NCBI Conserved Domain Search

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 258.74 E-value: 2.00e-80

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886   162 LFKGEYLMVNRsIDNNKCRCDVGSTM--MDRNPYPDTLPYDYNRVILPRIDGdENSHYINASYVNSWLRDKAYVVTQAvr 239
Cdd:smart00194   1 GLEEEFEKLDR-LKPDDESCTVAAFPenRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQG-- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886   240 tkPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL---TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPE 313
Cdd:smart00194  77 --PLpstVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDeegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886   314 siETRIVKHFHFTEWELDSFP-YISAFIELRRRVRQFMEKNpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFF 392
Cdd:smart00194 155 --ETRTVTHYHYTNWPDHGVPeSPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIF 230

                          250       260
                   ....*....|....*....|....*....
gi 392890886   393 EYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:smart00194 231 EIVKELRSQRPGMVQTEEQYIFLYRAILE 259

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 226.74 E-value: 7.88e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886  188 MDRNPYPDTLPYDYNRVILPriDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTK 264
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQG----PLPntvEDFWRMVWEEKVTIIVMLTE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886  265 VFDFMRVMCLQYWPLTKFQ---FREIEVETTEVKTY-SHFVIRTFKLTRTTPEsiETRIVKHFHFTEW-ELDSFPYISAF 339
Cdd:pfam00102  76 LEEKGREKCAQYWPEEEGEsleYGDFTVTLKKEKEDeKDYTVRTLEVSNGGSE--ETRTVKHFHYTGWpDHGVPESPNSL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886  340 IELRRRVRQfMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:pfam00102 154 LDLLRKVRK-SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                  ..
gi 392890886  420 SE 421
Cdd:pfam00102 233 LE 234

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: 221.39 E-value: 2.64e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL---TKFQFREIEVE 290
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQG----PLPntvEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEeggKPLEYGDITVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 291 TTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFP-YISAFIELRRRVRQFMEKNpvEAPMVVHCSNGAGR 369
Cdd:cd00047   77 LVSEEELSDYTIRTLELSPKGCS--ESREVTHLHYTGWPDHGVPsSPEDLLALVRRVRKEARKP--NGPIVVHCSAGVGR 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 392890886 370 SGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd00047  153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 206.36 E-value: 7.91e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886   473 DCAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 552
Cdd:smart00194  18 SCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDY--INASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886   553 TVVNLSNQGS------QRHYPSFIHnkGKANYGPFIVEIMNYHQYPAMTSHMVKVMKRTfmisdimatgaqnqqiDAEVR 626
Cdd:smart00194  96 VIVMLTELVEkgrekcAQYWPDEEG--EPLTYGDITVTLKSVEKVDDYTIRTLEVTNTG----------------CSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886   627 ICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKrapdrPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFH 706
Cdd:smart00194 158 TVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQS-----TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 392890886   707 AVKMMRINRPQLIDMKDEYKYLYDVMLH 734
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259

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

Pssm-ID: 350401 [Multi-domain] Cd Length: 238 Bit Score: 199.55 E-value: 1.06e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 266
Cdd:cd14553    6 KNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQG----PLPetfGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 267 DFMRVMCLQYWPLTKFQ-FREIEV---ETTEVKTYShfvIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIE 341
Cdd:cd14553   82 ERSRVKCDQYWPTRGTEtYGLIQVtllDTVELATYT---VRTFALHKNG--SSEKREVRQFQFTAWPDHGVPeHPTPFLA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 342 LRRRVRQFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 420
Cdd:cd14553  157 FLRRVKAC---NPPDAgPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233


                 ....*
gi 392890886 421 EAVMC 425
Cdd:cd14553  234 EAVTC 238

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: 182.95 E-value: 3.73e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 158 KKRILFKgEYLMVNRSIDNNKCRCDVGSTMMDRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQA 237
Cdd:cd14543    1 QKRGIYE-EYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 238 VRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTK---FQFREIEVETTEVKTYSHFVIRTFKLTRTtpES 314
Cdd:cd14543   80 PLPKTYS-DFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgssLRYGDLTVTNLSVENKEHYKKTTLEIHNT--ET 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 315 IETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQFME-----------KNPVEAPMVVHCSNGAGRSGAFLALDANLEL 382
Cdd:cd14543  157 DESRQVTHFQFTSWPDFGVPSSAAaLLDFLGEVRQQQAlavkamgdrwkGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQ 236

                        250       260       270
                 ....*....|....*....|....*....|....
gi 392890886 383 MKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 416
Cdd:cd14543  237 LEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270

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

Pssm-ID: 350396 [Multi-domain] Cd Length: 222 Bit Score: 175.62 E-value: 3.14e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 193 YPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVM 272
Cdd:cd14548    2 YTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKD-DFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 273 CLQYWPLTKFQ--FREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQF 349
Cdd:cd14548   81 CDHYWPFDQDPvyYGDITVTMLSESVLPDWTIREFKLERGD----EVRSVRQFHFTAWPDHGVPEAPDsLLRFVRLVRDY 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392890886 350 MEKNpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14548  157 IKQE--KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

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: 174.25 E-value: 1.60e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 266
Cdd:cd14554    9 KNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQG----PLAettEDFWRMLWEHNSTIIVMLTKLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 267 DFMRVMCLQYWPL-TKFQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYIS-AFIELRR 344
Cdd:cd14554   85 EMGREKCHQYWPAeRSARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTVRQFQFTDWPEQGVPKSGeGFIDFIG 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392890886 345 RVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 416
Cdd:cd14554  163 QVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234

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

Pssm-ID: 350474 [Multi-domain] Cd Length: 276 Bit Score: 173.30 E-value: 1.26e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 269
Cdd:cd14626   44 KNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETL-SDFWRMVWEQRTATIVMMTRLEEKS 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 270 RVMCLQYWPLTKFQ-FREIEV---ETTEVKTYShfvIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIELRR 344
Cdd:cd14626  123 RVKCDQYWPIRGTEtYGMIQVtllDTVELATYS---VRTFALYKNG--SSEKREVRQFQFMAWPDHGVPeYPTPILAFLR 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 345 RVRQFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 423
Cdd:cd14626  198 RVKAC---NPPDAgPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274


                 ..
gi 392890886 424 MC 425
Cdd:cd14626  275 TC 276

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: 168.28 E-value: 2.53e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 189 DRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKV 265
Cdd:cd14630    5 NKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQG----PMQEtvkDFWRMIWQENSASVVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 266 FDFMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPESIetRIVKHFHFTEWELDSFP-YISAFIELRR 344
Cdd:cd14630   81 VEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEI--REIRQFHFTSWPDHGVPcYATGLLGFVR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 345 RVRqFMekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 423
Cdd:cd14630  159 QVK-FL--NPPDAgPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEAC 235


                 ..
gi 392890886 424 MC 425
Cdd:cd14630  236 LC 237

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: 162.07 E-value: 1.24e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN---QGSQRHYPSFIHNKGK-ANYGPFIVEIMNY 588
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNlveKGREKCERYWPEEGGKpLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 589 HQYPAMTshmvkvmKRTFMISDIMatgaqnqqiDAEVRICCVIQVRMWPiENKVPLSTtglIDVIKMARSWRKRAPDRpe 668
Cdd:cd00047   81 EELSDYT-------IRTLELSPKG---------CSESREVTHLHYTGWP-DHGVPSSP---EDLLALVRRVRKEARKP-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392890886 669 TKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 730
Cdd:cd00047  139 NGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 160.87 E-value: 8.57e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886  482 NRGKNRDVMVVPPDHARPYLQtlhGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN-- 559
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT---GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEle 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886  560 ----QGSQRHYPSfiHNKGKANYGPFIVEIMNYHQYPAmtshmvKVMKRTFMIsdimatgaQNQQIDAEVRiccVIQVRM 635
Cdd:pfam00102  78 ekgrEKCAQYWPE--EEGESLEYGDFTVTLKKEKEDEK------DYTVRTLEV--------SNGGSEETRT---VKHFHY 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886  636 --WPiENKVPLSTTGLIDVIKMARSWRkrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRI 713
Cdd:pfam00102 139 tgWP-DHGVPESPNSLLDLLRKVRKSS----LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRS 213

                         250       260
                  ....*....|....*....|
gi 392890886  714 NRPQLIDMKDEYKYLYDVML 733
Cdd:pfam00102 214 QRPGMVQTLEQYIFLYDAIL 233

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: 160.19 E-value: 1.12e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 203 RVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL 279
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQG----PVHEtvyDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 280 TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPY-ISAFIELRRRVRqfMEKNPVEAP 358
Cdd:cd14631   77 DTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYN--EIREVKQFHFTGWPDHGVPYhATGLLSFIRRVK--LSNPPSAGP 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392890886 359 MVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 424
Cdd:cd14631  153 IVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218

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: 162.18 E-value: 1.39e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 269
Cdd:cd14625   50 KNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETF-GDFWRMVWEQRSATVVMMTKLEEKS 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 270 RVMCLQYWPLTKFQ-FREIEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIELRRRVR 347
Cdd:cd14625  129 RIKCDQYWPSRGTEtYGMIQVTLLDTIELATFCVRTFSLHKNG--SSEKREVRQFQFTAWPDHGVPeYPTPFLAFLRRVK 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392890886 348 QFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVMC 425
Cdd:cd14625  207 TC---NPPDAgPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282

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: 160.11 E-value: 1.44e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 193 YPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVM 272
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVN-DFWRMVWEQKSATIVMLTNLKERKEEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 273 CLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTTPESIE-TRIVKHFHFTEWELDSFPYISafIELRRRVRQFM 350
Cdd:cd14620   80 CYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKaPRLVTQLHFTSWPDFGVPFTP--IGMLKFLKKVK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392890886 351 EKNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14620  158 SVNPVHAgPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

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: 159.11 E-value: 1.77e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVfDFMRVMCLQYWPL-TKFQFREIEVETT 292
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQH----PLPntvTDFWRLVYDYGCTSIVMLNQL-DPKDQSCPQYWPDeGSGTYGPIQVEFV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 293 EVKTYSHFVIRTFKLTRTTPESIETRIVKHFHFTEW--ELDSFPYISAFIELRRRVRQFMEKNPvEAPMVVHCSNGAGRS 370
Cdd:cd14556   76 STTIDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWprDRDTPPSKRALLKLLSEVEKWQEQSG-EGPIVVHCLNGVGRS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 392890886 371 GAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14556  155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

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: 160.98 E-value: 2.93e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVF 266
Cdd:cd14633   43 KNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQG----PMQEtiyDFWRMVWHENTASIIMVTNLV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 267 DFMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYISAfiELRRRV 346
Cdd:cd14633  119 EVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVH--EIREIRQFHFTGWPDHGVPYHAT--GLLGFV 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392890886 347 RQFMEKNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 424
Cdd:cd14633  195 RQVKSKSPPNAgPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273

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: 158.51 E-value: 6.65e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 191 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMR 270
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVG-DFWRMIWEQQSSTIVMLTNCMEAGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 271 VMCLQYWPL--TKFQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPY-ISAFIELRRRVR 347
Cdd:cd14619   80 VKCEHYWPLdyTPCTYGHLRVTVVSEEVMENWTVREFLLKQV--EEQKTLSVRHFHFTAWPDHGVPSsTDTLLAFRRLLR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392890886 348 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd14619  158 QWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229

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: 159.90 E-value: 8.71e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 269
Cdd:cd14624   50 KNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETF-GDFWRMIWEQRSATVVMMTKLEERS 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 270 RVMCLQYWPL----TKFQFREIEVETTEVKTYshfVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIELRR 344
Cdd:cd14624  129 RVKCDQYWPSrgteTYGLIQVTLLDTVELATY---CVRTFALYKNG--SSEKREVRQFQFTAWPDHGVPeHPTPFLAFLR 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 345 RVRQFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 423
Cdd:cd14624  204 RVKTC---NPPDAgPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280


                 ..
gi 392890886 424 MC 425
Cdd:cd14624  281 TC 282

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: 156.75 E-value: 1.34e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAVRTKpMNAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTEVKT 296
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQE-MVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 297 YSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPY----ISAFIelrRRVRQfmeKNPVEA-PMVVHCSNGAGRSG 371
Cdd:cd14632   80 LAEYSVRTFALERRGYSARHE--VKQFHFTSWPEHGVPYhatgLLAFI---RRVKA---STPPDAgPVVVHCSAGAGRTG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392890886 372 AFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVMC 425
Cdd:cd14632  152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205

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: 155.85 E-value: 2.65e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTE 293
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQG----PMQEtvyDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 294 VKTYSHFVIRTFKLTRTTPESIetRIVKHFHFTEWELDSFPYISAfiELRRRVRQFMEKNPVEA-PMVVHCSNGAGRSGA 372
Cdd:cd14555   77 TEPLAEYVVRTFALERRGYHEI--REVRQFHFTGWPDHGVPYHAT--GLLGFIRRVKASNPPSAgPIVVHCSAGAGRTGC 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 392890886 373 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 424
Cdd:cd14555  153 YIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204

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: 154.72 E-value: 1.26e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 191 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMR 270
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIE-DFWRLVWEQQVCNIIMLTVGMENGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 271 VMCLQYWP--LTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFP----YISAFIELrr 344
Cdd:cd14618   80 VLCDHYWPseSTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLR--KERRVKHLHYTAWPDHGIPestsSLMAFREL-- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392890886 345 rVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd14618  156 -VREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229

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: 153.66 E-value: 1.42e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETT 292
Cdd:cd14549    1 YINANYVDGYNKARAYIATQG----PLPStfdDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 293 EVKTYSHFVIRTF-----KLTRTTPESIEtRIVKHFHFTEWE-----LDSFPYISaFielrrrVRQFMEKNPVEA-PMVV 361
Cdd:cd14549   77 STEVLATYTVRTFslknlKLKKVKGRSSE-RVVYQYHYTQWPdhgvpDYTLPVLS-F------VRKSSAANPPGAgPIVV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392890886 362 HCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14549  149 HCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204

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: 153.28 E-value: 3.80e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 197 LPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQY 276
Cdd:cd14623    6 IPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIE-DFWRMIWEWKSCSIVMLTELEERGQEKCAQY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 277 WPLT-KFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYI-SAFIELRRRVrQFMEKNP 354
Cdd:cd14623   85 WPSDgSVSYGDITIELKKEEECESYTVRDLLVTNTREN--KSRQIRQFHFHGWPEVGIPSDgKGMINIIAAV-QKQQQQS 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890886 355 VEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14623  162 GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

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

Pssm-ID: 350406 [Multi-domain] Cd Length: 203 Bit Score: 152.16 E-value: 5.31e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTE 293
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQG----PLPdtiADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 294 VKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEW---ELDSFPyiSAFIELRRRVRQ----FMEKNPVEAPMVVHCSNG 366
Cdd:cd14558   77 TEKSPTYTVRVFEITHL--KRKDSRTVYQYQYHKWkgeELPEKP--KDLVDMIKSIKQklpyKNSKHGRSVPIVVHCSDG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392890886 367 AGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14558  153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203

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: 150.11 E-value: 2.19e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETTEVK 295
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVE-DFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDgSVSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 296 TYSHFVIRTFKLTRTTPESieTRIVKHFHFTEWELDSFPY-ISAFIELRRRVrQFMEKNPVEAPMVVHCSNGAGRSGAFL 374
Cdd:cd14552   80 DYEDYTLRDFLVTKGKGGS--TRTVRQFHFHGWPEVGIPDnGKGMIDLIAAV-QKQQQQSGNHPITVHCSAGAGRTGTFC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 392890886 375 ALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd14552  157 ALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

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: 151.80 E-value: 8.39e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFM 269
Cdd:cd14629   56 KNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE-DFWRMLWEHNSTIVVMLTKLREMG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 270 RVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYI-SAFIELRRRVR 347
Cdd:cd14629  135 REKCHQYWPAERsARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTIRQFQFTDWPEQGVPKTgEGFIDFIGQVH 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890886 348 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14629  213 KTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286

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: 148.43 E-value: 1.83e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 191 NPYPDTLPYDYNRVILpRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMR 270
Cdd:cd14615    1 NRYNNVLPYDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVK-DFWRMVWEKNVYAIVMLTKCVEQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 271 VMCLQYWPLT-KFQFREIEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFPYIS-AFIELRRRVRQ 348
Cdd:cd14615   79 TKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQ--TNESRTVRHFHFTSWPDHGVPETTdLLINFRHLVRE 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890886 349 FMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFI 415
Cdd:cd14615  157 YMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223

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: 148.14 E-value: 2.75e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 191 NPYPDTLPYDYNRVILPRIDGDENSHYINASYV--NSWLRDkaYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKV 265
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIpgNNFRRE--YIATQG----PLPGtkdDFWKMVWEQNVHNIVMVTQC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 266 FDFMRVMCLQYWPLTK--FQFREIEVETTEVKTYSHFVIRTFKLTrtTPESIET-RIVKHFHFTEWELDSFPYIS-AFIE 341
Cdd:cd14617   75 VEKGRVKCDHYWPADQdsLYYGDLIVQMLSESVLPEWTIREFKIC--SEEQLDApRLVRHFHYTVWPDHGVPETTqSLIQ 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392890886 342 LRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14617  153 FVRTVRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 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: 149.88 E-value: 3.70e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKpMNAEFWRMVWELGSNCIVMLTKVFDFM 269
Cdd:cd14627   56 KNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAE-TTEDFWRMLWENNSTIVVMLTKLREMG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 270 RVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYI-SAFIELRRRVR 347
Cdd:cd14627  135 REKCHQYWPAERsARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTVRQFQFTDWPEQGVPKSgEGFIDFIGQVH 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890886 348 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14627  213 KTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286

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: 149.88 E-value: 4.17e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKpMNAEFWRMVWELGSNCIVMLTKVFDFM 269
Cdd:cd14628   55 KNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAE-TTEDFWRMLWEHNSTIVVMLTKLREMG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 270 RVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYI-SAFIELRRRVR 347
Cdd:cd14628  134 REKCHQYWPAERsARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTVRQFQFTDWPEQGVPKSgEGFIDFIGQVH 211

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890886 348 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14628  212 KTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285

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: 142.92 E-value: 1.96e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDenSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFM 269
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSG-HFWQMVWEQNSKAVIMLNKLMEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 270 RVMCLQYWPL-----TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYI-SAFIELR 343
Cdd:cd14545   78 QIKCAQYWPQgegnaMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQ--ETREVLHFHYTTWPDFGVPESpAAFLNFL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392890886 344 RRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKtGQLDFFEYAKTLVNSRPH---LIDSVEQYMFIY 416
Cdd:cd14545  156 QKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEK-GNPSSVDVKKVLLEMRKYrmgLIQTPDQLRFSY 230

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

Pssm-ID: 350470 [Multi-domain] Cd Length: 205 Bit Score: 140.91 E-value: 5.36e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETTEVK 295
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVE-DFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEgSVTHGEITIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 296 TYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYI-SAFIELRRRVrQFMEKNPVEAPMVVHCSNGAGRSGAFL 374
Cdd:cd14622   81 LLETISIRDFLVTYNQEK--QTRLVRQFHFHGWPEIGIPAEgKGMIDLIAAV-QKQQQQTGNHPIVVHCSAGAGRTGTFI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 392890886 375 ALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14622  158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204

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: 142.10 E-value: 1.35e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSH--YINASYVNSWLRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFD 267
Cdd:cd17667   30 KNRYINILAYDHSRVKLRPLPGKDSKHsdYINANYVDGYNKAKAYIATQG-PLKSTFEDFWRMIWEQNTGIIVMITNLVE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 268 FMRVMCLQYWPL-TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPESIET---------RIVKHFHFTEWELDSFP-YI 336
Cdd:cd17667  109 KGRRKCDQYWPTeNSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKgnpkgrqneRTVIQYHYTQWPDMGVPeYA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 337 SAFIELRRRVRQfmEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 416
Cdd:cd17667  189 LPVLTFVRRSSA--ARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266


                 ....*...
gi 392890886 417 EVLSEAVM 424
Cdd:cd17667  267 DALLEAIL 274

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: 139.45 E-value: 2.71e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 191 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSW-LRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 266
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQG----PLPntvADFWRMVWQEKTPIIVMITNLT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 267 DfMRVMCLQYWP-LTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYIS-AFIELRR 344
Cdd:cd14547   77 E-AKEKCAQYWPeEENETYGDFEVTVQSVKETDGYTVRKLTLKYGG----EKRYLKHYWYTSWPDHKTPEAAqPLLSLVQ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392890886 345 RVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 416
Cdd:cd14547  152 EVEEARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223

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: 136.22 E-value: 2.67e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVN-SWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFR--EIEVE 290
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQG----PLPAtigDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEygDLTVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 291 TTEVKTYSH--FVIRTFKLTRTTPESietRIVKHFHFTEW-ELDSFPYISAFIELRRRVRQFMEKNPVEAPMVVHCSNGA 367
Cdd:cd18533   77 LVSEEENDDggFIVREFELSKEDGKV---KKVYHIQYKSWpDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGV 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 368 GRSGAFLALDANLELMKKTGQLDFFEY------AKTlVNS----RPHLIDSVEQYMFIYE 417
Cdd:cd18533  154 GRTGTFIALDSLLDELKRGLSDSQDLEdsedpvYEI-VNQlrkqRMSMVQTLRQYIFLYD 212

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

Pssm-ID: 350462 [Multi-domain] Cd Length: 245 Bit Score: 136.56 E-value: 4.27e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFM 269
Cdd:cd14614   15 KNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRN-DFWKMVLQQKSQIIVMLTQCNEKR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 270 RVMCLQYWPLTK--FQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYISA---FIELRR 344
Cdd:cd14614   94 RVKCDHYWPFTEepVAYGDITVEMLSEEEQPDWAIREFRVSYAD----EVQDVMHFNYTAWPDHGVPTANAaesILQFVQ 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392890886 345 RVRQFMEKNPveAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14614  170 MVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240

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: 137.85 E-value: 6.81e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 189 DRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDF 268
Cdd:cd14621   54 EKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVN-DFWRMIWEQNTATIVMVTNLKER 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 269 MRVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTF------KLTRTTPEsietRIVKHFHFTEWELDSFPYISafIE 341
Cdd:cd14621  133 KECKCAQYWPDQGcWTYGNIRVSVEDVTVLVDYTVRKFciqqvgDVTNKKPQ----RLITQFHFTSWPDFGVPFTP--IG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 342 LRRRVRQFMEKNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 420
Cdd:cd14621  207 MLKFLKKVKNCNPQYAgAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286


                 .
gi 392890886 421 E 421
Cdd:cd14621  287 E 287

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: 135.15 E-value: 3.72e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 189 DRNPYPDTLPYDYNRVILPRIDGDenshYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKV 265
Cdd:cd14608   27 NRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQG----PLPntcGHFWEMVWEQKSRGVVMLNRV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 266 FDFMRVMCLQYWPltKFQFREIEVETTEVK-------TYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYISA 338
Cdd:cd14608   99 MEKGSLKCAQYWP--QKEEKEMIFEDTNLKltlisedIKSYYTVRQLELENLTTQ--ETREILHFHYTTWPDFGVPESPA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 339 -FIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPH---LIDSVEQYMF 414
Cdd:cd14608  175 sFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFrmgLIQTADQLRF 254


                 ..
gi 392890886 415 IY 416
Cdd:cd14608  255 SY 256

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: 132.15 E-value: 4.39e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLsNQGSQRH--YPSFIHNKGKANYGPFIVEIMNyhq 590
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDqsCPQYWPDEGSGTYGPIQVEFVS--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 591 ypamTSHMVKVMKRTFMISDIMATgaqnqqiDAEVRICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRAPDrpetK 670
Cdd:cd14556   77 ----TTIDEDVISRIFRLQNTTRP-------QEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGE----G 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 671 PTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 730
Cdd:cd14556  142 PIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

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: 131.19 E-value: 1.14e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETTEVK 295
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVN-DFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQgCWTYGNLRVRVEDTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 296 TYSHFVIRTFKLTRTTPESIE--TRIVKHFHFTEWELDSFPYISafIELRRRVRQFMEKNPVEA-PMVVHCSNGAGRSGA 372
Cdd:cd14551   80 VLVDYTTRKFCIQKVNRGIGEkrVRLVTQFHFTSWPDFGVPFTP--IGMLKFLKKVKSANPPRAgPIVVHCSAGVGRTGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 392890886 373 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14551  158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

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: 130.33 E-value: 1.93e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT---KFQFREIEVETTE 293
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVD-DFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMeegSRAFGDVVVKINE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 294 VKTYSHFVIRTFKLTRTTpESIETRIVKHFHFTEWELDSFPY-ISAFIELRRRVRQFmeKNPVEAPMVVHCSNGAGRSGA 372
Cdd:cd14557   80 EKICPDYIIRKLNINNKK-EKGSGREVTHIQFTSWPDHGVPEdPHLLLKLRRRVNAF--NNFFSGPIVVHCSAGVGRTGT 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 392890886 373 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14557  157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

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

Pssm-ID: 350457 [Multi-domain] Cd Length: 281 Bit Score: 132.08 E-value: 3.89e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 150 VAYVQE--RRKKRILFKGEYLMVNRSiDNNKCRCDVGSTMMDRNPYPDTLPYDYNRVILPRIDGDENSHYINAS-YVNSW 226
Cdd:cd14609    4 LAYMEDhlRNRDRLAKEWQALCAYQA-EPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 227 LRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWP---LTKFQFREIEVETTEVKTySHFVIR 303
Cdd:cd14609   83 PRMPAYIATQGPLSHTI-ADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPdegSSLYHIYEVNLVSEHIWC-EDFLVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 304 TFKLTRTtpESIETRIVKHFHFTEWELDSFPYIS-AFIELRRRVRQFMEKNpvEAPMVVHCSNGAGRSGAFLALDANLEL 382
Cdd:cd14609  161 SFYLKNV--QTQETRTLTQFHFLSWPAEGIPSSTrPLLDFRRKVNKCYRGR--SCPIIVHCSDGAGRTGTYILIDMVLNR 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 392890886 383 MKK-TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 423
Cdd:cd14609  237 MAKgVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278

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: 131.87 E-value: 3.96e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 154 QERRKKRILFKGEYlmvnrsidnnKCRCDVGSTM--MDRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKA 231
Cdd:cd14603    5 SEIRACSAAFKADY----------VCSTVAGGRKenVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 232 YVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKfqfreievettEVKTYSHFVIRTFKLT 308
Cdd:cd14603   75 YIATQG----PLSHtvlDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQ-----------EPLQTGPFTITLVKEK 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 309 RTTPESI----------ETRIVKHFHFTEWE----LDSFPYISAFIELrrrVRQFMEKNPVeaPMVVHCSNGAGRSGAFL 374
Cdd:cd14603  140 RLNEEVIlrtlkvtfqkESRSVSHFQYMAWPdhgiPDSPDCMLAMIEL---ARRLQGSGPE--PLCVHCSAGCGRTGVIC 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 392890886 375 ALD-ANLELMKKTGQLDF--FEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14603  215 TVDyVRQLLLTQRIPPDFsiFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264

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: 130.56 E-value: 1.41e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 188 MDRNPYPDTLPYDYNRVILPRIDGDENSHYINASYV-NSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVF 266
Cdd:cd14610   45 VQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImDHDPRNPAYIATQGPLPATV-ADFWQMVWESGCVVIVMLTPLA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 267 DFMRVMCLQYWPLTKFQFREI-EVETTEVKTYSH-FVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYIS-AFIELR 343
Cdd:cd14610  124 ENGVKQCYHYWPDEGSNLYHIyEVNLVSEHIWCEdFLVRSFYLKNL--QTNETRTVTQFHFLSWNDQGVPASTrSLLDFR 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 344 RRVRQFMEKNpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTG-QLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEA 422
Cdd:cd14610  202 RKVNKCYRGR--SCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEE 279


                 .
gi 392890886 423 V 423
Cdd:cd14610  280 V 280

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: 128.73 E-value: 2.59e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDE-NSHYINASYVNSWL-------RDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVM 261
Cdd:cd14544    4 KNRYKNILPFDHTRVILKDRDPNVpGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVS-DFWSMVWQENSRVIVM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 262 LTKVFDFMRVMCLQYWP--LTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpESIETRIVKHFHFTEWE---LDSFPY- 335
Cdd:cd14544   83 TTKEVERGKNKCVRYWPdeGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLD-QGDPIREIWHYQYLSWPdhgVPSDPGg 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 336 ISAFIElrrRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTG---QLDFFEYAKTLVNSRPHLIDSVEQY 412
Cdd:cd14544  162 VLNFLE---DVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQY 238


                 ....
gi 392890886 413 MFIY 416
Cdd:cd14544  239 KFIY 242

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: 126.25 E-value: 7.32e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL-TKFQFREIEVETTEVK 295
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQG-PLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAdGSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 296 TYSHFVIRTFKLTRTTPES------IETRIVKHFHFTEWELDSFP-YISAFIELRRRVRQfmEKNPVEAPMVVHCSNGAG 368
Cdd:cd17668   80 VLAYYTVRNFTLRNTKIKKgsqkgrPSGRVVTQYHYTQWPDMGVPeYTLPVLTFVRKASY--AKRHAVGPVVVHCSAGVG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392890886 369 RSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd17668  158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208

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: 125.95 E-value: 9.28e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKA--YVVTQAvrtkPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWP----LTKFQFREI 287
Cdd:cd14538    1 YINASHIRIPVGGDTyhYIACQG----PLpntTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslnKPLICGGRL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 288 EVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPyiSAFIELRRRVRqFMEKNPVEAPMVVHCSNGA 367
Cdd:cd14538   77 EVSLEKYQSLQDFVIRRISLRDK--ETGEVHHITHLNFTTWPDHGTP--QSADPLLRFIR-YMRRIHNSGPIVVHCSAGI 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392890886 368 GRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEA 422
Cdd:cd14538  152 GRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206

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: 126.52 E-value: 2.27e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRID-GDENSHYINASYVNSW-LRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFD 267
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYgGEEKVYIATQG-PTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 268 fMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFP-YISAFIELRRRV 346
Cdd:cd14613  107 -MNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG----EERGLKHYWYTSWPDQKTPdNAPPLLQLVQEV 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392890886 347 RQFMEK-NPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 420
Cdd:cd14613  182 EEARQQaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256

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: 125.71 E-value: 2.53e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV---NL 557
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPIRGvEGSDY--INASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVmltKL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 558 SNQGSQRHYPSFIHNKGkANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVRMWP 637
Cdd:cd14554   84 REMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTVRQFQFTDWP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 638 iENKVPLSTTGLIDVIKMARswrKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQ 717
Cdd:cd14554  147 -EQGVPKSGEGFIDFIGQVH---KTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPA 222

                        250
                 ....*....|..
gi 392890886 718 LIDMKDEYKYLY 729
Cdd:cd14554  223 MVQTEDQYQFCY 234

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: 126.89 E-value: 2.59e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 188 MDRNPYPDTLPYDYNRVILpridgDENSHYINASYVNSWLrDKAYVVTQAVRTK-PMN---AEFWRMVWELGSNCIVMLT 263
Cdd:cd14600   41 MDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNMEI-PSANIVNKYIATQgPLPhtcAQFWQVVWEQKLSLIVMLT 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 264 KVFDFMRVMCLQYWPltkfqfreievETTEVKTYSHF-------------VIRTFKLTRTtpESIETRIVKHFHFTEWEL 330
Cdd:cd14600  115 TLTERGRTKCHQYWP-----------DPPDVMEYGGFrvqchsedctiayVFREMLLTNT--QTGEERTVTHLQYVAWPD 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 331 DSFPYISA-FIELRRRVRQFMEKNpveAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSV 409
Cdd:cd14600  182 HGVPDDSSdFLEFVNYVRSKRVEN---EPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTS 258

                        250
                 ....*....|
gi 392890886 410 EQYMFIYEVL 419
Cdd:cd14600  259 SQYKFVCEAI 268

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: 125.34 E-value: 3.00e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 266
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQG----PLSttlLDFWRMIWEYSVLIIVMACMEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 267 DFMRVMCLQYWPLT---KFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPY-ISAFIEL 342
Cdd:cd14602   77 EMGKKKCERYWAEPgemQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS----ETRTIYQFHYKNWPDHDVPSsIDPILEL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 343 RRRVRQFMEKNPVeaPMVVHCSNGAGRSGAFLALDANLELMKK---TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd14602  153 IWDVRCYQEDDSV--PICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230


                 ..
gi 392890886 420 SE 421
Cdd:cd14602  231 IE 232

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: 124.63 E-value: 4.32e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 191 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMR 270
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTV-GDFWRMVWETRAKTIVMLTQCFEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 271 VMCLQYWPLTKFQ---FREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYISA----FIELR 343
Cdd:cd14616   80 IRCHQYWPEDNKPvtvFGDIVITKLMEDVQIDWTIRDLKIERHG----DYMMVRQCNFTSWPEHGVPESSAplihFVKLV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890886 344 RRVRQfmEKNpveAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14616  156 RASRA--HDN---TPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

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: 123.21 E-value: 8.37e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVfDFMRvMCLQYWP-LTKFQFREIEVETTEVK 295
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTV-ADFWRLVFDYNCSSVVMLNEM-DAAQ-LCMQYWPeKTSCCYGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 296 TYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEK-NPVEAPMVVHCSNGAGRSGA 372
Cdd:cd14634   78 IDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAyrDTPPSKRSILKVVRRLEKWQEQyDGREGRTVVHCLNGGGRSGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392890886 373 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14634  158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 125.50 E-value: 1.51e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 146 ASKFVAYVQERRKKRILfKGEYLMVNRSIDNNKCRCDVGSTMMDRNPYPDTLPYDYNRVILPRIDGdeNSHYINASYVNS 225
Cdd:PHA02742  12 AKNCEQLIEESNLAEIL-KEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 226 WLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYW---PLTKFQFREIEVETTEVKTYSHFVI 302
Cdd:PHA02742  89 HNAKGRFICTQAPLEETAL-DFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmphERGKATHGEFKIKTKKIKSFRNYAV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 303 RTFKLTRT-TPESIEtriVKHFHFTEWELDSFPY-ISAFIELRRRVRQFMEKNPV---------EAPMVVHCSNGAGRSG 371
Cdd:PHA02742 168 TNLCLTDTnTGASLD---IKHFAYEDWPHGGLPRdPNKFLDFVLAVREADLKADVdikgenivkEPPILVHCSAGLDRAG 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 392890886 372 AFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 416
Cdd:PHA02742 245 AFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289

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: 123.54 E-value: 1.98e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDenshYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 266
Cdd:cd14607   27 RNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQG----PLPntcCHFWLMVWQQKTKAVVMLNRIV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 267 DFMRVMCLQYWPLTK---FQFRE----IEVETTEVKTYshFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYISA- 338
Cdd:cd14607   99 EKDSVKCAQYWPTDEeevLSFKEtgfsVKLLSEDVKSY--YTVHLLQLENI--NSGETRTISHFHYTTWPDFGVPESPAs 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 339 FIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDfFEYAKTLVNSRPH---LIDSVEQYMFI 415
Cdd:cd14607  175 FLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDS-VDIKQVLLDMRKYrmgLIQTPDQLRFS 253


                 .
gi 392890886 416 Y 416
Cdd:cd14607  254 Y 254

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: 120.41 E-value: 1.26e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVIL-PRIDGDENSHYINASYVNSWL-RDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFD 267
Cdd:cd14611    2 KNRYKTILPNPHSRVCLkPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVN-DFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 268 fMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFP-YISAFIELRRRV 346
Cdd:cd14611   81 -KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGS----QSRSVKHYWYTSWPDHKTPdSAQPLLQLMLDV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 347 RQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 416
Cdd:cd14611  156 EEDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225

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: 118.97 E-value: 2.45e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVN-----SWLRDKaYVVTQAvrtkPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT--KFQFRE 286
Cdd:cd14541    2 YINANYVNmeipgSGIVNR-YIAAQG----PLpntCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLgeTMQFGN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 287 IEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQFmEKNPVEaPMVVHCSN 365
Cdd:cd14541   77 LQITCVSEEVTPSFAFREFILTNT--NTGEERHITQMQYLAWPDHGVPDDSSdFLDFVKRVRQN-RVGMVE-PTVVHCSA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 392890886 366 GAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14541  153 GIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCE 204

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: 119.94 E-value: 3.22e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDG-DENSHYINASYVNSWL-RDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTK 264
Cdd:cd14612   18 KDRYKTILPNPQSRVCLRRAGSqEEEGSYINANYIRGYDgKEKAYIATQG----PMLntvSDFWEMVWQEECPIIVMITK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 265 VFDfMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFkltrTTPESIETRIVKHFHFTEWELDSFPYIS-AFIELR 343
Cdd:cd14612   94 LKE-KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDL----TIQLEEESRSVKHYWFSSWPDHQTPESAgPLLRLV 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890886 344 RRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 420
Cdd:cd14612  169 AEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLA 245

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: 118.78 E-value: 5.03e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILpridGDENShYINASYVNSWLRDKAYVVTQAVRTKPMN-AEFWRMVWELGSNCIVMLTKVFDF 268
Cdd:cd14597    6 KNRYKNILPYDTTRVPL----GDEGG-YINASFIKMPVGDEEFVYIACQGPLPTTvADFWQMVWEQKSTVIAMMTQEVEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 269 MRVMCLQYWP--LTKFQFREIEVETTEVKT--YSHFVIRTFKLTRTtpESIETRIVKHFHFTEW---ELDSFPY-ISAFI 340
Cdd:cd14597   81 GKIKCQRYWPeiLGKTTMVDNRLQLTLVRMqqLKNFVIRVLELEDI--QTREVRHITHLNFTAWpdhDTPSQPEqLLTFI 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392890886 341 ELRRRVRQfmeknpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd14597  159 SYMRHIHK-------SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230

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: 117.93 E-value: 5.93e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYV-NSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIeVETTEVK 295
Cdd:cd14546    1 YINASTIyDHDPRNPAYIATQGPLPHTI-ADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHI-YEVHLVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 296 TYS---HFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPY-ISAFIELRRRV-RQFMEKNpveAPMVVHCSNGAGRS 370
Cdd:cd14546   79 EHIwcdDYLVRSFYLKNL--QTSETRTVTQFHFLSWPDEGIPAsAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAGRT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392890886 371 GAFLALDANLE-LMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 423
Cdd:cd14546  154 GTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207

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: 116.77 E-value: 1.31e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKA--YVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWP--------LTKFQFRe 286
Cdd:cd14596    1 YINASYITMPVGEEElfYIATQGPLPSTID-DFWQMVWENRSDVIAMMTREVERGKVKCHRYWPetlqepmeLENYQLR- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 287 ieVETTEVKTYshFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYISA----FIELRRRVRQfmeknpvEAPMVVH 362
Cdd:cd14596   79 --LENYQALQY--FIIRIIKLVEK--ETGENRLIKHLQFTTWPDHGTPQSSDqlvkFICYMRKVHN-------TGPIVVH 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392890886 363 CSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 423
Cdd:cd14596  146 CSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206

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: 116.55 E-value: 1.58e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTqavrTKPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVM-CLQYWPLTKFQ-FREIEVET 291
Cdd:cd14637    1 YINAALTDSYTRSAAFIVT----LHPLQnttTDFWRLVYDYGCTSVVMLNQLNQSNSAWpCLQYWPEPGLQqYGPMEVEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 292 TEVKTYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEKNPvEAPMVVHCSNGAGR 369
Cdd:cd14637   77 VSGSADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAyrDTPDSKKAFLHLLASVEKWQRESG-EGRTVVHCLNGGGR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 392890886 370 SGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14637  156 SGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207

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: 116.02 E-value: 3.70e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKA--YVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWP-----LTKFQFRE 286
Cdd:cd14540    1 YINASHITATVGGKQrfYIAAQG----PLQNtvgDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggeHDALTFGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 287 IEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEW-------ELDSF-PYISAFIELRRRVRQFMEKNPVEAP 358
Cdd:cd14540   77 YKVSTKFSVSSGCYTTTGLRVKHTL--SGQSRTVWHLQYTDWpdhgcpeDVSGFlDFLEEINSVRRHTNQDVAGHNRNPP 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392890886 359 MVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd14540  155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVL 215

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: 117.04 E-value: 3.74e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 189 DRNPYPDTLPYDYNRVILPriDGDEN---SHYINASYV---------NSWLRdKAYVVTQAVRTKPMNaEFWRMVWELGS 256
Cdd:cd14605    4 NKNRYKNILPFDHTRVVLH--DGDPNepvSDYINANIImpefetkcnNSKPK-KSYIATQGCLQNTVN-DFWRMVFQENS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 257 NCIVMLTKVFDFMRVMCLQYWPlTKFQFRE---IEVETTEVKTYSHFVIRTFKLTRTTPESIEtRIVKHFHFTEWELDSF 333
Cdd:cd14605   80 RVIVMTTKEVERGKSKCVKYWP-DEYALKEygvMRVRNVKESAAHDYILRELKLSKVGQGNTE-RTVWQYHFRTWPDHGV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 334 PY-ISAFIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTG---QLDFFEYAKTLVNSRPHLIDSV 409
Cdd:cd14605  158 PSdPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTE 237


                 ....*..
gi 392890886 410 EQYMFIY 416
Cdd:cd14605  238 AQYRFIY 244

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: 114.83 E-value: 4.62e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTK---FQFREIEVETTE 293
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVL-DFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeeqLQFGPFKISLEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 294 VKTYSH-FVIRTFKLTRTTpesiETRIVKHFHFTEW-ELDSFPYISAFIELRRRVRQFMEKNPVeaPMVVHCSNGAGRSG 371
Cdd:cd14542   80 EKRVGPdFLIRTLKVTFQK----ESRTVYQFHYTAWpDHGVPSSVDPILDLVRLVRDYQGSEDV--PICVHCSAGCGRTG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 392890886 372 AFLALDANLELMKK---TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 416
Cdd:cd14542  154 TICAIDYVWNLLKTgkiPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 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: 114.37 E-value: 1.21e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 491 VVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN---QGSQR--H 565
Cdd:cd14548    5 ILPYDHSRVKLIPINEEEGS-DYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQcmeKGRVKcdH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 566 YPSFihNKGKANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISDImatgaqnqqidAEVRICCVIQVRMWPiENKVPLS 645
Cdd:cd14548   84 YWPF--DQDPVYYGDITVTMLSESVLPDWT-------IREFKLERG-----------DEVRSVRQFHFTAWP-DHGVPEA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 646 TTGLIDVIKMARSWRKRapdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEY 725
Cdd:cd14548  143 PDSLLRFVRLVRDYIKQ-----EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQY 217


                 ....
gi 392890886 726 KYLY 729
Cdd:cd14548  218 IFLH 221

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 116.18 E-value: 3.31e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 191 NPYPDTLPYDYNRVILP--RIDGDenshYINASYVNSWLRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFDF 268
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPaeRNRGD----YINANYVDGFEYKKKFICGQA-PTRQTCYDFYRMLWMEHVQIIVMLCKKKEN 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 269 MRVMCLQYW---PLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpESIETriVKHFHFTEWELDSFP-----YISAFI 340
Cdd:PHA02738 128 GREKCFPYWsdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQT--VTHFNFTAWPDHDVPkntseFLNFVL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 341 ELRRRVRQFME-------KNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYM 413
Cdd:PHA02738 205 EVRQCQKELAQeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                 ....*.
gi 392890886 414 FIYEVL 419
Cdd:PHA02738 285 FCYRAV 290

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 115.10 E-value: 6.69e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILpRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 266
Cdd:PHA02747  54 KNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQG----PFAetcADFWKAVWQEHCSIIVMLTPTK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 267 DFM-RVMCLQYWPLTK---FQFREIEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP----YISA 338
Cdd:PHA02747 129 GTNgEEKCYQYWCLNEdgnIDMEDFRIETLKTSVRAKYILTLIEITDKI--LKDSRKISHFQCSEWFEDETPsdhpDFIK 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 339 FIELRRRVRQ-----FMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYM 413
Cdd:PHA02747 207 FIKIIDINRKksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                 ....*....
gi 392890886 414 FI---YEVL 419
Cdd:PHA02747 287 FIqpgYEVL 295

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 107.83 E-value: 9.64e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886   319 IVKHFHFTEWELDSFPYIS-AFIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLE-LMKKTGQLDFFEYAK 396
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPdSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQqLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 392890886   397 TLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.

Pssm-ID: 214469 [Multi-domain] Cd Length: 105 Bit Score: 107.83 E-value: 9.64e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886   319 IVKHFHFTEWELDSFPYIS-AFIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLE-LMKKTGQLDFFEYAK 396
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPdSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQqLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 392890886   397 TLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105

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: 110.89 E-value: 1.43e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVfDFMRvMCLQYWPLT-KFQFREIEVETTEVK 295
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVK-DFWRLVYDYGCTSIVMLNEV-DLAQ-GCPQYWPEEgMLRYGPIQVECMSCS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 296 TYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWELDSFPYIS--AFIELRRRVRQFMEK-NPVEAPMVVHCSNGAGRSGA 372
Cdd:cd14636   78 MDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSkrSFLKLILQVEKWQEEcDEGEGRTIIHCLNGGGRSGM 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392890886 373 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14636  158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206

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: 111.95 E-value: 5.17e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 269
Cdd:cd14604   60 KNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTV-IDFWRMIWEYNVAIIVMACREFEMG 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 270 RVMCLQYWPL---TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWE----LDSFPYISAFIEL 342
Cdd:cd14604  139 RKKCERYWPLygeEPMTFGPFRISCEAEQARTDYFIRTLLLEFQN----ETRRLYQFHYVNWPdhdvPSSFDSILDMISL 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 343 rrrVRQFMEKNPVeaPMVVHCSNGAGRSGAFLALDANLELMKK---TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd14604  215 ---MRKYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289


                 ..
gi 392890886 420 SE 421
Cdd:cd14604  290 AQ 291

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: 108.57 E-value: 1.04e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNyhqyp 592
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMS----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 593 amTSHMVKVMKRTFMISDImatgAQNQQIDAEVRiccVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRApDRPETKpT 672
Cdd:cd14636   76 --CSMDCDVISRIFRICNL----TRPQEGYLMVQ---QFQYLGWASHREVPGSKRSFLKLILQVEKWQEEC-DEGEGR-T 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392890886 673 IVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd14636  145 IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205

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: 107.08 E-value: 2.82e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMrvMCLQYWPLTKF-QFREIEVETTEVK 295
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVK-DFWRLVLDYHCTSIVMLNDVDPAQ--LCPQYWPENGVhRHGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 296 TYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEK-NPVEAPMVVHCSNGAGRSGA 372
Cdd:cd14635   78 LEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMyrDTPVSKRSFLKLIRQVDKWQEEyNGGEGRTVVHCLNGGGRSGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392890886 373 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 421
Cdd:cd14635  158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206

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

Pssm-ID: 350483 [Multi-domain] Cd Length: 206 Bit Score: 106.31 E-value: 5.06e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNYHQYP 592
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 593 AMTSHMVKVMkrtfmisdimaTGAQNQQidaEVRICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRApDRPETKpT 672
Cdd:cd14635   81 DIISRIFRIY-----------NAARPQD---GYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEY-NGGEGR-T 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392890886 673 IVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd14635  145 VVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205

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: 108.67 E-value: 5.46e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN- 559
Cdd:cd14628   52 NKFKNRLVNIMPYESTRVCLQPIRGvEGSDY--INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKl 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 560 -----QGSQRHYPSfihnKGKANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVR 634
Cdd:cd14628  130 remgrEKCHQYWPA----ERSARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTVRQFQFT 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 635 MWPiENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 714
Cdd:cd14628  190 DWP-EQGVPKSGEGFIDFIGQVHKTKEQFG---QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 265

                        250       260
                 ....*....|....*....|.
gi 392890886 715 RPQLIDMKDEYKYLYDVMLHW 735
Cdd:cd14628  266 RPAMVQTEDQYQFCYRAALEY 286

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: 108.67 E-value: 6.57e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN- 559
Cdd:cd14627   53 NKFKNRLVNIMPYETTRVCLQPIRGvEGSDY--INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKl 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 560 -----QGSQRHYPSfihnKGKANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVR 634
Cdd:cd14627  131 remgrEKCHQYWPA----ERSARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTVRQFQFT 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 635 MWPiENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 714
Cdd:cd14627  191 DWP-EQGVPKSGEGFIDFIGQVHKTKEQFG---QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 266

                        250       260
                 ....*....|....*....|.
gi 392890886 715 RPQLIDMKDEYKYLYDVMLHW 735
Cdd:cd14627  267 RPAMVQTEDEYQFCYQAALEY 287

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: 105.38 E-value: 1.38e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--NQgSQRHYPSFIH--NKGKANYGPFIVEIMNy 588
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqlNQ-SNSAWPCLQYwpEPGLQQYGPMEVEFVS- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 589 hqypamTSHMVKVMKRTFMISDImaTGAQNQQIdaevrICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRAPDrpe 668
Cdd:cd14637   79 ------GSADEDIVTRLFRVQNI--TRLQEGHL-----MVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGE--- 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392890886 669 tKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd14637  143 -GRTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206

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: 104.58 E-value: 7.86e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 190 RNPYPDTLPYDYNRVILPriDGDEN---SHYINASYVNS--WLRD---KAYVVTQAVRTKPMNaEFWRMVWELGSNCIVM 261
Cdd:cd14606   21 KNRYKNILPFDHSRVILQ--GRDSNipgSDYINANYVKNqlLGPDenaKTYIASQGCLEATVN-DFWQMAWQENSRVIVM 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 262 LTKVFDFMRVMCLQYWPLTKFQ--FREIEVETTEVKTYSHFVIRTFKLtrTTPESIET-RIVKHFHFTEWELDSFPY--- 335
Cdd:cd14606   98 TTREVEKGRNKCVPYWPEVGMQraYGPYSVTNCGEHDTTEYKLRTLQV--SPLDNGELiREIWHYQYLSWPDHGVPSepg 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 336 -ISAFIElrrRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTG---QLDFFEYAKTLVNSRPHLIDSVEQ 411
Cdd:cd14606  176 gVLSFLD---QINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEAQ 252


                 ....*
gi 392890886 412 YMFIY 416
Cdd:cd14606  253 YKFIY 257

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: 100.87 E-value: 4.16e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNyhqyp 592
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVS----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 593 amTSHMVKVMKRTFMISDImatgAQNQQidaEVRICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRApDRPETKpT 672
Cdd:cd14634   76 --ADIDEDIISRIFRICNM----ARPQD---GYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQY-DGREGR-T 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890886 673 IVMSHNGVSRVGVYIG-ANIC--IDQMDIdheVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd14634  145 VVHCLNGGGRSGTFCAiCSVCemIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205

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: 100.54 E-value: 4.90e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINAS----YVNSWLRdkaYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQ---FRE 286
Cdd:cd14539    1 YINASliedLTPYCPR---FIATQA----PLPgtaADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQalvYGA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 287 IEVETTEVKTYSHFVIRTFKLTrtTPESIETRIVKHFHFTEW-ELDSFPYISAFIELRRRVRQFMEK-NPVEAPMVVHCS 364
Cdd:cd14539   74 ITVSLQSVRTTPTHVERIISIQ--HKDTRLSRSVVHLQFTTWpELGLPDSPNPLLRFIEEVHSHYLQqRSLQTPIVVHCS 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392890886 365 NGAGRSGAF-LALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14539  152 SGVGRTGAFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

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: 100.08 E-value: 7.80e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS------NQGSQRHYPSfihnKGKANYGPFIVEIM 586
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTelqereQEKCVQYWPS----EGSVTHGEITIEIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 587 NyhqypamtshmvKVMKRTFMISDIMATGAQNQQidaeVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDR 666
Cdd:cd14622   78 N------------DTLLETISIRDFLVTYNQEKQ----TRLVRQFHFHGWP-EIGIPAEGKGMIDLIAAVQKQQQQTGNH 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392890886 667 petkPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVM 732
Cdd:cd14622  141 ----PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202

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: 100.96 E-value: 2.47e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN- 559
Cdd:cd14629   53 NKFKNRLVNIMPYELTRVCLQPIRGvEGSDY--INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKl 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 560 -----QGSQRHYPSfihnKGKANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVR 634
Cdd:cd14629  131 remgrEKCHQYWPA----ERSARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTIRQFQFT 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 635 MWPiENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 714
Cdd:cd14629  191 DWP-EQGVPKTGEGFIDFIGQVHKTKEQFG---QDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQ 266

                        250       260
                 ....*....|....*....|.
gi 392890886 715 RPQLIDMKDEYKYLYDVMLHW 735
Cdd:cd14629  267 RPAMVQTEDQYQLCYRAALEY 287

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

Pssm-ID: 350398 [Multi-domain] Cd Length: 200 Bit Score: 97.78 E-value: 3.74e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQavrtKPMN---AEFWRMVWELGSNCIVMLTKvfDFMRVMCLQYWPLtkfQFREIEVETTE 293
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQ----HPLEhtiKDFWQMIWDHNSQTIVMLTD--NELNEDEPIYWPT---KEKPLECETFK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 294 VK----------TYSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPYISAFiELRRRVRQfmEKNPVEAPMVVHC 363
Cdd:cd14550   72 VTlsgedhsclsNEIRLIVRDFILESTQDDYVLE--VRQFQCPSWPNPCSPIHTVF-ELINTVQE--WAQQRDGPIVVHD 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392890886 364 SNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 417
Cdd:cd14550  147 RYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

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: 98.09 E-value: 6.86e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 486 NRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS---NQGS 562
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHS-DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmENGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 563 ---QRHYPSfihNKGKANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMIsdimatgaQNQQIDAEVRICcVIQVRMWPiE 639
Cdd:cd14618   80 vlcDHYWPS---ESTPVSYGHITVHLLAQSSEDEWT-------RREFKL--------WHEDLRKERRVK-HLHYTAWP-D 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 640 NKVPLSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 719
Cdd:cd14618  140 HGIPESTSSLMAFRELVREHVQATKGK---GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMI 216

                        250
                 ....*....|....
gi 392890886 720 DMKDEYKYLYDVML 733
Cdd:cd14618  217 QTLSQYIFLHSCIL 230

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 100.49 E-value: 7.30e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 199 YDYNRVILPRIDGDENshYINASYVNSWLRDKAYVVTQAVRtKPMNAEFWRMVWELGSNCIVMLTKVFDFMRVmCLQYWP 278
Cdd:PHA02746  84 SDGKKIEVTSEDNAEN--YIHANFVDGFKEANKFICAQGPK-EDTSEDFFKLISEHESQVIVSLTDIDDDDEK-CFELWT 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 279 LTK---FQFREIEVETTEVKTYSHFVIRTFKLTRTTPESieTRIVKHFHFTEWELDSFPY-ISAFIELRRRV---RQFME 351
Cdd:PHA02746 160 KEEdseLAFGRFVAKILDIIEELSFTKTRLMITDKISDT--SREIHHFWFPDWPDNGIPTgMAEFLELINKVneeQAELI 237

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392890886 352 KN-----PVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 424
Cdd:PHA02746 238 KQadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315

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: 99.33 E-value: 1.12e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 474 CAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGeSKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHT 553
Cdd:cd14621   44 CEAASKEENKEKNRYVNILPYDHSRVHLTPVEG-VPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTAT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 554 VVNLSNQGSQRH--YPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMISDIMATGAQNQQidaevRICCVI 631
Cdd:cd14621  123 IVMVTNLKERKEckCAQYWPDQGCWTYGNIRVSVED-------VTVLVDYTVRKFCIQQVGDVTNKKPQ-----RLITQF 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 632 QVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMM 711
Cdd:cd14621  191 HFTSWP-DFGVPFTPIGMLKFLK-----KVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRI 264

                        250       260
                 ....*....|....*....|....*.
gi 392890886 712 RINRPQLIDMKDEYKYLYDVMLHWYM 737
Cdd:cd14621  265 RAQRCQMVQTDMQYVFIYQALLEHYL 290

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: 96.93 E-value: 1.53e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 491 VVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFI 570
Cdd:cd14620    4 ILPYDHSRVILSQLDGIPCS-DYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 571 H--NKGKANYGPFIVEIMNYhqypamtSHMVKVMKRTFMISDIMATGAQNQqidaevRICCVIQVRMWPiENKVPLSTTG 648
Cdd:cd14620   83 YwpDQGCWTYGNIRVAVEDC-------VVLVDYTIRKFCIQPQLPDGCKAP------RLVTQLHFTSWP-DFGVPFTPIG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 649 LIDVIKMARSWrkrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYL 728
Cdd:cd14620  149 MLKFLKKVKSV-----NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFI 223


                 ....*
gi 392890886 729 YDVML 733
Cdd:cd14620  224 YQALL 228

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: 95.40 E-value: 3.91e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQAVRTKPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT--KFQFREIEVET 291
Cdd:cd14601    2 YINANYINMEIPSSSIINRYIACQGPLPntcSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPsgSSSYGGFQVTC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 292 TEVKTYSHFVIRtfKLTRTTPESIETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQfmEKNPVEAPMVVHCSNGAGRS 370
Cdd:cd14601   82 HSEEGNPAYVFR--EMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSdFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392890886 371 GAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd14601  158 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAI 206

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: 93.87 E-value: 9.35e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--NQGSQRHYPSFIHNKGKANYGPFIVEIMNYHQ 590
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTeiKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 591 YPAMTshmvkvmkrtfmISDIMATGAQNQQidaeVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDRPETk 670
Cdd:cd14552   81 YEDYT------------LRDFLVTKGKGGS----TRTVRQFHFHGWP-EVGIPDNGKGMIDLIAAVQKQQQQSGNHPIT- 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392890886 671 ptiVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVM 732
Cdd:cd14552  143 ---VHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

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: 95.45 E-value: 1.67e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 189 DRNPYPDTLPYDYNRV-ILPriDGDENSHYINASYVNSWLRDKA--YVVTQAvrtkPMN---AEFWRMVWELGSNCIVML 262
Cdd:cd14599   40 ERNRIREVVPYEENRVeLVP--TKENNTGYINASHIKVTVGGEEwhYIATQG----PLPhtcHDFWQMVWEQGVNVIAMV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 263 TKVFDFMRVMCLQYWP----------------LTKFQFREIEVETTEVKTySHFVirtfkltrttpeSIETRIVKHFHFT 326
Cdd:cd14599  114 TAEEEGGRSKSHRYWPklgskhssatygkfkvTTKFRTDSGCYATTGLKV-KHLL------------SGQERTVWHLQYT 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 327 EW-------ELDSF-PYISAFIELRRRVRQFME-KNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKT 397
Cdd:cd14599  181 DWpdhgcpeEVQGFlSYLEEIQSVRRHTNSMLDsTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRH 260

                        250       260
                 ....*....|....*....|..
gi 392890886 398 LVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd14599  261 LREQRMFMIQTIAQYKFVYQVL 282

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: 92.46 E-value: 3.12e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQR---HYpsfiHNKGKANYGPFIVEIMN 587
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElkEGDQEqcaQY----WGDEKKTYGDIEVELKD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 588 YHQYPAMTshmvkvmKRTFMIsdimatgaQNQQIDaEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDR- 666
Cdd:cd14558   77 TEKSPTYT-------VRVFEI--------THLKRK-DSRTVYQYQYHKWK-GEELPEKPKDLVDMIKSIKQKLPYKNSKh 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890886 667 PETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 730
Cdd:cd14558  140 GRSVPIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203

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: 93.17 E-value: 3.61e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 481 ENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ 560
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHS-DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 561 ------GSQRHYPSfihnkGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMIsdimatgaqNQQIDAEVRICCVIQVR 634
Cdd:cd14630   81 vevgrvKCVRYWPD-----DTEVYGDIKVTLIE-------TEPLAEYVIRTFTV---------QKKGYHEIREIRQFHFT 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 635 MWPiENKVPLSTTGLIDVIKMARSWrkrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 714
Cdd:cd14630  140 SWP-DHGVPCYATGLLGFVRQVKFL-----NPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQ 213

                        250
                 ....*....|....*....
gi 392890886 715 RPQLIDMKDEYKYLYDVML 733
Cdd:cd14630  214 RVNMVQTEEQYVFVHDAIL 232

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: 92.67 E-value: 5.29e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 486 NRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVnLSNQGSQR- 564
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCS-DYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIV-MVTQCVEKg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 565 -----HYPSFIHNKgkANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDimatgaqNQQIDAEvRICCVIQVRMWPiE 639
Cdd:cd14617   79 rvkcdHYWPADQDS--LYYGDLIVQMLSESVLPEWTI-------REFKICS-------EEQLDAP-RLVRHFHYTVWP-D 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 640 NKVPLSTTGLIDVIKMARSWRKRAPDrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 719
Cdd:cd14617  141 HGVPETTQSLIQFVRTVRDYINRTPG---SGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMV 217

                        250
                 ....*....|
gi 392890886 720 DMKDEYKYLY 729
Cdd:cd14617  218 QTECQYVYLH 227

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: 91.10 E-value: 1.93e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 486 NRDVMVVPPDHARPYLQTLHgESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQ 563
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIH-EEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNcmEAGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 564 ---RHYPSFihNKGKANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDIMatgaqnQQIDAEVRiccVIQVRMWPiEN 640
Cdd:cd14619   80 vkcEHYWPL--DYTPCTYGHLRVTVVSEEVMENWTV-------REFLLKQVE------EQKTLSVR---HFHFTAWP-DH 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 641 KVPLSTTGLIDVIKMARSWRKRapdRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLID 720
Cdd:cd14619  141 GVPSSTDTLLAFRRLLRQWLDQ---TMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQ 217

                        250
                 ....*....|...
gi 392890886 721 MKDEYKYLYDVML 733
Cdd:cd14619  218 TESQYVFLHQCIL 230

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: 91.25 E-value: 4.14e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 481 ENRGKNRDVMVVPPDHARPYLQTLHG-ESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN 559
Cdd:cd17667   26 DNKHKNRYINILAYDHSRVKLRPLPGkDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 560 --QGSQRHYPSFIHNKGKANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDIMATGAQNQQIDAEVRICCVIQVR--M 635
Cdd:cd17667  106 lvEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTV-------RRFSIRNTKVKKGQKGNPKGRQNERTVIQYHytQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 636 WPiENKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINR 715
Cdd:cd17667  179 WP-DMGVPEYALPVLTFVR-----RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQR 252

                        250
                 ....*....|....*...
gi 392890886 716 PQLIDMKDEYKYLYDVML 733
Cdd:cd17667  253 NYLVQTEEQYIFIHDALL 270

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: 89.88 E-value: 4.78e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 486 NRDVMVVPPDHARPYLQTLHGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN---QGS 562
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTDDY--INANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcveQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 563 ---QRHYPSfihnKGKANYGPFIVeimnyhqypAMTSHMVKvmkRTFMISDIMATGAQNQQIDaevricCVIQVRM--WP 637
Cdd:cd14615   79 tkcEEYWPS----KQKKDYGDITV---------TMTSEIVL---PEWTIRDFTVKNAQTNESR------TVRHFHFtsWP 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 638 iENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQ 717
Cdd:cd14615  137 -DHGVPETTDLLINFRHLVREYMKQNP---PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPL 212

                        250
                 ....*....|.
gi 392890886 718 LIDMKDEYKYL 728
Cdd:cd14615  213 MVQTEDQYVFL 223

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: 88.99 E-value: 1.25e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARPYLQTLHGeSKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQG 561
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEG-VPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 562 SQ------RHYPsfihNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMIsdiMATGAQNQQidaEVRiccVIQVRM 635
Cdd:cd14553   82 ERsrvkcdQYWP----TRGTETYGLIQVTLLD-------TVELATYTVRTFAL---HKNGSSEKR---EVR---QFQFTA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 636 WPiENKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIganiCIDQM--DIDHE--VDVFHAVKMM 711
Cdd:cd14553  142 WP-DHGVPEHPTPFLAFLR-----RVKACNPPDAGPIVVHCSAGVGRTGCFI----VIDSMleRIKHEktVDIYGHVTCL 211

                        250       260
                 ....*....|....*....|..
gi 392890886 712 RINRPQLIDMKDEYKYLYDVML 733
Cdd:cd14553  212 RAQRNYMVQTEDQYIFIHDALL 233

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: 87.13 E-value: 2.69e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYV--NSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMR-VMCLQYWPLTKFQFRE---IEVE 290
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTF-EDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREfgrISVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 291 TTEVKTYSH-FVIRTFKLTRTtpESIET-RIVKHFHFTEWELDSFPYISAFI-ELRRRVRQFmekNPVEAPMVVHCSNGA 367
Cdd:cd17658   80 NKKLKHSQHsITLRVLEVQYI--ESEEPpLSVLHIQYPEWPDHGVPKDTRSVrELLKRLYGI---PPSAGPIVVHCSAGI 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392890886 368 GRSGAFLALDANLELMKKtGQLDFFEYAKTLVNSRPHLIDSV---EQYMFIYE 417
Cdd:cd17658  155 GRTGAYCTIHNTIRRILE-GDMSAVDLSKTVRKFRSQRIGMVqtqDQYIFCYA 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: 86.61 E-value: 3.55e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKA-NYGPFIVEIMNYHQY 591
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEKPlECETFKVTLSGEDHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 592 PAMTSHMVKVmkRTFMIsdimatgaQNQQID--AEVRIccvIQVRMWPIENKvPLSTT-GLIDVIkmarswRKRAPDRpe 668
Cdd:cd14550   81 CLSNEIRLIV--RDFIL--------ESTQDDyvLEVRQ---FQCPSWPNPCS-PIHTVfELINTV------QEWAQQR-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392890886 669 TKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd14550  139 DGPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199

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: 88.18 E-value: 4.28e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 481 ENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNq 560
Cdd:cd14633   39 ENRMKNRYGNIIAYDHSRVRLQPIEGETSS-DYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTN- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 561 gsqrhypsfihnkgkanygpfIVEI--MNYHQYPAMTSHMVKVMKRTFMISDIMA-----TGAQNQQIDAEVRICCVIQV 633
Cdd:cd14633  117 ---------------------LVEVgrVKCCKYWPDDTEIYKDIKVTLIETELLAeyvirTFAVEKRGVHEIREIRQFHF 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 634 RMWPiENKVPLSTTGLIDVIKMARSwrkRAPdrPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRI 713
Cdd:cd14633  176 TGWP-DHGVPYHATGLLGFVRQVKS---KSP--PNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRS 249

                        250       260
                 ....*....|....*....|
gi 392890886 714 NRPQLIDMKDEYKYLYDVML 733
Cdd:cd14633  250 RRVNMVQTEEQYVFIHDAIL 269

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: 86.57 E-value: 4.81e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKA--YVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPltKFQFREIEVet 291
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQG----PLQNtcqDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWP--RLGSRHNTV-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 292 tevkTYSHFVIRT-FKLTR----TTPESI------ETRIVKHFHFTEWELDSFP--------YISAFIELRRRVRQFMEK 352
Cdd:cd14598   73 ----TYGRFKITTrFRTDSgcyaTTGLKIkhlltgQERTVWHLQYTDWPEHGCPedlkgflsYLEEIQSVRRHTNSTIDP 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890886 353 NPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd14598  149 KSPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215

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: 87.46 E-value: 7.81e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--N 559
Cdd:cd14625   47 NKPKNRYANVIAYDHSRVILQPIEGIMGS-DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTklE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 560 QGSQRHYPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFmisDIMATGAQNQQidaEVRiccVIQVRMWPiE 639
Cdd:cd14625  126 EKSRIKCDQYWPSRGTETYGMIQVTLLD-------TIELATFCVRTF---SLHKNGSSEKR---EVR---QFQFTAWP-D 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 640 NKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 719
Cdd:cd14625  189 HGVPEYPTPFLAFLR-----RVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMV 263

                        250
                 ....*....|....
gi 392890886 720 DMKDEYKYLYDVML 733
Cdd:cd14625  264 QTEDQYSFIHDALL 277

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: 85.12 E-value: 1.05e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNL-SNQGSQR----HYPSfihNKGKANYGPFIVEIMN 587
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQGLAEdefvYWPS---REESMNCEAFTVTLIS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 588 yhqypamTSHMVKVMKRTFMISDIMATGAQNQQIdAEVRiccVIQVRMWPIENKVPLSTTGLIDVIKmarswrKRAPDRp 667
Cdd:cd17670   78 -------KDRLCLSNEEQIIIHDFILEATQDDYV-LEVR---HFQCPKWPNPDAPISSTFELINVIK------EEALTR- 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392890886 668 eTKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd17670  140 -DGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

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: 85.10 E-value: 1.14e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ------GSQRHYPsfihnKGKANYGPFIVEIM 586
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLvevgrvKCSKYWP-----DDSDTYGDIKITLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 587 NyhqypamTSHMVKVMKRTFMISdimatgAQNQQIDAEVricCVIQVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDR 666
Cdd:cd14632   76 K-------TETLAEYSVRTFALE------RRGYSARHEV---KQFHFTSWP-EHGVPYHATGLLAFIR-----RVKASTP 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890886 667 PETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd14632  134 PDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200

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: 87.01 E-value: 1.21e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--N 559
Cdd:cd14626   41 NKPKNRYANVIAYDHSRVILTSVDGVPGS-DYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTrlE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 560 QGSQRHYPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMisdIMATGAQNQQidaEVRiccVIQVRMWPiE 639
Cdd:cd14626  120 EKSRVKCDQYWPIRGTETYGMIQVTLLD-------TVELATYSVRTFA---LYKNGSSEKR---EVR---QFQFMAWP-D 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 640 NKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 719
Cdd:cd14626  183 HGVPEYPTPILAFLR-----RVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMV 257

                        250
                 ....*....|....
gi 392890886 720 DMKDEYKYLYDVML 733
Cdd:cd14626  258 QTEDQYIFIHEALL 271

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: 84.66 E-value: 1.60e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQavrtKPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLqYWP-------LTKFQFRE 286
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQ----HPLlhtIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPnkdepinCETFKVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 287 IEVETTEVKTYSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPyISAFIELRRRVRQfmEKNPVEAPMVVHCSNG 366
Cdd:cd17669   76 IAEEHKCLSNEEKLIIQDFILEATQDDYVLE--VRHFQCPKWPNPDSP-ISKTFELISIIKE--EAANRDGPMIVHDEHG 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392890886 367 AGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd17669  151 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203

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: 83.42 E-value: 3.61e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQRHYPSFIHNKGKANYGPFIVEIMNyhq 590
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNlkERKEKKCSQYWPDQGCWTYGNLRVRVED--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 591 ypamTSHMVKVMKRTFMISDIMATGAQNQQidaevRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSwrkraPDRPETK 670
Cdd:cd14551   78 ----TVVLVDYTTRKFCIQKVNRGIGEKRV-----RLVTQFHFTSWP-DFGVPFTPIGMLKFLKKVKS-----ANPPRAG 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392890886 671 PTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd14551  143 PIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201

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: 85.09 E-value: 5.89e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 474 CAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVE-VDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 552
Cdd:cd14609   34 CSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRS-DYINASPiIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 553 TVVNLSN------QGSQRHYPsfihNKGKANYGPFIVEIMNYHqypamtshmvkVMKRTFMISDIMATGAQNQqidaEVR 626
Cdd:cd14609  113 VIVMLTPlvedgvKQCDRYWP----DEGSSLYHIYEVNLVSEH-----------IWCEDFLVRSFYLKNVQTQ----ETR 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 627 ICCVIQVRMWPIENkVPLSTTGLIDV-IKMARSWRKRapdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDID-HEVDV 704
Cdd:cd14609  174 TLTQFHFLSWPAEG-IPSSTRPLLDFrRKVNKCYRGR------SCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDI 246

                        250       260
                 ....*....|....*....|...
gi 392890886 705 FHAVKMMRINRPQLIDMKDEYKY 727
Cdd:cd14609  247 AATLEHVRDQRPGMVRTKDQFEF 269

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: 82.78 E-value: 7.40e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV---NLSNQGSQ---RHYPsfihNKGKANYGPFIVEIM 586
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVmitNLVERGRRkcdQYWP----KEGTETYGNIQVTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 587 NyhqypamTSHMVKVMKRTFMISDimaTGAQNQQIDAEVRIccVIQVRM--WPiENKVPLSTTGLIDVIKmarswRKRAP 664
Cdd:cd14549   77 S-------TEVLATYTVRTFSLKN---LKLKKVKGRSSERV--VYQYHYtqWP-DHGVPDYTLPVLSFVR-----KSSAA 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392890886 665 DRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 730
Cdd:cd14549  139 NPPGAGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204

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: 81.42 E-value: 5.41e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 477 GHRLENRGKNrdvmVVPPDHARPYLQTLHGESKDYTYINAVEVDGFT-RKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV 555
Cdd:cd14612   14 GHASKDRYKT----ILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 556 NLS-----NQGSQRHYPsfihnKGKANYGPFIVEIMNYHQYPAMTshmvkvmkrtfmISDIMAtgaqnqQIDAEVRICCV 630
Cdd:cd14612   90 MITklkekKEKCVHYWP-----EKEGTYGRFEIRVQDMKECDGYT------------IRDLTI------QLEEESRSVKH 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 631 IQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKM 710
Cdd:cd14612  147 YWFSSWP-DHQTPESAGPLLRLVAEVEESRQTAASP---GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQ 222

                        250
                 ....*....|....*....
gi 392890886 711 MRINRPQLIDMKDEYKYLY 729
Cdd:cd14612  223 LRLDRGGMIQTSEQYQFLH 241

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: 80.09 E-value: 9.41e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 487 RDVMVVPPDHARPYLQTLHGEsKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYD-HACHTVV--NLSNQGSQ 563
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGE-ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEwKSCSIVMltELEERGQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 564 R---HYPSfihnKGKANYGPFIVEIMNYHQypamtshmvkvmKRTFMISDIMATGAQNQQiDAEVRiccVIQVRMWPiEN 640
Cdd:cd14623   80 KcaqYWPS----DGSVSYGDITIELKKEEE------------CESYTVRDLLVTNTRENK-SRQIR---QFHFHGWP-EV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 641 KVPLSTTGLIDVIKMARSWRKRAPDRPETkptiVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLID 720
Cdd:cd14623  139 GIPSDGKGMINIIAAVQKQQQQSGNHPIT----VHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQ 214

                        250
                 ....*....|..
gi 392890886 721 MKDEYKYLYDVM 732
Cdd:cd14623  215 TLEQYEFCYKVV 226

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: 79.19 E-value: 1.19e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ------GSQRHYPsfihnKGKANYGPFIVEIM 586
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLvevgrvKCSRYWP-----DDTEVYGDIKVTLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 587 NyhqypamTSHMVKVMKRTFMISdimatgaqnQQIDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDR 666
Cdd:cd14555   76 E-------TEPLAEYVVRTFALE---------RRGYHEIREVRQFHFTGWP-DHGVPYHATGLLGFIR-----RVKASNP 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890886 667 PETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd14555  134 PSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200

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: 79.25 E-value: 1.31e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQRHYPSFIHNKGKANYGPFIVeimnyhq 590
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNlvEKGRRKCDQYWPADGSEEYGNFLV------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 591 ypamTSHMVKVMK----RTFMISDI-MATGAQNQQidAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRkrapd 665
Cdd:cd17668   74 ----TQKSVQVLAyytvRNFTLRNTkIKKGSQKGR--PSGRVVTQYHYTQWP-DMGVPEYTLPVLTFVRKASYAK----- 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392890886 666 RPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd17668  142 RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

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: 80.93 E-value: 1.46e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN-- 559
Cdd:cd14624   47 NKPKNRYANVIAYDHSRVLLSAIEGIPGS-DYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKle 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 560 QGSQRHYPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMisdIMATGAQNQQidaEVRiccVIQVRMWPiE 639
Cdd:cd14624  126 ERSRVKCDQYWPSRGTETYGLIQVTLLD-------TVELATYCVRTFA---LYKNGSSEKR---EVR---QFQFTAWP-D 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 640 NKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 719
Cdd:cd14624  189 HGVPEHPTPFLAFLR-----RVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMV 263

                        250
                 ....*....|....
gi 392890886 720 DMKDEYKYLYDVML 733
Cdd:cd14624  264 QTEDQYIFIHDALL 277

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: 78.57 E-value: 2.18e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 217 YINASYVNSWLRDKAYVVTQavrtKPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLqYWPLTK-------FQFRE 286
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQ----HPLphtTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPSREesmnceaFTVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 287 IEVETTEVKTYSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPyISAFIELRRRVRQfmEKNPVEAPMVVHCSNG 366
Cdd:cd17670   76 ISKDRLCLSNEEQIIIHDFILEATQDDYVLE--VRHFQCPKWPNPDAP-ISSTFELINVIKE--EALTRDGPTIVHDEFG 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392890886 367 AGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:cd17670  151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203

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: 80.10 E-value: 2.92e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 474 CAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEV-DGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 552
Cdd:cd14610   36 TNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHS-DYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 553 TVVNLS---NQGSQRHYpSFIHNKGKANYGPFIVEIMNYHQYPAmtshmvKVMKRTFMISDIMATgaqnqqidaEVRICC 629
Cdd:cd14610  115 VIVMLTplaENGVKQCY-HYWPDEGSNLYHIYEVNLVSEHIWCE------DFLVRSFYLKNLQTN---------ETRTVT 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 630 VIQVRMWpIENKVPLSTTGLIDV-IKMARSWRKRapdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDID-HEVDVFHA 707
Cdd:cd14610  179 QFHFLSW-NDQGVPASTRSLLDFrRKVNKCYRGR------SCPIIVHCSDGAGRSGTYILIDMVLNKMAKGaKEIDIAAT 251

                        250       260
                 ....*....|....*....|
gi 392890886 708 VKMMRINRPQLIDMKDEYKY 727
Cdd:cd14610  252 LEHLRDQRPGMVQTKEQFEF 271

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: 74.32 E-value: 5.69e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886   636 WPiENKVPLSTTGLIDVIKMARSWRKrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD-IDHEVDVFHAVKMMRIN 714
Cdd:smart00012  10 WP-DHGVPESPDSILELLRAVKKNLN---QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVKELRSQ 85

                           90       100
                   ....*....|....*....|
gi 392890886   715 RPQLIDMKDEYKYLYDVMLH 734
Cdd:smart00012  86 RPGMVQTEEQYLFLYRALLE 105

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 74.32 E-value: 5.69e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886   636 WPiENKVPLSTTGLIDVIKMARSWRKrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD-IDHEVDVFHAVKMMRIN 714
Cdd:smart00404  10 WP-DHGVPESPDSILELLRAVKKNLN---QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVKELRSQ 85

                           90       100
                   ....*....|....*....|
gi 392890886   715 RPQLIDMKDEYKYLYDVMLH 734
Cdd:smart00404  86 RPGMVQTEEQYLFLYRALLE 105

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: 77.75 E-value: 6.00e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDH--ACHTVV-NLSNQGSQRHYPSFIHNkgKANYGPFIVEIMNyh 589
Cdd:cd14631   15 YINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEqsACIVMVtNLVEVGRVKCYKYWPDD--TEVYGDFKVTCVE-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 590 qypamTSHMVKVMKRTFMISdimatgaqnQQIDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDRPET 669
Cdd:cd14631   91 -----MEPLAEYVVRTFTLE---------RRGYNEIREVKQFHFTGWP-DHGVPYHATGLLSFIR-----RVKLSNPPSA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890886 670 KPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd14631  151 GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214

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: 76.57 E-value: 9.55e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-NQGSQRHYPSFIHNKGKA-NYGPFIVEIMNyhq 590
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPdGQNMAEDEFVYWPNKDEPiNCETFKVTLIA--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 591 ypamTSHMVKVMKRTFMISDIMATGAQNQQIdAEVRiccVIQVRMWPIENKvPLSTT-GLIDVIKMARSWRKrapdrpet 669
Cdd:cd17669   78 ----EEHKCLSNEEKLIIQDFILEATQDDYV-LEVR---HFQCPKWPNPDS-PISKTfELISIIKEEAANRD-------- 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890886 670 KPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd17669  141 GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

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: 75.70 E-value: 4.37e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARPYLQTLHGEsKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQG 561
Cdd:cd14614   12 NRCKNRYTNILPYDFSRVKLVSMHEE-EGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 562 SQR-----HYPSFihNKGKANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISdiMATGAQnqqidaevricCVIQVRM- 635
Cdd:cd14614   91 EKRrvkcdHYWPF--TEEPVAYGDITVEMLSEEEQPDWA-------IREFRVS--YADEVQ-----------DVMHFNYt 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 636 -WPiENKVPLSTTG--LIDVIKMARSWRKRAPDrpetkPTIVMSHNGVSRVGVYIGANiCIDQMDIDHE-VDVFHAVKMM 711
Cdd:cd14614  149 aWP-DHGVPTANAAesILQFVQMVRQQAVKSKG-----PMIIHCSAGVGRTGTFIALD-RLLQHIRDHEfVDILGLVSEM 221

                        250
                 ....*....|....*...
gi 392890886 712 RINRPQLIDMKDEYKYLY 729
Cdd:cd14614  222 RSYRMSMVQTEEQYIFIH 239

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 75.42 E-value: 1.49e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 481 ENRGKNRDVMVVPPDHARPYLQTLHGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-- 558
Cdd:PHA02747  50 ENQPKNRYWDIPCWDHNRVILDSGGGSTSDY--IHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTpt 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 559 --NQGSQRHYPSFIHNK-GKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMISDimatgaqnqQIDAEVRICCVIQVRM 635
Cdd:PHA02747 128 kgTNGEEKCYQYWCLNEdGNIDMEDFRIETLK-------TSVRAKYILTLIEITD---------KILKDSRKISHFQCSE 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 636 WPIENkVPLSTTGLIDVIKMARSWRKRA-----PDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKM 710
Cdd:PHA02747 192 WFEDE-TPSDHPDFIKFIKIIDINRKKSgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                        250       260
                 ....*....|....*....|....*..
gi 392890886 711 MRINRPQLIDMKDEYKYL---YDVMLH 734
Cdd:PHA02747 271 IREQRHAGIMNFDDYLFIqpgYEVLHY 297

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: 73.32 E-value: 4.18e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 477 GHRLENRGKNRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDH------- 549
Cdd:cd14603   25 GGRKENVKKNRYKDILPYDQTRVIL-SLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYgvkvilm 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 550 ACHTVVNlSNQGSQRHYPSfihNKGKANYGPFIVEIMNYHQYPAMTshMVKVMKRTFmisdimatgaqnQQidaEVRICC 629
Cdd:cd14603  104 ACREIEM-GKKKCERYWAQ---EQEPLQTGPFTITLVKEKRLNEEV--ILRTLKVTF------------QK---ESRSVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 630 VIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDrpetkPTIVMSHNGVSRVGV-----YIgANICIDQMdIDHEVDV 704
Cdd:cd14603  163 HFQYMAWP-DHGIPDSPDCMLAMIELARRLQGSGPE-----PLCVHCSAGCGRTGVictvdYV-RQLLLTQR-IPPDFSI 234

                        250       260
                 ....*....|....*....|....*
gi 392890886 705 FHAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd14603  235 FDVVLEMRKQRPAAVQTEEQYEFLY 259

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: 73.13 E-value: 4.23e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 481 ENRGKNRDVMVVPPDHARPYLQTLHGESKDYTYINA--------VEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 552
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINAniimpefeTKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 553 TVVnLSNQGSQRhypsfihnkGKANYGPFIVEIMNYHQYPAMTSHMVK-VMKRTFMISDIMAT--GAQNQQidaevRICC 629
Cdd:cd14605   81 VIV-MTTKEVER---------GKSKCVKYWPDEYALKEYGVMRVRNVKeSAAHDYILRELKLSkvGQGNTE-----RTVW 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 630 VIQVRMWPiENKVPLSTTGLIDVIKMARswrKRAPDRPETKPTIVMSHNGVSRVGVYIGANICID---QMDIDHEVDVFH 706
Cdd:cd14605  146 QYHFRTWP-DHGVPSDPGGVLDFLEEVH---HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDiirEKGVDCDIDVPK 221

                        250       260       270
                 ....*....|....*....|....*....|..
gi 392890886 707 AVKMMRINRPQLIDMKDEYKYLYDVMLHWYMT 738
Cdd:cd14605  222 TIQMVRSQRSGMVQTEAQYRFIYMAVQHYIET 253

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: 73.17 E-value: 4.60e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNR--DVMVVppDHARPYLQTLHGEskDYT-YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS 558
Cdd:cd14543   29 NQEKNRygDVLCL--DQSRVKLPKRNGD--ERTdYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 559 N--QGSQRHYPSFIHNKGKA--NYGPFIV---EIMNYHQYpamtshmvkvMKRTFMIsdimatgaQNQQIDaEVRicCVI 631
Cdd:cd14543  105 RvvERGRVKCGQYWPLEEGSslRYGDLTVtnlSVENKEHY----------KKTTLEI--------HNTETD-ESR--QVT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 632 QVRM--WPiENKVPLSTTGLID------------VIKMARSWRKrapdRPETKPTIVMSHNGVSRVGVYIGANICIDQMD 697
Cdd:cd14543  164 HFQFtsWP-DFGVPSSAAALLDflgevrqqqalaVKAMGDRWKG----HPPGPPIVVHCSAGIGRTGTFCTLDICLSQLE 238

                        250       260       270
                 ....*....|....*....|....*....|..
gi 392890886 698 IDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd14543  239 DVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270

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: 71.40 E-value: 5.85e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-------NQGSQrHYPSFihNKGKANYGPFIVEI 585
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTrceegnrNKCAQ-YWPSM--EEGSRAFGDVVVKI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 586 MNYHQYPamtshmvKVMKRTFMISdimatgaqNQQIDAEVRICCVIQVRMWPiENKVPLSTTGLidvIKMARswRKRAPD 665
Cdd:cd14557   78 NEEKICP-------DYIIRKLNIN--------NKKEKGSGREVTHIQFTSWP-DHGVPEDPHLL---LKLRR--RVNAFN 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890886 666 RPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd14557  137 NFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200

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: 72.66 E-value: 1.07e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 468 TLRIGDCAGGHRLENRGKNRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIY 547
Cdd:cd14604   43 TEKIYPTATGEKEENVKKNRYKDILPFDHSRVKL-TLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIW 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 548 DHACHTVV------NLSNQGSQRHYPsfIHNKGKANYGPFIVEIMNYHqypAMTSHMVkvmkRTFMIsdimatgaqnqQI 621
Cdd:cd14604  122 EYNVAIIVmacrefEMGRKKCERYWP--LYGEEPMTFGPFRISCEAEQ---ARTDYFI----RTLLL-----------EF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 622 DAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRapdrpETKPTIVMSHNGVSRVGVyiganIC-IDQM---- 696
Cdd:cd14604  182 QNETRRLYQFHYVNWP-DHDVPSSFDSILDMISLMRKYQEH-----EDVPICIHCSAGCGRTGA-----ICaIDYTwnll 250

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 392890886 697 ---DIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd14604  251 kagKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 286

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: 67.87 E-value: 1.28e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINA----VEVDGFTRKaeFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFihnkgkaNYGPFiveiMNY 588
Cdd:cd14540    1 YINAshitATVGGKQRF--YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCF-------RYWPT----LGG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 589 HqYPAMTSHMVKVMKRTFMISDIMATGA---QNQQIDAEvRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKR--- 662
Cdd:cd14540   68 E-HDALTFGEYKVSTKFSVSSGCYTTTGlrvKHTLSGQS-RTVWHLQYTDWP-DHGCPEDVSGFLDFLEEINSVRRHtnq 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392890886 663 --APDRPETkPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd14540  145 dvAGHNRNP-PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216

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: 68.01 E-value: 1.35e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNqgsqrhypsfIHNKGKanygpfiveiMNYHQYP 592
Cdd:cd14616   27 YINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQ----------CFEKGR----------IRCHQYW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 593 AMTSHMVKVMkrtfmiSDIMATG-AQNQQIDAEVRICCV------IQVRM-----WPiENKVPLSTTGLIDVIKMARSWR 660
Cdd:cd14616   87 PEDNKPVTVF------GDIVITKlMEDVQIDWTIRDLKIerhgdyMMVRQcnftsWP-EHGVPESSAPLIHFVKLVRASR 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 661 KRapdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDiDHE-VDVFHAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd14616  160 AH-----DNTPMIVHCSAGVGRTGVFIALDHLTQHIN-DHDfVDIYGLVAELRSERMCMVQNLAQYIFLH 223

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 69.29 E-value: 1.94e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 479 RLENRGKNRDVMVVPPDHAR------------------PYLQTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVD 540
Cdd:PHA02746  48 KKENLKKNRFHDIPCWDHSRvvinaheslkmfdvgdsdGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 541 SFWTLIYDHACHTVVNLS--NQGSQRHYPSFIHNKG-KANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISDIMATGAq 617
Cdd:PHA02746 128 DFFKLISEHESQVIVSLTdiDDDDEKCFELWTKEEDsELAFGRFVAKILDIIEELSFT-------KTRLMITDKISDTS- 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 618 nqqidaevRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKR----APDRPETK-PTIVMSHNGVSRVGVYIGANIC 692
Cdd:PHA02746 200 --------REIHHFWFPDWP-DNGIPTGMAEFLELINKVNEEQAElikqADNDPQTLgPIVVHCSAGIGRAGTFCAIDNA 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 392890886 693 IDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVM 732
Cdd:PHA02746 271 LEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310

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: 66.70 E-value: 2.87e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEV-DGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS------NQGSQRHYPsfihNKGKANYGPFIVEI 585
Cdd:cd14546    1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTrlqengVKQCARYWP----EEGSEVYHIYEVHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 586 MNYHQYPAmtSHMVkvmkRTFMISDImatgaQNQqidaEVRICCVIQVRMWPIENkVPLSTTGLIDV-IKMARSWRKRap 664
Cdd:cd14546   77 VSEHIWCD--DYLV----RSFYLKNL-----QTS----ETRTVTQFHFLSWPDEG-IPASAKPLLEFrRKVNKSYRGR-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392890886 665 drpeTKPTIVMSHNGVSRVGVYIGANICIDQMDID-HEVDVFHAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd14546  139 ----SCPIVVHCSDGAGRTGTYILIDMVLNRMAKGaKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200

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: 65.88 E-value: 6.64e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 486 NRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRK-AEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGS 562
Cdd:cd14547    1 NRYKTILPNEHSRVCL-PSVDDDPLSSYINANYIRGYDGEeKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNltEAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 563 QR--HYPSFIHNKgkaNYGPFIVEIMNYHQYPAMTShmvkvmkRTFMIsdimatgaqnqQIDAEVRICCVIQVRMWPiEN 640
Cdd:cd14547   80 EKcaQYWPEEENE---TYGDFEVTVQSVKETDGYTV-------RKLTL-----------KYGGEKRYLKHYWYTSWP-DH 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 641 KVPLSTTGLIDVIKMARSWRKRAPDRPetkPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLID 720
Cdd:cd14547  138 KTPEAAQPLLSLVQEVEEARQTEPHRG---PIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQ 214


                 ....*....
gi 392890886 721 MKDEYKYLY 729
Cdd:cd14547  215 TAEQYEFVH 223

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 67.33 E-value: 6.86e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 479 RLENRGKNRDVMVVPPDHARPYLQTLHGESKdytYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS 558
Cdd:PHA02742  49 ELKNMKKCRYPDAPCFDRNRVILKIEDGGDD---FINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMIT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 559 ---NQGSQRHYPSFI-HNKGKANYGPFIV---EIMNYHQYPAMTSHMVKVmkRTFMISDIMATGAQNqqidaevriccvi 631
Cdd:PHA02742 126 kimEDGKEACYPYWMpHERGKATHGEFKIktkKIKSFRNYAVTNLCLTDT--NTGASLDIKHFAYED------------- 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 632 qvrmWPiENKVPLSTTGLIDVIKMARSWRKRA------PDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVF 705
Cdd:PHA02742 191 ----WP-HGGLPRDPNKFLDFVLAVREADLKAdvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLL 265

                        250       260       270
                 ....*....|....*....|....*....|
gi 392890886 706 HAVKMMRINRPQLIDMKDEYKYLYDVMLHW 735
Cdd:PHA02742 266 SIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 295

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 66.91 E-value: 7.59e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 203 RVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDfmRVMCLQYWPL--- 279
Cdd:PHA02740  64 RLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACD-KFLQALSDNKVQIIVLISRHAD--KKCFNQFWSLkeg 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 280 TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPESietRIVKHFHFTEWELDSFPY-ISAFIELRRRVRQF---MEKNPV 355
Cdd:PHA02740 141 CVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA---QKISHFQYTAWPADGFSHdPDAFIDFFCNIDDLcadLEKHKA 217

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890886 356 E---APMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 419
Cdd:PHA02740 218 DgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284

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: 65.67 E-value: 1.35e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 477 GHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDYTYINAVEVD----GFTRKAE-FIVTEWPKQSTVDSFWTLIYDHAC 551
Cdd:cd14606   13 GQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAWQENS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 552 HTVVNLSNQ---GSQRHYPSFIHNKGKANYGPFIVEIMNYHQypaMTSHMVKVMKrtfmISDIMATGAqnqqidaeVRIC 628
Cdd:cd14606   93 RVIVMTTREvekGRNKCVPYWPEVGMQRAYGPYSVTNCGEHD---TTEYKLRTLQ----VSPLDNGEL--------IREI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 629 CVIQVRMWPiENKVPLSTTGlidVIKMARSWRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD---IDHEVDVF 705
Cdd:cd14606  158 WHYQYLSWP-DHGVPSEPGG---VLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIStkgLDCDIDIQ 233

                        250       260
                 ....*....|....*....|....
gi 392890886 706 HAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd14606  234 KTIQMVRAQRSGMVQTEAQYKFIY 257

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: 64.88 E-value: 2.35e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 485 KNRDVMVVPPDHARPYLQTLHGESKDYTYINAVEVDGFTRKAE-FIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNqgsq 563
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITN---- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 564 rhypsfihnkgkanygpfiVEIMN-----YHQYPAMTSHMVKVMKRTFMISDIMATGAQNQQIDAEVRICCVIQVRMWPi 638
Cdd:cd14613  104 -------------------IEEMNekcteYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWP- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 639 ENKVPLSTTGLIDVIKMARSWRKRAPdrPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQL 718
Cdd:cd14613  164 DQKTPDNAPPLLQLVQEVEEARQQAE--PNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241

                        250
                 ....*....|....
gi 392890886 719 IDMKDEYKYLYDVM 732
Cdd:cd14613  242 IQTCEQYQFVHHVL 255

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: 63.01 E-value: 6.75e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 485 KNRDVMVVPPDHARPYLQTLHGESKDYTYINAVEVDGFTRKAE-FIVTEWPKQSTVDSFWTLIYDHACHTVVNLS----- 558
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITklkek 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 559 NQGSQRHYPsfihnKGKANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDimatGAQNQQIDAevriccvIQVRMWPi 638
Cdd:cd14611   82 NEKCVLYWP-----EKRGIYGKVEVLVNSVKECDNYTI-------RNLTLKQ----GSQSRSVKH-------YWYTSWP- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 639 ENKVPLSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQL 718
Cdd:cd14611  138 DHKTPDSAQPLLQLMLDVEEDRLASPGR---GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGM 214

                        250
                 ....*....|.
gi 392890886 719 IDMKDEYKYLY 729
Cdd:cd14611  215 VQTSEQYEFVH 225

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: 62.40 E-value: 7.22e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKA-EFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQG------SQRHYPSfihNKGKA-NYGPFIVE 584
Cdd:cd14539    1 YINASLIEDLTPYCpRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQenekqkVHRYWPT---ERGQAlVYGAITVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 585 IMNYHQYPAMTSHMVKVMKRTfmisdimatgaqnqqiDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRap 664
Cdd:cd14539   78 LQSVRTTPTHVERIISIQHKD----------------TRLSRSVVHLQFTTWP-ELGLPDSPNPLLRFIEEVHSHYLQ-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890886 665 DRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEV-DVFHAVKMMRINRPQLIDMKDEYKYLYD 730
Cdd:cd14539  139 QRSLQTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 64.18 E-value: 8.69e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARpylQTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ- 560
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSR---VILPAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKk 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 561 --GSQRHYPSFIH-NKGKANYGPFIVEIMNYHQYPamtsHMVkvmKRTFMISDimATGAQNQQIDaevriccvIQVRMWP 637
Cdd:PHA02738 126 enGREKCFPYWSDvEQGSIRFGKFKITTTQVETHP----HYV---KSTLLLTD--GTSATQTVTH--------FNFTAWP 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 638 iENKVPLSTTGLIDVIKMARSWRKR--------APDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVK 709
Cdd:PHA02738 189 -DHDVPKNTSEFLNFVLEVRQCQKElaqeslqiGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVS 267

                        250       260
                 ....*....|....*....|...
gi 392890886 710 MMRINRPQLIDMKDEYKYLYDVM 732
Cdd:PHA02738 268 SIRNQRYYSLFIPFQYFFCYRAV 290

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: 61.71 E-value: 1.17e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINA--VEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSnqgsqrhypSFIHNKGKANYGPFIVEIMNYHQ 590
Cdd:cd17658    1 YINAslVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLT---------RLVDNYSTAKCADYFPAEENESR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 591 YPAMTSHMVKVMKRTfmISDIMATGAQNQQIDAEVRICCV--IQVRMWPiENKVPLSTTGLIDVIKmaRSWrkRAPdrPE 668
Cdd:cd17658   72 EFGRISVTNKKLKHS--QHSITLRVLEVQYIESEEPPLSVlhIQYPEWP-DHGVPKDTRSVRELLK--RLY--GIP--PS 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392890886 669 TKPTIVMSHNGVSRVGVYIGANICIDQ-MDIDHE-VDVFHAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd17658  143 AGPIVVHCSAGIGRTGAYCTIHNTIRRiLEGDMSaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205

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: 60.55 E-value: 6.28e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 482 NRGKNRDVMVVPPDHARPYLQTLHGESKDYTYINA----VEVDGFTRKAE---FIVTEWPKQSTVDSFWTLIYDHACHTV 554
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINAnyirNENEGPTTDENaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 555 VNLS---NQGSQ---RHYPSFIHNKgkaNYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISdimaTGAQNqqidAEVRIC 628
Cdd:cd14544   81 VMTTkevERGKNkcvRYWPDEGMQK---QYGPYRVQNVSEHDTTDYT-------LRELQVS----KLDQG----DPIREI 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 629 CVIQVRMWPiENKVPLSTTGLIDVIKMArswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD---IDHEVDVF 705
Cdd:cd14544  143 WHYQYLSWP-DHGVPSDPGGVLNFLEDV---NQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKrkgLDCDIDIQ 218

                        250       260       270
                 ....*....|....*....|....*....|...
gi 392890886 706 HAVKMMRINRPQLIDMKDEYKYLYDVMLHWYMT 738
Cdd:cd14544  219 KTIQMVRSQRSGMVQTEAQYKFIYVAVAQYIET 251

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: 59.86 E-value: 1.40e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 481 ENRGKNRDVMVVPPDHARPYLQtlhgESKDY---TYINaVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNL 557
Cdd:cd14600   39 QNMDKNRYKDVLPYDATRVVLQ----GNEDYinaSYVN-MEIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 558 SNqgsqrhypsfIHNKGKA---NYGPFIVEIMNYHQYpAMTSHM----VKVMKRTFMISDImATGAQnqqidaevRICCV 630
Cdd:cd14600  114 TT----------LTERGRTkchQYWPDPPDVMEYGGF-RVQCHSedctIAYVFREMLLTNT-QTGEE--------RTVTH 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 631 IQVRMWPiENKVPLSTTGLIDVIKMARSWRKrapdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKM 710
Cdd:cd14600  174 LQYVAWP-DHGVPDDSSDFLEFVNYVRSKRV------ENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRK 246

                        250       260
                 ....*....|....*....|....*.
gi 392890886 711 MRINRPQLIDMKDEYKYLYDVMLHWY 736
Cdd:cd14600  247 MRDQRAMMVQTSSQYKFVCEAILRVY 272

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: 58.70 E-value: 2.25e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 485 KNRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV------NLS 558
Cdd:cd14602    1 KNRYKDILPYDHSRVEL-SLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVmacmefEMG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 559 NQGSQRHYPSFihNKGKANYGPFIVEIMNYHQypaMTSHMVKVMKRTFmisdimatgaqnqqiDAEVRICCVIQVRMWPi 638
Cdd:cd14602   80 KKKCERYWAEP--GEMQLEFGPFSVTCEAEKR---KSDYIIRTLKVKF---------------NSETRTIYQFHYKNWP- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 639 ENKVPLSTTGLIDVIKMARSWRKRapdrpETKPTIVMSHNGVSRVGVyiganIC-IDQM-------DIDHEVDVFHAVKM 710
Cdd:cd14602  139 DHDVPSSIDPILELIWDVRCYQED-----DSVPICIHCSAGCGRTGV-----ICaIDYTwmllkdgIIPENFSVFSLIQE 208

                        250       260
                 ....*....|....*....|....*.
gi 392890886 711 MRINRPQLIDMKDEYKYLYDVMLHWY 736
Cdd:cd14602  209 MRTQRPSLVQTKEQYELVYNAVIELF 234

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: 55.89 E-value: 1.17e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ------GSQRHYPSfihNKGKA-NYGPFIVEi 585
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREfemgkkKCERYWPE---EGEEQlQFGPFKIS- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 586 mnYHQYPAMTS-HMVKVMKRTFmisdimatgaqnqqiDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRap 664
Cdd:cd14542   77 --LEKEKRVGPdFLIRTLKVTF---------------QKESRTVYQFHYTAWP-DHGVPSSVDPILDLVRLVRDYQGS-- 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890886 665 drpETKPTIVMSHNGVSRVGVyiganIC-ID--------QMdIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 729
Cdd:cd14542  137 ---EDVPICVHCSAGCGRTGT-----ICaIDyvwnllktGK-IPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201

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: 56.57 E-value: 1.94e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 481 ENRGKNRDVMVVPPDHARPylqTLHGESKDYTYINAVEVDGFTRKaeFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-- 558
Cdd:cd14608   24 KNKNRNRYRDVSPFDHSRI---KLHQEDNDYINASLIKMEEAQRS--YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNrv 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 559 -NQGS---QRHYPsfihnkgKANYGPFIVEIMNYHqypamTSHMVKVMKRTFMISDIMATGAQNQqidaEVRICCVIQVR 634
Cdd:cd14608   99 mEKGSlkcAQYWP-------QKEEKEMIFEDTNLK-----LTLISEDIKSYYTVRQLELENLTTQ----ETREILHFHYT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 635 MWPiENKVPLSTTGLIDVIKMArswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHE---VDVFHAVKMM 711
Cdd:cd14608  163 TWP-DFGVPESPASFLNFLFKV---RESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpssVDIKKVLLEM 238

                        250
                 ....*....|....*...
gi 392890886 712 RINRPQLIDMKDEYKYLY 729
Cdd:cd14608  239 RKFRMGLIQTADQLRFSY 256

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: 54.84 E-value: 3.95e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 481 ENRGKNRDVMVVPPDHARPYLQTLHGeskdytYINAVEVDGFTRKAEF--IVTEWPKQSTVDSFWTLIYDHACHTVVNLS 558
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLGDEGG------YINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 559 NQ------GSQRHYPsfihnkgkanygpfiveimnyhqypamtshmvKVMKRTFMISD-IMATGAQNQQIDA-------- 623
Cdd:cd14597   76 QEveggkiKCQRYWP--------------------------------EILGKTTMVDNrLQLTLVRMQQLKNfvirvlel 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 624 ------EVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKrapdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMD 697
Cdd:cd14597  124 ediqtrEVRHITHLNFTAWP-DHDTPSQPEQLLTFISYMRHIHK-------SGPIITHCSAGIGRSGTLICIDVVLGLIS 195

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 392890886 698 IDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVMLH 734
Cdd:cd14597  196 KDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILY 232

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: 52.44 E-value: 1.83e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 513 YINA--VEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ------GSQRHYPSFIHNKGK-ANYGPFIV 583
Cdd:cd14596    1 YINAsyITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREvergkvKCHRYWPETLQEPMElENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 584 eimnyhQYPAMTSHMVKVMKRTfmisdimatgaqnQQIDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKra 663
Cdd:cd14596   81 ------NYQALQYFIIRIIKLV-------------EKETGENRLIKHLQFTTWP-DHGTPQSSDQLVKFICYMRKVHN-- 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 664 pdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 733
Cdd:cd14596  139 -----TGPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203

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

Pssm-ID: 350455 [Multi-domain] Cd Length: 257 Bit Score: 50.73 E-value: 1.36e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 481 ENRGKNRDVMVVPPDHARPYLQTLHGEskdytYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNq 560
Cdd:cd14607   23 ENRNRNRYRDVSPYDHSRVKLQNTEND-----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 561 gsqrhypsfIHNKGK---ANYGPFIVEIMNYHQYPAMTSHMVKVMKRTFMISDIMatgaQNQQIDA-EVRICCVIQVRMW 636
Cdd:cd14607   97 ---------IVEKDSvkcAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLL----QLENINSgETRTISHFHYTTW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 637 PiENKVPLSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDH--EVDVFHAVKMMRIN 714
Cdd:cd14607  164 P-DFGVPESPASFLNFLFKVRESGSLSPEH---GPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKY 239

                        250
                 ....*....|....*
gi 392890886 715 RPQLIDMKDEYKYLY 729
Cdd:cd14607  240 RMGLIQTPDQLRFSY 254

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: 42.76 E-value: 3.37e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 483 RGKNRDVMVVPPDHARPYLQtlhGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--- 559
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLK---QGDNDY--INASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKlme 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 560 QGSQRHYPSFIHNKGKANYGP---FIVEIMNYHQYPAMTshmvkvmKRTFMISDImATGaqnqqidaEVRICCVIQVRMW 636
Cdd:cd14545   76 KGQIKCAQYWPQGEGNAMIFEdtgLKVTLLSEEDKSYYT-------VRTLELENL-KTQ--------ETREVLHFHYTTW 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890886 637 PiENKVPLSTTGLIDVIKMARSWRKRAPDrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDIDH--EVDVFHAVKMMRIN 714
Cdd:cd14545  140 P-DFGVPESPAAFLNFLQKVRESGSLSSD---VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKY 215

                        250
                 ....*....|....*
gi 392890886 715 RPQLIDMKDEYKYLY 729
Cdd:cd14545  216 RMGLIQTPDQLRFSY 230