NCBI Conserved Domain Search

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 259.13 E-value: 3.80e-81

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547    93 LFKGEYLMVNRsIDNNKCRCDVGSTM--MDRNPYPDTLPYDYNRVILPRIDGdENSHYINASYVNSWLRDKAYVVTQAvr 170
Cdd:smart00194   1 GLEEEFEKLDR-LKPDDESCTVAAFPenRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQG-- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547   171 tkPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL---TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPE 244
Cdd:smart00194  77 --PLpstVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDeegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547   245 siETRIVKHFHFTEWELDSFP-YISAFIELRRRVRQFMEKNpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFF 323
Cdd:smart00194 155 --ETRTVTHYHYTNWPDHGVPeSPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIF 230

                          250       260
                   ....*....|....*....|....*....
gi 212645547   324 EYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
Cdd:smart00194 231 EIVKELRSQRPGMVQTEEQYIFLYRAILE 259

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 226.74 E-value: 3.23e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547  119 MDRNPYPDTLPYDYNRVILPriDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTK 195
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQG----PLPntvEDFWRMVWEEKVTIIVMLTE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547  196 VFDFMRVMCLQYWPLTKFQ---FREIEVETTEVKTY-SHFVIRTFKLTRTTPEsiETRIVKHFHFTEW-ELDSFPYISAF 270
Cdd:pfam00102  76 LEEKGREKCAQYWPEEEGEsleYGDFTVTLKKEKEDeKDYTVRTLEVSNGGSE--ETRTVKHFHYTGWpDHGVPESPNSL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547  271 IELRRRVRQfMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
Cdd:pfam00102 154 LDLLRKVRK-SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                  ..
gi 212645547  351 SE 352
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: 1.05e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL---TKFQFREIEVE 221
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQG----PLPntvEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEeggKPLEYGDITVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 222 TTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFP-YISAFIELRRRVRQFMEKNpvEAPMVVHCSNGAGR 300
Cdd:cd00047   77 LVSEEELSDYTIRTLELSPKGCS--ESREVTHLHYTGWPDHGVPsSPEDLLALVRRVRKEARKP--NGPIVVHCSAGVGR 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 212645547 301 SGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
Cdd:cd00047  153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 206.74 E-value: 2.37e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547   404 DCAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 483
Cdd:smart00194  18 SCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDY--INASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547   484 TVVNLSNQGS------QRHYPSFIHnkGKANYGPFIVEIMNYHQYPAMTSHMVKVMKRTfmisdimatgaqnqqiDAEVR 557
Cdd:smart00194  96 VIVMLTELVEkgrekcAQYWPDEEG--EPLTYGDITVTLKSVEKVDDYTIRTLEVTNTG----------------CSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547   558 ICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKrapdrPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFH 637
Cdd:smart00194 158 TVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQS-----TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 212645547   638 AVKMMRINRPQLIDMKDEYKYLYDVMLH 665
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: 199.16 E-value: 7.00e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 197
Cdd:cd14553    6 KNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQG----PLPetfGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 198 DFMRVMCLQYWPLTKFQ-FREIEV---ETTEVKTYShfvIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIE 272
Cdd:cd14553   82 ERSRVKCDQYWPTRGTEtYGLIQVtllDTVELATYT---VRTFALHKNG--SSEKREVRQFQFTAWPDHGVPeHPTPFLA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 273 LRRRVRQFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 351
Cdd:cd14553  157 FLRRVKAC---NPPDAgPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233


                 ....*
gi 212645547 352 EAVMC 356
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: 181.41 E-value: 6.04e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547  89 KKRILFKgEYLMVNRSIDNNKCRCDVGSTMMDRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQA 168
Cdd:cd14543    1 QKRGIYE-EYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 169 VRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTK---FQFREIEVETTEVKTYSHFVIRTFKLTRTtpES 245
Cdd:cd14543   80 PLPKTYS-DFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgssLRYGDLTVTNLSVENKEHYKKTTLEIHNT--ET 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 246 IETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQFME-----------KNPVEAPMVVHCSNGAGRSGAFLALDANLEL 313
Cdd:cd14543  157 DESRQVTHFQFTSWPDFGVPSSAAaLLDFLGEVRQQQAlavkamgdrwkGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQ 236

                        250       260       270
                 ....*....|....*....|....*....|....
gi 212645547 314 MKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 347
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: 174.85 E-value: 4.37e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 124 YPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVM 203
Cdd:cd14548    2 YTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKD-DFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 204 CLQYWPLTKFQ--FREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQF 280
Cdd:cd14548   81 CDHYWPFDQDPvyYGDITVTMLSESVLPDWTIREFKLERGD----EVRSVRQFHFTAWPDHGVPEAPDsLLRFVRLVRDY 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212645547 281 MEKNpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
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: 173.48 E-value: 1.96e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 197
Cdd:cd14554    9 KNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQG----PLAettEDFWRMLWEHNSTIIVMLTKLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 198 DFMRVMCLQYWPL-TKFQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYIS-AFIELRR 275
Cdd:cd14554   85 EMGREKCHQYWPAeRSARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTVRQFQFTDWPEQGVPKSGeGFIDFIG 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645547 276 RVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 347
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: 172.91 E-value: 1.06e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 200
Cdd:cd14626   44 KNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETL-SDFWRMVWEQRTATIVMMTRLEEKS 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 201 RVMCLQYWPLTKFQ-FREIEV---ETTEVKTYShfvIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIELRR 275
Cdd:cd14626  123 RVKCDQYWPIRGTEtYGMIQVtllDTVELATYS---VRTFALYKNG--SSEKREVRQFQFMAWPDHGVPeYPTPILAFLR 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 276 RVRQFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 354
Cdd:cd14626  198 RVKAC---NPPDAgPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274


                 ..
gi 212645547 355 MC 356
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: 1.57e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 120 DRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKV 196
Cdd:cd14630    5 NKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQG----PMQEtvkDFWRMIWQENSASVVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 197 FDFMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPESIetRIVKHFHFTEWELDSFP-YISAFIELRR 275
Cdd:cd14630   81 VEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEI--REIRQFHFTSWPDHGVPcYATGLLGFVR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 276 RVRqFMekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 354
Cdd:cd14630  159 QVK-FL--NPPDAgPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEAC 235


                 ..
gi 212645547 355 MC 356
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: 8.94e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN---QGSQRHYPSFIHNKGK-ANYGPFIVEIMNY 519
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNlveKGREKCERYWPEEGGKpLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 520 HQYPAMTshmvkvmKRTFMISDIMatgaqnqqiDAEVRICCVIQVRMWPiENKVPLSTtglIDVIKMARSWRKRAPDRpe 599
Cdd:cd00047   81 EELSDYT-------IRTLELSPKG---------CSESREVTHLHYTGWP-DHGVPSSP---EDLLALVRRVRKEARKP-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645547 600 TKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 661
Cdd:cd00047  139 NGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 160.87 E-value: 6.20e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547  413 NRGKNRDVMVVPPDHARPYLQtlhGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN-- 490
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT---GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEle 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547  491 ----QGSQRHYPSfiHNKGKANYGPFIVEIMNYHQYPAmtshmvKVMKRTFMIsdimatgaQNQQIDAEVRiccVIQVRM 566
Cdd:pfam00102  78 ekgrEKCAQYWPE--EEGESLEYGDFTVTLKKEKEDEK------DYTVRTLEV--------SNGGSEETRT---VKHFHY 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547  567 --WPiENKVPLSTTGLIDVIKMARSWRkrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRI 644
Cdd:pfam00102 139 tgWP-DHGVPESPNSLLDLLRKVRKSS----LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRS 213

                         250       260
                  ....*....|....*....|
gi 212645547  645 NRPQLIDMKDEYKYLYDVML 664
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: 159.80 E-value: 8.65e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 134 RVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL 210
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQG----PVHEtvyDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 211 TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPY-ISAFIELRRRVRqfMEKNPVEAP 289
Cdd:cd14631   77 DTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYN--EIREVKQFHFTGWPDHGVPYhATGLLSFIRRVK--LSNPPSAGP 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645547 290 MVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 355
Cdd:cd14631  153 IVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218

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: 159.72 E-value: 1.51e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 124 YPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVM 203
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVN-DFWRMVWEQKSATIVMLTNLKERKEEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 204 CLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTTPESIE-TRIVKHFHFTEWELDSFPYISafIELRRRVRQFM 281
Cdd:cd14620   80 CYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKaPRLVTQLHFTSWPDFGVPFTP--IGMLKFLKKVK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645547 282 EKNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
Cdd:cd14620  158 SVNPVHAgPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

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: 161.41 E-value: 1.53e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 200
Cdd:cd14625   50 KNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETF-GDFWRMVWEQRSATVVMMTKLEEKS 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 201 RVMCLQYWPLTKFQ-FREIEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIELRRRVR 278
Cdd:cd14625  129 RIKCDQYWPSRGTEtYGMIQVTLLDTIELATFCVRTFSLHKNG--SSEKREVRQFQFTAWPDHGVPeYPTPFLAFLRRVK 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212645547 279 QFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVMC 356
Cdd:cd14625  207 TC---NPPDAgPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282

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: 1.89e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVF 197
Cdd:cd14633   43 KNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQG----PMQEtiyDFWRMVWHENTASIIMVTNLV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 198 DFMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYISAfiELRRRV 277
Cdd:cd14633  119 EVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVH--EIREIRQFHFTGWPDHGVPYHAT--GLLGFV 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212645547 278 RQFMEKNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 355
Cdd:cd14633  195 RQVKSKSPPNAgPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273

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: 157.95 E-value: 2.94e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVfDFMRVMCLQYWPL-TKFQFREIEVETT 223
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQH----PLPntvTDFWRLVYDYGCTSIVMLNQL-DPKDQSCPQYWPDeGSGTYGPIQVEFV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 224 EVKTYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEKNPvEAPMVVHCSNGAGRS 301
Cdd:cd14556   76 STTIDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRdrDTPPSKRALLKLLSEVEKWQEQSG-EGPIVVHCLNGVGRS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 212645547 302 GAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
Cdd:cd14556  155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

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: 9.21e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAVRTKpMNAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTEVKT 227
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQE-MVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 228 YSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPY----ISAFIelrRRVRQfmeKNPVEA-PMVVHCSNGAGRSG 302
Cdd:cd14632   80 LAEYSVRTFALERRGYSARHE--VKQFHFTSWPEHGVPYhatgLLAFI---RRVKA---STPPDAgPVVVHCSAGAGRTG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 212645547 303 AFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVMC 356
Cdd:cd14632  152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205

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: 158.74 E-value: 1.34e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 200
Cdd:cd14624   50 KNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETF-GDFWRMIWEQRSATVVMMTKLEERS 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 201 RVMCLQYWPL----TKFQFREIEVETTEVKTYshfVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIELRR 275
Cdd:cd14624  129 RVKCDQYWPSrgteTYGLIQVTLLDTVELATY---CVRTFALYKNG--SSEKREVRQFQFTAWPDHGVPeHPTPFLAFLR 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 276 RVRQFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 354
Cdd:cd14624  204 RVKTC---NPPDAgPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280


                 ..
gi 212645547 355 MC 356
Cdd:cd14624  281 TC 282

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: 156.97 E-value: 1.46e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 122 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMR 201
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVG-DFWRMIWEQQSSTIVMLTNCMEAGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 202 VMCLQYWPL--TKFQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPY-ISAFIELRRRVR 278
Cdd:cd14619   80 VKCEHYWPLdyTPCTYGHLRVTVVSEEVMENWTVREFLLKQV--EEQKTLSVRHFHFTAWPDHGVPSsTDTLLAFRRLLR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645547 279 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
Cdd:cd14619  158 QWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229

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

Pssm-ID: 350403 [Multi-domain] Cd Length: 204 Bit Score: 155.85 E-value: 1.87e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTE 224
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQG----PMQEtvyDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 225 VKTYSHFVIRTFKLTRTTPESIetRIVKHFHFTEWELDSFPYISAfiELRRRVRQFMEKNPVEA-PMVVHCSNGAGRSGA 303
Cdd:cd14555   77 TEPLAEYVVRTFALERRGYHEI--REVRQFHFTGWPDHGVPYHAT--GLLGFIRRVKASNPPSAgPIVVHCSAGAGRTGC 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212645547 304 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 355
Cdd:cd14555  153 YIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204

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: 152.89 E-value: 2.12e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETT 223
Cdd:cd14549    1 YINANYVDGYNKARAYIATQG----PLPStfdDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 224 EVKTYSHFVIRTF-----KLTRTTPESIEtRIVKHFHFTEWE-----LDSFPYISaFielrrrVRQFMEKNPVEA-PMVV 292
Cdd:cd14549   77 STEVLATYTVRTFslknlKLKKVKGRSSE-RVVYQYHYTQWPdhgvpDYTLPVLS-F------VRKSSAANPPGAgPIVV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 212645547 293 HCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
Cdd:cd14549  149 HCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 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: 153.17 E-value: 3.09e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 122 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMR 201
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIE-DFWRLVWEQQVCNIIMLTVGMENGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 202 VMCLQYWP--LTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFP----YISAFIELrr 275
Cdd:cd14618   80 VLCDHYWPseSTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLR--KERRVKHLHYTAWPDHGIPestsSLMAFREL-- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212645547 276 rVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
Cdd:cd14618  156 -VREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229

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: 152.51 E-value: 4.84e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 128 LPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQY 207
Cdd:cd14623    6 IPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIE-DFWRMIWEWKSCSIVMLTELEERGQEKCAQY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 208 WPLT-KFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYI-SAFIELRRRVrQFMEKNP 285
Cdd:cd14623   85 WPSDgSVSYGDITIELKKEEECESYTVRDLLVTNTREN--KSRQIRQFHFHGWPEVGIPSDgKGMINIIAAV-QKQQQQS 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645547 286 VEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
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: 151.39 E-value: 5.72e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTE 224
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQG----PLPdtiADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 225 VKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEW---ELDSFPyiSAFIELRRRVRQ----FMEKNPVEAPMVVHCSNG 297
Cdd:cd14558   77 TEKSPTYTVRVFEITHL--KRKDSRTVYQYQYHKWkgeELPEKP--KDLVDMIKSIKQklpyKNSKHGRSVPIVVHCSDG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 212645547 298 AGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
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: 1.60e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETTEVK 226
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVE-DFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDgSVSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 227 TYSHFVIRTFKLTRTTPESieTRIVKHFHFTEWELDSFPY-ISAFIELRRRVrQFMEKNPVEAPMVVHCSNGAGRSGAFL 305
Cdd:cd14552   80 DYEDYTLRDFLVTKGKGGS--TRTVRQFHFHGWPEVGIPDnGKGMIDLIAAV-QKQQQQSGNHPITVHCSAGAGRTGTFC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 212645547 306 ALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
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: 150.65 E-value: 1.53e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFM 200
Cdd:cd14629   56 KNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE-DFWRMLWEHNSTIVVMLTKLREMG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 201 RVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYI-SAFIELRRRVR 278
Cdd:cd14629  135 REKCHQYWPAERsARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTIRQFQFTDWPEQGVPKTgEGFIDFIGQVH 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645547 279 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
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: 148.04 E-value: 1.89e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 122 NPYPDTLPYDYNRVILpRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMR 201
Cdd:cd14615    1 NRYNNVLPYDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVK-DFWRMVWEKNVYAIVMLTKCVEQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 202 VMCLQYWPLT-KFQFREIEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFPYIS-AFIELRRRVRQ 279
Cdd:cd14615   79 TKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQ--TNESRTVRHFHFTSWPDHGVPETTdLLINFRHLVRE 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645547 280 FMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFI 346
Cdd:cd14615  157 YMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223

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: 148.73 E-value: 5.64e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKpMNAEFWRMVWELGSNCIVMLTKVFDFM 200
Cdd:cd14627   56 KNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAE-TTEDFWRMLWENNSTIVVMLTKLREMG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 201 RVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYI-SAFIELRRRVR 278
Cdd:cd14627  135 REKCHQYWPAERsARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTVRQFQFTDWPEQGVPKSgEGFIDFIGQVH 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645547 279 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
Cdd:cd14627  213 KTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286

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: 146.60 E-value: 5.86e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 122 NPYPDTLPYDYNRVILPRIDGDENSHYINASYV--NSWLRDkaYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKV 196
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIpgNNFRRE--YIATQG----PLPGtkdDFWKMVWEQNVHNIVMVTQC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 197 FDFMRVMCLQYWPLTK--FQFREIEVETTEVKTYSHFVIRTFKLTrtTPESIET-RIVKHFHFTEWELDSFPYIS-AFIE 272
Cdd:cd14617   75 VEKGRVKCDHYWPADQdsLYYGDLIVQMLSESVLPEWTIREFKIC--SEEQLDApRLVRHFHYTVWPDHGVPETTqSLIQ 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645547 273 LRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
Cdd:cd14617  153 FVRTVRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

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: 148.73 E-value: 5.99e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKpMNAEFWRMVWELGSNCIVMLTKVFDFM 200
Cdd:cd14628   55 KNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAE-TTEDFWRMLWEHNSTIVVMLTKLREMG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 201 RVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYI-SAFIELRRRVR 278
Cdd:cd14628  134 REKCHQYWPAERsARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTVRQFQFTDWPEQGVPKSgEGFIDFIGQVH 211

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645547 279 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
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: 142.15 E-value: 2.41e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDenSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFM 200
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSG-HFWQMVWEQNSKAVIMLNKLMEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 201 RVMCLQYWPL-----TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYI-SAFIELR 274
Cdd:cd14545   78 QIKCAQYWPQgegnaMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQ--ETREVLHFHYTTWPDFGVPESpAAFLNFL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645547 275 RRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKtGQLDFFEYAKTLVNSRPH---LIDSVEQYMFIY 347
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: 139.76 E-value: 8.43e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETTEVK 226
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVE-DFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEgSVTHGEITIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 227 TYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYI-SAFIELRRRVrQFMEKNPVEAPMVVHCSNGAGRSGAFL 305
Cdd:cd14622   81 LLETISIRDFLVTYNQEK--QTRLVRQFHFHGWPEIGIPAEgKGMIDLIAAV-QKQQQQTGNHPIVVHCSAGAGRTGTFI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 212645547 306 ALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
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: 141.33 E-value: 1.72e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSH--YINASYVNSWLRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFD 198
Cdd:cd17667   30 KNRYINILAYDHSRVKLRPLPGKDSKHsdYINANYVDGYNKAKAYIATQG-PLKSTFEDFWRMIWEQNTGIIVMITNLVE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 199 FMRVMCLQYWPL-TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPESIET---------RIVKHFHFTEWELDSFP-YI 267
Cdd:cd17667  109 KGRRKCDQYWPTeNSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKgnpkgrqneRTVIQYHYTQWPDMGVPeYA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 268 SAFIELRRRVRQfmEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 347
Cdd:cd17667  189 LPVLTFVRRSSA--ARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266


                 ....*...
gi 212645547 348 EVLSEAVM 355
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: 138.68 E-value: 3.49e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 122 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSW-LRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 197
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQG----PLPntvADFWRMVWQEKTPIIVMITNLT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 198 DfMRVMCLQYWP-LTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYIS-AFIELRR 275
Cdd:cd14547   77 E-AKEKCAQYWPeEENETYGDFEVTVQSVKETDGYTVRKLTLKYGG----EKRYLKHYWYTSWPDHKTPEAAqPLLSLVQ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645547 276 RVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 347
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: 135.84 E-value: 2.70e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVN-SWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFR--EIEVE 221
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQG----PLPAtigDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEygDLTVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 222 TTEVKTYSH--FVIRTFKLTRTTPESietRIVKHFHFTEW-ELDSFPYISAFIELRRRVRQFMEKNPVEAPMVVHCSNGA 298
Cdd:cd18533   77 LVSEEENDDggFIVREFELSKEDGKV---KKVYHIQYKSWpDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGV 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 299 GRSGAFLALDANLELMKKTGQLDFFEY------AKTlVNS----RPHLIDSVEQYMFIYE 348
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: 4.05e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFM 200
Cdd:cd14614   15 KNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRN-DFWKMVLQQKSQIIVMLTQCNEKR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 201 RVMCLQYWPLTK--FQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYISA---FIELRR 275
Cdd:cd14614   94 RVKCDHYWPFTEepVAYGDITVEMLSEEEQPDWAIREFRVSYAD----EVQDVMHFNYTAWPDHGVPTANAaesILQFVQ 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212645547 276 RVRQFMEKNPveAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
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: 137.46 E-value: 5.94e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 120 DRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDF 199
Cdd:cd14621   54 EKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVN-DFWRMIWEQNTATIVMVTNLKER 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 200 MRVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTF------KLTRTTPEsietRIVKHFHFTEWELDSFPYISafIE 272
Cdd:cd14621  133 KECKCAQYWPDQGcWTYGNIRVSVEDVTVLVDYTVRKFciqqvgDVTNKKPQ----RLITQFHFTSWPDFGVPFTP--IG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 273 LRRRVRQFMEKNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 351
Cdd:cd14621  207 MLKFLKKVKNCNPQYAgAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286


                 .
gi 212645547 352 E 352
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: 134.77 E-value: 3.79e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 120 DRNPYPDTLPYDYNRVILPRIDGDenshYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKV 196
Cdd:cd14608   27 NRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQG----PLPntcGHFWEMVWEQKSRGVVMLNRV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 197 FDFMRVMCLQYWPltKFQFREIEVETTEVK-------TYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYISA 269
Cdd:cd14608   99 MEKGSLKCAQYWP--QKEEKEMIFEDTNLKltlisedIKSYYTVRQLELENLTTQ--ETREILHFHYTTWPDFGVPESPA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 270 -FIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPH---LIDSVEQYMF 345
Cdd:cd14608  175 sFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFrmgLIQTADQLRF 254


                 ..
gi 212645547 346 IY 347
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: 131.38 E-value: 7.54e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLsNQGSQRH--YPSFIHNKGKANYGPFIVEIMNyhq 521
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDqsCPQYWPDEGSGTYGPIQVEFVS--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 522 ypamTSHMVKVMKRTFMISDIMATgaqnqqiDAEVRICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRAPDrpetK 601
Cdd:cd14556   77 ----TTIDEDVISRIFRLQNTTRP-------QEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGE----G 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 602 PTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 661
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: 130.80 E-value: 1.39e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETTEVK 226
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVN-DFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQgCWTYGNLRVRVEDTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 227 TYSHFVIRTFKLTRTTPESIE--TRIVKHFHFTEWELDSFPYISafIELRRRVRQFMEKNPVEA-PMVVHCSNGAGRSGA 303
Cdd:cd14551   80 VLVDYTTRKFCIQKVNRGIGEkrVRLVTQFHFTSWPDFGVPFTP--IGMLKFLKKVKSANPPRAgPIVVHCSAGVGRTGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 212645547 304 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
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: 1.63e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT---KFQFREIEVETTE 224
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVD-DFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMeegSRAFGDVVVKINE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 225 VKTYSHFVIRTFKLTRTTpESIETRIVKHFHFTEWELDSFPY-ISAFIELRRRVRQFmeKNPVEAPMVVHCSNGAGRSGA 303
Cdd:cd14557   80 EKICPDYIIRKLNINNKK-EKGSGREVTHIQFTSWPDHGVPEdPHLLLKLRRRVNAF--NNFFSGPIVVHCSAGVGRTGT 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 212645547 304 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
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: 3.35e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547  81 VAYVQE--RRKKRILFKGEYLMVNRSiDNNKCRCDVGSTMMDRNPYPDTLPYDYNRVILPRIDGDENSHYINAS-YVNSW 157
Cdd:cd14609    4 LAYMEDhlRNRDRLAKEWQALCAYQA-EPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 158 LRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWP---LTKFQFREIEVETTEVKTySHFVIR 234
Cdd:cd14609   83 PRMPAYIATQGPLSHTI-ADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPdegSSLYHIYEVNLVSEHIWC-EDFLVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 235 TFKLTRTtpESIETRIVKHFHFTEWELDSFPYIS-AFIELRRRVRQFMEKNpvEAPMVVHCSNGAGRSGAFLALDANLEL 313
Cdd:cd14609  161 SFYLKNV--QTQETRTLTQFHFLSWPAEGIPSSTrPLLDFRRKVNKCYRGR--SCPIIVHCSDGAGRTGTYILIDMVLNR 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 212645547 314 MKK-TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 354
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: 131.10 E-value: 5.13e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547  85 QERRKKRILFKGEYlmvnrsidnnKCRCDVGSTM--MDRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKA 162
Cdd:cd14603    5 SEIRACSAAFKADY----------VCSTVAGGRKenVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 163 YVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKfqfreievettEVKTYSHFVIRTFKLT 239
Cdd:cd14603   75 YIATQG----PLSHtvlDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQ-----------EPLQTGPFTITLVKEK 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 240 RTTPESI----------ETRIVKHFHFTEWE----LDSFPYISAFIELrrrVRQFMEKNPVeaPMVVHCSNGAGRSGAFL 305
Cdd:cd14603  140 RLNEEVIlrtlkvtfqkESRSVSHFQYMAWPdhgiPDSPDCMLAMIEL---ARRLQGSGPE--PLCVHCSAGCGRTGVIC 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 212645547 306 ALD-ANLELMKKTGQLDF--FEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
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: 1.18e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 119 MDRNPYPDTLPYDYNRVILPRIDGDENSHYINASYV-NSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVF 197
Cdd:cd14610   45 VQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImDHDPRNPAYIATQGPLPATV-ADFWQMVWESGCVVIVMLTPLA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 198 DFMRVMCLQYWPLTKFQFREI-EVETTEVKTYSH-FVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYIS-AFIELR 274
Cdd:cd14610  124 ENGVKQCYHYWPDEGSNLYHIyEVNLVSEHIWCEdFLVRSFYLKNL--QTNETRTVTQFHFLSWNDQGVPASTrSLLDFR 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 275 RRVRQFMEKNpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTG-QLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEA 353
Cdd:cd14610  202 RKVNKCYRGR--SCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEE 279


                 .
gi 212645547 354 V 354
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: 2.71e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDE-NSHYINASYVNSWL-------RDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVM 192
Cdd:cd14544    4 KNRYKNILPFDHTRVILKDRDPNVpGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVS-DFWSMVWQENSRVIVM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 193 LTKVFDFMRVMCLQYWP--LTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpESIETRIVKHFHFTEWE---LDSFPY- 266
Cdd:cd14544   83 TTKEVERGKNKCVRYWPdeGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLD-QGDPIREIWHYQYLSWPdhgVPSDPGg 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 267 ISAFIElrrRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTG---QLDFFEYAKTLVNSRPHLIDSVEQY 343
Cdd:cd14544  162 VLNFLE---DVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQY 238


                 ....
gi 212645547 344 MFIY 347
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: 125.48 E-value: 1.29e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL-TKFQFREIEVETTEVK 226
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQG-PLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAdGSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 227 TYSHFVIRTFKLTRTTPES------IETRIVKHFHFTEWELDSFP-YISAFIELRRRVRQfmEKNPVEAPMVVHCSNGAG 299
Cdd:cd17668   80 VLAYYTVRNFTLRNTKIKKgsqkgrPSGRVVTQYHYTQWPDMGVPeYTLPVLTFVRKASY--AKRHAVGPVVVHCSAGVG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 212645547 300 RSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
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: 125.18 E-value: 1.31e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKA--YVVTQAvrtkPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWP----LTKFQFREI 218
Cdd:cd14538    1 YINASHIRIPVGGDTyhYIACQG----PLpntTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslnKPLICGGRL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 219 EVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPyiSAFIELRRRVRqFMEKNPVEAPMVVHCSNGA 298
Cdd:cd14538   77 EVSLEKYQSLQDFVIRRISLRDK--ETGEVHHITHLNFTTWPDHGTP--QSADPLLRFIR-YMRRIHNSGPIVVHCSAGI 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 212645547 299 GRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEA 353
Cdd:cd14538  152 GRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206

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: 2.34e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 197
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQG----PLSttlLDFWRMIWEYSVLIIVMACMEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 198 DFMRVMCLQYWPLT---KFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPY-ISAFIEL 273
Cdd:cd14602   77 EMGKKKCERYWAEPgemQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS----ETRTIYQFHYKNWPDHDVPSsIDPILEL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 274 RRRVRQFMEKNPVeaPMVVHCSNGAGRSGAFLALDANLELMKK---TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
Cdd:cd14602  153 IWDVRCYQEDDSV--PICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230


                 ..
gi 212645547 351 SE 352
Cdd:cd14602  231 IE 232

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: 125.75 E-value: 2.79e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRID-GDENSHYINASYVNSW-LRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFD 198
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYgGEEKVYIATQG-PTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 199 fMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFP-YISAFIELRRRV 277
Cdd:cd14613  107 -MNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG----EERGLKHYWYTSWPDQKTPdNAPPLLQLVQEV 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212645547 278 RQFMEK-NPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 351
Cdd:cd14613  182 EEARQQaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256

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: 126.12 E-value: 3.26e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 119 MDRNPYPDTLPYDYNRVILpridgDENSHYINASYVNSWLrDKAYVVTQAVRTK-PMN---AEFWRMVWELGSNCIVMLT 194
Cdd:cd14600   41 MDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNMEI-PSANIVNKYIATQgPLPhtcAQFWQVVWEQKLSLIVMLT 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 195 KVFDFMRVMCLQYWPltkfqfreievETTEVKTYSHF-------------VIRTFKLTRTtpESIETRIVKHFHFTEWEL 261
Cdd:cd14600  115 TLTERGRTKCHQYWP-----------DPPDVMEYGGFrvqchsedctiayVFREMLLTNT--QTGEERTVTHLQYVAWPD 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 262 DSFPYISA-FIELRRRVRQFMEKNpveAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSV 340
Cdd:cd14600  182 HGVPDDSSdFLEFVNYVRSKRVEN---EPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTS 258

                        250
                 ....*....|
gi 212645547 341 EQYMFIYEVL 350
Cdd:cd14600  259 SQYKFVCEAI 268

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: 124.94 E-value: 3.80e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV---NL 488
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPIRGvEGSDY--INASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVmltKL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 489 SNQGSQRHYPSFIHNKGkANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVRMWP 568
Cdd:cd14554   84 REMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTVRQFQFTDWP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 569 iENKVPLSTTGLIDVIKMARswrKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQ 648
Cdd:cd14554  147 -EQGVPKSGEGFIDFIGQVH---KTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPA 222

                        250
                 ....*....|..
gi 212645547 649 LIDMKDEYKYLY 660
Cdd:cd14554  223 MVQTEDQYQFCY 234

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: 124.25 E-value: 4.98e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 122 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMR 201
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTV-GDFWRMVWETRAKTIVMLTQCFEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 202 VMCLQYWPLTK---FQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYISA----FIELR 274
Cdd:cd14616   80 IRCHQYWPEDNkpvTVFGDIVITKLMEDVQIDWTIRDLKIERHG----DYMMVRQCNFTSWPEHGVPESSAplihFVKLV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645547 275 RRVRQfmEKNpveAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
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: 7.28e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVfDFMRvMCLQYWP-LTKFQFREIEVETTEVK 226
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTV-ADFWRLVFDYNCSSVVMLNEM-DAAQ-LCMQYWPeKTSCCYGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 227 TYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEK-NPVEAPMVVHCSNGAGRSGA 303
Cdd:cd14634   78 IDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAyrDTPPSKRSILKVVRRLEKWQEQyDGREGRTVVHCLNGGGRSGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 212645547 304 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
Cdd:cd14634  158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 125.11 E-value: 1.56e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547  77 ASKFVAYVQERRKKRILfKGEYLMVNRSIDNNKCRCDVGSTMMDRNPYPDTLPYDYNRVILPRIDGdeNSHYINASYVNS 156
Cdd:PHA02742  12 AKNCEQLIEESNLAEIL-KEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 157 WLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYW---PLTKFQFREIEVETTEVKTYSHFVI 233
Cdd:PHA02742  89 HNAKGRFICTQAPLEETAL-DFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmphERGKATHGEFKIKTKKIKSFRNYAV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 234 RTFKLTRT-TPESIEtriVKHFHFTEWELDSFPY-ISAFIELRRRVRQFMEKNPV---------EAPMVVHCSNGAGRSG 302
Cdd:PHA02742 168 TNLCLTDTnTGASLD---IKHFAYEDWPHGGLPRdPNKFLDFVLAVREADLKADVdikgenivkEPPILVHCSAGLDRAG 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 212645547 303 AFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 347
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: 123.15 E-value: 2.61e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDenshYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 197
Cdd:cd14607   27 RNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQG----PLPntcCHFWLMVWQQKTKAVVMLNRIV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 198 DFMRVMCLQYWPLTK---FQFRE----IEVETTEVKTYshFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYISA- 269
Cdd:cd14607   99 EKDSVKCAQYWPTDEeevLSFKEtgfsVKLLSEDVKSY--YTVHLLQLENI--NSGETRTISHFHYTTWPDFGVPESPAs 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 270 FIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDfFEYAKTLVNSRPH---LIDSVEQYMFI 346
Cdd:cd14607  175 FLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDS-VDIKQVLLDMRKYrmgLIQTPDQLRFS 253


                 .
gi 212645547 347 Y 347
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: 119.25 E-value: 2.34e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVIL-PRIDGDENSHYINASYVNSWL-RDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFD 198
Cdd:cd14611    2 KNRYKTILPNPHSRVCLkPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVN-DFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 199 fMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFP-YISAFIELRRRV 277
Cdd:cd14611   81 -KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGS----QSRSVKHYWYTSWPDHKTPdSAQPLLQLMLDV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 278 RQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 347
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: 2.49e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVN-----SWLRDKaYVVTQAvrtkPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT--KFQFRE 217
Cdd:cd14541    2 YINANYVNmeipgSGIVNR-YIAAQG----PLpntCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLgeTMQFGN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 218 IEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQFmEKNPVEaPMVVHCSN 296
Cdd:cd14541   77 LQITCVSEEVTPSFAFREFILTNT--NTGEERHITQMQYLAWPDHGVPDDSSdFLDFVKRVRQN-RVGMVE-PTVVHCSA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212645547 297 GAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
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: 119.17 E-value: 4.71e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDG-DENSHYINASYVNSWL-RDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTK 195
Cdd:cd14612   18 KDRYKTILPNPQSRVCLRRAGSqEEEGSYINANYIRGYDgKEKAYIATQG----PMLntvSDFWEMVWQEECPIIVMITK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 196 VFDfMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFkltrTTPESIETRIVKHFHFTEWELDSFPYIS-AFIELR 274
Cdd:cd14612   94 LKE-KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDL----TIQLEEESRSVKHYWFSSWPDHQTPESAgPLLRLV 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645547 275 RRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 351
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: 118.39 E-value: 6.47e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILpridGDENShYINASYVNSWLRDKAYVVTQAVRTKPMN-AEFWRMVWELGSNCIVMLTKVFDF 199
Cdd:cd14597    6 KNRYKNILPYDTTRVPL----GDEGG-YINASFIKMPVGDEEFVYIACQGPLPTTvADFWQMVWEQKSTVIAMMTQEVEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 200 MRVMCLQYWP--LTKFQFREIEVETTEVKT--YSHFVIRTFKLTRTtpESIETRIVKHFHFTEW---ELDSFPY-ISAFI 271
Cdd:cd14597   81 GKIKCQRYWPeiLGKTTMVDNRLQLTLVRMqqLKNFVIRVLELEDI--QTREVRHITHLNFTAWpdhDTPSQPEqLLTFI 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212645547 272 ELRRRVRQfmeknpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
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: 117.55 E-value: 7.05e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYV-NSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIeVETTEVK 226
Cdd:cd14546    1 YINASTIyDHDPRNPAYIATQGPLPHTI-ADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHI-YEVHLVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 227 TYS---HFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPY-ISAFIELRRRV-RQFMEKNpveAPMVVHCSNGAGRS 301
Cdd:cd14546   79 EHIwcdDYLVRSFYLKNL--QTSETRTVTQFHFLSWPDEGIPAsAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAGRT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 212645547 302 GAFLALDANLE-LMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 354
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: 116.39 E-value: 1.53e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKA--YVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTEV 225
Cdd:cd14596    1 YINASYITMPVGEEElfYIATQGPLPSTID-DFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 226 KTYS---HFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYISA----FIELRRRVRQfmeknpvEAPMVVHCSNGA 298
Cdd:cd14596   80 ENYQalqYFIIRIIKLVEK--ETGENRLIKHLQFTTWPDHGTPQSSDqlvkFICYMRKVHN-------TGPIVVHCSAGI 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 212645547 299 GRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 354
Cdd:cd14596  151 GRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206

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: 2.81e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 120 DRNPYPDTLPYDYNRVILPriDGDEN---SHYINASYV---------NSWLRdKAYVVTQAVRTKPMNaEFWRMVWELGS 187
Cdd:cd14605    4 NKNRYKNILPFDHTRVVLH--DGDPNepvSDYINANIImpefetkcnNSKPK-KSYIATQGCLQNTVN-DFWRMVFQENS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 188 NCIVMLTKVFDFMRVMCLQYWPlTKFQFRE---IEVETTEVKTYSHFVIRTFKLTRTTPESIEtRIVKHFHFTEWELDSF 264
Cdd:cd14605   80 RVIVMTTKEVERGKSKCVKYWP-DEYALKEygvMRVRNVKESAAHDYILRELKLSKVGQGNTE-RTVWQYHFRTWPDHGV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 265 PY-ISAFIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTG---QLDFFEYAKTLVNSRPHLIDSV 340
Cdd:cd14605  158 PSdPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTE 237


                 ....*..
gi 212645547 341 EQYMFIY 347
Cdd:cd14605  238 AQYRFIY 244

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

Pssm-ID: 350485 [Multi-domain] Cd Length: 207 Bit Score: 115.78 E-value: 2.91e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTqavrTKPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVM-CLQYWPLTKFQ-FREIEVET 222
Cdd:cd14637    1 YINAALTDSYTRSAAFIVT----LHPLQnttTDFWRLVYDYGCTSVVMLNQLNQSNSAWpCLQYWPEPGLQqYGPMEVEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 223 TEVKTYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEKNPvEAPMVVHCSNGAGR 300
Cdd:cd14637   77 VSGSADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAyrDTPDSKKAFLHLLASVEKWQRESG-EGRTVVHCLNGGGR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212645547 301 SGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
Cdd:cd14637  156 SGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207

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: 114.44 E-value: 5.79e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTK---FQFREIEVETTE 224
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVL-DFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeeqLQFGPFKISLEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 225 VKTYSH-FVIRTFKLTRTTpesiETRIVKHFHFTEW-ELDSFPYISAFIELRRRVRQFMEKNPVeaPMVVHCSNGAGRSG 302
Cdd:cd14542   80 EKRVGPdFLIRTLKVTFQK----ESRTVYQFHYTAWpDHGVPSSVDPILDLVRLVRDYQGSEDV--PICVHCSAGCGRTG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 212645547 303 AFLALDANLELMKK---TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 347
Cdd:cd14542  154 TICAIDYVWNLLKTgkiPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201

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: 114.48 E-value: 9.80e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKA--YVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWP-----LTKFQFRE 217
Cdd:cd14540    1 YINASHITATVGGKQrfYIAAQG----PLQNtvgDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggeHDALTFGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 218 IEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEW-------ELDSF-PYISAFIELRRRVRQFMEKNPVEAP 289
Cdd:cd14540   77 YKVSTKFSVSSGCYTTTGLRVKHTL--SGQSRTVWHLQYTDWpdhgcpeDVSGFlDFLEEINSVRRHTNQDVAGHNRNPP 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212645547 290 MVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
Cdd:cd14540  155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVL 215

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: 113.60 E-value: 2.16e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 422 VVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN---QGSQR--H 496
Cdd:cd14548    5 ILPYDHSRVKLIPINEEEGS-DYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQcmeKGRVKcdH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 497 YPSFihNKGKANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISDImatgaqnqqidAEVRICCVIQVRMWPiENKVPLS 576
Cdd:cd14548   84 YWPF--DQDPVYYGDITVTMLSESVLPDWT-------IREFKLERG-----------DEVRSVRQFHFTAWP-DHGVPEA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 577 TTGLIDVIKMARSWRKRapdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEY 656
Cdd:cd14548  143 PDSLLRFVRLVRDYIKQ-----EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQY 217


                 ....
gi 212645547 657 KYLY 660
Cdd:cd14548  218 IFLH 221

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 116.18 E-value: 2.92e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 122 NPYPDTLPYDYNRVILP--RIDGDenshYINASYVNSWLRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFDF 199
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPaeRNRGD----YINANYVDGFEYKKKFICGQA-PTRQTCYDFYRMLWMEHVQIIVMLCKKKEN 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 200 MRVMCLQYW---PLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpESIETriVKHFHFTEWELDSFP-----YISAFI 271
Cdd:PHA02738 128 GREKCFPYWsdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQT--VTHFNFTAWPDHDVPkntseFLNFVL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 272 ELRRRVRQFME-------KNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYM 344
Cdd:PHA02738 205 EVRQCQKELAQeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                 ....*.
gi 212645547 345 FIYEVL 350
Cdd:PHA02738 285 FCYRAV 290

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 114.33 E-value: 8.84e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILpRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 197
Cdd:PHA02747  54 KNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQG----PFAetcADFWKAVWQEHCSIIVMLTPTK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 198 DFM-RVMCLQYWPLTK---FQFREIEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP----YISA 269
Cdd:PHA02747 129 GTNgEEKCYQYWCLNEdgnIDMEDFRIETLKTSVRAKYILTLIEITDKI--LKDSRKISHFQCSEWFEDETPsdhpDFIK 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 270 FIELRRRVRQ-----FMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYM 344
Cdd:PHA02747 207 FIKIIDINRKksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                 ....*....
gi 212645547 345 FI---YEVL 350
Cdd:PHA02747 287 FIqpgYEVL 295

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 107.44 E-value: 1.10e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547   250 IVKHFHFTEWELDSFPYIS-AFIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLE-LMKKTGQLDFFEYAK 327
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPdSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQqLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 212645547   328 TLVNSRPHLIDSVEQYMFIYEVLSE 352
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: 107.44 E-value: 1.10e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547   250 IVKHFHFTEWELDSFPYIS-AFIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLE-LMKKTGQLDFFEYAK 327
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPdSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQqLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 212645547   328 TLVNSRPHLIDSVEQYMFIYEVLSE 352
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: 110.50 E-value: 1.99e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVfDFMRvMCLQYWPLT-KFQFREIEVETTEVK 226
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVK-DFWRLVYDYGCTSIVMLNEV-DLAQ-GCPQYWPEEgMLRYGPIQVECMSCS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 227 TYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWELDSFPYIS--AFIELRRRVRQFMEK-NPVEAPMVVHCSNGAGRSGA 303
Cdd:cd14636   78 MDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSkrSFLKLILQVEKWQEEcDEGEGRTIIHCLNGGGRSGM 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 212645547 304 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
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: 4.49e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 200
Cdd:cd14604   60 KNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTV-IDFWRMIWEYNVAIIVMACREFEMG 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 201 RVMCLQYWPL---TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWE----LDSFPYISAFIEL 273
Cdd:cd14604  139 RKKCERYWPLygeEPMTFGPFRISCEAEQARTDYFIRTLLLEFQN----ETRRLYQFHYVNWPdhdvPSSFDSILDMISL 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 274 rrrVRQFMEKNPVeaPMVVHCSNGAGRSGAFLALDANLELMKK---TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
Cdd:cd14604  215 ---MRKYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289


                 ..
gi 212645547 351 SE 352
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: 107.80 E-value: 1.39e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNyhqyp 523
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMS----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 524 amTSHMVKVMKRTFMISDImatgAQNQQIDAEVRiccVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRApDRPETKpT 603
Cdd:cd14636   76 --CSMDCDVISRIFRICNL----TRPQEGYLMVQ---QFQYLGWASHREVPGSKRSFLKLILQVEKWQEEC-DEGEGR-T 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212645547 604 IVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
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: 106.70 E-value: 3.76e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMrvMCLQYWPLTKFQFR-EIEVETTEVK 226
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVK-DFWRLVLDYHCTSIVMLNDVDPAQ--LCPQYWPENGVHRHgPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 227 TYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEK-NPVEAPMVVHCSNGAGRSGA 303
Cdd:cd14635   78 LEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMyrDTPVSKRSFLKLIRQVDKWQEEyNGGEGRTVVHCLNGGGRSGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 212645547 304 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 352
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: 105.93 E-value: 6.58e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNYHQYP 523
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 524 AMTSHMVKVMkrtfmisdimaTGAQNQQidaEVRICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRApDRPETKpT 603
Cdd:cd14635   81 DIISRIFRIY-----------NAARPQD---GYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEY-NGGEGR-T 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212645547 604 IVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
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: 108.28 E-value: 8.01e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN- 490
Cdd:cd14628   52 NKFKNRLVNIMPYESTRVCLQPIRGvEGSDY--INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKl 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 491 -----QGSQRHYPSfihnKGKANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVR 565
Cdd:cd14628  130 remgrEKCHQYWPA----ERSARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTVRQFQFT 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 566 MWPiENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 645
Cdd:cd14628  190 DWP-EQGVPKSGEGFIDFIGQVHKTKEQFG---QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 265

                        250       260
                 ....*....|....*....|.
gi 212645547 646 RPQLIDMKDEYKYLYDVMLHW 666
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: 107.90 E-value: 9.29e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN- 490
Cdd:cd14627   53 NKFKNRLVNIMPYETTRVCLQPIRGvEGSDY--INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKl 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 491 -----QGSQRHYPSfihnKGKANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVR 565
Cdd:cd14627  131 remgrEKCHQYWPA----ERSARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTVRQFQFT 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 566 MWPiENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 645
Cdd:cd14627  191 DWP-EQGVPKSGEGFIDFIGQVHKTKEQFG---QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 266

                        250       260
                 ....*....|....*....|.
gi 212645547 646 RPQLIDMKDEYKYLYDVMLHW 666
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: 104.22 E-value: 2.54e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--NQgSQRHYPSFIH--NKGKANYGPFIVEIMNy 519
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqlNQ-SNSAWPCLQYwpEPGLQQYGPMEVEFVS- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 520 hqypamTSHMVKVMKRTFMISDImaTGAQNQQIdaevrICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRAPDrpe 599
Cdd:cd14637   79 ------GSADEDIVTRLFRVQNI--TRLQEGHL-----MVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGE--- 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212645547 600 tKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
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: 8.74e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 121 RNPYPDTLPYDYNRVILPriDGDEN---SHYINASYVNS--WLRD---KAYVVTQAVRTKPMNaEFWRMVWELGSNCIVM 192
Cdd:cd14606   21 KNRYKNILPFDHSRVILQ--GRDSNipgSDYINANYVKNqlLGPDenaKTYIASQGCLEATVN-DFWQMAWQENSRVIVM 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 193 LTKVFDFMRVMCLQYWPLTKFQ--FREIEVETTEVKTYSHFVIRTFKLtrTTPESIET-RIVKHFHFTEWELDSFPY--- 266
Cdd:cd14606   98 TTREVEKGRNKCVPYWPEVGMQraYGPYSVTNCGEHDTTEYKLRTLQV--SPLDNGELiREIWHYQYLSWPDHGVPSepg 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 267 -ISAFIElrrRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTG---QLDFFEYAKTLVNSRPHLIDSVEQ 342
Cdd:cd14606  176 gVLSFLD---QINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEAQ 252


                 ....*
gi 212645547 343 YMFIY 347
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: 3.72e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNyhqyp 523
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVS----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 524 amTSHMVKVMKRTFMISDImatgAQNQQidaEVRICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRApDRPETKpT 603
Cdd:cd14634   76 --ADIDEDIISRIFRICNM----ARPQD---GYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQY-DGREGR-T 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645547 604 IVMSHNGVSRVGVYIG-ANIC--IDQMDIdheVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
Cdd:cd14634  145 VVHCLNGGGRSGTFCAiCSVCemIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 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: 99.31 E-value: 1.20e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS------NQGSQRHYPSfihnKGKANYGPFIVEIM 517
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTelqereQEKCVQYWPS----EGSVTHGEITIEIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 518 NyhqypamtshmvKVMKRTFMISDIMATGAQNQQidaeVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDR 597
Cdd:cd14622   78 N------------DTLLETISIRDFLVTYNQEKQ----TRLVRQFHFHGWP-EIGIPAEGKGMIDLIAAVQKQQQQTGNH 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645547 598 petkPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVM 663
Cdd:cd14622  141 ----PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202

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: 99.38 E-value: 1.28e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINAS----YVNSWLRdkaYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQ---FRE 217
Cdd:cd14539    1 YINASliedLTPYCPR---FIATQA----PLPgtaADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQalvYGA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 218 IEVETTEVKTYSHFVIRTFKLTrtTPESIETRIVKHFHFTEW-ELDSFPYISAFIELRRRVRQFMEK-NPVEAPMVVHCS 295
Cdd:cd14539   74 ITVSLQSVRTTPTHVERIISIQ--HKDTRLSRSVVHLQFTTWpELGLPDSPNPLLRFIEEVHSHYLQqRSLQTPIVVHCS 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 212645547 296 NGAGRSGAF-LALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
Cdd:cd14539  152 SGVGRTGAFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

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: 100.19 E-value: 4.73e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN- 490
Cdd:cd14629   53 NKFKNRLVNIMPYELTRVCLQPIRGvEGSDY--INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKl 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 491 -----QGSQRHYPSfihnKGKANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVR 565
Cdd:cd14629  131 remgrEKCHQYWPA----ERSARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTIRQFQFT 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 566 MWPiENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 645
Cdd:cd14629  191 DWP-EQGVPKTGEGFIDFIGQVHKTKEQFG---QDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQ 266

                        250       260
                 ....*....|....*....|.
gi 212645547 646 RPQLIDMKDEYKYLYDVMLHW 666
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: 97.39 E-value: 5.48e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQavrtKPMN---AEFWRMVWELGSNCIVMLTKvfDFMRVMCLQYWPLtkfQFREIEVETTE 224
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQ----HPLEhtiKDFWQMIWDHNSQTIVMLTD--NELNEDEPIYWPT---KEKPLECETFK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 225 VK----------TYSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPYISAFiELRRRVRQfmEKNPVEAPMVVHC 294
Cdd:cd14550   72 VTlsgedhsclsNEIRLIVRDFILESTQDDYVLE--VRQFQCPSWPNPCSPIHTVF-ELINTVQE--WAQQRDGPIVVHD 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 212645547 295 SNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 348
Cdd:cd14550  147 RYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 100.49 E-value: 6.40e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 130 YDYNRVILPRIDGDENshYINASYVNSWLRDKAYVVTQAVRtKPMNAEFWRMVWELGSNCIVMLTKVFDFMRVmCLQYWP 209
Cdd:PHA02746  84 SDGKKIEVTSEDNAEN--YIHANFVDGFKEANKFICAQGPK-EDTSEDFFKLISEHESQVIVSLTDIDDDDEK-CFELWT 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 210 LTK---FQFREIEVETTEVKTYSHFVIRTFKLTRTTPESieTRIVKHFHFTEWELDSFPY-ISAFIELRRRV---RQFME 282
Cdd:PHA02746 160 KEEdseLAFGRFVAKILDIIEELSFTKTRLMITDKISDT--SREIHHFWFPDWPDNGIPTgMAEFLELINKVneeQAELI 237

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212645547 283 KN-----PVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 355
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: 1.04e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 405 CAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGeSKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHT 484
Cdd:cd14621   44 CEAASKEENKEKNRYVNILPYDHSRVHLTPVEG-VPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTAT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 485 VVNLSNQGSQRH--YPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMISDIMATGAQNQQidaevRICCVI 562
Cdd:cd14621  123 IVMVTNLKERKEckCAQYWPDQGCWTYGNIRVSVED-------VTVLVDYTVRKFCIQQVGDVTNKKPQ-----RLITQF 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 563 QVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMM 642
Cdd:cd14621  191 HFTSWP-DFGVPFTPIGMLKFLK-----KVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRI 264

                        250       260
                 ....*....|....*....|....*.
gi 212645547 643 RINRPQLIDMKDEYKYLYDVMLHWYM 668
Cdd:cd14621  265 RAQRCQMVQTDMQYVFIYQALLEHYL 290

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: 96.94 E-value: 1.70e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 417 NRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS---NQGS 493
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHS-DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmENGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 494 ---QRHYPSfihNKGKANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMIsdimatgaQNQQIDAEVRICcVIQVRMWPiE 570
Cdd:cd14618   80 vlcDHYWPS---ESTPVSYGHITVHLLAQSSEDEWT-------RREFKL--------WHEDLRKERRVK-HLHYTAWP-D 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 571 NKVPLSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 650
Cdd:cd14618  140 HGIPESTSSLMAFRELVREHVQATKGK---GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMI 216

                        250
                 ....*....|....
gi 212645547 651 DMKDEYKYLYDVML 664
Cdd:cd14618  217 QTLSQYIFLHSCIL 230

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: 96.55 E-value: 2.05e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 422 VVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFI 501
Cdd:cd14620    4 ILPYDHSRVILSQLDGIPCS-DYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 502 H--NKGKANYGPFIVEIMNYhqypamtSHMVKVMKRTFMISDIMATGAQNQqidaevRICCVIQVRMWPiENKVPLSTTG 579
Cdd:cd14620   83 YwpDQGCWTYGNIRVAVEDC-------VVLVDYTIRKFCIQPQLPDGCKAP------RLVTQLHFTSWP-DFGVPFTPIG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 580 LIDVIKMARSWrkrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYL 659
Cdd:cd14620  149 MLKFLKKVKSV-----NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFI 223


                 ....*
gi 212645547 660 YDVML 664
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: 94.63 E-value: 5.76e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQAVRTKPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT--KFQFREIEVET 222
Cdd:cd14601    2 YINANYINMEIPSSSIINRYIACQGPLPntcSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPsgSSSYGGFQVTC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 223 TEVKTYSHFVIRtfKLTRTTPESIETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQfmEKNPVEAPMVVHCSNGAGRS 301
Cdd:cd14601   82 HSEEGNPAYVFR--EMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSdFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 212645547 302 GAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
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: 8.38e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--NQGSQRHYPSFIHNKGKANYGPFIVEIMNYHQ 521
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTeiKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 522 YPAMTshmvkvmkrtfmISDIMATGAQNQQidaeVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDRPETk 601
Cdd:cd14552   81 YEDYT------------LRDFLVTKGKGGS----TRTVRQFHFHGWP-EVGIPDNGKGMIDLIAAVQKQQQQSGNHPIT- 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645547 602 ptiVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVM 663
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: 95.06 E-value: 2.38e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 120 DRNPYPDTLPYDYNRV-ILPriDGDENSHYINASYVNSWLRDKA--YVVTQAvrtkPMN---AEFWRMVWELGSNCIVML 193
Cdd:cd14599   40 ERNRIREVVPYEENRVeLVP--TKENNTGYINASHIKVTVGGEEwhYIATQG----PLPhtcHDFWQMVWEQGVNVIAMV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 194 TKVFDFMRVMCLQYWP----------------LTKFQFREIEVETTEVKTySHFVirtfkltrttpeSIETRIVKHFHFT 257
Cdd:cd14599  114 TAEEEGGRSKSHRYWPklgskhssatygkfkvTTKFRTDSGCYATTGLKV-KHLL------------SGQERTVWHLQYT 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 258 EW-------ELDSF-PYISAFIELRRRVRQFME-KNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKT 328
Cdd:cd14599  181 DWpdhgcpeEVQGFlSYLEEIQSVRRHTNSMLDsTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRH 260

                        250       260
                 ....*....|....*....|..
gi 212645547 329 LVNSRPHLIDSVEQYMFIYEVL 350
Cdd:cd14599  261 LREQRMFMIQTIAQYKFVYQVL 282

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: 3.28e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 412 ENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ 491
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHS-DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 492 ------GSQRHYPSfihnkGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMIsdimatgaqNQQIDAEVRICCVIQVR 565
Cdd:cd14630   81 vevgrvKCVRYWPD-----DTEVYGDIKVTLIE-------TEPLAEYVIRTFTV---------QKKGYHEIREIRQFHFT 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 566 MWPiENKVPLSTTGLIDVIKMARSWrkrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 645
Cdd:cd14630  140 SWP-DHGVPCYATGLLGFVRQVKFL-----NPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQ 213

                        250
                 ....*....|....*....
gi 212645547 646 RPQLIDMKDEYKYLYDVML 664
Cdd:cd14630  214 RVNMVQTEEQYVFVHDAIL 232

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: 92.07 E-value: 3.58e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQR---HYpsfiHNKGKANYGPFIVEIMN 518
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElkEGDQEqcaQY----WGDEKKTYGDIEVELKD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 519 YHQYPAMTshmvkvmKRTFMIsdimatgaQNQQIDaEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDR- 597
Cdd:cd14558   77 TEKSPTYT-------VRVFEI--------THLKRK-DSRTVYQYQYHKWK-GEELPEKPKDLVDMIKSIKQKLPYKNSKh 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645547 598 PETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 661
Cdd:cd14558  140 GRSVPIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203

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: 91.52 E-value: 9.95e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 417 NRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVnLSNQGSQR- 495
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCS-DYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIV-MVTQCVEKg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 496 -----HYPSFIHNKgkANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDimatgaqNQQIDAEvRICCVIQVRMWPiE 570
Cdd:cd14617   79 rvkcdHYWPADQDS--LYYGDLIVQMLSESVLPEWTI-------REFKICS-------EEQLDAP-RLVRHFHYTVWP-D 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 571 NKVPLSTTGLIDVIKMARSWRKRAPDrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 650
Cdd:cd14617  141 HGVPETTQSLIQFVRTVRDYINRTPG---SGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMV 217

                        250
                 ....*....|
gi 212645547 651 DMKDEYKYLY 660
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: 89.95 E-value: 4.46e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 417 NRDVMVVPPDHARPYLQTLHgESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQ 494
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIH-EEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNcmEAGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 495 ---RHYPSFihNKGKANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDIMatgaqnQQIDAEVRiccVIQVRMWPiEN 571
Cdd:cd14619   80 vkcEHYWPL--DYTPCTYGHLRVTVVSEEVMENWTV-------REFLLKQVE------EQKTLSVR---HFHFTAWP-DH 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 572 KVPLSTTGLIDVIKMARSWRKRapdRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLID 651
Cdd:cd14619  141 GVPSSTDTLLAFRRLLRQWLDQ---TMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQ 217

                        250
                 ....*....|...
gi 212645547 652 MKDEYKYLYDVML 664
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: 90.48 E-value: 5.62e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 412 ENRGKNRDVMVVPPDHARPYLQTLHG-ESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN 490
Cdd:cd17667   26 DNKHKNRYINILAYDHSRVKLRPLPGkDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 491 --QGSQRHYPSFIHNKGKANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDIMATGAQNQQIDAEVRICCVIQVR--M 566
Cdd:cd17667  106 lvEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTV-------RRFSIRNTKVKKGQKGNPKGRQNERTVIQYHytQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 567 WPiENKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINR 646
Cdd:cd17667  179 WP-DMGVPEYALPVLTFVR-----RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQR 252

                        250
                 ....*....|....*...
gi 212645547 647 PQLIDMKDEYKYLYDVML 664
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: 89.49 E-value: 5.74e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 417 NRDVMVVPPDHARPYLQTLHGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN---QGS 493
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTDDY--INANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcveQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 494 ---QRHYPSfihnKGKANYGPFIVeimnyhqypAMTSHMVKvmkRTFMISDIMATGAQNQQIDaevricCVIQVRM--WP 568
Cdd:cd14615   79 tkcEEYWPS----KQKKDYGDITV---------TMTSEIVL---PEWTIRDFTVKNAQTNESR------TVRHFHFtsWP 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 569 iENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQ 648
Cdd:cd14615  137 -DHGVPETTDLLINFRHLVREYMKQNP---PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPL 212

                        250
                 ....*....|.
gi 212645547 649 LIDMKDEYKYL 659
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: 88.22 E-value: 1.56e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARPYLQTLHGeSKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQG 492
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEG-VPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 493 SQ------RHYPsfihNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMIsdiMATGAQNQQidaEVRiccVIQVRM 566
Cdd:cd14553   82 ERsrvkcdQYWP----TRGTETYGLIQVTLLD-------TVELATYTVRTFAL---HKNGSSEKR---EVR---QFQFTA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 567 WPiENKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIganiCIDQM--DIDHE--VDVFHAVKMM 642
Cdd:cd14553  142 WP-DHGVPEHPTPFLAFLR-----RVKACNPPDAGPIVVHCSAGVGRTGCFI----VIDSMleRIKHEktVDIYGHVTCL 211

                        250       260
                 ....*....|....*....|..
gi 212645547 643 RINRPQLIDMKDEYKYLYDVML 664
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: 86.36 E-value: 3.50e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYV--NSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMR-VMCLQYWPLTKFQFRE---IEVE 221
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTF-EDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREfgrISVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 222 TTEVKTYSH-FVIRTFKLTRTtpESIET-RIVKHFHFTEWELDSFPYISAFI-ELRRRVRQFmekNPVEAPMVVHCSNGA 298
Cdd:cd17658   80 NKKLKHSQHsITLRVLEVQYI--ESEEPpLSVLHIQYPEWPDHGVPKDTRSVrELLKRLYGI---PPSAGPIVVHCSAGI 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 212645547 299 GRSGAFLALDANLELMKKtGQLDFFEYAKTLVNSRPHLIDSV---EQYMFIYE 348
Cdd:cd17658  155 GRTGAYCTIHNTIRRILE-GDMSAVDLSKTVRKFRSQRIGMVqtqDQYIFCYA 206

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: 3.76e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 412 ENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNq 491
Cdd:cd14633   39 ENRMKNRYGNIIAYDHSRVRLQPIEGETSS-DYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTN- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 492 gsqrhypsfihnkgkanygpfIVEI--MNYHQYPAMTSHMVKVMKRTFMISDIMA-----TGAQNQQIDAEVRICCVIQV 564
Cdd:cd14633  117 ---------------------LVEVgrVKCCKYWPDDTEIYKDIKVTLIETELLAeyvirTFAVEKRGVHEIREIRQFHF 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 565 RMWPiENKVPLSTTGLIDVIKMARSwrkRAPdrPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRI 644
Cdd:cd14633  176 TGWP-DHGVPYHATGLLGFVRQVKS---KSP--PNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRS 249

                        250       260
                 ....*....|....*....|
gi 212645547 645 NRPQLIDMKDEYKYLYDVML 664
Cdd:cd14633  250 RRVNMVQTEEQYVFIHDAIL 269

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: 85.84 E-value: 4.67e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKA-NYGPFIVEIMNYHQY 522
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEKPlECETFKVTLSGEDHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 523 PAMTSHMVKVmkRTFMIsdimatgaQNQQID--AEVRIccvIQVRMWPIENKvPLSTT-GLIDVIkmarswRKRAPDRpe 599
Cdd:cd14550   81 CLSNEIRLIV--RDFIL--------ESTQDDyvLEVRQ---FQCPSWPNPCS-PIHTVfELINTV------QEWAQQR-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212645547 600 TKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 660
Cdd:cd14550  139 DGPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199

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: 86.18 E-value: 6.48e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKA--YVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPltKFQFREIEVet 222
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQG----PLQNtcqDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWP--RLGSRHNTV-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 223 tevkTYSHFVIRT-FKLTR----TTPESI------ETRIVKHFHFTEWELDSFP--------YISAFIELRRRVRQFMEK 283
Cdd:cd14598   73 ----TYGRFKITTrFRTDSgcyaTTGLKIkhlltgQERTVWHLQYTDWPEHGCPedlkgflsYLEEIQSVRRHTNSTIDP 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645547 284 NPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
Cdd:cd14598  149 KSPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215

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: 9.33e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNL-SNQGSQR----HYPSfihNKGKANYGPFIVEIMN 518
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQGLAEdefvYWPS---REESMNCEAFTVTLIS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 519 yhqypamTSHMVKVMKRTFMISDIMATGAQNQQIdAEVRiccVIQVRMWPIENKVPLSTTGLIDVIKmarswrKRAPDRp 598
Cdd:cd17670   78 -------KDRLCLSNEEQIIIHDFILEATQDDYV-LEVR---HFQCPKWPNPDAPISSTFELINVIK------EEALTR- 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645547 599 eTKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
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: 1.03e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ------GSQRHYPsfihnKGKANYGPFIVEIM 517
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLvevgrvKCSKYWP-----DDSDTYGDIKITLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 518 NyhqypamTSHMVKVMKRTFMISdimatgAQNQQIDAEVricCVIQVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDR 597
Cdd:cd14632   76 K-------TETLAEYSVRTFALE------RRGYSARHEV---KQFHFTSWP-EHGVPYHATGLLAFIR-----RVKASTP 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645547 598 PETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
Cdd:cd14632  134 PDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200

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

Pssm-ID: 350473 [Multi-domain] Cd Length: 282 Bit Score: 87.07 E-value: 1.04e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--N 490
Cdd:cd14625   47 NKPKNRYANVIAYDHSRVILQPIEGIMGS-DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTklE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 491 QGSQRHYPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFmisDIMATGAQNQQidaEVRiccVIQVRMWPiE 570
Cdd:cd14625  126 EKSRIKCDQYWPSRGTETYGMIQVTLLD-------TIELATFCVRTF---SLHKNGSSEKR---EVR---QFQFTAWP-D 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 571 NKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 650
Cdd:cd14625  189 HGVPEYPTPFLAFLR-----RVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMV 263

                        250
                 ....*....|....
gi 212645547 651 DMKDEYKYLYDVML 664
Cdd:cd14625  264 QTEDQYSFIHDALL 277

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: 85.05 E-value: 1.19e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQavrtKPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLqYWP-------LTKFQFRE 217
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQ----HPLlhtIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPnkdepinCETFKVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 218 IEVETTEVKTYSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPyISAFIELRRRVRQfmEKNPVEAPMVVHCSNG 297
Cdd:cd17669   76 IAEEHKCLSNEEKLIIQDFILEATQDDYVLE--VRHFQCPKWPNPDSP-ISKTFELISIIKE--EAANRDGPMIVHDEHG 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 212645547 298 AGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
Cdd:cd17669  151 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203

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: 86.63 E-value: 1.39e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--N 490
Cdd:cd14626   41 NKPKNRYANVIAYDHSRVILTSVDGVPGS-DYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTrlE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 491 QGSQRHYPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMisdIMATGAQNQQidaEVRiccVIQVRMWPiE 570
Cdd:cd14626  120 EKSRVKCDQYWPIRGTETYGMIQVTLLD-------TVELATYSVRTFA---LYKNGSSEKR---EVR---QFQFMAWP-D 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 571 NKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 650
Cdd:cd14626  183 HGVPEYPTPILAFLR-----RVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMV 257

                        250
                 ....*....|....
gi 212645547 651 DMKDEYKYLYDVML 664
Cdd:cd14626  258 QTEDQYIFIHEALL 271

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: 4.15e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQRHYPSFIHNKGKANYGPFIVEIMNyhq 521
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNlkERKEKKCSQYWPDQGCWTYGNLRVRVED--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 522 ypamTSHMVKVMKRTFMISDIMATGAQNQQidaevRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSwrkraPDRPETK 601
Cdd:cd14551   78 ----TVVLVDYTTRKFCIQKVNRGIGEKRV-----RLVTQFHFTSWP-DFGVPFTPIGMLKFLKKVKS-----ANPPRAG 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 212645547 602 PTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 660
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: 5.37e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 405 CAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVE-VDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 483
Cdd:cd14609   34 CSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRS-DYINASPiIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 484 TVVNLSN------QGSQRHYPsfihNKGKANYGPFIVEIMNYHqypamtshmvkVMKRTFMISDIMATGAQNQqidaEVR 557
Cdd:cd14609  113 VIVMLTPlvedgvKQCDRYWP----DEGSSLYHIYEVNLVSEH-----------IWCEDFLVRSFYLKNVQTQ----ETR 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 558 ICCVIQVRMWPIENkVPLSTTGLIDV-IKMARSWRKRapdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDID-HEVDV 635
Cdd:cd14609  174 TLTQFHFLSWPAEG-IPSSTRPLLDFrRKVNKCYRGR------SCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDI 246

                        250       260
                 ....*....|....*....|...
gi 212645547 636 FHAVKMMRINRPQLIDMKDEYKY 658
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: 82.40 E-value: 9.73e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV---NLSNQGSQ---RHYPsfihNKGKANYGPFIVEIM 517
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVmitNLVERGRRkcdQYWP----KEGTETYGNIQVTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 518 NyhqypamTSHMVKVMKRTFMISDimaTGAQNQQIDAEVRIccVIQVRM--WPiENKVPLSTTGLIDVIKmarswRKRAP 595
Cdd:cd14549   77 S-------TEVLATYTVRTFSLKN---LKLKKVKGRSSERV--VYQYHYtqWP-DHGVPDYTLPVLSFVR-----KSSAA 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645547 596 DRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 661
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: 81.04 E-value: 6.46e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 408 GHRLENRGKNrdvmVVPPDHARPYLQTLHGESKDYTYINAVEVDGFT-RKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV 486
Cdd:cd14612   14 GHASKDRYKT----ILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 487 NLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNYHQYPAMTshmvkvmkrtfmISDIMAtgaqnqQIDAEVRICCVIQVRM 566
Cdd:cd14612   90 MITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYT------------IRDLTI------QLEEESRSVKHYWFSS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 567 WPiENKVPLSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINR 646
Cdd:cd14612  152 WP-DHQTPESAGPLLRLVAEVEESRQTAASP---GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDR 227

                        250
                 ....*....|....
gi 212645547 647 PQLIDMKDEYKYLY 660
Cdd:cd14612  228 GGMIQTSEQYQFLH 241

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: 1.09e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ------GSQRHYPsfihnKGKANYGPFIVEIM 517
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLvevgrvKCSRYWP-----DDTEVYGDIKVTLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 518 NyhqypamTSHMVKVMKRTFMISdimatgaqnQQIDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDR 597
Cdd:cd14555   76 E-------TEPLAEYVVRTFALE---------RRGYHEIREVRQFHFTGWP-DHGVPYHATGLLGFIR-----RVKASNP 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645547 598 PETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
Cdd:cd14555  134 PSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200

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: 79.70 E-value: 1.23e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 418 RDVMVVPPDHARPYLQTLHGEsKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYD-HACHTVV--NLSNQGSQ 494
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGE-ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEwKSCSIVMltELEERGQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 495 R---HYPSfihnKGKANYGPFIVEIMNYHQypamtshmvkvmKRTFMISDIMATGAQNQQiDAEVRiccVIQVRMWPiEN 571
Cdd:cd14623   80 KcaqYWPS----DGSVSYGDITIELKKEEE------------CESYTVRDLLVTNTRENK-SRQIR---QFHFHGWP-EV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 572 KVPLSTTGLIDVIKMARSWRKRAPDRPETkptiVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLID 651
Cdd:cd14623  139 GIPSDGKGMINIIAAVQKQQQQSGNHPIT----VHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQ 214

                        250
                 ....*....|..
gi 212645547 652 MKDEYKYLYDVM 663
Cdd:cd14623  215 TLEQYEFCYKVV 226

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: 78.87 E-value: 1.90e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQRHYPSFIHNKGKANYGPFIVeimnyhq 521
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNlvEKGRRKCDQYWPADGSEEYGNFLV------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 522 ypamTSHMVKVMK----RTFMISDI-MATGAQNQQidAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRkrapd 596
Cdd:cd17668   74 ----TQKSVQVLAyytvRNFTLRNTkIKKGSQKGR--PSGRVVTQYHYTQWP-DMGVPEYTLPVLTFVRKASYAK----- 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212645547 597 RPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
Cdd:cd17668  142 RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

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: 1.99e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 148 YINASYVNSWLRDKAYVVTQavrtKPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLqYWPLTK-------FQFRE 217
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQ----HPLphtTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPSREesmnceaFTVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 218 IEVETTEVKTYSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPyISAFIELRRRVRQfmEKNPVEAPMVVHCSNG 297
Cdd:cd17670   76 ISKDRLCLSNEEQIIIHDFILEATQDDYVLE--VRHFQCPKWPNPDAP-ISSTFELINVIKE--EALTRDGPTIVHDEFG 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 212645547 298 AGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
Cdd:cd17670  151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).

Pssm-ID: 350472 [Multi-domain] Cd Length: 284 Bit Score: 80.16 E-value: 2.31e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN-- 490
Cdd:cd14624   47 NKPKNRYANVIAYDHSRVLLSAIEGIPGS-DYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKle 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 491 QGSQRHYPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMisdIMATGAQNQQidaEVRiccVIQVRMWPiE 570
Cdd:cd14624  126 ERSRVKCDQYWPSRGTETYGLIQVTLLD-------TVELATYCVRTFA---LYKNGSSEKR---EVR---QFQFTAWP-D 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 571 NKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 650
Cdd:cd14624  189 HGVPEHPTPFLAFLR-----RVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMV 263

                        250
                 ....*....|....
gi 212645547 651 DMKDEYKYLYDVML 664
Cdd:cd14624  264 QTEDQYIFIHDALL 277

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: 2.58e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 405 CAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEV-DGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 483
Cdd:cd14610   36 TNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHS-DYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 484 TVVNLS---NQGSQRHYpSFIHNKGKANYGPFIVEIMNYHQYPAmtshmvKVMKRTFMISDIMATgaqnqqidaEVRICC 560
Cdd:cd14610  115 VIVMLTplaENGVKQCY-HYWPDEGSNLYHIYEVNLVSEHIWCE------DFLVRSFYLKNLQTN---------ETRTVT 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 561 VIQVRMWpIENKVPLSTTGLIDV-IKMARSWRKRapdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDID-HEVDVFHA 638
Cdd:cd14610  179 QFHFLSW-NDQGVPASTRSLLDFrRKVNKCYRGR------SCPIIVHCSDGAGRSGTYILIDMVLNKMAKGaKEIDIAAT 251

                        250       260
                 ....*....|....*....|
gi 212645547 639 VKMMRINRPQLIDMKDEYKY 658
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: 73.93 E-value: 5.80e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547   567 WPiENKVPLSTTGLIDVIKMARSWRKrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD-IDHEVDVFHAVKMMRIN 645
Cdd:smart00012  10 WP-DHGVPESPDSILELLRAVKKNLN---QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVKELRSQ 85

                           90       100
                   ....*....|....*....|
gi 212645547   646 RPQLIDMKDEYKYLYDVMLH 665
Cdd:smart00012  86 RPGMVQTEEQYLFLYRALLE 105

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 73.93 E-value: 5.80e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547   567 WPiENKVPLSTTGLIDVIKMARSWRKrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD-IDHEVDVFHAVKMMRIN 645
Cdd:smart00404  10 WP-DHGVPESPDSILELLRAVKKNLN---QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVKELRSQ 85

                           90       100
                   ....*....|....*....|
gi 212645547   646 RPQLIDMKDEYKYLYDVMLH 665
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: 77.37 E-value: 5.90e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDH--ACHTVV-NLSNQGSQRHYPSFIHNkgKANYGPFIVEIMNyh 520
Cdd:cd14631   15 YINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEqsACIVMVtNLVEVGRVKCYKYWPDD--TEVYGDFKVTCVE-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 521 qypamTSHMVKVMKRTFMISdimatgaqnQQIDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDRPET 600
Cdd:cd14631   91 -----MEPLAEYVVRTFTLE---------RRGYNEIREVKQFHFTGWP-DHGVPYHATGLLSFIR-----RVKLSNPPSA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645547 601 KPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
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: 76.96 E-value: 7.49e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-NQGSQRHYPSFIHNKGKA-NYGPFIVEIMNyhq 521
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPdGQNMAEDEFVYWPNKDEPiNCETFKVTLIA--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 522 ypamTSHMVKVMKRTFMISDIMATGAQNQQIdAEVRiccVIQVRMWPIENKvPLSTT-GLIDVIKMARSWRKrapdrpet 600
Cdd:cd17669   78 ----EEHKCLSNEEKLIIQDFILEATQDDYV-LEVR---HFQCPKWPNPDS-PISKTfELISIIKEEAANRD-------- 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645547 601 KPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
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: 4.53e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARPYLQTLHGEsKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQG 492
Cdd:cd14614   12 NRCKNRYTNILPYDFSRVKLVSMHEE-EGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 493 SQR-----HYPSFihNKGKANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISdiMATGAQnqqidaevricCVIQVRM- 566
Cdd:cd14614   91 EKRrvkcdHYWPF--TEEPVAYGDITVEMLSEEEQPDWA-------IREFRVS--YADEVQ-----------DVMHFNYt 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 567 -WPiENKVPLSTTG--LIDVIKMARSWRKRAPDrpetkPTIVMSHNGVSRVGVYIGANiCIDQMDIDHE-VDVFHAVKMM 642
Cdd:cd14614  149 aWP-DHGVPTANAAesILQFVQMVRQQAVKSKG-----PMIIHCSAGVGRTGTFIALD-RLLQHIRDHEfVDILGLVSEM 221

                        250
                 ....*....|....*...
gi 212645547 643 RINRPQLIDMKDEYKYLY 660
Cdd:cd14614  222 RSYRMSMVQTEEQYIFIH 239

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 75.04 E-value: 1.69e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 412 ENRGKNRDVMVVPPDHARPYLQTLHGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-- 489
Cdd:PHA02747  50 ENQPKNRYWDIPCWDHNRVILDSGGGSTSDY--IHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTpt 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 490 --NQGSQRHYPSFIHNK-GKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMISDimatgaqnqQIDAEVRICCVIQVRM 566
Cdd:PHA02747 128 kgTNGEEKCYQYWCLNEdGNIDMEDFRIETLK-------TSVRAKYILTLIEITD---------KILKDSRKISHFQCSE 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 567 WPIENkVPLSTTGLIDVIKMARSWRKRA-----PDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKM 641
Cdd:PHA02747 192 WFEDE-TPSDHPDFIKFIKIIDINRKKSgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                        250       260
                 ....*....|....*....|....*..
gi 212645547 642 MRINRPQLIDMKDEYKYL---YDVMLH 665
Cdd:PHA02747 271 IREQRHAGIMNFDDYLFIqpgYEVLHY 297

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: 3.21e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 412 ENRGKNRDVMVVPPDHARPYLQTLHGESKDYTYINA--------VEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 483
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINAniimpefeTKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 484 TVVnLSNQGSQRhypsfihnkGKANYGPFIVEIMNYHQYPAMTSHMVK-VMKRTFMISDIMAT--GAQNQQidaevRICC 560
Cdd:cd14605   81 VIV-MTTKEVER---------GKSKCVKYWPDEYALKEYGVMRVRNVKeSAAHDYILRELKLSkvGQGNTE-----RTVW 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 561 VIQVRMWPiENKVPLSTTGLIDVIKMARswrKRAPDRPETKPTIVMSHNGVSRVGVYIGANICID---QMDIDHEVDVFH 637
Cdd:cd14605  146 QYHFRTWP-DHGVPSDPGGVLDFLEEVH---HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDiirEKGVDCDIDVPK 221

                        250       260       270
                 ....*....|....*....|....*....|..
gi 212645547 638 AVKMMRINRPQLIDMKDEYKYLYDVMLHWYMT 669
Cdd:cd14605  222 TIQMVRSQRSGMVQTEAQYRFIYMAVQHYIET 253

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: 72.94 E-value: 4.96e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 408 GHRLENRGKNRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDH------- 480
Cdd:cd14603   25 GGRKENVKKNRYKDILPYDQTRVIL-SLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYgvkvilm 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 481 ACHTVVNlSNQGSQRHYPSfihNKGKANYGPFIVEIMNYHQYPAMTshMVKVMKRTFmisdimatgaqnQQidaEVRICC 560
Cdd:cd14603  104 ACREIEM-GKKKCERYWAQ---EQEPLQTGPFTITLVKEKRLNEEV--ILRTLKVTF------------QK---ESRSVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 561 VIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDrpetkPTIVMSHNGVSRVGV-----YIgANICIDQMdIDHEVDV 635
Cdd:cd14603  163 HFQYMAWP-DHGIPDSPDCMLAMIELARRLQGSGPE-----PLCVHCSAGCGRTGVictvdYV-RQLLLTQR-IPPDFSI 234

                        250       260
                 ....*....|....*....|....*
gi 212645547 636 FHAVKMMRINRPQLIDMKDEYKYLY 660
Cdd:cd14603  235 FDVVLEMRKQRPAAVQTEEQYEFLY 259

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: 5.20e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-------NQGSQrHYPSFihNKGKANYGPFIVEI 516
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTrceegnrNKCAQ-YWPSM--EEGSRAFGDVVVKI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 517 MNYHQYPamtshmvKVMKRTFMISdimatgaqNQQIDAEVRICCVIQVRMWPiENKVPLSTTGLidvIKMARswRKRAPD 596
Cdd:cd14557   78 NEEKICP-------DYIIRKLNIN--------NKKEKGSGREVTHIQFTSWP-DHGVPEDPHLL---LKLRR--RVNAFN 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645547 597 RPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 660
Cdd:cd14557  137 NFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200

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: 72.40 E-value: 8.30e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNR--DVMVVppDHARPYLQTLHGEskDYT-YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS 489
Cdd:cd14543   29 NQEKNRygDVLCL--DQSRVKLPKRNGD--ERTdYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 490 N--QGSQRHYPSFIHNKGKA--NYGPFIV---EIMNYHQYpamtshmvkvMKRTFMIsdimatgaQNQQIDaEVRicCVI 562
Cdd:cd14543  105 RvvERGRVKCGQYWPLEEGSslRYGDLTVtnlSVENKEHY----------KKTTLEI--------HNTETD-ESR--QVT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 563 QVRM--WPiENKVPLSTTGLID------------VIKMARSWRKrapdRPETKPTIVMSHNGVSRVGVYIGANICIDQMD 628
Cdd:cd14543  164 HFQFtsWP-DFGVPSSAAALLDflgevrqqqalaVKAMGDRWKG----HPPGPPIVVHCSAGIGRTGTFCTLDICLSQLE 238

                        250       260       270
                 ....*....|....*....|....*....|..
gi 212645547 629 IDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 660
Cdd:cd14543  239 DVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270

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: 9.20e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 399 TLRIGDCAGGHRLENRGKNRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIY 478
Cdd:cd14604   43 TEKIYPTATGEKEENVKKNRYKDILPFDHSRVKL-TLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIW 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 479 DHACHTVV------NLSNQGSQRHYPsfIHNKGKANYGPFIVEIMNYHqypAMTSHMVkvmkRTFMIsdimatgaqnqQI 552
Cdd:cd14604  122 EYNVAIIVmacrefEMGRKKCERYWP--LYGEEPMTFGPFRISCEAEQ---ARTDYFI----RTLLL-----------EF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 553 DAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRapdrpETKPTIVMSHNGVSRVGVyiganIC-IDQM---- 627
Cdd:cd14604  182 QNETRRLYQFHYVNWP-DHDVPSSFDSILDMISLMRKYQEH-----EDVPICIHCSAGCGRTGA-----ICaIDYTwnll 250

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 212645547 628 ---DIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 660
Cdd:cd14604  251 kagKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 286

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: 67.62 E-value: 1.52e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNqgsqrhypsfIHNKGKanygpfiveiMNYHQYP 523
Cdd:cd14616   27 YINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQ----------CFEKGR----------IRCHQYW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 524 AMTSHMVKVMkrtfmiSDIMATG-AQNQQIDAEVRICCV------IQVRM-----WPiENKVPLSTTGLIDVIKMARSWR 591
Cdd:cd14616   87 PEDNKPVTVF------GDIVITKlMEDVQIDWTIRDLKIerhgdyMMVRQcnftsWP-EHGVPESSAPLIHFVKLVRASR 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 592 KRapdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDiDHE-VDVFHAVKMMRINRPQLIDMKDEYKYLY 660
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: 1.68e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 410 RLENRGKNRDVMVVPPDHAR------------------PYLQTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVD 471
Cdd:PHA02746  48 KKENLKKNRFHDIPCWDHSRvvinaheslkmfdvgdsdGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 472 SFWTLIYDHACHTVVNLS--NQGSQRHYPSFIHNKG-KANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISDIMATGAq 548
Cdd:PHA02746 128 DFFKLISEHESQVIVSLTdiDDDDEKCFELWTKEEDsELAFGRFVAKILDIIEELSFT-------KTRLMITDKISDTS- 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 549 nqqidaevRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKR----APDRPETK-PTIVMSHNGVSRVGVYIGANIC 623
Cdd:PHA02746 200 --------REIHHFWFPDWP-DNGIPTGMAEFLELINKVNEEQAElikqADNDPQTLgPIVVHCSAGIGRAGTFCAIDNA 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 212645547 624 IDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVM 663
Cdd:PHA02746 271 LEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310

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: 66.71 E-value: 2.49e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINA----VEVDGFTRKaeFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFihnkgkaNYGPFiveiMNY 519
Cdd:cd14540    1 YINAshitATVGGKQRF--YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCF-------RYWPT----LGG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 520 HqYPAMTSHMVKVMKRTFMISDIMATGA---QNQQIDAEvRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKR--- 593
Cdd:cd14540   68 E-HDALTFGEYKVSTKFSVSSGCYTTTGlrvKHTLSGQS-RTVWHLQYTDWP-DHGCPEDVSGFLDFLEEINSVRRHtnq 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212645547 594 --APDRPETkPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
Cdd:cd14540  145 dvAGHNRNP-PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216

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: 66.31 E-value: 3.42e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEV-DGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS------NQGSQRHYPsfihNKGKANYGPFIVEI 516
Cdd:cd14546    1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTrlqengVKQCARYWP----EEGSEVYHIYEVHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 517 MNYHQYPAmtSHMVkvmkRTFMISDImatgaQNQqidaEVRICCVIQVRMWPIENkVPLSTTGLIDV-IKMARSWRKRap 595
Cdd:cd14546   77 VSEHIWCD--DYLV----RSFYLKNL-----QTS----ETRTVTQFHFLSWPDEG-IPASAKPLLEFrRKVNKSYRGR-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645547 596 drpeTKPTIVMSHNGVSRVGVYIGANICIDQMDID-HEVDVFHAVKMMRINRPQLIDMKDEYKYLY 660
Cdd:cd14546  139 ----SCPIVVHCSDGAGRTGTYILIDMVLNRMAKGaKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 67.30 E-value: 5.30e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 134 RVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDfmRVMCLQYWPL--- 210
Cdd:PHA02740  64 RLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACD-KFLQALSDNKVQIIVLISRHAD--KKCFNQFWSLkeg 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 211 TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPESietRIVKHFHFTEWELDSFPY-ISAFIELRRRVRQF---MEKNPV 286
Cdd:PHA02740 141 CVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA---QKISHFQYTAWPADGFSHdPDAFIDFFCNIDDLcadLEKHKA 217

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645547 287 E---APMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 350
Cdd:PHA02740 218 DgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 66.95 E-value: 6.91e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 410 RLENRGKNRDVMVVPPDHARPYLQTLHGESKdytYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS 489
Cdd:PHA02742  49 ELKNMKKCRYPDAPCFDRNRVILKIEDGGDD---FINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMIT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 490 ---NQGSQRHYPSFI-HNKGKANYGPFIV---EIMNYHQYPAMTSHMVKVmkRTFMISDIMATGAQNqqidaevriccvi 562
Cdd:PHA02742 126 kimEDGKEACYPYWMpHERGKATHGEFKIktkKIKSFRNYAVTNLCLTDT--NTGASLDIKHFAYED------------- 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 563 qvrmWPiENKVPLSTTGLIDVIKMARSWRKRA------PDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVF 636
Cdd:PHA02742 191 ----WP-HGGLPRDPNKFLDFVLAVREADLKAdvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLL 265

                        250       260       270
                 ....*....|....*....|....*....|
gi 212645547 637 HAVKMMRINRPQLIDMKDEYKYLYDVMLHW 666
Cdd:PHA02742 266 SIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 295

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: 65.50 E-value: 8.11e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 417 NRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRK-AEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGS 493
Cdd:cd14547    1 NRYKTILPNEHSRVCL-PSVDDDPLSSYINANYIRGYDGEeKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNltEAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 494 QR--HYPSFIHNKgkaNYGPFIVEIMNYHQYPAMTShmvkvmkRTFMIsdimatgaqnqQIDAEVRICCVIQVRMWPiEN 571
Cdd:cd14547   80 EKcaQYWPEEENE---TYGDFEVTVQSVKETDGYTV-------RKLTL-----------KYGGEKRYLKHYWYTSWP-DH 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 572 KVPLSTTGLIDVIKMARSWRKRAPDRPetkPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLID 651
Cdd:cd14547  138 KTPEAAQPLLSLVQEVEEARQTEPHRG---PIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQ 214


                 ....*....
gi 212645547 652 MKDEYKYLY 660
Cdd:cd14547  215 TAEQYEFVH 223

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: 1.44e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 408 GHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDYTYINAVEVD----GFTRKAE-FIVTEWPKQSTVDSFWTLIYDHAC 482
Cdd:cd14606   13 GQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAWQENS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 483 HTVVNLSNQ---GSQRHYPSFIHNKGKANYGPFIVEIMNYHQypaMTSHMVKVMKrtfmISDIMATGAqnqqidaeVRIC 559
Cdd:cd14606   93 RVIVMTTREvekGRNKCVPYWPEVGMQRAYGPYSVTNCGEHD---TTEYKLRTLQ----VSPLDNGEL--------IREI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 560 CVIQVRMWPiENKVPLSTTGlidVIKMARSWRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD---IDHEVDVF 636
Cdd:cd14606  158 WHYQYLSWP-DHGVPSEPGG---VLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIStkgLDCDIDIQ 233

                        250       260
                 ....*....|....*....|....
gi 212645547 637 HAVKMMRINRPQLIDMKDEYKYLY 660
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: 2.43e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 416 KNRDVMVVPPDHARPYLQTLHGESKDYTYINAVEVDGFTRKAE-FIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNqgsq 494
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITN---- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 495 rhypsfihnkgkanygpfiVEIMN-----YHQYPAMTSHMVKVMKRTFMISDIMATGAQNQQIDAEVRICCVIQVRMWPi 569
Cdd:cd14613  104 -------------------IEEMNekcteYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWP- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 570 ENKVPLSTTGLIDVIKMARSWRKRAPdrPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQL 649
Cdd:cd14613  164 DQKTPDNAPPLLQLVQEVEEARQQAE--PNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241

                        250
                 ....*....|....
gi 212645547 650 IDMKDEYKYLYDVM 663
Cdd:cd14613  242 IQTCEQYQFVHHVL 255

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 64.18 E-value: 7.83e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARpylQTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ- 491
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSR---VILPAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKk 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 492 --GSQRHYPSFIH-NKGKANYGPFIVEIMNYHQYPamtsHMVkvmKRTFMISDimATGAQNQQIDaevriccvIQVRMWP 568
Cdd:PHA02738 126 enGREKCFPYWSDvEQGSIRFGKFKITTTQVETHP----HYV---KSTLLLTD--GTSATQTVTH--------FNFTAWP 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 569 iENKVPLSTTGLIDVIKMARSWRKR--------APDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVK 640
Cdd:PHA02738 189 -DHDVPKNTSEFLNFVLEVRQCQKElaqeslqiGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVS 267

                        250       260
                 ....*....|....*....|...
gi 212645547 641 MMRINRPQLIDMKDEYKYLYDVM 663
Cdd:PHA02738 268 SIRNQRYYSLFIPFQYFFCYRAV 290

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: 62.24 E-value: 1.08e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 416 KNRDVMVVPPDHARPYLQTLHGESKDYTYINAVEVDGFTRKAE-FIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQ 494
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 495 RHYPSFIHNKGKANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDimatGAQNQQIDAevriccvIQVRMWPiENKVP 574
Cdd:cd14611   82 NEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTI-------RNLTLKQ----GSQSRSVKH-------YWYTSWP-DHKTP 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 575 LSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKD 654
Cdd:cd14611  143 DSAQPLLQLMLDVEEDRLASPGR---GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSE 219


                 ....*.
gi 212645547 655 EYKYLY 660
Cdd:cd14611  220 QYEFVH 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: 61.63 E-value: 1.34e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKA-EFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQG------SQRHYPSfihNKGKA-NYGPFIVE 515
Cdd:cd14539    1 YINASLIEDLTPYCpRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQenekqkVHRYWPT---ERGQAlVYGAITVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 516 IMNYHQYPAMTSHMVKVMKRTfmisdimatgaqnqqiDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRap 595
Cdd:cd14539   78 LQSVRTTPTHVERIISIQHKD----------------TRLSRSVVHLQFTTWP-ELGLPDSPNPLLRFIEEVHSHYLQ-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645547 596 DRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEV-DVFHAVKMMRINRPQLIDMKDEYKYLYD 661
Cdd:cd14539  139 QRSLQTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

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

Pssm-ID: 350496 [Multi-domain] Cd Length: 206 Bit Score: 61.33 E-value: 1.45e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINA--VEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSnqgsqrhypSFIHNKGKANYGPFIVEIMNYHQ 521
Cdd:cd17658    1 YINAslVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLT---------RLVDNYSTAKCADYFPAEENESR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 522 YPAMTSHMVKVMKRTfmISDIMATGAQNQQIDAEVRICCV--IQVRMWPiENKVPLSTTGLIDVIKmaRSWrkRAPdrPE 599
Cdd:cd17658   72 EFGRISVTNKKLKHS--QHSITLRVLEVQYIESEEPPLSVlhIQYPEWP-DHGVPKDTRSVRELLK--RLY--GIP--PS 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212645547 600 TKPTIVMSHNGVSRVGVYIGANICIDQ-MDIDHE-VDVFHAVKMMRINRPQLIDMKDEYKYLY 660
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: 60.17 E-value: 6.45e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 413 NRGKNRDVMVVPPDHARPYLQTLHGESKDYTYINA----VEVDGFTRKAE---FIVTEWPKQSTVDSFWTLIYDHACHTV 485
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINAnyirNENEGPTTDENaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 486 VNLS---NQGSQ---RHYPSFIHNKgkaNYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISdimaTGAQNqqidAEVRIC 559
Cdd:cd14544   81 VMTTkevERGKNkcvRYWPDEGMQK---QYGPYRVQNVSEHDTTDYT-------LRELQVS----KLDQG----DPIREI 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 560 CVIQVRMWPiENKVPLSTTGLIDVIKMArswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD---IDHEVDVF 636
Cdd:cd14544  143 WHYQYLSWP-DHGVPSDPGGVLNFLEDV---NQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKrkgLDCDIDIQ 218

                        250       260       270
                 ....*....|....*....|....*....|...
gi 212645547 637 HAVKMMRINRPQLIDMKDEYKYLYDVMLHWYMT 669
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: 59.48 E-value: 1.58e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 412 ENRGKNRDVMVVPPDHARPYLQtlhgESKDY---TYINaVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNL 488
Cdd:cd14600   39 QNMDKNRYKDVLPYDATRVVLQ----GNEDYinaSYVN-MEIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 489 SNqgsqrhypsfIHNKGKA---NYGPFIVEIMNYHQYpAMTSHM----VKVMKRTFMISDImATGAQnqqidaevRICCV 561
Cdd:cd14600  114 TT----------LTERGRTkchQYWPDPPDVMEYGGF-RVQCHSedctIAYVFREMLLTNT-QTGEE--------RTVTH 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 562 IQVRMWPiENKVPLSTTGLIDVIKMARSWRKrapdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKM 641
Cdd:cd14600  174 LQYVAWP-DHGVPDDSSDFLEFVNYVRSKRV------ENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRK 246

                        250       260
                 ....*....|....*....|....*.
gi 212645547 642 MRINRPQLIDMKDEYKYLYDVMLHWY 667
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: 1.82e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 416 KNRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV------NLS 489
Cdd:cd14602    1 KNRYKDILPYDHSRVEL-SLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVmacmefEMG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 490 NQGSQRHYPSFihNKGKANYGPFIVEIMNYHQypaMTSHMVKVMKRTFmisdimatgaqnqqiDAEVRICCVIQVRMWPi 569
Cdd:cd14602   80 KKKCERYWAEP--GEMQLEFGPFSVTCEAEKR---KSDYIIRTLKVKF---------------NSETRTIYQFHYKNWP- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 570 ENKVPLSTTGLIDVIKMARSWRKRapdrpETKPTIVMSHNGVSRVGVyiganIC-IDQM-------DIDHEVDVFHAVKM 641
Cdd:cd14602  139 DHDVPSSIDPILELIWDVRCYQED-----DSVPICIHCSAGCGRTGV-----ICaIDYTwmllkdgIIPENFSVFSLIQE 208

                        250       260
                 ....*....|....*....|....*.
gi 212645547 642 MRINRPQLIDMKDEYKYLYDVMLHWY 667
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: 55.51 E-value: 1.23e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV------NLSNQGSQRHYPSfihNKGKA-NYGPFIVEi 516
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVmacrefEMGKKKCERYWPE---EGEEQlQFGPFKIS- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 517 mnYHQYPAMTS-HMVKVMKRTFmisdimatgaqnqqiDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRap 595
Cdd:cd14542   77 --LEKEKRVGPdFLIRTLKVTF---------------QKESRTVYQFHYTAWP-DHGVPSSVDPILDLVRLVRDYQGS-- 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645547 596 drpETKPTIVMSHNGVSRVGVyiganIC-ID--------QMdIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 660
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: 56.19 E-value: 1.90e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 412 ENRGKNRDVMVVPPDHARPylqTLHGESKDYTYINAVEVDGFTRKaeFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-- 489
Cdd:cd14608   24 KNKNRNRYRDVSPFDHSRI---KLHQEDNDYINASLIKMEEAQRS--YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNrv 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 490 -NQGS---QRHYPsfihnkgKANYGPFIVEIMNYHqypamTSHMVKVMKRTFMISDIMATGAQNQqidaEVRICCVIQVR 565
Cdd:cd14608   99 mEKGSlkcAQYWP-------QKEEKEMIFEDTNLK-----LTLISEDIKSYYTVRQLELENLTTQ----ETREILHFHYT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 566 MWPiENKVPLSTTGLIDVIKMArswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHE---VDVFHAVKMM 642
Cdd:cd14608  163 TWP-DFGVPESPASFLNFLFKV---RESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpssVDIKKVLLEM 238

                        250
                 ....*....|....*...
gi 212645547 643 RINRPQLIDMKDEYKYLY 660
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: 4.10e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 412 ENRGKNRDVMVVPPDHARPYLQTLHGeskdytYINAVEVDGFTRKAEF--IVTEWPKQSTVDSFWTLIYDHACHTVVNLS 489
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLGDEGG------YINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 490 NQ------GSQRHYPsfihnkgkanygpfiveimnyhqypamtshmvKVMKRTFMISD-IMATGAQNQQIDA-------- 554
Cdd:cd14597   76 QEveggkiKCQRYWP--------------------------------EILGKTTMVDNrLQLTLVRMQQLKNfvirvlel 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 555 ------EVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKrapdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMD 628
Cdd:cd14597  124 ediqtrEVRHITHLNFTAWP-DHDTPSQPEQLLTFISYMRHIHK-------SGPIITHCSAGIGRSGTLICIDVVLGLIS 195

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 212645547 629 IDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVMLH 665
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: 52.06 E-value: 2.24e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 444 YINA--VEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ------GSQRHYPSFIHNKGK-ANYGPFIV 514
Cdd:cd14596    1 YINAsyITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREvergkvKCHRYWPETLQEPMElENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 515 eimnyhQYPAMTSHMVKVMKRTfmisdimatgaqnQQIDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKra 594
Cdd:cd14596   81 ------NYQALQYFIIRIIKLV-------------EKETGENRLIKHLQFTTWP-DHGTPQSSDQLVKFICYMRKVHN-- 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 595 pdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 664
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: 50.35 E-value: 1.46e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 412 ENRGKNRDVMVVPPDHARPYLQTLHGEskdytYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNq 491
Cdd:cd14607   23 ENRNRNRYRDVSPYDHSRVKLQNTEND-----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 492 gsqrhypsfIHNKGK---ANYGPFIVEIMNYHQYPAMTSHMVKVMKRTFMISDIMatgaQNQQIDA-EVRICCVIQVRMW 567
Cdd:cd14607   97 ---------IVEKDSvkcAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLL----QLENINSgETRTISHFHYTTW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 568 PiENKVPLSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDH--EVDVFHAVKMMRIN 645
Cdd:cd14607  164 P-DFGVPESPASFLNFLFKVRESGSLSPEH---GPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKY 239

                        250
                 ....*....|....*
gi 212645547 646 RPQLIDMKDEYKYLY 660
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: 3.87e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 414 RGKNRDVMVVPPDHARPYLQtlhGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--- 490
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLK---QGDNDY--INASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKlme 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 491 QGSQRHYPSFIHNKGKANYGP---FIVEIMNYHQYPAMTshmvkvmKRTFMISDImATGaqnqqidaEVRICCVIQVRMW 567
Cdd:cd14545   76 KGQIKCAQYWPQGEGNAMIFEdtgLKVTLLSEEDKSYYT-------VRTLELENL-KTQ--------ETREVLHFHYTTW 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645547 568 PiENKVPLSTTGLIDVIKMARSWRKRAPDrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDIDH--EVDVFHAVKMMRIN 645
Cdd:cd14545  140 P-DFGVPESPAAFLNFLQKVRESGSLSSD---VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKY 215

                        250
                 ....*....|....*
gi 212645547 646 RPQLIDMKDEYKYLY 660
Cdd:cd14545  216 RMGLIQTPDQLRFSY 230