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: 413.95 E-value: 4.23e-142

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14620    32 DGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIR 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQASDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14620   112 KFCIQPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMM 191

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14620   192 HAEQKVDVFE-FVSRIRNQRPQMVQTDMQYSFIYQALLE 229

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: 401.69 E-value: 1.07e-137

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 416 DYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAET 495
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 496 QCDdTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSGNHPIVVHCSAGAGRTGTFIAL 575
Cdd:cd14622    81 LLE-TISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1709608747 576 SNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTL 192

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: 383.93 E-value: 7.42e-131

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAETQ 496
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 497 CDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSGNHPIVVHCSAGAGRTGTFIALS 576
Cdd:cd14552    81 YED-YTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALS 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1709608747 577 NILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14552   160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTL 191

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: 382.47 E-value: 6.91e-130

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 392 RVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDK 471
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 472 CCQYWPTEDSVKYGDYTVEIKAETQCDdTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQ 551
Cdd:cd14623    81 CAQYWPSDGSVSYGDITIELKKEEECE-SYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1709608747 552 QSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14623   160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTL 216

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: 384.76 E-value: 1.16e-129

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  99 TSKTYFPIPVDSLEDEYRVRSADDGKLLREEYN----------------------------------------------- 131
Cdd:cd14621     1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNalpacpiqatceaaskeenkeknryvnilpydhsrvhltpvegvpds 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 ---------GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDIT 202
Cdd:cd14621    81 dyinasfinGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 203 VLVDYTIRKFCVQyQASD--GSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTF 280
Cdd:cd14621   161 VLVDYTVRKFCIQ-QVGDvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTF 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1709608747 281 IVIDAMIDMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEYFLYGDTEL 338
Cdd:cd14621   240 IVIDAMLDMMHAERKVDVYG-FVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296

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: 360.38 E-value: 1.18e-121

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14551     8 DGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVVLVDYTTR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQASD-GSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDM 289
Cdd:cd14551    88 KFCIQKVNRGiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIVIDAMLDM 167

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1709608747 290 MYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14551   168 MHAEGKVDVFG-FVSRIRQQRSQMVQTDMQYVFIYQ 202

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 330.78 E-value: 2.78e-109

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  361 GLEEEFKKLTNMRIMKENMRTGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEfTDYINASFIDGYRQKDYFIATQGPLT 440
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  441 HTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTE--DSVKYGDYTVEIKAETQCDDtFSLRDLVLTYDPEKETRL 518
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDD-YTIRTLEVTNTGCSETRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  519 VRHFHFHGWPEIGIPAEGKGMIDIIAAVqKQQQQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLR 598
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAV-RKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237


                   ....*....
gi 1709608747  599 MQRPHMVQT 607
Cdd:smart00194 238 SQRPGMVQT 246

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 323.81 E-value: 6.05e-107

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 387 NMKKNRVLQIIPYDFNRVILSMRRGQEftDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQE 466
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPS--DYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 467 REQDKCCQYWPT--EDSVKYGDYTVEIKAETQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIA 544
Cdd:pfam00102  79 KGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709608747 545 AVQKQQQQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:pfam00102 159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQT 221

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: 297.13 E-value: 1.54e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 383 NLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLT 462
Cdd:cd14554     2 NLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 463 ELQEREQDKCCQYWPTEDSVKYGDYTVEIKAETQCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDI 542
Cdd:cd14554    82 KLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709608747 543 IAAVQKQQQQSGNH-PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14554   161 IGQVHKTKEQFGQEgPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQT 226

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: 276.09 E-value: 5.07e-89

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTE--DSVKYGDYTVEIKAE 494
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEggKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 495 TQCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSgNHPIVVHCSAGAGRTGTFIA 574
Cdd:cd00047    81 EELSD-YTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKP-NGPIVVHCSAGVGRTGTFIA 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1709608747 575 LSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd00047   159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTL 192

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 276.85 E-value: 2.15e-88

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKG--CWTYGNVRVSVEDITVLVDYT 208
Cdd:smart00194  63 DGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYT 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  209 IRKFCVQYqasDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:smart00194 143 IRTLEVTN---TGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQ 219

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1709608747  289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:smart00194 220 QLEAGKEVDIFE-IVKELRSQRPGMVQTEEQYIFLYRAILE 259

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: 274.23 E-value: 3.51e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIRK 211
Cdd:cd14549     9 GYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEVLATYTVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 212 FCVQYQ---ASDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14549    89 FSLKNLklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTYIVIDSMLQ 168

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIY 324
Cdd:cd14549   169 QIQDKGTVNVFG-FLKHIRTQRNYLVQTEEQYIFIH 203

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

Pssm-ID: 350343 [Multi-domain] Cd Length: 200 Bit Score: 270.31 E-value: 7.61e-87

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKG--CWTYGNVRVSVEDITVLVDYT 208
Cdd:cd00047     8 DGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGgkPLEYGDITVTLVSEEELSDYT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 209 IRKFCVQYQasdGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd00047    88 IRTLELSPK---GCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAIDILLE 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd00047   165 RLEAEGEVDVFE-IVKALRKQRPGMVQTLEQYEFIYE 200

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: 272.38 E-value: 3.23e-86

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 335 DTELDVSSLEGHLHKLHNTCAPLDRLGLEEEFKKLTNMRIMKENMRTGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEF 414
Cdd:cd14627     1 NTEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 415 TDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAE 494
Cdd:cd14627    81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 495 TQCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSG-NHPIVVHCSAGAGRTGTFI 573
Cdd:cd14627   161 YNMPQ-YILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVGRTGVFI 239

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1709608747 574 ALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14627   240 TLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQT 273

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: 268.52 E-value: 1.04e-84

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 336 TELDVSSLEGHLHKLHNTCAPLDRLGLEEEFKKLTNMRIMKENMRTGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEFT 415
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 416 DYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAET 495
Cdd:cd14628    81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 496 QCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSG-NHPIVVHCSAGAGRTGTFIA 574
Cdd:cd14628   161 NMPQ-YILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVGRTGVFIT 239

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1709608747 575 LSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14628   240 LSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQT 272

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: 264.64 E-value: 4.33e-84

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14553    40 DGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVR 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQasdGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14553   120 TFALHKN---GSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERI 196

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14553   197 KHEKTVDIYG-HVTCLRAQRNYMVQTEDQYIFIHDALLE 234

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: 265.05 E-value: 1.90e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 336 TELDVSSLEGHLHKLHNTCAPLDRLGLEEEFKKLTNMRIMKENMRTGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEFT 415
Cdd:cd14629     2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 416 DYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAET 495
Cdd:cd14629    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 496 QCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSG-NHPIVVHCSAGAGRTGTFIA 574
Cdd:cd14629   162 NMPQ-YILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVGRTGVFIT 240

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1709608747 575 LSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14629   241 LSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQT 273

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 255.63 E-value: 1.05e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDK--GCWTYGNVRVSVEDIT-VLVDYT 208
Cdd:pfam00102  37 GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREKCAQYWPEEegESLEYGDFTVTLKKEKeDEKDYT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 209 IRKFCVQYqasDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQV-NPSYAGPIVVHCSAGVGRTGTFIVIDAMI 287
Cdd:pfam00102 117 VRTLEVSN---GGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKSsLDGRSGPIVVHCSAGIGRTGTFIAIDIAL 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1709608747 288 DMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:pfam00102 194 QQLEAEGEVDIFQ-IVKELRSQRPGMVQTLEQYIFLYDAILE 234

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: 253.06 E-value: 3.36e-79

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 358 DRLGLEEEFKKLTNMrIMKENMRTGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQG 437
Cdd:cd14543     1 QKRGIYEEYEDIRRE-PPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 438 PLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTED--SVKYGDYTVEiKAETQCDDTFSLRDLVLTYDPEKE 515
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVT-NLSVENKEHYKKTTLEIHNTETDE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 516 TRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQS------------GNHPIVVHCSAGAGRTGTFIALSNILERVK 583
Cdd:cd14543   159 SRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghpPGPPIVVHCSAGIGRTGTFCTLDICLSQLE 238

                         250       260
                  ....*....|....*....|....
gi 1709608747 584 AEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14543   239 DVGTLNVMQTVRRMRTQRAFSIQT 262

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: 241.49 E-value: 1.93e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 392 RVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDK 471
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 472 CCQYWP-TEDSVKYGDYTVEIKAETQCDDtFSLRDLVLTYdpEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQkQQ 550
Cdd:cd14548    81 CDHYWPfDQDPVYYGDITVTMLSESVLPD-WTIREFKLER--GDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVR-DY 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1709608747 551 QQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14548   157 IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQT 213

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: 241.15 E-value: 4.73e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 385 PANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTEL 464
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 465 QEREQDKCCQYWPTEDSVKYGDYTVEIkAETQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIA 544
Cdd:cd14553    81 EERSRVKCDQYWPTRGTETYGLIQVTL-LDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709608747 545 AVQK-QQQQSGnhPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14553   160 RVKAcNPPDAG--PIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQT 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: 236.86 E-value: 6.63e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14626    78 DGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVR 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQyqaSDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14626   158 TFALY---KNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM 234

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14626   235 KHEKTVDIYG-HVTCMRSQRNYMVQTEDQYIFIHEALLE 272

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

Pssm-ID: 350406 [Multi-domain] Cd Length: 203 Bit Score: 230.74 E-value: 1.39e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPtEDSVKYGDYTVEIKAETQ 496
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 497 CdDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQ----QQSGNH-PIVVHCSAGAGRTGT 571
Cdd:cd14558    80 S-PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLpyknSKHGRSvPIVVHCSDGSSRTGI 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1709608747 572 FIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14558   159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVST 194

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: 223.54 E-value: 1.48e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 391 NRVLQIIPYDFNRVILSMRrGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQD 470
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQ-SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 471 KCCQYWPTEDSVKYGDYTVEIKAETQCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAV-QKQ 549
Cdd:cd14615    80 KCEEYWPSKQKKDYGDITVTMTSEIVLPE-WTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVrEYM 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1709608747 550 QQQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14615   159 KQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQT 216

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: 225.36 E-value: 1.97e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14625    84 DGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFCVR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQyqaSDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14625   164 TFSLH---KNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI 240

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14625   241 KHEKTVDIYG-HVTLMRSQRNYMVQTEDQYSFIHDALLE 278

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: 219.40 E-value: 2.98e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKgCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14555     8 DGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETEPLAEYVVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQasdGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14555    87 TFALERR---GYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMA 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14555   164 EREGVVDIYN-CVKELRSRRVNMVQTEEQYIFIHDAILE 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: 216.49 E-value: 5.35e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 391 NRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKD-YFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQ 469
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEkAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 470 dKCCQYWPTEDSVKYGDYTVEIKAETQCDDtFSLRDLVLTYdpEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQ 549
Cdd:cd14547    81 -KCAQYWPEEENETYGDFEVTVQSVKETDG-YTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1709608747 550 QQQSGNH-PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14547   157 RQTEPHRgPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQT 215

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: 218.45 E-value: 8.89e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14624    84 DGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQyqaSDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14624   164 TFALY---KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI 240

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEYFLYGD 335
Cdd:cd14624   241 KHEKTVDIYG-HVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGN 284

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: 215.08 E-value: 9.02e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWP--DKGCWTYGNVRVSVEDITVLVDYT 208
Cdd:cd14557     8 DGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKINEEKICPDYI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 209 IRKFCVQYQASDGSKtpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14557    88 IRKLNINNKKEKGSG--REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGIDAMLE 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14557   166 GLEAEGRVDVYG-YVVKLRRQRCLMVQVEAQYILIHQ 201

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: 215.30 E-value: 1.57e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWP-DKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14548    34 GYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCDHYWPfDQDPVYYGDITVTMLSESVLPDWTIR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYqasdGSKTpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14548   114 EFKLER----GDEV-RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQI 188

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14548   189 ESEDYVDIFG-IVYDLRKHRPLMVQTEAQYIFLHQ 222

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: 215.58 E-value: 1.97e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 396 IIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQY 475
Cdd:cd14620     4 ILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 476 WPTEDSVKYGDYTVEIKAETQCDDtFSLRDLVLTY---DPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVqKQQQQ 552
Cdd:cd14620    84 WPDQGCWTYGNIRVAVEDCVVLVD-YTIRKFCIQPqlpDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKV-KSVNP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 553 SGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14620   162 VHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQT 216

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: 212.15 E-value: 1.95e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd17668     8 DGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQ-----ASDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDA 285
Cdd:cd17668    88 NFTLRNTkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTGTYIVLDS 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1709608747 286 MIDMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALL 328
Cdd:cd17668   168 MLQQIQHEGTVNIFG-FLKHIRSQRNYLVQTEEQYVFIHDALV 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: 210.57 E-value: 1.44e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 391 NRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQD 470
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 471 KCCQYWPTEDS-VKYGDYTVEIKAETQCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQ 549
Cdd:cd14618    81 LCDHYWPSESTpVSYGHITVHLLAQSSEDE-WTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 550 QQQS-GNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14618   160 VQATkGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTL 219

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: 207.49 E-value: 1.19e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFID-GYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPT-EDSVKYGDYTVEIKAE 494
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSgEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 495 TQCDDT-FSLRDLVLTYDpEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQ-KQQQQSGNHPIVVHCSAGAGRTGTF 572
Cdd:cd18533    81 EENDDGgFIVREFELSKE-DGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKReLNDSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1709608747 573 IAL--------SNILERVKAEGLLD-VFQTVKSLRMQRPHMVQTVH 609
Cdd:cd18533   160 IALdslldelkRGLSDSQDLEDSEDpVYEIVNQLRKQRMSMVQTLR 205

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: 208.20 E-value: 1.93e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 381 TGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVM 460
Cdd:cd14614     6 AADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 461 LTELQEREQDKCCQYWP-TEDSVKYGDYTVEIKAETQCDDtFSLRDLVLTYdpEKETRLVRHFHFHGWPEIGIPAEGKGM 539
Cdd:cd14614    86 LTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPD-WAIREFRVSY--ADEVQDVMHFNYTAWPDHGVPTANAAE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 540 iDIIAAVQKQQQQSGNH--PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14614   163 -SILQFVQMVRQQAVKSkgPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQT 231

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: 207.19 E-value: 3.78e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKgCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14630    40 DGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVGRVKCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQasdGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14630   119 TFTVQKK---GYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMA 195

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14630   196 ENEGVVDIFN-CVRELRAQRVNMVQTEEQYVFVHDAILE 233

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: 207.58 E-value: 7.67e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd17667    66 DGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVR 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCV--------QYQASDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIV 282
Cdd:cd17667   146 RFSIrntkvkkgQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIV 225

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1709608747 283 IDAMIDMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEYFL 332
Cdd:cd17667   226 IDSMLQQIKDKSTVNVLG-FLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274

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: 204.90 E-value: 8.50e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCwTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14632     8 DGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD-TYGDIKITLLKTETLAEYSVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQasdGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14632    87 TFALERR---GYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVMLDMA 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14632   164 ECEGVVDIYN-CVKTLCSRRINMIQTEEQYIFIHDAILE 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: 207.22 E-value: 9.69e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 113 DEYRVRSADDGKLLREEY------NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDK 186
Cdd:cd14543    42 DQSRVKLPKRNGDERTDYinanfmDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 187 G--CWTYGNVRVSVEDITVLVDYTIRKFCVQYQASDGSktpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQ------- 257
Cdd:cd14543   122 EgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDES---RQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQqqalavk 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709608747 258 -VNPSYAG-----PIVVHCSAGVGRTGTFIVIDAMIDMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIY 324
Cdd:cd14543   199 aMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQ-TVRRMRTQRAFSIQTPDQYYFCY 270

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: 204.42 E-value: 1.08e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14552     8 DGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTDYEDYTLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQASDGSKTPRlltQLHFTSWPDFGVPFSPIGMLKFLKKV-KQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDM 289
Cdd:cd14552    88 DFLVTKGKGGSTRTVR---QFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLER 164

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1709608747 290 MYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQAL 327
Cdd:cd14552   165 VKAEGVLDVFQ-VVKSLRLQRPHMVQTLEQYEFCYKVV 201

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: 204.48 E-value: 1.65e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKgCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14631    22 DGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDFKVTCVEMEPLAEYVVR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQasdGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14631   101 TFTLERR---GYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMA 177

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14631   178 EREGVVDIYN-CVKALRSRRINMVQTEEQYIFIHDAILE 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: 203.41 E-value: 2.65e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDkCCQYWPTEDSVKYGDYTVEIKAETQ 496
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDEGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 497 cDDTFSLRDLVL--TYDPEKETRLVRHFHFHGWPEIG-IPAEGKGMIDIIAAVQKQQQQSGNHPIVVHCSAGAGRTGTFI 573
Cdd:cd14556    80 -DEDVISRIFRLqnTTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1709608747 574 ALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETE 193

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: 205.65 E-value: 3.79e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 383 NLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLT 462
Cdd:cd14626    37 NLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 463 ELQEREQDKCCQYWPTEDSVKYGDYTVEIKAETQCdDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDI 542
Cdd:cd14626   117 RLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVEL-ATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAF 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 543 IAAVqKQQQQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14626   196 LRRV-KACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQT 259

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: 202.97 E-value: 4.41e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAETQ 496
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 497 CDD----TFSLRDL-VLTYDPEKETRLVRHFHFHGWPEIGIPAEgkgMIDIIAAVQKQQ--QQSGNHPIVVHCSAGAGRT 569
Cdd:cd14549    81 LATytvrTFSLKNLkLKKVKGRSSERVVYQYHYTQWPDHGVPDY---TLPVLSFVRKSSaaNPPGAGPIVVHCSAGVGRT 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1709608747 570 GTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14549   158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQT 195

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: 203.58 E-value: 6.34e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 391 NRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQD 470
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 471 KCCQYWPTEDS-VKYGDYTVEIKAETQCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMI---DIIAAV 546
Cdd:cd14619    81 KCEHYWPLDYTpCTYGHLRVTVVSEEVMEN-WTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLafrRLLRQW 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709608747 547 QKQQQQSGnhPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14619   160 LDQTMSGG--PTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQT 218

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: 200.17 E-value: 6.67e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWT-YGNVRVSVEDITVLVD--YT 208
Cdd:cd18533    10 PGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGeYGDLTVELVSEEENDDggFI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 209 IRKFCVQYqasdGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVN--PSYAGPIVVHCSAGVGRTGTFIVIDAM 286
Cdd:cd18533    90 VREFELSK----EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNdsASLDPPIIVHCSAGVGRTGTFIALDSL 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1709608747 287 IDMM--------YEEQKIDVFGFFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd18533   166 LDELkrglsdsqDLEDSEDPVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

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: 200.15 E-value: 8.86e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 391 NRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQD 470
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 471 KCCQYWPTE-DSVKYGDYTVEIKAETQCDDtFSLRDLVLTYDPEKET-RLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQK 548
Cdd:cd14617    81 KCDHYWPADqDSLYYGDLIVQMLSESVLPE-WTIREFKICSEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 549 QQQQS-GNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14617   160 YINRTpGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQT 219

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: 198.19 E-value: 6.56e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWP-DKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14619    35 GYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRVKCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVR 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQASDGSKTPRlltQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSY--AGPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14619   115 EFLLKQVEEQKTLSVR---HFHFTAWPDHGVPSSTDTLLAFRRLLRQWLDQTmsGGPTVVHCSAGVGRTGTLIALDVLLQ 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:cd14619   192 QLQSEGLLGPFS-FVQKMRENRPLMVQTESQYVFLHQCILDF 232

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: 198.13 E-value: 1.88e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 382 GNLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVML 461
Cdd:cd14603    25 GGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 462 TELQEREQDKCCQYWP-TEDSVKYGDYTVEIKAETQCDDTFSLRDLVLTYdpEKETRLVRHFHFHGWPEIGIPAEGKGMI 540
Cdd:cd14603   105 CREIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTF--QKESRSVSHFQYMAWPDHGIPDSPDCML 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709608747 541 DIIAAVqKQQQQSGNHPIVVHCSAGAGRTGTFIALSNI-----LERVKAEglLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14603   183 AMIELA-RRLQGSGPEPLCVHCSAGCGRTGVICTVDYVrqlllTQRIPPD--FSIFDVVLEMRKQRPAAVQT 251

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: 195.52 E-value: 2.81e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAETQ 496
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 497 CDD----TFSLRDlVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSGNhPIVVHCSAGAGRTGTF 572
Cdd:cd14551    81 LVDyttrKFCIQK-VNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAG-PIVVHCSAGVGRTGTF 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1709608747 573 IALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14551   159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQT 193

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: 196.40 E-value: 3.16e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 387 NMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQE 466
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 467 REQDKCCQYWPTEDSVkYGDYTVEIkAETQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAV 546
Cdd:cd14630    83 VGRVKCVRYWPDDTEV-YGDIKVTL-IETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709608747 547 QKQQQQSGNhPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14630   161 KFLNPPDAG-PIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQT 220

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: 195.76 E-value: 8.15e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 387 NMKKNRVLQIIPYDFNRVILSMRRGQE-FTDYINASFI----DGYRQKDY---FIATQGPLTHTVEDFWRMVWEWKCHSI 458
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVpGSDYINANYIrnenEGPTTDENaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 459 VMLTELQEREQDKCCQYWPTEDSVK-YGDYTVEIKAETQCDDtFSLRDLVLTY-DPEKETRLVRHFHFHGWPEIGIPAEG 536
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKqYGPYRVQNVSEHDTTD-YTLRELQVSKlDQGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709608747 537 KGMIDIIAAVQkQQQQSGNH--PIVVHCSAGAGRTGTFIALSNILERVKAEGLL---DVFQTVKSLRMQRPHMVQT 607
Cdd:cd14544   160 GGVLNFLEDVN-QRQESLPHagPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcdiDIQKTIQMVRSQRSGMVQT 234

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: 194.07 E-value: 9.94e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14622     9 DGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDTLLETISIR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQAsdgSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKV-KQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDM 289
Cdd:cd14622    89 DFLVTYNQ---EKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIALSNILER 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1709608747 290 MYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:cd14622   166 VKAEGLLDVFQ-TVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.

Pssm-ID: 350460 [Multi-domain] Cd Length: 247 Bit Score: 195.05 E-value: 1.36e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 383 NLPANMKKNRVLQIIPYDFNRVILSMRRGQ-EFTDYINASFIDGY--RQKDYfIATQGPLTHTVEDFWRMVWEWKCHSIV 459
Cdd:cd14612    11 DIPGHASKDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYdgKEKAY-IATQGPMLNTVSDFWEMVWQEECPIIV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 460 MLTELQEReQDKCCQYWPTEDSvKYGDYTVEIKAETQCDDtFSLRDLVLTYdpEKETRLVRHFHFHGWPEIGIPAEGKGM 539
Cdd:cd14612    90 MITKLKEK-KEKCVHYWPEKEG-TYGRFEIRVQDMKECDG-YTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAGPL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709608747 540 IDIIAAVQKQQQQSGNH-PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14612   165 LRLVAEVEESRQTAASPgPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQT 233

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: 193.36 E-value: 1.90e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 134 KDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPD---KGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14538    13 GDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSLEKYQSLQDFVIR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQASDGSktpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSyaGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14538    93 RISLRDKETGEV---HHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS--GPIVVHCSAGIGRTGVLITIDVALGLI 167

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14538   168 ERDLPFDIQD-IVKDLREQRQGMIQTKDQYIFCYKACLE 205

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: 195.63 E-value: 3.47e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 362 LEEEFKKLTNMRImKENMRTGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTH 441
Cdd:cd14621    28 FREEFNALPACPI-QATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 442 TVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAETQCDDtFSLRDLVLT----YDPEKETR 517
Cdd:cd14621   107 TVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVD-YTVRKFCIQqvgdVTNKKPQR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 518 LVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSGNhPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSL 597
Cdd:cd14621   186 LITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAG-AIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRI 264

                         250
                  ....*....|
gi 1709608747 598 RMQRPHMVQT 607
Cdd:cd14621   265 RAQRCQMVQT 274

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: 194.54 E-value: 6.97e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 340 VSSLEGHLHKLHNTcaplDRLGLEEEFKKLTNMRimKENMRTGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYIN 419
Cdd:cd14625     6 ISELAEHTERLKAN----DNLKLSQEYESIDPGQ--QFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYIN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 420 ASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAETQCdD 499
Cdd:cd14625    80 ANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIEL-A 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 500 TFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSGNhPIVVHCSAGAGRTGTFIALSNIL 579
Cdd:cd14625   159 TFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAG-PIVVHCSAGVGRTGCFIVIDAML 237

                         250       260
                  ....*....|....*....|....*...
gi 1709608747 580 ERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14625   238 ERIKHEKTVDIYGHVTLMRSQRNYMVQT 265

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: 191.84 E-value: 1.24e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNK-FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEdKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14547    35 GYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE-KCAQYWPEEENETYGDFEVTVQSVKETDGYTVR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQASDgsktpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQV--NPSYAGPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14547   114 KLTLKYGGEK-----RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEArqTEPHRGPIVVHCSAGIGRTGCFIATSIGCQ 188

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14547   189 QLREEGVVDVLG-IVCQLRLDRGGMVQTAEQYEFVHR 224

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: 192.68 E-value: 1.37e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 117 VRSADDGKLLREEyngykdKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKG-CWTYGNVR 195
Cdd:cd14544    38 IRNENEGPTTDEN------AKTYIATQGCLENTVSDFWSMVWQENSRVIVMTTKEVERGKNKCVRYWPDEGmQKQYGPYR 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 196 VSVEDITVLVDYTIRKFCVQYQasDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSY--AGPIVVHCSAG 273
Cdd:cd14544   112 VQNVSEHDTTDYTLRELQVSKL--DQGDPIREIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQESLphAGPIVVHCSAG 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 274 VGRTGTFIVIDAMIDMMYEEQ---KIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:cd14544   190 IGRTGTFIVIDMLLDQIKRKGldcDIDIQK-TIQMVRSQRSGMVQTEAQYKFIYVAVAQY 248

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: 193.33 E-value: 1.41e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 364 EEFKKLT-NMRIMKENmrtGNLPANMKKNRVLQIIPYDFNRVILSMRRGQE--FTDYINASFIDGYRQKDYFIATQGPLT 440
Cdd:cd17667     6 EEVQRCTaDMNITAEH---SNHPDNKHKNRYINILAYDHSRVKLRPLPGKDskHSDYINANYVDGYNKAKAYIATQGPLK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 441 HTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAeTQCDDTFSLRDLVLTYDPEKE----- 515
Cdd:cd17667    83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKS-TKIHACYTVRRFSIRNTKVKKgqkgn 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 516 ------TRLVRHFHFHGWPEIGIPAEGkgmIDIIAAVQKQQ--QQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGL 587
Cdd:cd17667   162 pkgrqnERTVIQYHYTQWPDMGVPEYA---LPVLTFVRRSSaaRTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                         250       260
                  ....*....|....*....|
gi 1709608747 588 LDVFQTVKSLRMQRPHMVQT 607
Cdd:cd17667   239 VNVLGFLKHIRTQRNYLVQT 258

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: 193.34 E-value: 1.47e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKgCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14633    77 DGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAEYVIR 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQasdGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMM 290
Cdd:cd14633   156 TFAVEKR---GVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMA 232

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 291 YEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14633   233 EREGVVDIYN-CVRELRSRRVNMVQTEEQYVFIHDAILE 270

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: 192.94 E-value: 2.77e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 358 DRLglEEEFKKLTNMRIMKENMRTGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINAS-FIDGYRQKDYFIATQ 436
Cdd:cd14609    15 DRL--AKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPAYIATQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 437 GPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAE-TQCDDtFSLRDLVLTYDPEKE 515
Cdd:cd14609    93 GPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEhIWCED-FLVRSFYLKNVQTQE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 516 TRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSgNHPIVVHCSAGAGRTGTFIALSNILERVkAEGL--LDVFQT 593
Cdd:cd14609   172 TRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAAT 249

                         250
                  ....*....|....
gi 1709608747 594 VKSLRMQRPHMVQT 607
Cdd:cd14609   250 LEHVRDQRPGMVRT 263

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: 190.41 E-value: 4.70e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIRK 211
Cdd:cd14615    34 GYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 212 FCVQYQASDGSKTPRlltQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYA--GPIVVHCSAGVGRTGTFIVIDAMIDM 289
Cdd:cd14615   114 FTVKNAQTNESRTVR---HFHFTSWPDHGVPETTDLLINFRHLVREYMKQNPpnSPILVHCSAGVGRTGTFIAIDRLIYQ 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1709608747 290 MYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14615   191 IENENVVDVYG-IVYDLRMHRPLMVQTEDQYVFLNQCALD 229

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: 189.36 E-value: 5.26e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPtEDSVKYGDYTVEIkAETQ 496
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTL-VETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 497 CDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSGNhPIVVHCSAGAGRTGTFIALS 576
Cdd:cd14555    79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAG-PIVVHCSAGAGRTGCYIVID 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1709608747 577 NILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14555   158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQT 188

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: 191.42 E-value: 1.08e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 362 LEEEFKKLTNMRIMKENMRTGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFI-DGYRQKDYFIATQGPLT 440
Cdd:cd14610    19 LEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImDHDPRNPAYIATQGPLP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 441 HTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAE-TQCDDtFSLRDLVLTYDPEKETRLV 519
Cdd:cd14610    99 ATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEhIWCED-FLVRSFYLKNLQTNETRTV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 520 RHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSgNHPIVVHCSAGAGRTGTFIALSNILERV-KAEGLLDVFQTVKSLR 598
Cdd:cd14610   178 TQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLR 256


                  ....*....
gi 1709608747 599 MQRPHMVQT 607
Cdd:cd14610   257 DQRPGMVQT 265

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: 191.10 E-value: 1.50e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 383 NLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLT 462
Cdd:cd14624    43 NLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 463 ELQEREQDKCCQYWPTEDSVKYGDYTVEIKAETQCdDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDI 542
Cdd:cd14624   123 KLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVEL-ATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAF 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 543 IAAVQKQQQQSGNhPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14624   202 LRRVKTCNPPDAG-PMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQT 265

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: 189.87 E-value: 3.14e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 387 NMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQE 466
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 467 REQDKCCQYWPtEDSVKYGDYTVEIkAETQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAV 546
Cdd:cd14633   120 VGRVKCCKYWP-DDTEIYKDIKVTL-IETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709608747 547 QKQQQQSGNhPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14633   198 KSKSPPNAG-PLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQT 257

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: 187.92 E-value: 7.30e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 129 EYNGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWT-YGNVRVSVEDITVLVDY 207
Cdd:cd14605    46 KCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKeYGVMRVRNVKESAAHDY 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 208 TIRKFCVQyQASDGSkTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKV--KQVNPSYAGPIVVHCSAGVGRTGTFIVIDA 285
Cdd:cd14605   126 ILRELKLS-KVGQGN-TERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDI 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1709608747 286 MIDMMYEEQ---KIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:cd14605   204 LIDIIREKGvdcDIDVPK-TIQMVRSQRSGMVQTEAQYRFIYMAVQHY 250

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: 183.71 E-value: 6.08e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPtEDSVKYGDYTVE-IKAET 495
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITlLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 496 QCDdtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSGNhPIVVHCSAGAGRTGTFIAL 575
Cdd:cd14632    80 LAE--YSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAG-PVVVHCSAGAGRTGCYIVL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1709608747 576 SNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14632   157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQT 188

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: 184.26 E-value: 1.09e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14554    43 DGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILR 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQASDGSKTPRlltQLHFTSWPDFGVPFSPIGMLKFlkkVKQVNPSYA-----GPIVVHCSAGVGRTGTFIVIDA 285
Cdd:cd14554   123 EFKVTDARDGQSRTVR---QFQFTDWPEQGVPKSGEGFIDF---IGQVHKTKEqfgqeGPITVHCSAGVGRTGVFITLSI 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1709608747 286 MIDMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALL 328
Cdd:cd14554   197 VLERMRYEGVVDVFQ-TVKLLRTQRPAMVQTEDQYQFCYRAAL 238

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: 181.56 E-value: 3.35e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPT--EDSVKYGDYTVEIKAE 494
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 495 TQCDDtFSLRDLVLTYDPEKET-RLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQkQQQQSGNHPIVVHCSAGAGRTGTFI 573
Cdd:cd14557    81 KICPD-YIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVN-AFNNFFSGPIVVHCSAGVGRTGTYI 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1709608747 574 ALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQ 606
Cdd:cd14557   159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQ 191

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: 181.76 E-value: 4.42e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 137 NKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKG-CWTYGNVRVSVEDITVLVDYTIRKFCVQ 215
Cdd:cd14541    19 NRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQITCVSEEVTPSFAFREFILT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 216 YQASDGSktpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMMYEEQK 295
Cdd:cd14541    99 NTNTGEE---RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVLITMETAMCLIEANEP 175

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1709608747 296 IDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALL 328
Cdd:cd14541   176 VYPLD-IVRTMRDQRAMLIQTPSQYRFVCEAIL 207

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: 182.44 E-value: 2.99e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 381 TGNLPANMKKNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVM 460
Cdd:cd14604    51 TGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVM 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 461 LTELQEREQDKCCQYWPT--EDSVKYGDYTVEIKAETQCDDTFsLRDLVLTYDpeKETRLVRHFHFHGWPEIGIPAEGKG 538
Cdd:cd14604   131 ACREFEMGRKKCERYWPLygEEPMTFGPFRISCEAEQARTDYF-IRTLLLEFQ--NETRRLYQFHYVNWPDHDVPSSFDS 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709608747 539 MIDIIAAVQKQQQQSgNHPIVVHCSAGAGRTGTFIALS---NILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14604   208 ILDMISLMRKYQEHE-DVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQT 278

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

Pssm-ID: 350461 [Multi-domain] Cd Length: 258 Bit Score: 181.21 E-value: 3.04e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 383 NLPANMKKNRVLQIIPYDFNRVIL-SMRRGQEFTDYINASFIDGYRQKD-YFIATQGPLTHTVEDFWRMVWEWKCHSIVM 460
Cdd:cd14613    21 DIPGLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWRMVWQERSPIIVM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 461 LTELQEREQdKCCQYWPtEDSVKYGDYTVEIKAETQCDDtFSLRdlVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMI 540
Cdd:cd14613   101 ITNIEEMNE-KCTEYWP-EEQVTYEGIEITVKQVIHADD-YRLR--LITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLL 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 541 DIIAAVQKQQQQSGNH--PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14613   176 QLVQEVEEARQQAEPNcgPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTC 245

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: 179.06 E-value: 5.40e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 403 RVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPtEDSV 482
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 483 KYGDYTVEIkAETQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVqKQQQQSGNHPIVVHC 562
Cdd:cd14631    80 VYGDFKVTC-VEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV-KLSNPPSAGPIVVHC 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1709608747 563 SAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14631   158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQT 202

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: 178.41 E-value: 6.65e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFI--DGYRQKDYfIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAE 494
Cdd:cd14546     1 YINASTIydHDPRNPAY-IATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 495 -TQCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSGNhPIVVHCSAGAGRTGTFI 573
Cdd:cd14546    80 hIWCDD-YLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSC-PIVVHCSDGAGRTGTYI 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1709608747 574 ALSNILERV-KAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14546   158 LIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKT 192

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: 178.95 E-value: 7.94e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 391 NRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQD 470
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 471 KCCQYWPTEDS--VKYGDYTV-EIKAETQCDdtFSLRDLVLtyDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQ 547
Cdd:cd14616    81 RCHQYWPEDNKpvTVFGDIVItKLMEDVQID--WTIRDLKI--ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709608747 548 KQQQQSgNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14616   157 ASRAHD-NTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNL 216

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: 178.25 E-value: 7.97e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVKYGDYTVEIKAETQ 496
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 497 CD----DTFSLRDLVLTYDPEK---ETRLVRHFHFHGWPEIGIPaegKGMIDIIAAVQK--QQQQSGNHPIVVHCSAGAG 567
Cdd:cd17668    81 LAyytvRNFTLRNTKIKKGSQKgrpSGRVVTQYHYTQWPDMGVP---EYTLPVLTFVRKasYAKRHAVGPVVVHCSAGVG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1709608747 568 RTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd17668   158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQT 197

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: 179.44 E-value: 1.03e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 387 NMKKNRVLQIIPYDFNRVILSMRRGQE-FTDYINASFI--------DGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHS 457
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDGDPNEpVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 458 IVMLTELQEREQDKCCQYWPTEDSVK-YGDYTVEIKAETQCDDtFSLRDLVLTYDPEKET-RLVRHFHFHGWPEIGIPAE 535
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPDEYALKeYGVMRVRNVKESAAHD-YILRELKLSKVGQGNTeRTVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709608747 536 GKGMIDIIAAVQ-KQQQQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGL---LDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14605   161 PGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQT 236

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: 177.14 E-value: 2.03e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 416 DYINASFID----GYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWP-TEDSVKYGDYTVE 490
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 491 IKAETqCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVqKQQQQSGNHPIVVHCSAGAGRTG 570
Cdd:cd14541    81 CVSEE-VTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRV-RQNRVGMVEPTVVHCSAGIGRTG 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1709608747 571 TFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14541   159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTP 196

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: 178.12 E-value: 6.32e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 384 LPANMKKNRVLQIIPYDFNRVILsmrrgQEFTDYINASFID----GYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIV 459
Cdd:cd14600    37 LPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 460 MLTELQEREQDKCCQYWP-TEDSVKYGDYTVEIKAEtQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKG 538
Cdd:cd14600   112 MLTTLTERGRTKCHQYWPdPPDVMEYGGFRVQCHSE-DCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709608747 539 MIDIIAAVQKQQQQsgNHPIVVHCSAGAGRTGTFIALSN---ILERVKAEGLLDVfqtVKSLRMQRPHMVQT 607
Cdd:cd14600   191 FLEFVNYVRSKRVE--NEPVLVHCSAGIGRTGVLVTMETamcLTERNQPVYPLDI---VRKMRDQRAMMVQT 257

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: 175.66 E-value: 1.26e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 390 KNRVLQIIPYDFNRVILSMRRGQefTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQ 469
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 470 DKCCQYWPTEDS----VKYGDYTVEIKAETQCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAA 545
Cdd:cd14545    79 IKCAQYWPQGEGnamiFEDTGLKVTLLSEEDKSY-YTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 546 VQKQQQQSGNH-PIVVHCSAGAGRTGTFIALSNILERVKAEGL--LDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14545   158 VRESGSLSSDVgPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQT 222

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: 174.08 E-value: 5.83e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14623    33 DGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSDGSVSYGDITIELKKEEECESYTVR 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQASDGSKTPRlltQLHFTSWPDFGVPFSPIGMLKFLKKV-KQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDM 289
Cdd:cd14623   113 DLLVTNTRENKSRQIR---QFHFHGWPEVGIPSDGKGMINIIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLER 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1709608747 290 MYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14623   190 VKAEGILDVFQ-TVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

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

Pssm-ID: 350390 [Multi-domain] Cd Length: 202 Bit Score: 172.22 E-value: 9.32e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPT--EDSVKYGDYTVEIKAE 494
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEegEEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 495 TQCDDTFSLRDLVLTYDpeKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKqQQQSGNHPIVVHCSAGAGRTGTFIA 574
Cdd:cd14542    81 KRVGPDFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRD-YQGSEDVPICVHCSAGCGRTGTICA 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1709608747 575 LS---NILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14542   158 IDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQT 193

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

Pssm-ID: 350459 [Multi-domain] Cd Length: 226 Bit Score: 172.80 E-value: 1.22e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 390 KNRVLQIIPYDFNRVILSMRRGQEF-TDYINASFIDGYRQKD-YFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQER 467
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEkAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 468 EQdKCCQYWPTEDSVkYGDYTVEIKAETQCDDtFSLRDLVLTYDpeKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQ 547
Cdd:cd14611    82 NE-KCVLYWPEKRGI-YGKVEVLVNSVKECDN-YTIRNLTLKQG--SQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709608747 548 KQQQQS-GNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14611   157 EDRLASpGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQT 217

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: 171.86 E-value: 1.97e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 139 FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVS-VEDITVLVDYTIRKFcvqYQ 217
Cdd:cd14546    17 YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHlVSEHIWCDDYLVRSF---YL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 218 ASDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKvkqVNPSYAG---PIVVHCSAGVGRTGTFIVIDAMIDMMYEEQ 294
Cdd:cd14546    94 KNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRK---VNKSYRGrscPIVVHCSDGAGRTGTYILIDMVLNRMAKGA 170

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1709608747 295 K-IDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14546   171 KeIDIAA-TLEHLRDQRPGMVKTKDQFEFVLTAVAE 205

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: 171.60 E-value: 1.29e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 368 KLTNMRimKENMRtgnlPANMKKNRVLQIIPYDFNRVILSMRRGQ-EFTDYINASFI------DGYRQKDYfIATQGPLT 440
Cdd:cd14606     5 KNLHQR--LEGQR----PENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVknqllgPDENAKTY-IASQGCLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 441 HTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTEDSVK-YGDYTVEIKAETQCDDtFSLRDLVLT-YDPEKETRL 518
Cdd:cd14606    78 ATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRaYGPYSVTNCGEHDTTE-YKLRTLQVSpLDNGELIRE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 519 VRHFHFHGWPEIGIPAEGKGMIDIIAAV-QKQQQQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGL---LDVFQTV 594
Cdd:cd14606   157 IWHYQYLSWPDHGVPSEPGGVLSFLDQInQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTI 236

                         250
                  ....*....|...
gi 1709608747 595 KSLRMQRPHMVQT 607
Cdd:cd14606   237 QMVRAQRSGMVQT 249

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: 168.56 E-value: 5.83e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 136 KNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWP-DKGCWTYGNVRVSVEDITVLVDYTIRKFcv 214
Cdd:cd14617    39 RREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREF-- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 215 QYQASDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQ-VNPS-YAGPIVVHCSAGVGRTGTFIVIDAMIDMMYE 292
Cdd:cd14617   117 KICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDyINRTpGSGPTVVHCSAGVGRTGTFIALDRILQQLDS 196

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1709608747 293 EQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14617   197 KDSVDIYG-AVHDLRLHRVHMVQTECQYVYLHQ 228

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

Pssm-ID: 350475 [Multi-domain] Cd Length: 290 Bit Score: 169.91 E-value: 1.02e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14627    90 DGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILR 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQyQASDGSKtpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYA--GPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14627   170 EFKVT-DARDGQS--RTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLE 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEYF 331
Cdd:cd14627   247 RMRYEGVVDIFQ-TVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288

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: 166.02 E-value: 2.48e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQ-KDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTE--DSVKYGDYTVEIkA 493
Cdd:cd14539     1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSL-Q 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 494 ETQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQK--QQQQSGNHPIVVHCSAGAGRTGT 571
Cdd:cd14539    80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShyLQQRSLQTPIVVHCSSGVGRTGA 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1709608747 572 FIALSNILERVKAE-GLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14539   160 FCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQE 196

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: 168.37 E-value: 3.98e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14628    89 DGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILR 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQyQASDGSKtpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYA--GPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14628   169 EFKVT-DARDGQS--RTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLE 245

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEYF 331
Cdd:cd14628   246 RMRYEGVVDIFQ-TVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287

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: 165.26 E-value: 4.58e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCwTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14558     8 DGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK-TYGDIEVELKDTEKSPTYTVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQASDGSKTprlLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQ---VNPSYAG---PIVVHCSAGVGRTGTFIVID 284
Cdd:cd14558    87 VFEITHLKRKDSRT---VYQYQYHKWKGEELPEKPKDLVDMIKSIKQklpYKNSKHGrsvPIVVHCSDGSSRTGIFCALW 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1709608747 285 AMIDMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIY 324
Cdd:cd14558   164 NLLESAETEKVVDVFQ-VVKALRKQRPGMVSTLEQYQFLY 202

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: 165.32 E-value: 5.23e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 139 FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKG----CWTYGNVRVSVEDITVLVDYTIRKFCV 214
Cdd:cd14540    18 YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgehdALTFGEYKVSTKFSVSSGCYTTTGLRV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 215 QYQASDGSKTprlLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQV-------------NPsyagPIVVHCSAGVGRTGTFI 281
Cdd:cd14540    98 KHTLSGQSRT---VWHLQYTDWPDHGCPEDVSGFLDFLEEINSVrrhtnqdvaghnrNP----PTLVHCSAGVGRTGVVI 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1709608747 282 VIDAMIDMMYEEQKIDVfGFFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:cd14540   171 LADLMLYCLDHNEELDI-PRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218

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: 164.24 E-value: 3.26e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 101 KTYFPIPVDSLEDEYRVRSADDGKLLREEY-NGYKDKNK-FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEdK 178
Cdd:cd14612    22 KTILPNPQSRVCLRRAGSQEEEGSYINANYiRGYDGKEKaYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEKKE-K 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 179 CYQYWPDKGCwTYGNVRVSVEDITVLVDYTIRKFCVQYQASDgsktpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQV 258
Cdd:cd14612   101 CVHYWPEKEG-TYGRFEIRVQDMKECDGYTIRDLTIQLEEES-----RSVKHYWFSSWPDHQTPESAGPLLRLVAEVEES 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709608747 259 NPSYA--GPIVVHCSAGVGRTGTFIVIDAMIDMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:cd14612   175 RQTAAspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILG-IVCQLRLDRGGMIQTSEQYQFLHHTLALY 247

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: 165.05 E-value: 3.50e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 139 FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCW-TYGnvRVSVEDITVL--VDYTIRKFCVq 215
Cdd:cd14606    69 YIASQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQrAYG--PYSVTNCGEHdtTEYKLRTLQV- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 216 yQASDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPS--YAGPIVVHCSAGVGRTGTFIVIDAMIDMMYE- 292
Cdd:cd14606   146 -SPLDNGELIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTk 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1709608747 293 --EQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:cd14606   225 glDCDIDIQK-TIQMVRAQRSGMVQTEAQYKFIYVAIAQF 263

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: 163.19 E-value: 4.88e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGC-WTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14618    35 GYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRVLCDHYWPSESTpVSYGHITVHLLAQSSEDEWTRR 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQasdGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVK-QVNPSY-AGPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14618   115 EFKLWHE---DLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVReHVQATKgKGPTLVHCSAGVGRSGTFIALDRLLR 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALL 328
Cdd:cd14618   192 QLKEEKVVDVFN-TVYILRMHRYLMIQTLSQYIFLHSCIL 230

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: 163.14 E-value: 7.90e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWP-DKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14614    50 GYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYqaSDGSKTprlLTQLHFTSWPDFGVPFSPIG--MLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14614   130 EFRVSY--ADEVQD---VMHFNYTAWPDHGVPTANAAesILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQ 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALL 328
Cdd:cd14614   205 HIRDHEFVDILG-LVSEMRSYRMSMVQTEEQYIFIHQCVQ 243

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

Pssm-ID: 350477 [Multi-domain] Cd Length: 291 Bit Score: 164.51 E-value: 9.88e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14629    90 DGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILR 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQyQASDGSKtpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYA--GPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14629   170 EFKVT-DARDGQS--RTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGqdGPITVHCSAGVGRTGVFITLSIVLE 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEYF 331
Cdd:cd14629   247 RMRYEGVVDMFQ-TVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288

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: 160.65 E-value: 1.81e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDkCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14556     8 DSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDEGSGTYGPIQVEFVSTTIDEDVISR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYQASDGSKTpRLLTQLHFTSWPDFG-VPFSPIGMLKFLKKVKQVNPSYA-GPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14556    87 IFRLQNTTRPQEGY-RMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGeGPIVVHCLNGVGRSGVFCAISSVCE 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1709608747 289 MMYEEQKIDVFgFFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14556   166 RIKVENVVDVF-QAVKTLRNHRPNMVETEEQYKFCYD 201

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: 161.55 E-value: 2.45e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 390 KNRVLQIIPYDFNRVILSMRRGQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQ 469
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 470 DKCCQYW--PTEDSVKYGDYTVEIKAETQCDDtFSLRDLVLTYDpeKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVq 547
Cdd:cd14602    81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSD-YIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDV- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709608747 548 KQQQQSGNHPIVVHCSAGAGRTGTFIALSNILERVKaEGLL----DVFQTVKSLRMQRPHMVQT 607
Cdd:cd14602   157 RCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQT 219

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: 161.23 E-value: 2.46e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPD--KGCWTYGNVRVSVEDITVLVDYT 208
Cdd:cd14616    34 SGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCHQYWPEdnKPVTVFGDIVITKLMEDVQIDWT 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 209 IRKFCVQYQASdgsktPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14616   114 IRDLKIERHGD-----YMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQ 188

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14616   189 HINDHDFVDIYG-LVAELRSERMCMVQNLAQYIFLHQ 224

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: 159.46 E-value: 5.96e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYF--IATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWP---TEDSVKYGDYTVEI 491
Cdd:cd14538     1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 492 KAETQCDDtFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKqQQQSGnhPIVVHCSAGAGRTGT 571
Cdd:cd14538    81 EKYQSLQD-FVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRR-IHNSG--PIVVHCSAGIGRTGV 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1709608747 572 FIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14538   157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQT 192

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

Pssm-ID: 350390 [Multi-domain] Cd Length: 202 Bit Score: 159.13 E-value: 6.65e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 139 FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKG--CWTYGNVRVSVE-DITVLVDYTIRKFCVQ 215
Cdd:cd14542    16 YIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeeQLQFGPFKISLEkEKRVGPDFLIRTLKVT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 216 YQasdgsKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMMYEEQK 295
Cdd:cd14542    96 FQ-----KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDYVWNLLKTGKI 170

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1709608747 296 IDVFGFF--VSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14542   171 PEEFSLFdlVREMRKQRPAMVQTKEQYELVYR 202

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: 159.48 E-value: 1.11e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 136 KNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWP----DKGCWTYGNVRVSVEDITVLVDYTIRK 211
Cdd:cd14545    38 KRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKCAQYWPqgegNAMIFEDTGLKVTLLSEEDKSYYTVRT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 212 FCVQYQAsdgSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQ--VNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDM 289
Cdd:cd14545   118 LELENLK---TQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVREsgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVL 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1709608747 290 MyeeQKIDVFGFFVSRI----RDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14545   195 I---EKGNPSSVDVKKVllemRKYRMGLIQTPDQLRFSYL 231

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: 157.80 E-value: 2.75e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 137 NKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPD-KGCWTYGNVRVSVEDITVLVDYTIRKFCVQ 215
Cdd:cd14601    19 NRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVTCHSEEGNPAYVFREMTLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 216 YQASDGSktpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMMYEEQK 295
Cdd:cd14601    99 NLEKNES---RPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVLITMETAMCLIECNQP 175

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 296 I---DVfgffVSRIRDQRSQLVQTDMQYSFIYQALLEYF 331
Cdd:cd14601   176 VyplDI----VRTMRDQRAMMIQTPSQYRFVCEAILKVY 210

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: 159.84 E-value: 4.42e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 139 FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVS-VEDITVLVDYTIRKFCVQYQ 217
Cdd:cd14610    90 YIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNlVSEHIWCEDFLVRSFYLKNL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 218 ASDGSKTprlLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMMYEEQK-I 296
Cdd:cd14610   170 QTNETRT---VTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeI 246

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1709608747 297 DVfGFFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14610   247 DI-AATLEHLRDQRPGMVQTKEQFEFALTAVAE 278

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: 159.25 E-value: 4.89e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 137 NKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPD-KGCWTYGNVRVSVEDITVLVDYTIRKFCVQ 215
Cdd:cd14600    82 NKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDpPDVMEYGGFRVQCHSEDCTIAYVFREMLLT 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 216 YQASDGSKTprlLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSyAGPIVVHCSAGVGRTGTFIVIDAMIDMMYEEQK 295
Cdd:cd14600   162 NTQTGEERT---VTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVE-NEPVLVHCSAGIGRTGVLVTMETAMCLTERNQP 237

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 296 I---DVfgffVSRIRDQRSQLVQTDMQYSFIYQALLEYF 331
Cdd:cd14600   238 VyplDI----VRKMRDQRAMMVQTSSQYKFVCEAILRVY 272

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: 157.68 E-value: 5.37e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 387 NMKKNRVLQIIPYDFNRVILsmrrGQEfTDYINASFIDGYRQKDYF--IATQGPLTHTVEDFWRMVWEWKCHSIVMLTEL 464
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDE-GGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 465 QEREQDKCCQYWPTE-DSVKYGDYTVEIKAE-TQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDI 542
Cdd:cd14597    78 VEGGKIKCQRYWPEIlGKTTMVDNRLQLTLVrMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 543 IAAVqKQQQQSGnhPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14597   158 ISYM-RHIHKSG--PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQT 219

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

Pssm-ID: 350444 [Multi-domain] Cd Length: 207 Bit Score: 156.06 E-value: 9.67e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 135 DKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPD--KGCWTYGNVRVSVEDITVLVDYTIRKF 212
Cdd:cd14596    14 EELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlQEPMELENYQLRLENYQALQYFIIRII 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 213 CVqYQASDGSKtpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSyaGPIVVHCSAGVGRTGTFIVIDAMIDMMYE 292
Cdd:cd14596    94 KL-VEKETGEN--RLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT--GPIVVHCSAGIGRAGVLICVDVLLSLIEK 168

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1709608747 293 EQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14596   169 DLSFNIKD-IVREMRQQRYGMIQTKDQYLFCYKVVLE 204

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: 155.56 E-value: 1.31e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQdkCCQYWPTEDSVKYGDYTVE-IKAET 495
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL--CMQYWPEKTSCCYGPIQVEfVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 496 QCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEI-GIPAEGKGMIDIIAAVQKQQQQ--SGNHPIVVHCSAGAGRTGTF 572
Cdd:cd14634    79 DEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSGTF 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1709608747 573 IALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14634   159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETL 194

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: 157.89 E-value: 2.04e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 139 FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCWTYGNVRVS-VEDITVLVDYTIRKFcvqYQ 217
Cdd:cd14609    88 YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNlVSEHIWCEDFLVRSF---YL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 218 ASDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVkqvNPSYAG---PIVVHCSAGVGRTGTFIVIDAMIDMMYEEQ 294
Cdd:cd14609   165 KNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKV---NKCYRGrscPIIVHCSDGAGRTGTYILIDMVLNRMAKGV 241

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1709608747 295 K-IDVfGFFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14609   242 KeIDI-AATLEHVRDQRPGMVRTKDQFEFALTAVAE 276

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: 154.22 E-value: 1.18e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 139 FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDkgcwtygnvrvsVEDITVLVDYTIRKFCVQYQA 218
Cdd:cd14597    45 YIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGGKIKCQRYWPE------------ILGKTTMVDNRLQLTLVRMQQ 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 219 SDG------------SKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSyaGPIVVHCSAGVGRTGTFIVIDAM 286
Cdd:cd14597   113 LKNfvirvlelediqTREVRHITHLNFTAWPDHDTPSQPEQLLTFISYMRHIHKS--GPIITHCSAGIGRSGTLICIDVV 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1709608747 287 IDMMYEEQKIDVfGFFVSRIRDQRSQLVQTDMQYSFIYQALL 328
Cdd:cd14597   191 LGLISKDLDFDI-SDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231

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: 153.00 E-value: 2.13e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFID---GYRQKDYfIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPTE----DSVKYGDYTV 489
Cdd:cd14540     1 YINASHITatvGGKQRFY-IAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLggehDALTFGEYKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 490 EIKAeTQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDII--------AAVQKQQQQSGNHPIVVH 561
Cdd:cd14540    80 STKF-SVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLeeinsvrrHTNQDVAGHNRNPPTLVH 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1709608747 562 CSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14540   159 CSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTL 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: 152.10 E-value: 2.82e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREqdKCCQYWPTEDSVKYGDYTVE-IKAET 495
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWPEEGMLRYGPIQVEcMSCSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 496 QCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWP-EIGIPAEGKGMIDIIAAVQKQQQQ--SGNHPIVVHCSAGAGRTGTF 572
Cdd:cd14636    79 DCDVISRIFRICNLTRPQEGYLMVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEEcdEGEGRTIIHCLNGGGRSGMF 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1709608747 573 IALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14636   159 CAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVET 193

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

Pssm-ID: 350496 [Multi-domain] Cd Length: 206 Bit Score: 151.85 E-value: 3.23e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDY--FIATQGPLTHTVEDFWRMVWEWKCHSIVMLTEL-QEREQDKCCQYWPTED--SVKYGDYTVEI 491
Cdd:cd17658     1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLvDNYSTAKCADYFPAEEneSREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 492 KAETQCDDTFSLRDLVLTY-DPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVqkQQQQSGNHPIVVHCSAGAGRTG 570
Cdd:cd17658    81 KKLKHSQHSITLRVLEVQYiESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRL--YGIPPSAGPIVVHCSAGIGRTG 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 571 TFIALSNILERVKAEGL--LDVFQTVKSLRMQRPHMVQT 607
Cdd:cd17658   159 AYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQT 197

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: 152.87 E-value: 1.05e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 380 RTGNLPANMKKNRVLQIIPYDFNRVILSmrrgQEFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIV 459
Cdd:cd14608    18 RVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 460 MLTELQEREQDKCCQYWPT--EDSVKYGDYTVEIKAETQ-CDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEG 536
Cdd:cd14608    94 MLNRVMEKGSLKCAQYWPQkeEKEMIFEDTNLKLTLISEdIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESP 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 537 KGMIDIIAAVQKQQQQSGNH-PIVVHCSAGAGRTGTFIALSN---ILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14608   174 ASFLNFLFKVRESGSLSPEHgPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQT 248

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: 152.87 E-value: 1.16e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 136 KNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDK----GCWTYGNVRVSV--EDITVLvdYTI 209
Cdd:cd14608    63 QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKeekeMIFEDTNLKLTLisEDIKSY--YTV 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 210 RKFCVQYQAsdgSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQ---VNPSYaGPIVVHCSAGVGRTGTFIVIDAM 286
Cdd:cd14608   141 RQLELENLT---TQETREILHFHYTTWPDFGVPESPASFLNFLFKVREsgsLSPEH-GPVVVHCSAGIGRSGTFCLADTC 216

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1709608747 287 IDMMyeEQKIDVFGFFVSRI----RDQRSQLVQTDMQYSFIYQALLE--YFLYGDTEL 338
Cdd:cd14608   217 LLLM--DKRKDPSSVDIKKVllemRKFRMGLIQTADQLRFSYLAVIEgaKFIMGDSSV 272

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 153.65 E-value: 1.56e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLkERKEDKCYQYW--PDKGCWTYGNVRVSVEDITVLVDYT 208
Cdd:PHA02746  107 DGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFT 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 209 IRKFCVQYQASDgskTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQ----------VNPSYAGPIVVHCSAGVGRTG 278
Cdd:PHA02746  186 KTRLMITDKISD---TSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAG 262

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1709608747 279 TFIVIDAMIDMMYEEQKIDVfGFFVSRIRDQRSQLVQTDMQYSFIYQAL 327
Cdd:PHA02746  263 TFCAIDNALEQLEKEKEVCL-GEIVLKIRKQRHSSVFLPEQYAFCYKAL 310

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: 149.01 E-value: 2.53e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREqdKCCQYWPTED-SVKYGDYTVEIKAET 495
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEkPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 496 -QCDDTFSL---RDLVLTYDPEKETRLVRHFHFHGWPEIGIPAegKGMIDIIAAVQKQQQQSgNHPIVVHCSAGAGRTGT 571
Cdd:cd14550    79 hSCLSNEIRlivRDFILESTQDDYVLEVRQFQCPSWPNPCSPI--HTVFELINTVQEWAQQR-DGPIVVHDRYGGVQAAT 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1709608747 572 FIALSNILERVKAEGLLDVFQTVKSLRMQRP 602
Cdd:cd14550   156 FCALTTLHQQLEHESSVDVYQVAKLYHLMRP 186

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: 150.78 E-value: 3.44e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNK-FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEdKCYQYWPDKGCwTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14613    64 GYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWPEEQV-TYEGIEITVKQVIHADDYRLR 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQyqaSDGSKtpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKV---KQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMI 287
Cdd:cd14613   142 LITLK---SGGEE--RGLKHYWYTSWPDQKTPDNAPPLLQLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICC 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1709608747 288 DMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:cd14613   217 KQLRNEGVVDILR-TTCQLRLDRGGMIQTCEQYQFVHHVLSLY 258

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 152.08 E-value: 4.38e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 387 NMKKNRVLQIIPYDFNRVILSMRRGqeFTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQE 466
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 467 REQDKCCQYWPTED--SVKYGDYTVEIKaETQCDDTFSLRDLVLTyDPEKETRL-VRHFHFHGWPEIGIPAEGKGMIDII 543
Cdd:PHA02742  130 DGKEACYPYWMPHErgKATHGEFKIKTK-KIKSFRNYAVTNLCLT-DTNTGASLdIKHFAYEDWPHGGLPRDPNKFLDFV 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709608747 544 AAVQKQQQQS----------GNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQR 601
Cdd:PHA02742  208 LAVREADLKAdvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQR 275

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 152.49 E-value: 4.63e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 385 PANMKKNRVLQIIPYDFNRVILSMR-------------RGQEFT------DYINASFIDGYRQKDYFIATQGPLTHTVED 445
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVVINAHeslkmfdvgdsdgKKIEVTsednaeNYIHANFVDGFKEANKFICAQGPKEDTSED 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 446 FWRMVWEWKCHSIVMLTELqEREQDKCCQYWPTED--SVKYGDYTVEIkAETQCDDTFSLRDLVLTYDPEKETRLVRHFH 523
Cdd:PHA02746  129 FFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEdsELAFGRFVAKI-LDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 524 FHGWPEIGIPAEGKGMIDIIAAVQKQQ---------QQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTV 594
Cdd:PHA02746  207 FPDWPDNGIPTGMAEFLELINKVNEEQaelikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIV 286


                  ....*..
gi 1709608747 595 KSLRMQR 601
Cdd:PHA02746  287 LKIRKQR 293

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

Pssm-ID: 350387 [Multi-domain] Cd Length: 205 Bit Score: 147.15 E-value: 1.78e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 139 FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWP-DKG-CWTYGNVRVSVEDITVLVDYTIRKFCVQY 216
Cdd:cd14539    17 FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPtERGqALVYGAITVSLQSVRTTPTHVERIISIQH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 217 QASDGSktpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVK---QVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMMYEE 293
Cdd:cd14539    97 KDTRLS---RSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshyLQQRSLQTPIVVHCSSGVGRTGAFCLLYAAVQEIEAG 173

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1709608747 294 QKIDVFGFFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14539   174 NGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

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

Pssm-ID: 350455 [Multi-domain] Cd Length: 257 Bit Score: 148.19 E-value: 2.78e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 380 RTGNLPANMKKNRVLQIIPYDFNRVILSMRRgqefTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIV 459
Cdd:cd14607    17 RVAKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 460 MLTELQEREQDKCCQYWPTED----SVKYGDYTVEIKAEtQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAE 535
Cdd:cd14607    93 MLNRIVEKDSVKCAQYWPTDEeevlSFKETGFSVKLLSE-DVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPES 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 536 GKGMIDIIAAVQKQQQQSGNH-PIVVHCSAGAGRTGTFIALSN--ILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14607   172 PASFLNFLFKVRESGSLSPEHgPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRMGLIQT 246

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: 148.22 E-value: 5.80e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 359 RLGLEEEFKKLTNMRIMKEN----MRTGNLPANMKKNRVLQIIPYDFNRVILSMRRgQEFTDYINASFID-GYRQKDY-F 432
Cdd:cd14599     6 ERKLEEGMVFTEYEQIPKKKadgvFTTATLPENAERNRIREVVPYEENRVELVPTK-ENNTGYINASHIKvTVGGEEWhY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 433 IATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWP----TEDSVKYGDYTVEIKAETQ--CDDTFSLRDL 506
Cdd:cd14599    85 IATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgsKHSSATYGKFKVTTKFRTDsgCYATTGLKVK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 507 VLTYDPEketRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSG---------NHPIVVHCSAGAGRTGTFIALSN 577
Cdd:cd14599   165 HLLSGQE---RTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNsmldstkncNPPIVVHCSAGVGRTGVVILTEL 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1709608747 578 ILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14599   242 MIGCLEHNEKVEVPVMLRHLREQRMFMIQTI 272

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: 146.22 E-value: 6.02e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNK-FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEdKCYQYWPDKGcWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14611    38 GYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKR-GIYGKVEVLVNSVKECDNYTIR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVQYqasdGSKTpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYA--GPIVVHCSAGVGRTGTFIVIDAMID 288
Cdd:cd14611   116 NLTLKQ----GSQS-RSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASPgrGPVVVHCSAGIGRTGCFIATTIGCQ 190

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1709608747 289 MMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14611   191 QLKEEGVVDVLS-IVCQLRVDRGGMVQTSEQYEFVHH 226

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 148.61 E-value: 8.91e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 385 PANMKKNRVLQIIPYDFNRVILSMRRGQEfTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTEL 464
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 465 QERE-QDKCCQYW-PTED-SVKYGDYTVEiKAETQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMID 541
Cdd:PHA02747  128 KGTNgEEKCYQYWcLNEDgNIDMEDFRIE-TLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIK 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 542 IIAAVQKQQQQSGNH---------PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:PHA02747  207 FIKIIDINRKKSGKLfnpkdallcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMN 281

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: 144.67 E-value: 1.46e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTEL-QEREQDKCCQYWPTEDSVKYGDYTVEIKAET 495
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLnQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 496 QCDDTFSLRDLVLTYDPEKETRL-VRHFHFHGW-PEIGIPAEGKGMIDIIAAVQKQQQQSGNHPIVVHCSAGAGRTGTFI 573
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLmVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1709608747 574 ALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETL 195

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: 146.12 E-value: 2.15e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 125 LLREEYN----------GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWP-DKGCWTYGN 193
Cdd:cd14603    51 LLQEEGHsdyinanfikGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 194 VRVS-VEDITVLVDYTIRKFCVQYQasdgsKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSA 272
Cdd:cd14603   131 FTITlVKEKRLNEEVILRTLKVTFQ-----KESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSA 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709608747 273 GVGRTGTFIVIDAMIDMMYEEQKIDVFGFF--VSRIRDQRSQLVQTDMQYSFIYQALLEYF 331
Cdd:cd14603   206 GCGRTGVICTVDYVRQLLLTQRIPPDFSIFdvVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266

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: 143.55 E-value: 4.11e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 416 DYINASFID----GYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWP-TEDSVKYGDYTVE 490
Cdd:cd14601     1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 491 IKAEtQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVqKQQQQSGNHPIVVHCSAGAGRTG 570
Cdd:cd14601    81 CHSE-EGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLV-RNKRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1709608747 571 TFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQT 195

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: 142.44 E-value: 7.38e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  73 VDKKIPNGILeeqeaqTVVLLPRSTSTSKTYFPIPVDsledEYRVRSADDgkllREEYNGYKDKNK-----------FIA 141
Cdd:cd14599    21 IPKKKADGVF------TTATLPENAERNRIREVVPYE----ENRVELVPT----KENNTGYINASHikvtvggeewhYIA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 142 AQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGC----WTYGNVRVSVEDITVLVDYTIRKFCVQYQ 217
Cdd:cd14599    87 TQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSkhssATYGKFKVTTKFRTDSGCYATTGLKVKHL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 218 ASDGSKTprlLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQV----NPSYAG------PIVVHCSAGVGRTGTFIVIDAMI 287
Cdd:cd14599   167 LSGQERT---VWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVrrhtNSMLDStkncnpPIVVHCSAGVGRTGVVILTELMI 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1709608747 288 DMMYEEQKIDVfGFFVSRIRDQRSQLVQTDMQYSFIYQALLEYF 331
Cdd:cd14599   244 GCLEHNEKVEV-PVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286

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: 141.26 E-value: 7.64e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 136 KNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWP--DKGCWTYGNVRVSV----EDITVLvdYTI 209
Cdd:cd14607    62 QRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPtdEEEVLSFKETGFSVkllsEDVKSY--YTV 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 210 RkfCVQYQASDGSKTpRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQ---VNPSYaGPIVVHCSAGVGRTGTFIVIDAM 286
Cdd:cd14607   140 H--LLQLENINSGET-RTISHFHYTTWPDFGVPESPASFLNFLFKVREsgsLSPEH-GPAVVHCSAGIGRSGTFSLVDTC 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1709608747 287 IDMMyeeQKIDVFGFFVSRI----RDQRSQLVQTDMQYSFIYQAL 327
Cdd:cd14607   216 LVLM---EKKDPDSVDIKQVlldmRKYRMGLIQTPDQLRFSYMAV 257

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 142.37 E-value: 1.63e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPD--KGCWTYGNVRVSVEDITVLVDYT 208
Cdd:PHA02738   84 DGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHYV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 209 IRKFCVqyqaSDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQV-------------NPSYAGPIVVHCSAGVG 275
Cdd:PHA02738  164 KSTLLL----TDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCqkelaqeslqighNRLQPPPIVVHCNAGLG 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 276 RTGTFIVIDAMIDMMYEEQKIDVfGFFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:PHA02738  240 RTPCYCVVDISISRFDACATVSI-PSIVSSIRNQRYYSLFIPFQYFFCYRAVKRY 293

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 141.38 E-value: 1.70e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 383 NLPANMKKNRVLQIIPYDFNRVilsmrrgQEFTDYINASFIDGYRQKDYfIATQGPLTHTVEDFWRMVWEWKCHSIVMLT 462
Cdd:COG5599    38 QNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNHRY-IATQYPLEEQLEDFFQMLFDNNTPVLVVLA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 463 ---ELQEReQDKCCQYWPTEDSvkYGDYTVEIK--AETQCDDTFSLRDLVLT-YDPEKETRLVRHFHFHGWPEI-GIPAE 535
Cdd:COG5599   110 sddEISKP-KVKMPVYFRQDGE--YGKYEVSSEltESIQLRDGIEARTYVLTiKGTGQKKIEIPVLHVKNWPDHgAISAE 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709608747 536 G-KGMIDIIAAVQKQQQQSGNhPIVVHCSAGAGRTGTFIALSNILERVKAEGL--LDVFQTVKSLRMQR-PHMVQT 607
Cdd:COG5599   187 AlKNLADLIDKKEKIKDPDKL-LPVVHCRAGVGRTGTLIACLALSKSINALVQitLSVEEIVIDMRTSRnGGMVQT 261

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: 1.71e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  228 LTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYA--GPIVVHCSAGVGRTGTFIVIDAMIDMMYEEQ-KIDVFGfFVS 304
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFD-TVK 80

                           90       100
                   ....*....|....*....|....*
gi 1709608747  305 RIRDQRSQLVQTDMQYSFIYQALLE 329
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: 1.71e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  228 LTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYA--GPIVVHCSAGVGRTGTFIVIDAMIDMMYEEQ-KIDVFGfFVS 304
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFD-TVK 80

                           90       100
                   ....*....|....*....|....*
gi 1709608747  305 RIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105

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: 137.21 E-value: 5.23e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 129 EYNGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKE-RKEDKCYQYWP--DKGCWTYGNVRVSVEDI-TVL 204
Cdd:cd17658     8 ETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPaeENESREFGRISVTNKKLkHSQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 205 VDYTIRKFCVQYQASDgsKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSyAGPIVVHCSAGVGRTGTFIVID 284
Cdd:cd17658    88 HSITLRVLEVQYIESE--EPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPS-AGPIVVHCSAGIGRTGAYCTIH 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1709608747 285 AMIDMMYEEQKIDV-FGFFVSRIRDQRSQLVQTDMQYSFIY 324
Cdd:cd17658   165 NTIRRILEGDMSAVdLSKTVRKFRSQRIGMVQTQDQYIFCY 205

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: 138.14 E-value: 3.08e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKG--CWTYGNVRVSVEDITVLVDYTI 209
Cdd:cd14604    95 GVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGeePMTFGPFRISCEAEQARTDYFI 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 210 RKFCVQYQasdgsKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDM 289
Cdd:cd14604   175 RTLLLEFQ-----NETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNL 249

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1709608747 290 MYEEQKIDVFGFF--VSRIRDQRSQLVQTDMQYSFIYQALLEYF 331
Cdd:cd14604   250 LKAGKIPEEFNVFnlIQEMRTQRHSAVQTKEQYELVHRAIAQLF 293

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: 134.20 E-value: 1.47e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 139 FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKG--CWTYGNVRVSVEDITVLVDYTIRKFCVQY 216
Cdd:cd14602    43 YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGKKKCERYWAEPGemQLEFGPFSVTCEAEKRKSDYIIRTLKVKF 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 217 QasdgsKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMMYEEQKI 296
Cdd:cd14602   123 N-----SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIP 197

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1709608747 297 DVFGFF--VSRIRDQRSQLVQTDMQYSFIYQALLEYF 331
Cdd:cd14602   198 ENFSVFslIQEMRTQRPSLVQTKEQYELVYNAVIELF 234

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: 133.27 E-value: 1.55e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQdkCCQYWPTEDSVKYGDYTVE-IKAET 495
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWPENGVHRHGPIQVEfVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 496 QCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEI-GIPAEGKGMIDIIAAVQKQQQQ--SGNHPIVVHCSAGAGRTGTF 572
Cdd:cd14635    79 EEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGTF 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1709608747 573 IALSNILERVKAEGLLDVFQTVKSLRMQRPHMV 605
Cdd:cd14635   159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMV 191

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: 133.18 E-value: 2.35e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 139 FIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWPDKGCW----TYGNVRVSVEDITVLVDYtirkfcv 214
Cdd:cd14598    18 YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYGRFKITTRFRTDSGCY------- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 215 qyqASDGSKTPRLLT-------QLHFTSWPDFGVPFSPIGMLKFLKKVKQV-------------NPsyagPIVVHCSAGV 274
Cdd:cd14598    91 ---ATTGLKIKHLLTgqertvwHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstidpkspNP----PVLVHCSAGV 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1709608747 275 GRTGTFIVIDAMIDMMYEEQKIDVfGFFVSRIRDQRSQLVQTDMQYSFIYQALLEYF 331
Cdd:cd14598   164 GRTGVVILSEIMIACLEHNEMLDI-PRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219

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: 131.79 E-value: 4.43e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGY--RQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWPT--EDSVKYGDYTVEIK 492
Cdd:cd14596     1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 493 aETQCDDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQQSgnhPIVVHCSAGAGRTGTF 572
Cdd:cd14596    81 -NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTG---PIVVHCSAGIGRAGVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1709608747 573 IALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQT 607
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQT 191

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 133.90 E-value: 1.51e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 386 ANMKKNRVLQIIPYDFNRVILSMRRGQefTDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQ 465
Cdd:PHA02738   48 KNRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 466 EREQDKCCQYWPT--EDSVKYGDYTV-EIKAETQcdDTFSLRDLVLTyDPEKETRLVRHFHFHGWPEIGIPAEGKGMIDI 542
Cdd:PHA02738  126 ENGREKCFPYWSDveQGSIRFGKFKItTTQVETH--PHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNF 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709608747 543 IAAVQKQQQ-------QSGNH-----PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPH 603
Cdd:PHA02738  203 VLEVRQCQKelaqeslQIGHNrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYY 275

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: 129.71 E-value: 3.73e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFID---GYRQKDYfIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWP----TEDSVKYGDY-- 487
Cdd:cd14598     1 YINASHIKvtvGGKEWDY-IATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFki 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 488 TVEIKAETQCDDTFSLRDLVLTYDPEketRLVRHFHFHGWPEIGIPAEGKGMIDIIAAVQKQQQ--------QSGNHPIV 559
Cdd:cd14598    80 TTRFRTDSGCYATTGLKIKHLLTGQE---RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRhtnstidpKSPNPPVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1709608747 560 VHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQRPHMVQTV 608
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTL 205

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: 127.42 E-value: 1.49e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCqYWPTEDS-VKYGDYTVEIKAET 495
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpINCETFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 496 -QC---DDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIP-AEGKGMIDIIaavqKQQQQSGNHPIVVHCSAGAGRTG 570
Cdd:cd17669    80 hKClsnEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISII----KEEAANRDGPMIVHDEHGGVTAG 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1709608747 571 TFIALSNILERVKAEGLLDVFQTVKSLRMQRP 602
Cdd:cd17669   156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRP 187

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 123.24 E-value: 2.56e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  519 VRHFHFHGWPEIGIPAEGKGMIDIIAAVQK-QQQQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGL-LDVFQTVKS 596
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKnLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVKE 81

                           90
                   ....*....|...
gi 1709608747  597 LRMQRPHMVQTVH 609
Cdd:smart00404  82 LRSQRPGMVQTEE 94

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: 123.24 E-value: 2.56e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  519 VRHFHFHGWPEIGIPAEGKGMIDIIAAVQK-QQQQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGL-LDVFQTVKS 596
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKnLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVKE 81

                           90
                   ....*....|...
gi 1709608747  597 LRMQRPHMVQTVH 609
Cdd:smart00012  82 LRSQRPGMVQTEE 94

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 130.12 E-value: 2.91e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERK-EDKCYQYW--PDKGCWTYGNVRVSVEDITVLVDY 207
Cdd:PHA02747   87 DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 208 TIRKFCVQYQAsdgSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKVKQVNPSYAG----------PIVVHCSAGVGRT 277
Cdd:PHA02747  167 ILTLIEITDKI---LKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKlfnpkdallcPIVVHCSDGVGKT 243

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1709608747 278 GTFIVIDAMIDMMYEEQKIDVfGFFVSRIRDQRSQLVQTDMQYSFIYQA--LLEYFLY 333
Cdd:PHA02747  244 GIFCAVDICLNQLVKRKAICL-AKTAEKIREQRHAGIMNFDDYLFIQPGyeVLHYFLS 300

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 127.90 E-value: 7.95e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 134 KDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKE--DKCYQYWPDKGcwTYGNVRVSVEDITVLV---DYT 208
Cdd:COG5599    74 IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDG--EYGKYEVSSELTESIQlrdGIE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 209 IRKFCVQYQASDGSKTPrlLTQLHFTSWPDFGVPFSPI--GMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVIDAM 286
Cdd:COG5599   152 ARTYVLTIKGTGQKKIE--IPVLHVKNWPDHGAISAEAlkNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLAL 229

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709608747 287 IDMMYEEQKIDV-FGFFVSRIRDQR-SQLVQTDMQYSFI 323
Cdd:COG5599   230 SKSINALVQITLsVEEIVIDMRTSRnGGMVQTSEQLDVL 268

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: 122.82 E-value: 6.89e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKedKCYQYWPDKGCWTYGNVRVSV--EDITVLVDYT 208
Cdd:cd14634     8 DSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQ--LCMQYWPEKTSCCYGPIQVEFvsADIDEDIISR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 209 IRKFCVQYQASDGSktpRLLTQLHFTSWPDF-GVPFSPIGMLKFLKKVKQVNPSY---AGPIVVHCSAGVGRTGTFIVID 284
Cdd:cd14634    86 IFRICNMARPQDGY---RIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYdgrEGRTVVHCLNGGGRSGTFCAIC 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1709608747 285 AMIDMMYEEQKIDVFgFFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14634   163 SVCEMIQQQNIIDVF-HTVKTLRNNKSNMVETLEQYKFVYEVALE 206

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 123.57 E-value: 3.77e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYW--PDKGCWTYGNVRVSVEDITVLVDYT 208
Cdd:PHA02742   87 DGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmpHERGKATHGEFKIKTKKIKSFRNYA 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 209 IRKFCVQyqasdGSKTPRLLTQLHF--TSWPDFGVPFSPIGMLKFLKKVKQV-----------NPSYAGPIVVHCSAGVG 275
Cdd:PHA02742  167 VTNLCLT-----DTNTGASLDIKHFayEDWPHGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLD 241

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 276 RTGTFIVIDAMIDmMYEEQKIDVFGFFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:PHA02742  242 RAGAFCAIDICIS-KYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 295

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: 118.63 E-value: 2.34e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 417 YINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCqYWPT-EDSVKYGDYTVE-IKAE 494
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPSrEESMNCEAFTVTlISKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 495 TQC---DDTFSLRDLVLTYDPEKETRLVRHFHFHGWPEIGIPAEGK-GMIDIIaavqKQQQQSGNHPIVVHCSAGAGRTG 570
Cdd:cd17670    80 RLClsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVI----KEEALTRDGPTIVHDEFGAVSAG 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1709608747 571 TFIALSNILERVKAEGLLDVFQTVKSLRMQRP 602
Cdd:cd17670   156 TLCALTTLSQQLENENAVDVYQVAKMINLMRP 187

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

Pssm-ID: 350483 [Multi-domain] Cd Length: 206 Bit Score: 108.62 E-value: 7.15e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKedKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14635     8 DSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQ--LCPQYWPENGVHRHGPIQVEFVSADLEEDIISR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KFCVqYQASDGSKTPRLLTQLHFTSWPDF-GVPFSPIGMLKFLKKVKQVNPSY---AGPIVVHCSAGVGRTGTFIVIDAM 286
Cdd:cd14635    86 IFRI-YNAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYnggEGRTVVHCLNGGGRSGTFCAISIV 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1709608747 287 IDMMYEEQKIDVFgFFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14635   165 CEMLRHQRAVDVF-HAVKTLRNNKPNMVDLLDQYKFCYEVALE 206

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: 104.71 E-value: 1.30e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLkERKEDKCyQYWPDKG----CWTYgNVRVSVEDITVL--- 204
Cdd:cd14550     9 GYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNEDEP-IYWPTKEkpleCETF-KVTLSGEDHSCLsne 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 205 VDYTIRKFCVQYQASDGSKTPRlltQLHFTSWPDFGVPFSPIgmLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVID 284
Cdd:cd14550    86 IRLIVRDFILESTQDDYVLEVR---QFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHDRYGGVQAATFCALT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1709608747 285 AMIDMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14550   161 TLHQQLEHESSVDVYQ-VAKLYHLMRPGVFTSKEDYQFLYK 200

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: 96.13 E-value: 1.49e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKED-KCYQYWPDKGCWTYGNVRVSVEDITVLVDYTI 209
Cdd:cd14637     8 DSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGSADEDIVT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 210 RKFCVQyQASDGSKTPRLLTQLHFTSWPDF-GVPFSPIGMLKFLKKVKQ-VNPSYAGPIVVHCSAGVGRTGTFIVIDAMI 287
Cdd:cd14637    88 RLFRVQ-NITRLQEGHLMVRHFQFLRWSAYrDTPDSKKAFLHLLASVEKwQRESGEGRTVVHCLNGGGRSGTYCASAMIL 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1709608747 288 DMMYEEQKIDVFgFFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14637   167 EMIRCHNIVDVF-YAVKTLRNYKPNMVETLEQYRFCYEIALE 207

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: 94.71 E-value: 5.05e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 131 NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKedKCYQYWPDKGCWTYGNVRVSVEDITVLVDYTIR 210
Cdd:cd14636     8 DSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWPEEGMLRYGPIQVECMSCSMDCDVISR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 211 KF--CVQYQASDGSktpRLLTQLHFTSWPDF-GVPFSPIGMLKFLKKVKQVNPSY---AGPIVVHCSAGVGRTGTFIVID 284
Cdd:cd14636    86 IFriCNLTRPQEGY---LMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECdegEGRTIIHCLNGGGRSGMFCAIS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1709608747 285 AMIDMMYEEQKIDVFgFFVSRIRDQRSQLVQTDMQYSFIYQALLE 329
Cdd:cd14636   163 IVCEMIKRQNVVDVF-HAVKTLRNSKPNMVETPEQYRFCYDVALE 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: 94.29 E-value: 5.73e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYqYWPDK----GCWTYgNVRVSVEDITVLVDY 207
Cdd:cd17669     9 GYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKdepiNCETF-KVTLIAEEHKCLSNE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 208 tiRKFCVQYQASDGSKTPRLLTQLHFT--SWPDfgvPFSPIG-MLKFLKKVKQVNPSYAGPIVVHCSAGVGRTGTFIVID 284
Cdd:cd17669    87 --EKLIIQDFILEATQDDYVLEVRHFQcpKWPN---PDSPISkTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALT 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1709608747 285 AMIDMMYEEQKIDVFGffVSRIRDQRSQLVQTDM-QYSFIYQALL 328
Cdd:cd17669   162 TLMHQLEKENSVDVYQ--VAKMINLMRPGVFTDIeQYQFLYKAIL 204

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: 83.96 E-value: 2.45e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 132 GYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKcYQYWPDK----GCWTYGNVRVSV-------ED 200
Cdd:cd17670     9 GYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWPSReesmNCEAFTVTLISKdrlclsnEE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 201 ITVLVDYTIRKFCVQYqasdgsktprLLTQLHFT--SWPDFGVPFSpiGMLKFLKKVKQVNPSYAGPIVVHCSAGVGRTG 278
Cdd:cd17670    88 QIIIHDFILEATQDDY----------VLEVRHFQcpKWPNPDAPIS--STFELINVIKEEALTRDGPTIVHDEFGAVSAG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1709608747 279 TFIVIDAMIDMMYEEQKIDVFGffVSRIRDQRSQLVQTDM-QYSFIYQALL 328
Cdd:cd17670   156 TLCALTTLSQQLENENAVDVYQ--VAKMINLMRPGVFTDIeQYQFLYKAML 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: 78.98 E-value: 1.72e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 118 RSADDGKLLREEYNGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWpdKGCWTYGnvRVS 197
Cdd:cd14559    10 VSTPVGKNLNANRVQIGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF--RQSGTYG--SVT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 198 VEDITVLVDYTIRKFCV-QY--QASDGSKTPRLLTqLHFTSWPDFGVpfSPIGMLKFL-----------------KKVKQ 257
Cdd:cd14559    86 VKSKKTGKDELVDGLKAdMYnlKITDGNKTITIPV-VHVTNWPDHTA--ISSEGLKELadlvnksaeekrnfyksKGSSA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709608747 258 VNPSYAGPIVVHCSAGVGRTGTFIvidAMIDMMYEEQKIDVFGfFVSRIRDQRS-QLVQTDMQY 320
Cdd:cd14559   163 INDKNKLLPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVED-IVSDMRTSRNgKMVQKDEQL 222

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 76.54 E-value: 4.08e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 389 KKNRVLQIIPYDFNRVILsmrRGQEftDYINASFIDGYRQKDYFIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQERe 468
Cdd:PHA02740   55 DENLALHITRLLHRRIKL---FNDE--KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 469 qdKC-CQYWPT-EDSVKYGD----YTVEIKAETQcddtFSLRDLVLTyDPEKETRLVRHFHFHGWPEIGIPAEGKGMID- 541
Cdd:PHA02740  129 --KCfNQFWSLkEGCVITSDkfqiETLEIIIKPH----FNLTLLSLT-DKFGQAQKISHFQYTAWPADGFSHDPDAFIDf 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709608747 542 ------IIAAVQKQQQQSGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRMQR 601
Cdd:PHA02740  202 fcniddLCADLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKK 267

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 66.14 E-value: 1.22e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 116 RVRSADDGKLLREEY-NGYKDKNKFIAAQGPKHETVADFWRMIWEQKSSTIVMLTNLKERkedKCY-QYWPDK-GC-WTY 191
Cdd:PHA02740   69 RIKLFNDEKVLDARFvDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCFnQFWSLKeGCvITS 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 192 GNVRVSVEDITVLVDYTIRKFCVqyqaSDGSKTPRLLTQLHFTSWPDFGVPFSPIGMLKFLKKV--------KQVNPSYA 263
Cdd:PHA02740  146 DKFQIETLEIIIKPHFNLTLLSL----TDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIddlcadleKHKADGKI 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709608747 264 GPIVVHCSAGVGRTGTFIVIDAMIDMMYEEQKIDVFGfFVSRIRDQRSQLVQTDMQYSFIYQALLEY 330
Cdd:PHA02740  222 APIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIAN-ALKKVRQKKYGCMNCLDDYVFCYHLIAAY 287

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: 62.03 E-value: 1.11e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 432 FIATQGPLTHTVEDFWRMVWEWKCHSIVMLTELQEREQDKCCQYWptEDSVKYGDYTVEIKAETQCD-------DTFSLR 504
Cdd:cd14559    31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF--RQSGTYGSVTVKSKKTGKDElvdglkaDMYNLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 505 dlvLTYDPEKETRLVrhFHFHGWPEIG-IPAEG-KGMIDIIAAVQKQQ----QQSGNHPI--------VVHCSAGAGRTG 570
Cdd:cd14559   109 ---ITDGNKTITIPV--VHVTNWPDHTaISSEGlKELADLVNKSAEEKrnfyKSKGSSAIndknkllpVIHCRAGVGRTG 183

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1709608747 571 TFIAlsnILERVKAEGLLDVFQTVKSLRMQR-PHMVQT 607
Cdd:cd14559   184 QLAA---AMELNKSPNNLSVEDIVSDMRTSRnGKMVQK 218

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

Pssm-ID: 350344 [Multi-domain] Cd Length: 113 Bit Score: 53.51 E-value: 1.13e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1709608747 549 QQQQSGNHPIVVHCSAGAGRTGTFIALsnileRVKAEGLLDVFQTVKSLRMQRPHMVQ 606
Cdd:cd14494    50 DQAEKPGEPVLVHCKAGVGRTGTLVAC-----YLVLLGGMSAEEAVRIVRLIRPGGIP 102

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

Pssm-ID: 350356 [Multi-domain] Cd Length: 206 Bit Score: 55.43 E-value: 1.39e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 509 TYDPEKETRLVRHFHFHGWPEIGIPAEGKgMIDIIAAVQKQQQQSGNhpIVVHCSAGAGRTGTFIALSNI-LERVKAEgl 587
Cdd:cd14506    66 SYLPEAFMRAGIYFYNFGWKDYGVPSLTT-ILDIVKVMAFALQEGGK--VAVHCHAGLGRTGVLIACYLVyALRMSAD-- 140

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1709608747 588 ldvfQTVKSLRMQRPHMVQTvhAGPLILVED 618
Cdd:cd14506   141 ----QAIRLVRSKRPNSIQT--RGQVLCVRE 165

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 49.58 E-value: 4.41e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 236 WPDFGVPfSPIGMLKFLKKVKQVNPSyAGPIVVHCSAGVGRTGTFIvidAMIDMMYEEQKIDVfgffVSRIRDQRSQLVQ 315
Cdd:COG2453    55 IPDFGAP-DDEQLQEAVDFIDEALRE-GKKVLVHCRGGIGRTGTVA---AAYLVLLGLSAEEA----LARVRAARPGAVE 125

                          90
                  ....*....|
gi 1709608747 316 TDMQYSFIYQ 325
Cdd:COG2453   126 TPAQRAFLER 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: 47.73 E-value: 9.80e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 248 MLKFLKKVKQVnPSYAGPIVVHCSAGVGRTGTFIVIDAMIDMMY--EEqkidvfgfFVSRIRDQRSQ-LVQTDMQYSFIY 324
Cdd:cd14494    42 VDRFLEVLDQA-EKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMsaEE--------AVRIVRLIRPGgIPQTIEQLDFLI 112


                  .
gi 1709608747 325 Q 325
Cdd:cd14494   113 K 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: 47.34 E-value: 8.60e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 235 SWPDFGVPfSPIGMLKFLKKVKQVnPSYAGPIVVHCSAGVGRTGtfIVIDAMIDM---MYEEQKIDVFgffvsriRDQRS 311
Cdd:cd14506    83 GWKDYGVP-SLTTILDIVKVMAFA-LQEGGKVAVHCHAGLGRTG--VLIACYLVYalrMSADQAIRLV-------RSKRP 151

                          90
                  ....*....|..
gi 1709608747 312 QLVQTDMQYSFI 323
Cdd:cd14506   152 NSIQTRGQVLCV 163

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: 45.73 E-value: 1.07e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1709608747 230 QLHFTSWPDFGVPfSPIGMLKFLKKVKQVNpSYAGPIVVHCSAGVGRTGTFI 281
Cdd:cd14504    51 RYHHIPIEDYTPP-TLEQIDEFLDIVEEAN-AKNEAVLVHCLAGKGRTGTML 100

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 44.58 E-value: 2.54e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709608747 539 MIDIIAAVQKQQQQsgNHPIVVHCSAGAGRTGTFIALSNILERVKAEgllDVFQTVKSLrmqRPHMVQT 607
Cdd:COG2453    66 LQEAVDFIDEALRE--GKKVLVHCRGGIGRTGTVAAAYLVLLGLSAE---EALARVRAA---RPGAVET 126

type III secretion system effector GTPase-activating protein SptP;

Pssm-ID: 185273 [Multi-domain] Cd Length: 535 Bit Score: 47.10 E-value: 3.16e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  70 ITVVDKKIPNGILEEQEAQTVVLLPRSTSTSK---TYFPIPVDSLEDEYRVRSADdGKLLREEYNGYKDKNKFIAAQGPK 146
Cdd:PRK15375  265 IHVIAKELKNVTAELEKIEAGAPMPQTMSGPTlglARFAVSSIPINQQTQVKLSD-GMPVPVNTLTFDGKPVALAGSYPK 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 147 H--ETVADFWRMIWEQKSSTIVMLTNLKERKEDKCYQYWpdKGCWTYGNVRVSVEDIT------VLVDYTIRKFCVQYQA 218
Cdd:PRK15375  344 NtpDALEAHMKMLLEKECSCLVVLTSEDQMQAKQLPPYF--RGSYTFGEVHTNSQKVSsasqgeAIDQYNMQLSCGEKRY 421

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 219 SdgsktprlLTQLHFTSWPDFGvPFSPIGMLKFL-KKVKQVNPSYAG---------PIVvHCSAGVGRTGTFIVIDAMID 288
Cdd:PRK15375  422 T--------IPVLHVKNWPDHQ-PLPSTDQLEYLaDRVKNSNQNGAPgrsssdkhlPMI-HCLGGVGRTGTMAAALVLKD 491

                         250       260       270
                  ....*....|....*....|....*....|
gi 1709608747 289 MMY---EEQKIDVFGFFVSRIRDQRSQLVQ 315
Cdd:PRK15375  492 NPHsnlEQVRADFRNSRNNRMLEDASQFVQ 521

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: 42.57 E-value: 1.62e-04

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1709608747 539 MIDIIAAVQKQQQQSGNHPIVVHCSAGAGRTGTFIA 574
Cdd:cd14497    79 LLEIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVIC 114

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: 42.05 E-value: 2.63e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1709608747 231 LHFtswPDFGVPFSPIgMLKFLKKVKQVNpsyaGPIVVHCSAGVGRTGTFI 281
Cdd:cd14499    85 LYF---PDGSTPSDDI-VKKFLDICENEK----GAIAVHCKAGLGRTGTLI 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: 40.71 E-value: 3.92e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 250 KFLKKVKQVNpsyaGPIVVHCSAGVGRTGTFIVidAMIdMMYEEQKIDVFGFFVsriRDQRSQLVQTDmqySFIYQaLLE 329
Cdd:pfam00782  60 EFIDDARQKG----GKVLVHCQAGISRSATLII--AYL-MKTRNLSLNEAYSFV---KERRPGISPNF---GFKRQ-LLE 125


                  ..
gi 1709608747 330 YF 331
Cdd:pfam00782 126 YE 127

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: 41.11 E-value: 4.56e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709608747 555 NHPIVVHCSAGAGRTGTFIALSNILERvKAEGLldvfQTVKSLRMQRPHMVQTVH 609
Cdd:cd14504    82 NEAVLVHCLAGKGRTGTMLACYLVKTG-KISAV----DAINEIRRIRPGSIETSE 131

unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized subfamily belongs to the plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) group of atypical DSPs that present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. This unknown subgroup contains the conserved the CxxxxxR catalytic motif present in active cysteine phosphatases.

Pssm-ID: 350514 [Multi-domain] Cd Length: 145 Bit Score: 40.43 E-value: 6.52e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 519 VRHFHfhgwpeIGIPAEGKGMIDIIAAVQKQQQQ----SGNHPIVVHCSAGAGRTGTFIA 574
Cdd:cd18538    56 IQHFH------IAMLGNKDPKVSIPDHTMNRILRiildKENHPILVHCNKGKHRTGCVIA 109

Dual specificity phosphatase, catalytic domain;

Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 39.19 E-value: 1.47e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747  261 SYAGPIVVHCSAGVGRTGTFIVidAMIdMMYEEQKIDVFGFFVsriRDQRSQLVQTDmqySFIYQaLLEY 330
Cdd:smart00195  76 SKGGKVLVHCQAGVSRSATLII--AYL-MKTRNMSLNDAYDFV---KDRRPIISPNF---GFLRQ-LIEY 135

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: 38.59 E-value: 4.88e-03

                          10        20
                  ....*....|....*....|.
gi 1709608747 555 NHPIVVHCSAGAGRTGTFIAL 575
Cdd:cd14499   109 KGAIAVHCKAGLGRTGTLIAC 129

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

Pssm-ID: 350355 [Multi-domain] Cd Length: 163 Bit Score: 38.01 E-value: 5.86e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709608747 195 RVSVEDITVLV-DYTIRKFCV-----QYQASDgsktprlLTQLHFtSWPDFGVPFSPIGMLKFLKKVKQVNPSYAGpIVV 268
Cdd:cd14505    41 DQGVDDVVTLCtDGELEELGVpdlleQYQQAG-------ITWHHL-PIPDGGVPSDIAQWQELLEELLSALENGKK-VLI 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709608747 269 HCSAGVGRTGTfivIDA----MIDMMYEEQKIdvfgffVSRIRDQRSQLVQTDMQYSFIYQ 325
Cdd:cd14505   112 HCKGGLGRTGL---IAAclllELGDTLDPEQA------IAAVRALRPGAIQTPKQENFLHQ 163