cd14616    2 RFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 535 CYQYWPTEGS--VTHGDITIEIKSDTLSEAISIRDFLVtfkqplaRQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAA 612
Cdd:cd14616   82 CHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKI-------ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 198386315 613 VQKQQQQTgNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
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: 184.84 E-value: 5.94e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 466 RVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSV 545
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 546 tHGDITIE-IKSDTLSEAIsIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVqKQQQQTGNHP 624
Cdd:cd14631   81 -YGDFKVTcVEMEPLAEYV-VRTFTLE-----RRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV-KLSNPPSAGP 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 198386315 625 ITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14631  153 IVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213

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: 186.40 E-value: 7.98e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 450 NMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQE 529
Cdd:cd14633   40 NRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 530 REQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAIsIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDL 609
Cdd:cd14633  120 VGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYV-IRTFAVE-----KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF 193

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198386315 610 IAAVQKQQQQTGNhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14633  194 VRQVKSKSPPNAG-PLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268

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: 186.01 E-value: 1.20e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 425 LEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINAS-FIDGYRQKDYFMATQGPLA 503
Cdd:cd14609   17 LAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPAYIATQGPLS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 504 HTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIksdtLSEAISIRDFLVTFKQPLARQEEQV 583
Cdd:cd14609   97 HTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNL----VSEHIWCEDFLVRSFYLKNVQTQET 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 584 RMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTgNHPITVHCSAGAGRTGTFIALSNILERVkAEGL--LDVFQAV 661
Cdd:cd14609  173 RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAATL 250

                        250       260
                 ....*....|....*....|....*....
gi 198386315 662 KSLRLQRPHMVQTLEQYEFCYKVVQDFID 690
Cdd:cd14609  251 EHVRDQRPGMVRTKDQFEFALTAVAEEVN 279

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: 186.29 E-value: 1.64e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 444 TGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVM 523
Cdd:cd14604   51 TGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVM 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 524 LTEVQEREQDKCYQYWPT--EGSVTHGDITIEIKSDTLSEAISIRDFLVTFKQplarqeeQVRMVRQFHFHGWPEVGIPT 601
Cdd:cd14604  131 ACREFEMGRKKCERYWPLygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQN-------ETRRLYQFHYVNWPDHDVPS 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 602 EGKGMIDLIAAVQKQQQQTgNHPITVHCSAGAGRTGTFIALS---NILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQY 678
Cdd:cd14604  204 SFDSILDMISLMRKYQEHE-DVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 282


                 ....*..
gi 198386315 679 EFCYKVV 685
Cdd:cd14604  283 ELVHRAI 289

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: 183.88 E-value: 2.43e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 446 NLPANMKKARVIQIIPYDFNRVILSMKRGQ-EFTDYINASFIDGY--RQKDYfMATQGPLAHTVEDFWRMVWEWKSHTIV 522
Cdd:cd14612   11 DIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYdgKEKAY-IATQGPMLNTVSDFWEMVWQEECPIIV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 523 MLTEVQEReQDKCYQYWPTEGSvTHGDITIEIKSDTLSEAISIRDFLVtfkqplaRQEEQVRMVRQFHFHGWPEVGIPTE 602
Cdd:cd14612   90 MITKLKEK-KEKCVHYWPEKEG-TYGRFEIRVQDMKECDGYTIRDLTI-------QLEEESRSVKHYWFSSWPDHQTPES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 603 GKGMIDLIAAVQKQQQQTGNH-PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFC 681
Cdd:cd14612  161 AGPLLRLVAEVEESRQTAASPgPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                 .
gi 198386315 682 Y 682
Cdd:cd14612  241 H 241

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: 181.33 E-value: 6.70e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTL 559
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 560 SEAISIRDFLV---TFKQPLARQEEQVRMVRQFHFHGWPEVGIPtegKGMIDLIAAVQK--QQQQTGNHPITVHCSAGAG 634
Cdd:cd17668   81 LAYYTVRNFTLrntKIKKGSQKGRPSGRVVTQYHYTQWPDMGVP---EYTLPVLTFVRKasYAKRHAVGPVVVHCSAGVG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 198386315 635 RTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 680
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: 181.37 E-value: 2.73e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 450 NMKKARVIQIIPYDFNRVILSMKRGQE-FTDYINASFI--------DGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHT 520
Cdd:cd14605    2 NKNKNRYKNILPFDHTRVVLHDGDPNEpVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 521 IVMLTEVQEREQDKCYQYWPTEGSVT-HGDITIEIKSDTLSEAISIRDflvtFKQPLARQEEQVRMVRQFHFHGWPEVGI 599
Cdd:cd14605   82 IVMTTKEVERGKSKCVKYWPDEYALKeYGVMRVRNVKESAAHDYILRE----LKLSKVGQGNTERTVWQYHFRTWPDHGV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 600 PTEGKGMIDLIAAVQ-KQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGL---LDVFQAVKSLRLQRPHMVQTL 675
Cdd:cd14605  158 PSDPGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTE 237

                        250
                 ....*....|....*
gi 198386315 676 EQYEFCYKVVQDFID 690
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: 179.96 E-value: 3.16e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYID---GYKEKnKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG----CWTYGNIRV 260
Cdd:cd14540    1 YINASHITatvGGKQR-FYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgehdALTFGEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 261 CVEDCVVLVDYTIRKFCIHPQLPDSckaPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV-------------KTLNPsha 327
Cdd:cd14540   80 STKFSVSSGCYTTTGLRVKHTLSGQ---SRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrhtnqdvagHNRNP--- 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198386315 328 gPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
Cdd:cd14540  154 -PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 182.43 E-value: 7.32e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 130 DCKRF-REEFNSLPSGHIQGTFELANKeeNREKNRYPNILPNDHCRVILSQLDGIpcSDYINASYIDGYKEKNKFIAAQG 208
Cdd:PHA02738  22 DCEEViTREHQKVISEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 209 PKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPD--QGCWTYGNIRVC---VEDCVVLVDYTIrkfcihpQLP 283
Cdd:PHA02738  98 PTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITttqVETHPHYVKSTL-------LLT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 284 DSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTL-------------NPSHAGPIVVHCSAGVGRTGTFIVIDAM 350
Cdd:PHA02738 171 DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDIS 250

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 198386315 351 MDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
Cdd:PHA02738 251 ISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRY 293

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: 7.62e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 161 KNRYPNILPNDHCRVILSQLDGI-PCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKEr 238
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNdSLSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 239 KEEKCYQYWPDQGCwTYGNIRV---CVEDCVvlvDYTIRKFCIHpqlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKF 315
Cdd:cd14611   81 KNEKCVLYWPEKRG-IYGKVEVlvnSVKECD---NYTIRNLTLK-----QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198386315 316 LKKVKT--LNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd14611  152 MLDVEEdrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

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: 178.02 E-value: 1.16e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRV-CVEDC 265
Cdd:cd14546    1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVhLVSEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 266 VVLVDYTIRKFCIHpQLPDSckAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFI 345
Cdd:cd14546   81 IWCDDYLVRSFYLK-NLQTS--ETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 198386315 346 VIDAMMD-MIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14546  158 LIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205

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: 178.02 E-value: 1.38e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFI--DGYRQKDYfMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIksd 557
Cdd:cd14546    1 YINASTIydHDPRNPAY-IATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHL--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 558 tLSEAISIRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTGNhPITVHCSAGAGRTG 637
Cdd:cd14546   77 -VSEHIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSC-PIVVHCSDGAGRTG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 198386315 638 TFIALSNILERV-KAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14546  155 TYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

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: 179.39 E-value: 1.51e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 150 FELANKEENREKNRYPNILPNDHCRVILSQLDgipcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATI 229
Cdd:cd14607   16 HRVAKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 230 VMLTNLKERKEEKCYQYWP--DQGCWTYGNIRVCV----EDcvVLVDYTIRKFcihpQLPD-SCKAPRLVSQLHFTSWPD 302
Cdd:cd14607   92 VMLNRIVEKDSVKCAQYWPtdEEEVLSFKETGFSVkllsED--VKSYYTVHLL----QLENiNSGETRTISHFHYTTWPD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 303 FGVPFTPIGMLKFLKKVK---TLNPSHaGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ--KVDVFEFVSRIRNQRPQMV 377
Cdd:cd14607  166 FGVPESPASFLNFLFKVResgSLSPEH-GPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244

                        250
                 ....*....|...
gi 198386315 378 QTDVQYTFIYQAL 390
Cdd:cd14607  245 QTPDQLRFSYMAV 257

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: 177.23 E-value: 1.86e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTH--GDITIE-IKS 556
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLqfGPFKISlEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 557 DTLSEAISIRDFLVTFKqplarQEEqvRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKqQQQTGNHPITVHCSAGAGRT 636
Cdd:cd14542   81 KRVGPDFLIRTLKVTFQ-----KES--RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRD-YQGSEDVPICVHCSAGCGRT 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 198386315 637 GTFIALS---NILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
Cdd:cd14542  153 GTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 180.99 E-value: 3.28e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 131 CKRFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSD-------------------YINA 191
Cdd:PHA02746  24 CEFVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAHESLKMFDvgdsdgkkievtsednaenYIHA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 192 SYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLkERKEEKCYQYW--PDQGCWTYGNIRVCVEDCVVLV 269
Cdd:PHA02746 104 NFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWtkEEDSELAFGRFVAKILDIIEEL 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 270 DYTIRKFCIHPQLPDSckaPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV--------KTL--NPSHAGPIVVHCSAGVG 339
Cdd:PHA02746 183 SFTKTRLMITDKISDT---SREIHHFWFPDWPDNGIPTGMAEFLELINKVneeqaeliKQAdnDPQTLGPIVVHCSAGIG 259

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198386315 340 RTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQAL 390
Cdd:PHA02746 260 RAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310

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: 174.24 E-value: 2.62e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPT--EGSVTHGDITIEIKSD 557
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 558 TLSEAISIRDFLVTFKqplaRQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQkQQQQTGNHPITVHCSAGAGRTG 637
Cdd:cd14557   81 KICPDYIIRKLNINNK----KEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN-AFNNFFSGPIVVHCSAGVGRTG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 198386315 638 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
Cdd:cd14557  156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

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: 174.05 E-value: 4.41e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 479 DYINASFID----GYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWP-TEGSVTHGDITIE 553
Cdd:cd14541    1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 554 IKSDTLSEAISIRDFLVTFKQPLarqEEqvRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVqKQQQQTGNHPITVHCSAGA 633
Cdd:cd14541   81 CVSEEVTPSFAFREFILTNTNTG---EE--RHITQMQYLAWPDHGVPDDSSDFLDFVKRV-RQNRVGMVEPTVVHCSAGI 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 198386315 634 GRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 680
Cdd:cd14541  155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201

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

Pssm-ID: 350444 [Multi-domain] Cd Length: 207 Bit Score: 173.39 E-value: 5.71e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGY--KEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPD--QGCWTYGNIRVCVE 263
Cdd:cd14596    1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 264 DCVVLVDYTIRKFCIhpqLPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPShaGPIVVHCSAGVGRTGT 343
Cdd:cd14596   81 NYQALQYFIIRIIKL---VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT--GPIVVHCSAGIGRAGV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 198386315 344 FIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
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: 172.61 E-value: 9.21e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG--CWTYGNIRV-CVED 264
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeeQLQFGPFKIsLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 265 CVVLVDYTIRKFCIHPQlpdscKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTF 344
Cdd:cd14542   81 KRVGPDFLIRTLKVTFQ-----KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTI 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 198386315 345 IVIDAMMDMIHSE---QKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd14542  156 CAIDYVWNLLKTGkipEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 176.35 E-value: 1.02e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 135 REEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETV 214
Cdd:PHA02747  28 RDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIDGFEDDKKFIATQGPFAETC 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 215 NDFWRMVWEQRSATIVMLTNLKERK-EEKCYQYW-PDQgcwtygNIRVCVEDCVV-LVDYTIRKFCIHPQLP---DSCKA 288
Cdd:PHA02747 107 ADFWKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWcLNE------DGNIDMEDFRIeTLKTSVRAKYILTLIEitdKILKD 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 289 PRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV--------KTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ 358
Cdd:PHA02747 181 SRKISHFQCSEWFEDETPSDHPDFIKFIKIIdinrkksgKLFNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRK 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 198386315 359 KVDVFEFVSRIRNQRPQMVQTDVQYTFIYQA--LLEYYLY 396
Cdd:PHA02747 261 AICLAKTAEKIREQRHAGIMNFDDYLFIQPGyeVLHYFLS 300

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: 174.67 E-value: 1.03e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 446 NLPANMKKARVIQIIPYDFNRVIL-SMKRGQEFTDYINASFIDGYRQKD-YFMATQGPLAHTVEDFWRMVWEWKSHTIVM 523
Cdd:cd14613   21 DIPGLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 524 LTEVQEREQdKCYQYWPTEgSVTHGDITIEIKSDTLSEAISIRdfLVTFKQplarqEEQVRMVRQFHFHGWPEVGIPTEG 603
Cdd:cd14613  101 ITNIEEMNE-KCTEYWPEE-QVTYEGIEITVKQVIHADDYRLR--LITLKS-----GGEERGLKHYWYTSWPDQKTPDNA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 604 KGMIDLIAAVQKQQQQTGNH--PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFC 681
Cdd:cd14613  172 PPLLQLVQEVEEARQQAEPNcgPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFV 251


                 ....
gi 198386315 682 YKVV 685
Cdd:cd14613  252 HHVL 255

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: 173.19 E-value: 8.89e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 155 KEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTN 234
Cdd:cd14604   54 KEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACR 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 235 LKERKEEKCYQYWPDQG--CWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdscKAPRLVSQLHFTSWPDFGVPFTPIGM 312
Cdd:cd14604  134 EFEMGRKKCERYWPLYGeePMTFGPFRISCEAEQARTDYFIRTLLLEFQ-----NETRRLYQFHYVNWPDHDVPSSFDSI 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 313 LKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHS---EQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQA 389
Cdd:cd14604  209 LDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRA 288


                 ....*
gi 198386315 390 LLEYY 394
Cdd:cd14604  289 IAQLF 293

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: 169.74 E-value: 1.36e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 187 DYINASYID----GYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPD-QGCWTYGNIRVC 261
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 262 VEDCVVLVDYTIRKFCIHPQlpdSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRT 341
Cdd:cd14601   81 CHSEEGNPAYVFREMTLTNL---EKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRT 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 198386315 342 GTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYY 394
Cdd:cd14601  158 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210

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: 169.70 E-value: 1.55e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEV-QEREQDKCYQYWPTEGSVTHGDITIEIKSDT 558
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLnQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 559 LSEAISIRDFLVtfkQPLARQEEQVRMVRQFHFHGW-PEVGIPTEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTG 637
Cdd:cd14637   81 ADEDIVTRLFRV---QNITRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 198386315 638 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14637  158 TYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205

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: 170.01 E-value: 2.19e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 450 NMKKARVIQIIPYDFNRVILsmkrGQEfTDYINASFIDGYRQKDYFM--ATQGPLAHTVEDFWRMVWEWKSHTIVMLTEV 527
Cdd:cd14597    3 NRKKNRYKNILPYDTTRVPL----GDE-GGYINASFIKMPVGDEEFVyiACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 528 QEREQDKCYQYWPTE-GSVTHGDITIEIksdTLSEAISIRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGKGM 606
Cdd:cd14597   78 VEGGKIKCQRYWPEIlGKTTMVDNRLQL---TLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 198386315 607 IDLIAAVqKQQQQTGnhPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14597  155 LTFISYM-RHIHKSG--PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230

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: 167.51 E-value: 7.23e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQdkCYQYWPTEGSVTHGDITIEIKSDTL 559
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL--CMQYWPEKTSCCYGPIQVEFVSADI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 560 SEAISIRDFLVTfkqPLARQEEQVRMVRQFHFHGWPEV-GIPTEGKGMIDLIAAVQKQQQQ--TGNHPITVHCSAGAGRT 636
Cdd:cd14634   79 DEDIISRIFRIC---NMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198386315 637 GTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQD 687
Cdd:cd14634  156 GTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

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: 168.34 E-value: 7.45e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 461 PYDFNRVILSMKRGQefTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWP 540
Cdd:cd14545    9 PYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKCAQYWP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 541 TEGS----VTHGDITIEIKSDTLSEAISIRDFLVTfkqPLARQEEqvRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQ 616
Cdd:cd14545   87 QGEGnamiFEDTGLKVTLLSEEDKSYYTVRTLELE---NLKTQET--REVLHFHYTTWPDFGVPESPAAFLNFLQKVRES 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 617 QQQTGNH-PITVHCSAGAGRTGTFIALSNILERVKAEGL--LDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
Cdd:cd14545  162 GSLSSDVgPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231

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: 167.18 E-value: 1.16e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQ-KDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTE--GSVTHGDITIEIKS 556
Cdd:cd14539    1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 557 DTLSEAISIRDFLVTFKqplarQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQK--QQQQTGNHPITVHCSAGAG 634
Cdd:cd14539   81 VRTTPTHVERIISIQHK-----DTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShyLQQRSLQTPIVVHCSSGVG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 198386315 635 RTGTFIALSNILERVKAE-GLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
Cdd:cd14539  156 RTGAFCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

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: 166.35 E-value: 2.45e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREqdKCYQYWPTEGSVTHGDITIEIKSDTL 559
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWPEEGMLRYGPIQVECMSCSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 560 SEAISIRDFLVTfkqPLARQEEQVRMVRQFHFHGWP-EVGIPTEGKGMIDLIAAVQKQQQQT--GNHPITVHCSAGAGRT 636
Cdd:cd14636   79 DCDVISRIFRIC---NLTRPQEGYLMVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEECdeGEGRTIIHCLNGGGRS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 198386315 637 GTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKV 684
Cdd:cd14636  156 GMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203

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: 165.63 E-value: 3.44e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYF--MATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWP---TEGSVTHGDITIEI 554
Cdd:cd14538    1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 555 KSDTLSEAISIRDFLVTFKQplarqEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQqTGnhPITVHCSAGAG 634
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKE-----TGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN-SG--PIVVHCSAGIG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198386315 635 RTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14538  153 RTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203

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: 168.10 E-value: 3.66e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 447 LPANMKKARVIQIIPYDFNRVILsmkrgQEFTDYINASFID----GYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIV 522
Cdd:cd14600   37 LPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 523 MLTEVQEREQDKCYQYWPTEGSV-THGDITIEIKSDTLSEAISIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPT 601
Cdd:cd14600  112 MLTTLTERGRTKCHQYWPDPPDVmEYGGFRVQCHSEDCTIAYVFREMLLT-----NTQTGEERTVTHLQYVAWPDHGVPD 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 602 EGKGMIDLIAAVQKQQQQtgNHPITVHCSAGAGRTGTFIALSN---ILERVKAEGLLDVfqaVKSLRLQRPHMVQTLEQY 678
Cdd:cd14600  187 DSSDFLEFVNYVRSKRVE--NEPVLVHCSAGIGRTGVLVTMETamcLTERNQPVYPLDI---VRKMRDQRAMMVQTSSQY 261


                 ..
gi 198386315 679 EF 680
Cdd:cd14600  262 KF 263

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: 165.40 E-value: 1.20e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 161 KNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKE 240
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 241 EKCYQYWPDQG--CWTYGNIRVCVEDCVVLVDYTIRKFCIHPQlpdscKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKK 318
Cdd:cd14602   81 KKCERYWAEPGemQLEFGPFSVTCEAEKRKSDYIIRTLKVKFN-----SETRTIYQFHYKNWPDHDVPSSIDPILELIWD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 319 VKTLNPSHAGPIVVHCSAGVGRTGTFIVID----AMMDMIHSEQkVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYY 394
Cdd:cd14602  156 VRCYQEDDSVPICIHCSAGCGRTGVICAIDytwmLLKDGIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234

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: 165.82 E-value: 1.98e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 431 KLTNVRimKENMRtgnlPANMKKARVIQIIPYDFNRVILSMKRGQ-EFTDYINASFI------DGYRQKDYfMATQGPLA 503
Cdd:cd14606    5 KNLHQR--LEGQR----PENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVknqllgPDENAKTY-IASQGCLE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 504 HTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVT-HGDITIEIKSDTLSEAISIRDFLVTfkqPLARQeEQ 582
Cdd:cd14606   78 ATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRaYGPYSVTNCGEHDTTEYKLRTLQVS---PLDNG-EL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 583 VRMVRQFHFHGWPEVGIPTEGKGMIDLIAAV-QKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGL---LDVF 658
Cdd:cd14606  154 IREIWHYQYLSWPDHGVPSEPGGVLSFLDQInQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQ 233

                        250       260       270
                 ....*....|....*....|....*....|..
gi 198386315 659 QAVKSLRLQRPHMVQTLEQYEFCYKVVQDFID 690
Cdd:cd14606  234 KTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIE 265

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 167.10 E-value: 2.15e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 450 NMKKARVIQIIPYDFNRVILSMKRGqeFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQE 529
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 530 REQDKCYQYWPTE--GSVTHGDITIEIKsdtlsEAISIRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGKGMI 607
Cdd:PHA02742 130 DGKEACYPYWMPHerGKATHGEFKIKTK-----KIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 608 DLIAAVQKQQQQT----------GNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQ 677
Cdd:PHA02742 205 DFVLAVREADLKAdvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQ 284

                        250
                 ....*....|....*..
gi 198386315 678 YEFCYKVVQDFIDIFSD 694
Cdd:PHA02742 285 YIFCYFIVLIFAKLMAD 301

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: 163.78 E-value: 2.51e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFID---GYRQKDYfMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGS----VTHGDITI 552
Cdd:cd14540    1 YINASHITatvGGKQRFY-IAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGehdaLTFGEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 553 EIKSDTLSEAISIRDFLVtfKQPLARQEeqvRMVRQFHFHGWPEVGIPTEGKGMIDLI--------AAVQKQQQQTGNHP 624
Cdd:cd14540   80 STKFSVSSGCYTTTGLRV--KHTLSGQS---RTVWHLQYTDWPDHGCPEDVSGFLDFLeeinsvrrHTNQDVAGHNRNPP 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198386315 625 ITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 689
Cdd:cd14540  155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219

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

Pssm-ID: 350459 [Multi-domain] Cd Length: 226 Bit Score: 163.94 E-value: 3.07e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 453 KARVIQIIPYDFNRVILSMKRGQEF-TDYINASFIDGYRQKD-YFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQER 530
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEkAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 531 EQdKCYQYWPTEGSVtHGDITIEIKSDTLSEAISIRDFLVtfkqplaRQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLI 610
Cdd:cd14611   82 NE-KCVLYWPEKRGI-YGKVEVLVNSVKECDNYTIRNLTL-------KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 198386315 611 AAVQKQQQQ-TGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCY 682
Cdd:cd14611  153 LDVEEDRLAsPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225

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: 163.86 E-value: 4.22e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 453 KARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQ 532
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 533 DKCYQYW--PTEGSVTHGDITIEIKSDTLSEAISIRDFLVTFkqplarqEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLI 610
Cdd:cd14602   81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKF-------NSETRTIYQFHYKNWPDHDVPSSIDPILELI 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 198386315 611 AAVqKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKaEGLL----DVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
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: 2.60e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQdkCYQYWPTEGSVTHGDITIEIKSDTL 559
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWPENGVHRHGPIQVEFVSADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 560 SEAISIRDFLVtfkQPLARQEEQVRMVRQFHFHGWPEV-GIPTEGKGMIDLIAAVQKQQQQ--TGNHPITVHCSAGAGRT 636
Cdd:cd14635   79 EEDIISRIFRI---YNAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 198386315 637 GTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKV 684
Cdd:cd14635  156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 162.86 E-value: 5.83e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 101 LSRSPSGPKKYfpipvEHLEEEIRVRSAddckrFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQL 180
Cdd:PHA02742   5 CSKKNSFAKNC-----EQLIEESNLAEI-----LKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 181 DGIpcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYW--PDQGCWTYGNI 258
Cdd:PHA02742  75 DGG--DDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmpHERGKATHGEF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 259 RVCVEDCVVLVDYTIRKFCihpqLPDSCKAPRL-VSQLHFTSWPDFGVPFTPIGMLKFLKKV-----------KTLNPSH 326
Cdd:PHA02742 153 KIKTKKIKSFRNYAVTNLC----LTDTNTGASLdIKHFAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVK 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 327 AGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
Cdd:PHA02742 229 EPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 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: 162.09 E-value: 7.88e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 137 EFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILsqldgIPCSD----YINASYIDGY--KEKNKFIAAQGPK 210
Cdd:cd14599   17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVEL-----VPTKEnntgYINASHIKVTvgGEEWHYIATQGPL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 211 QETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQG----CWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSc 286
Cdd:cd14599   92 PHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ- 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 287 kaPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTL----NPSHAG------PIVVHCSAGVGRTGTFIVIDAMMDMIHS 356
Cdd:cd14599  171 --ERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVrrhtNSMLDStkncnpPIVVHCSAGVGRTGVVILTELMIGCLEH 248

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 198386315 357 EQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
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: 158.25 E-value: 1.34e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREqdKCYQYWPTEG--------SVTHGDit 551
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEkplecetfKVTLSG-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 552 IEIKSDTLSEAISIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTegKGMIDLIAAVQKQQQQTgNHPITVHCSA 631
Cdd:cd14550   77 EDHSCLSNEIRLIVRDFILE-----STQDDYVLEVRQFQCPSWPNPCSPI--HTVFELINTVQEWAQQR-DGPIVVHDRY 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 198386315 632 GAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
Cdd:cd14550  149 GGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

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: 155.23 E-value: 2.59e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKN-KFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWP-DQG-CWTYGNIRVCVED 264
Cdd:cd14539    1 YINASLIEDLTPYCpRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPtERGqALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 265 CVVLVDYTIRKFCI--HPQlpdscKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKV----KTLNPSHAgPIVVHCSAGV 338
Cdd:cd14539   81 VRTTPTHVERIISIqhKDT-----RLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhshyLQQRSLQT-PIVVHCSSGV 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198386315 339 GRTGTF-IVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd14539  155 GRTGAFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

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: 2.95e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 444 TGNLPANMKKARVIQIIPYDFNRVILSMKRgQEFTDYINASFID-GYRQKDY-FMATQGPLAHTVEDFWRMVWEWKSHTI 521
Cdd:cd14599   32 TATLPENAERNRIREVVPYEENRVELVPTK-ENNTGYINASHIKvTVGGEEWhYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 522 VMLTEVQEREQDKCYQYWPTEG----SVTHGDITIEIKSDTLSEAISIRDFLVtfKQPLARQEeqvRMVRQFHFHGWPEV 597
Cdd:cd14599  111 AMVTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKV--KHLLSGQE---RTVWHLQYTDWPDH 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 598 GIPTEGKGMIDLIAAVQKQQQQTG---------NHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQR 668
Cdd:cd14599  186 GCPEEVQGFLSYLEEIQSVRRHTNsmldstkncNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQR 265

                        250       260
                 ....*....|....*....|.
gi 198386315 669 PHMVQTLEQYEFCYKVVQDFI 689
Cdd:cd14599  266 MFMIQTIAQYKFVYQVLIQFL 286

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 156.79 E-value: 4.85e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 157 ENREKNRYPNILPNDHCRVilsQLDGipcsDYINASYIDGyKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLK 236
Cdd:COG5599   41 NGSPLNRFRDIQPYKETAL---RANL----GYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 237 ERKE--EKCYQYWPDQGcwTYG--NIRVCVEDCVVLVD-YTIRKFCIhpQLPDSCKAPRLVSQLHFTSWPDFGVPFTPI- 310
Cdd:COG5599  113 EISKpkVKMPVYFRQDG--EYGkyEVSSELTESIQLRDgIEARTYVL--TIKGTGQKKIEIPVLHVKNWPDHGAISAEAl 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 311 -GMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMI--HSEQKVDVFEFVSRIRNQR-PQMVQTDVQYTFI 386
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: 153.00 E-value: 1.54e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYI--DGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKE-RKEEKCYQYWP--DQGCWTYGNIRV-- 260
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPaeENESREFGRISVtn 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 261 ----CVEDCVVLvdytiRKFCIHPQlpDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPShAGPIVVHCSA 336
Cdd:cd17658   81 kklkHSQHSITL-----RVLEVQYI--ESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPS-AGPIVVHCSA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 198386315 337 GVGRTGTFIVIDAMMDMI--HSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIY 387
Cdd:cd17658  153 GIGRTGAYCTIHNTIRRIleGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 154.80 E-value: 7.26e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 448 PANMKKARVIQIIPYDFNRVILSMK-------------RGQEFT------DYINASFIDGYRQKDYFMATQGPLAHTVED 508
Cdd:PHA02746  49 KENLKKNRFHDIPCWDHSRVVINAHeslkmfdvgdsdgKKIEVTsednaeNYIHANFVDGFKEANKFICAQGPKEDTSED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 509 FWRMVWEWKSHTIVMLTEVqEREQDKCYQYWPTE--GSVTHGDITIEIKsdtlsEAISIRDFLVTFKQPLARQEEQVRMV 586
Cdd:PHA02746 129 FFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEedSELAFGRFVAKIL-----DIIEELSFTKTRLMITDKISDTSREI 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 587 RQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQ---------QQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDV 657
Cdd:PHA02746 203 HHFWFPDWPDNGIPTGMAEFLELINKVNEEQaelikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCL 282

                        250       260
                 ....*....|....*....|....*....
gi 198386315 658 FQAVKSLRLQRPHMVQTLEQYEFCYKVVQ 686
Cdd:PHA02746 283 GEIVLKIRKQRHSSVFLPEQYAFCYKALK 311

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

Pssm-ID: 350496 [Multi-domain] Cd Length: 206 Bit Score: 150.31 E-value: 1.44e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDY--FMATQGPLAHTVEDFWRMVWEWKSHTIVMLTE-VQEREQDKCYQYWPTE--GSVTHGDITIEI 554
Cdd:cd17658    1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRlVDNYSTAKCADYFPAEenESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 555 KSDTLSE-AISIRDFLVTFKQplarQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVqkQQQQTGNHPITVHCSAGA 633
Cdd:cd17658   81 KKLKHSQhSITLRVLEVQYIE----SEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRL--YGIPPSAGPIVVHCSAGI 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198386315 634 GRTGTFIALSNILERVKAEGL--LDVFQAVKSLRLQRPHMVQTLEQYEFCY 682
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: 149.13 E-value: 3.24e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGY--RQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVThgdITIEIKSD 557
Cdd:cd14596    1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEP---MELENYQL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 558 TLSEAISIRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQqTGnhPITVHCSAGAGRTG 637
Cdd:cd14596   78 RLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHN-TG--PIVVHCSAGIGRAG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 198386315 638 TFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd14596  155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202

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: 144.42 E-value: 8.73e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315   292 VSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ-KVDVFEFVSR 368
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVKE 81

                           90       100
                   ....*....|....*....|....
gi 198386315   369 IRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:smart00012  82 LRSQRPGMVQTEEQYLFLYRALLE 105

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 144.42 E-value: 8.73e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315   292 VSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHA--GPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQ-KVDVFEFVSR 368
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVKE 81

                           90       100
                   ....*....|....*....|....
gi 198386315   369 IRNQRPQMVQTDVQYTFIYQALLE 392
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: 147.81 E-value: 1.62e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYID---GYKEKNkFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCW----TYGNIRV 260
Cdd:cd14598    1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 261 CVE-----DCVVLVDYTIRKFCIHPQlpdsckapRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVK--------TLNPSHA 327
Cdd:cd14598   80 TTRfrtdsGCYATTGLKIKHLLTGQE--------RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnsTIDPKSP 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 328 G-PIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
Cdd:cd14598  152 NpPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218

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: 147.04 E-value: 3.55e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFID---GYRQKDYfMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGS----VTHG--DI 550
Cdd:cd14598    1 YINASHIKvtvGGKEWDY-IATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSrhntVTYGrfKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 551 TIEIKSDTLSEAISirdfLVTFKQPLARQEeqvRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTG--------N 622
Cdd:cd14598   80 TTRFRTDSGCYATT----GLKIKHLLTGQE---RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNstidpkspN 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 623 HPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 689
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: 146.71 E-value: 1.94e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 443 RTGNLPANMKKARVIQIIPYDFNRVILSmkrgQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIV 522
Cdd:cd14608   18 RVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 523 MLTEVQEREQDKCYQYWP----TEGSVTHGDITIEIKSDTLSEAISIRDFLVtfkQPLARQEeqVRMVRQFHFHGWPEVG 598
Cdd:cd14608   94 MLNRVMEKGSLKCAQYWPqkeeKEMIFEDTNLKLTLISEDIKSYYTVRQLEL---ENLTTQE--TREILHFHYTTWPDFG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 599 IPTEGKGMIDLIAAVQKQQQQTGNH-PITVHCSAGAGRTGTFIALSN---ILERVKAEGLLDVFQAVKSLRLQRPHMVQT 674
Cdd:cd14608  169 VPESPASFLNFLFKVRESGSLSPEHgPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQT 248

                        250
                 ....*....|.
gi 198386315 675 LEQYEFCYKVV 685
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: 140.47 E-value: 4.89e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 479 DYINASFID----GYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWP-TEGSVTHGDITIE 553
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 554 IKSDTLSEAISIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVqKQQQQTGNHPITVHCSAGA 633
Cdd:cd14601   81 CHSEEGNPAYVFREMTLT-----NLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLV-RNKRAGKDEPVVVHCSAGI 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 198386315 634 GRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEF 680
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: 139.36 E-value: 1.05e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYqYWPTEGSVTHGD------ITIE 553
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCEtfkvtlIAEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 554 IKSDTLSEAISIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEgkGMIDLIAAVqKQQQQTGNHPITVHCSAGA 633
Cdd:cd17669   80 HKCLSNEEKLIIQDFILE-----ATQDDYVLEVRHFQCPKWPNPDSPIS--KTFELISII-KEEAANRDGPMIVHDEHGG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 198386315 634 GRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd17669  152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203

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: 135.18 E-value: 1.96e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315   585 MVRQFHFHGWPEVGIPTEGKGMIDLIAAVQK-QQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGL-LDVFQAVK 662
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKnLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 198386315   663 SLRLQRPHMVQTLEQYEFCYKVVQD 687
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 135.18 E-value: 1.96e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315   585 MVRQFHFHGWPEVGIPTEGKGMIDLIAAVQK-QQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGL-LDVFQAVK 662
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKnLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 198386315   663 SLRLQRPHMVQTLEQYEFCYKVVQD 687
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 140.06 E-value: 1.31e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 449 ANMKKARVIQIIPYDFNRVILSMKRGQefTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQ 528
Cdd:PHA02738  48 KNRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKK 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 529 EREQDKCYQYWPT--EGSVTHGDITIeiksdtlsEAISIRDFLVTFKQPLARQE--EQVRMVRQFHFHGWPEVGIPTEGK 604
Cdd:PHA02738 126 ENGREKCFPYWSDveQGSIRFGKFKI--------TTTQVETHPHYVKSTLLLTDgtSATQTVTHFNFTAWPDHDVPKNTS 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 605 GMIDLIAAVQKQQQ-------QTGNH-----PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMV 672
Cdd:PHA02738 198 EFLNFVLEVRQCQKelaqeslQIGHNrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSL 277

                        250
                 ....*....|....*....
gi 198386315 673 QTLEQYEFCYKVVQDFIDI 691
Cdd:PHA02738 278 FIPFQYFFCYRAVKRYVNL 296

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 138.30 E-value: 2.35e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 429 FRKLTNVR--IMKENM-------RTGNLPANMKKARVIQIIPYDFNRVilsmkrgQEFTDYINASFIDGYRQKDYfMATQ 499
Cdd:COG5599   12 EEEKINSRlsTLTNELapshndpQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNHRY-IATQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 500 GPLAHTVEDFWRMVWEWKSHTIVMLTEVQE--REQDKCYQYWPTEGSVTHGDITIE-IKSDTLSEAISIRDFLVTFKQpl 576
Cdd:COG5599   84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGEYGKYEVSSElTESIQLRDGIEARTYVLTIKG-- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 577 arQEEQVRMVRQFHFHGWPEVGIPTEG--KGMIDLIAAVQKQQQQTGNHPItVHCSAGAGRTGTFIALSNILERVKAEGL 654
Cdd:COG5599  162 --TGQKKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPV-VHCRAGVGRTGTLIACLALSKSINALVQ 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 198386315 655 --LDVFQAVKSLRLQR-PHMVQTLEQYEFCYKVVQDFIDI 691
Cdd:COG5599  239 itLSVEEIVIDMRTSRnGGMVQTSEQLDVLVKLAEQQIRP 278

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: 137.02 E-value: 3.43e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 443 RTGNLPANMKKARVIQIIPYDFNRVILSMKRgqefTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIV 522
Cdd:cd14607   17 RVAKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 523 MLTEVQEREQDKCYQYWPTEGS--VTHGDITIEIKsdTLSEAISiRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIP 600
Cdd:cd14607   93 MLNRIVEKDSVKCAQYWPTDEEevLSFKETGFSVK--LLSEDVK-SYYTVHLLQLENINSGETRTISHFHYTTWPDFGVP 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 601 TEGKGMIDLIAAVQKQQQQTGNH-PITVHCSAGAGRTGTFIALSN--ILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQ 677
Cdd:cd14607  170 ESPASFLNFLFKVRESGSLSPEHgPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQ 249


                 ....*...
gi 198386315 678 YEFCYKVV 685
Cdd:cd14607  250 LRFSYMAV 257

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 138.60 E-value: 3.80e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 448 PANMKKARVIQIIPYDFNRVILSMKRGQEfTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEV 527
Cdd:PHA02747  49 PENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 528 QERE-QDKCYQYW-PTE-GSVTHGDITIEiksdTLSeaISIR-DFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEG 603
Cdd:PHA02747 128 KGTNgEEKCYQYWcLNEdGNIDMEDFRIE----TLK--TSVRaKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDH 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 604 KGMIDLIAAVQKQQQQTGNH---------PITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQT 674
Cdd:PHA02747 202 PDFIKFIKIIDINRKKSGKLfnpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMN 281


                 ....*.
gi 198386315 675 LEQYEF 680
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: 6.57e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCyqYWPDQG----CWTYgNIRVCVE 263
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEkpleCETF-KVTLSGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 264 DCVVL---VDYTIRKFCIHPQLPDSCKAprlVSQLHFTSWPDfgvPFTPI-GMLKFLKKVKTLNPSHAGPIVVHCSAGVG 339
Cdd:cd14550   78 DHSCLsneIRLIVRDFILESTQDDYVLE---VRQFQCPSWPN---PCSPIhTVFELINTVQEWAQQRDGPIVVHDRYGGV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 198386315 340 RTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
Cdd:cd14550  152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

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: 133.27 E-value: 1.94e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 480 YINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKcYQYWPT-EGSVTHGDITIE-IKSD 557
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWPSrEESMNCEAFTVTlISKD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 558 TL----SEAISIRDFLVTfkqplARQEEQVRMVRQFHFHGWPEVGIPTEgkGMIDLIAAVqKQQQQTGNHPITVHCSAGA 633
Cdd:cd17670   80 RLclsnEEQIIIHDFILE-----ATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVI-KEEALTRDGPTIVHDEFGA 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 198386315 634 GRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVV 685
Cdd:cd17670  152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203

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: 2.32e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKerKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 267
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD--AAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCI----HPQlpdscKAPRLVSQLHFTSWPDFGVpfTPIGMLKFLKKVKTLNP------SHAGPIVVHCSAG 337
Cdd:cd14634   79 DEDIISRIFRIcnmaRPQ-----DGYRIVQHLQYIGWPAYRD--TPPSKRSILKVVRRLEKwqeqydGREGRTVVHCLNG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 198386315 338 VGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
Cdd:cd14634  152 GGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

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: 5.26e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKerKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 267
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVD--PAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCIH----PQlpdscKAPRLVSQLHFTSWPDF-GVPFTPIGMLKFLKKVKTLNPSH---AGPIVVHCSAGVG 339
Cdd:cd14635   79 EEDIISRIFRIYnaarPQ-----DGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYnggEGRTVVHCLNGGG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 198386315 340 RTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
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: 123.21 E-value: 6.50e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKerKEEKCYQYWPDQGCWTYGNIRVCVEDCVV 267
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVD--LAQGCPQYWPEEGMLRYGPIQVECMSCSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 268 LVDYTIRKFCI----HPQlpdscKAPRLVSQLHFTSWPDF-GVPFTPIGMLKFLKKVKTLNPS---HAGPIVVHCSAGVG 339
Cdd:cd14636   79 DCDVISRIFRIcnltRPQ-----EGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdeGEGRTIIHCLNGGG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 198386315 340 RTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
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: 3.64e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYqYWPDQ----GCWTYgNIRVCVE 263
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKdepiNCETF-KVTLIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 264 DCVVLVDYtiRKFCIHPQLPDSCKAPRLVSQLHFT--SWPDfgvPFTPIG-MLKFLKKVKTLNPSHAGPIVVHCSAGVGR 340
Cdd:cd17669   79 EHKCLSNE--EKLIIQDFILEATQDDYVLEVRHFQcpKWPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEHGGVT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 198386315 341 TGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQmVQTDV-QYTFIYQALL 391
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: 117.70 E-value: 5.54e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEE-KCYQYWPDQGCWTYGNIRVCVEDCV 266
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 267 VLVDYTIRKFCIHpQLPDSCKAPRLVSQLHFTSWPDF-GVPFTPIGMLKFLKKV-KTLNPSHAGPIVVHCSAGVGRTGTF 344
Cdd:cd14637   81 ADEDIVTRLFRVQ-NITRLQEGHLMVRHFQFLRWSAYrDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGGRSGTY 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 198386315 345 IVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLE 392
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: 4.13e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 188 YINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKcYQYWPDQ----GCWTYgNIRVCVE 263
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWPSReesmNCEAF-TVTLISK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 264 DCVVLVDYtiRKFCIHPQLPDSCKAPRLVSQLHFT--SWPDfgvPFTPI-GMLKFLKKVKTLNPSHAGPIVVHCSAGVGR 340
Cdd:cd17670   79 DRLCLSNE--EQIIIHDFILEATQDDYVLEVRHFQcpKWPN---PDAPIsSTFELINVIKEEALTRDGPTIVHDEFGAVS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 198386315 341 TGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQmVQTDV-QYTFIYQALL 391
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: 86.30 E-value: 6.17e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 166 NILPNDHCRVilSQLDGIPcsdyINASYIDgYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQ 245
Cdd:cd14559    1 NRFTNIQTRV--STPVGKN----LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 246 YWPDQGcwTYGNIRVCVEDcvVLVDYTIRKFCIHP---QLPDSCKaPRLVSQLHFTSWPDFGVpfTPIGMLKFL------ 316
Cdd:cd14559   74 YFRQSG--TYGSVTVKSKK--TGKDELVDGLKADMynlKITDGNK-TITIPVVHVTNWPDHTA--ISSEGLKELadlvnk 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 198386315 317 ---KKVKTLNPSHAGPI--------VVHCSAGVGRTGTFIvidAMMDMIHSEQKVDVFEFVSRIRNQR-PQMVQTDVQY 383
Cdd:cd14559  147 saeEKRNFYKSKGSSAIndknkllpVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRnGKMVQKDEQL 222

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 84.63 E-value: 8.48e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 481 INASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEReqdKCY-QYWPT-EGSV-THGDITIEiksd 557
Cdd:PHA02740  79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCFnQFWSLkEGCViTSDKFQIE---- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 558 TLsEAISIRDFLVTFKQpLARQEEQVRMVRQFHFHGWPEVGIPTEGKGMID-------LIAAVQKQQQQTGNHPITVHCS 630
Cdd:PHA02740 152 TL-EIIIKPHFNLTLLS-LTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDffcniddLCADLEKHKADGKIAPIIIDCI 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 198386315 631 AGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFI 689
Cdd:PHA02740 230 DGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYL 288

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 81.55 E-value: 9.56e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 125 VRSADDCKRFREEFNSLPSGHIQGTFELANKEENREKNRyPNILPndHCRVILSQLDGIPCSDYINASYIDGYKEKNKFI 204
Cdd:PHA02740  18 INKPDLLSCIIKEYRAIVPEHEDEANKACAQAENKAKDE-NLALH--ITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 205 AAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERkeeKCY-QYWP-DQGC-WTYGNIRVCVEDCVVLVDYTIRKFCihpq 281
Cdd:PHA02740  95 CIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCFnQFWSlKEGCvITSDKFQIETLEIIIKPHFNLTLLS---- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 282 LPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTL--------NPSHAGPIVVHCSAGVGRTGTFIVIDAMMDM 353
Cdd:PHA02740 168 LTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadlekhkADGKIAPIIIDCIDGISSSAVFCVFDICATE 247

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 198386315 354 IHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEY 393
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: 66.22 E-value: 4.46e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 568 FLVTFKQPLARQEEQVRMVRQFhfhgwpevGIPTegkgMIDLI-----AAVQK-QQQQTGNHPITVHCSAGAGRTGTFIA 641
Cdd:cd14494    8 RLIAGALPLSPLEADSRFLKQL--------GVTT----IVDLTlamvdRFLEVlDQAEKPGEPVLVHCKAGVGRTGTLVA 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 198386315 642 LsnileRVKAEGLLDVFQAVKSLRLQRPH-MVQTLEQYEFCYK 683
Cdd:cd14494   76 C-----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: 66.65 E-value: 2.99e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 495 FMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWptEGSVTHGDITI---EIKSDTLSEAISIRDFLVT 571
Cdd:cd14559   31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF--RQSGTYGSVTVkskKTGKDELVDGLKADMYNLK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 572 FkqplaRQEEQVRMVRQFHFHGWPEVG-IPTEG-KGMIDLIAAVQKQQ----QQTGNHPIT--------VHCSAGAGRTG 637
Cdd:cd14559  109 I-----TDGNKTITIPVVHVTNWPDHTaISSEGlKELADLVNKSAEEKrnfyKSKGSSAINdknkllpvIHCRAGVGRTG 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 198386315 638 TFIAlsnILERVKAEGLLDVFQAVKSLRLQR-PHMVQTLEQYE 679
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: 1.79e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 279 HPQLPDSCKAPRLVSqLHFTsWPDFGVPfTPIGMLKFLKKVKTLNPSHaGPIVVHCSAGVGRTGTFIvidAMMDMihsEQ 358
Cdd:COG2453   36 EELLLGLLEEAGLEY-LHLP-IPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVA---AAYLV---LL 105

                         90       100       110
                 ....*....|....*....|....*....|
gi 198386315 359 KVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
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: 58.13 E-value: 2.33e-10

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198386315 312 MLKFLKKVKTLnPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSeqkvdVFEFVSRIRNQRPQ-MVQTDVQYTFIYQ 388
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: 56.20 E-value: 7.83e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 299 SWPDFGVPfTPIGMLKFLKkVKTLNPSHAGPIVVHCSAGVGRTGtfIVIDAMMDMIHSEQKVDVFEFVsriRNQRPQMVQ 378
Cdd:cd14506   83 GWKDYGVP-SLTTILDIVK-VMAFALQEGGKVAVHCHAGLGRTG--VLIACYLVYALRMSADQAIRLV---RSKRPNSIQ 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 198386315 379 TDVQYTFIYQ------ALLEYYLYGDTELDVSS---LERHLQTLHG 415
Cdd:cd14506  156 TRGQVLCVREfaqfllPLRNVFACPDPKAAVTLrqyLIRQRHLLHG 201

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: 54.66 E-value: 3.03e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 575 PLARQEEQVRmvrqFHFHGWPEVGIPTEGKgMIDLIAAVQKQQQQTGNhpITVHCSAGAGRTGTFIALSNI-LERVKAEg 653
Cdd:cd14506   69 PEAFMRAGIY----FYNFGWKDYGVPSLTT-ILDIVKVMAFALQEGGK--VAVHCHAGLGRTGVLIACYLVyALRMSAD- 140

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 198386315 654 lldvfQAVKSLRLQRPHMVQTLEQYEFcykvVQDF 688
Cdd:cd14506  141 -----QAIRLVRSKRPNSIQTRGQVLC----VREF 166

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 51.12 E-value: 1.34e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 588 QFHFHGWPEVGIPTEgKGMIDLIAAVQKQQQQtgNHPITVHCSAGAGRTGTFIALSNILERVKAEglldvfQAVKSLRLQ 667
Cdd:COG2453   49 EYLHLPIPDFGAPDD-EQLQEAVDFIDEALRE--GKKVLVHCRGGIGRTGTVAAAYLVLLGLSAE------EALARVRAA 119

                         90
                 ....*....|...
gi 198386315 668 RPHMVQTLEQYEF 680
Cdd:COG2453  120 RPGAVETPAQRAF 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: 48.81 E-value: 1.02e-06

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 198386315 622 NHPITVHCSAGAGRTGTFIALSNILERvKAEGLldvfQAVKSLRLQRPHMVQTLEQYEF 680
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: 3.76e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 294 QLHFTSWPDFGVP-FTPIG-MLKFLKKVKTLNpshaGPIVVHCSAGVGRTGTFIVIDAMMdmihsEQKVDVFEFVSRIRN 371
Cdd:cd14504   51 RYHHIPIEDYTPPtLEQIDeFLDIVEEANAKN----EAVLVHCLAGKGRTGTMLACYLVK-----TGKISAVDAINEIRR 121

                         90
                 ....*....|....*..
gi 198386315 372 QRPQMVQTDVQYTFIYQ 388
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: 6.20e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 262 VEDCVVLV-DYTIRKFCIhPQLPDSCKAPRLvSQLHFtSWPDFGVPfTPIG----MLKFLKKVKtlnpSHAGPIVVHCSA 336
Cdd:cd14505   44 VDDVVTLCtDGELEELGV-PDLLEQYQQAGI-TWHHL-PIPDGGVP-SDIAqwqeLLEELLSAL----ENGKKVLIHCKG 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 198386315 337 GVGRTGTfiVIDAMMDMIHseQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQ 388
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: 1.26e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315 627 VHCSAGAGRTGTfIALSNILERvkaEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYK 683
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: 1.25e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198386315 295 LHFtswPDFGVPFTPIgMLKFLKKVKtlnpSHAGPIVVHCSAGVGRTGTFI 345
Cdd:cd14499   85 LYF---PDGSTPSDDI-VKKFLDICE----NEKGAIAVHCKAGLGRTGTLI 127

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: 41.48 E-value: 2.24e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315  314 KFLKKVKTLNpshaGPIVVHCSAGVGRTGTfIVIDAMMDmihsEQKVDVFEFVSRIRNQRPQMVQTDvqyTFIYQaLLEY 393
Cdd:pfam00782  60 EFIDDARQKG----GKVLVHCQAGISRSAT-LIIAYLMK----TRNLSLNEAYSFVKERRPGISPNF---GFKRQ-LLEY 126


                  .
gi 198386315  394 Y 394
Cdd:pfam00782 127 E 127

type III secretion system effector GTPase-activating protein SptP;

Pssm-ID: 185273 [Multi-domain] Cd Length: 535 Bit Score: 44.02 E-value: 2.79e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 170 NDHCRVILSqlDGIPCSdyINASYIDGykeKNKFIAAQGPKQ--ETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYW 247
Cdd:PRK15375 310 NQQTQVKLS--DGMPVP--VNTLTFDG---KPVALAGSYPKNtpDALEAHMKMLLEKECSCLVVLTSEDQMQAKQLPPYF 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 248 pdQGCWTYGNIRVCVEDCVVLVDY-TIRKFCIHPqlpdSCKAPRL-VSQLHFTSWPDFGvPFTPIGMLKFL-KKVKTLNP 324
Cdd:PRK15375 383 --RGSYTFGEVHTNSQKVSSASQGeAIDQYNMQL----SCGEKRYtIPVLHVKNWPDHQ-PLPSTDQLEYLaDRVKNSNQ 455

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 198386315 325 SHAG---------PIVvHCSAGVGRTGTFIVIDAMMDMIHS 356
Cdd:PRK15375 456 NGAPgrsssdkhlPMI-HCLGGVGRTGTMAAALVLKDNPHS 495

Dual specificity phosphatase, catalytic domain;

Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 38.42 E-value: 3.63e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198386315   328 GPIVVHCSAGVGRTGTFIVidAMMDMIHSEQKVDVFEFVsriRNQRPQMVQTDvqyTFIYQaLLEYY 394
Cdd:smart00195  79 GKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFV---KDRRPIISPNF---GFLRQ-LIEYE 136

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: 6.94e-03

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 198386315  315 FLKKVKTlNPSHAgPIVVHCSAGVGRTGTFIVIDAMM 351
Cdd:pfam14566 122 LISIVKD-APEDT-ALVFNCQMGRGRTTTAMVIADLV 156

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: 37.94 E-value: 6.99e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198386315 300 WPDFGVPftPIGML-KFLKKVKT---LNPSHAgpIVVHCSAGVGRTGTFIV 346
Cdd:cd14497   68 FPDHHPP--PLGLLlEIVDDIDSwlsEDPNNV--AVVHCKAGKGRTGTVIC 114

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: 7.02e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198386315 314 KFLKKVKTLnPSHAGpIVVHCSAGVGRTGTFIVIDAMM--------DMIHSEQK----VDVFEFVSRIRN-------QRP 374
Cdd:cd14495  175 AFVAFYRSL-PADAW-LHFHCRAGKGRTTTFMVMYDMLknpkdvsfDDIIARQYliggNYLAYEVDKDKNwkrpyyeERA 252


                 ....*....
gi 198386315 375 QMVQTDVQY 383
Cdd:cd14495  253 QFLQKFYQY 261

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: 7.64e-03

                         10        20
                 ....*....|....*....|.
gi 198386315 622 NHPITVHCSAGAGRTGTFIAL 642
Cdd:cd14499  109 KGAIAVHCKAGLGRTGTLIAC 129